ID   GPD1_YEAST     STANDARD;      PRT;   391 AA.
AC   Q00055;
DT   01-JUL-1993 (REL. 26, CREATED)
DT   01-JUL-1993 (REL. 26, LAST SEQUENCE UPDATE)
DT   01-FEB-1997 (REL. 35, LAST ANNOTATION UPDATE)
DE   GLYCEROL-3-PHOSPHATE DEHYDROGENASE (NAD+) 1 (EC 1.1.1.8).
GN   GPD1 OR OSG1 OR DAR1 OR HOR1 OR YDL022W OR D2830.
OS   SACCHAROMYCES CEREVISIAE (BAKER'S YEAST).
OC   EUKARYOTA; FUNGI; ASCOMYCOTINA; HEMIASCOMYCETES.
RN   [1]
RP   SEQUENCE FROM N.A., AND SEQUENCE OF 30-49.
RX   MEDLINE; 95020570.
RA   LARSSON K., ANSELL R., ERIKSSON P., ADLER L.;
RL   MOL. MICROBIOL. 10:1101-1111(1993).
RN   [2]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 94254870.
RA   ALBERTYN J., HOHMANN S., THEVELEIN J.M., PRIOR B.A.;
RL   MOL. CELL. BIOL. 14:4135-4144(1994).
RN   [3]
RP   SEQUENCE FROM N.A.
RC   STRAIN=J132B;
RX   MEDLINE; 95050285.
RA   WANG H.T., RAHAIM P., ROBBINS P., YOCUM R.R.;
RL   J. BACTERIOL. 176:7091-7095(1994).
RN   [4]
RP   SEQUENCE FROM N.A.
RC   STRAIN=S288C;
RA   ANDRE B., VISSERS S., URRESTARAZU L.;
RL   SUBMITTED (FEB-1995) TO EMBL/GENBANK/DDBJ DATA BANKS.
RN   [5]
RP   SEQUENCE OF 1-102 FROM N.A.
RX   MEDLINE; 91285439.
RA   SLEEP D., OGDEN J.E., ROBERTS N.A., GOODEY A.R.;
RL   GENE 101:89-96(1991).
RN   [6]
RP   SEQUENCE OF 8-16; 95-108 AND 160-173.
RC   STRAIN=ATCC 38531 / Y41;
RX   MEDLINE; 97089742.
RA   NORBECK J., BLOMBERG A.;
RL   FEMS MICROBIOL. LETT. 137:1-8(1996).
CC   -!- CATALYTIC ACTIVITY: SN-GLYCEROL 3-PHOSPHATE + NAD(+) =
CC       GLYCERONE PHOSPHATE + NADH.
CC   -!- SUBCELLULAR LOCATION: CYTOPLASMIC (POTENTIAL).
CC   -!- INDUCTION: BY OSMOTIC STRESS.
CC   -!- CAUTION: WAS ORIGINALLY (REF.5) THOUGHT TO BE GUT2, THE FAD-
CC       DEPENDENT GLYCEROL-3-PHOSPHATE DEHYDROGENASE.
DR   EMBL; Z24454; G394741; -.
DR   EMBL; X76859; G439686; -.
DR   EMBL; U04621; G436875; -.
DR   EMBL; Z48432; G683675; -.
DR   EMBL; Z74071; E252981; -.
DR   EMBL; M38740; G495705; -.
DR   PIR; PQ0148; PQ0148.
DR   PIR; S34641; S34641.
DR   PIR; S40059; S40059.
DR   LISTA; SC00403; GPD1.
DR   SGD; L0000722; GPD1.
DR   PROSITE; PS00957; NAD_G3PDH.
KW   OXIDOREDUCTASE; NAD; MULTIGENE FAMILY.
FT   CONFLICT    103    107       DNLVA -> TIWLL (IN G495705).
SQ   SEQUENCE   391 AA;  42869 MW;  40476ED8 CRC32;
     MSAAADRLNL TSGHLNAGRK RSSSSVSLKA AEKPFKVTVI GSGNWGTTIA KVVAENCKGY
     PEVFAPIVQM WVFEEEINGE KLTEIINTRH QNVKYLPGIT LPDNLVANPD LIDSVKDVDI
     IVFNIPHQFL PRICSQLKGH VDSHVRAISC LKGFEVGAKG VQLLSSYITE ELGIQCGALS
     GANIATEVAQ EHWSETTVAY HIPKDFRGEG KDVDHKVLKA LFHRPYFHVS VIEDVAGISI
     CGALKNVVAL GCGFVEGLGW GNNASAAIQR VGLGEIIRFG QMFFPESREE TYYQESAGVA
     DLITTCAGGR NVKVARLMAT SGKDAWECEK ELLNGQSAQG LITCKEVHEW LETCGSVEDF
     PLFEAVYQIV YNNYPMKNLP DMIEELDLHE D
//
ID   GPD2_YEAST     STANDARD;      PRT;   440 AA.
AC   P41911; P50905;
DT   01-NOV-1995 (REL. 32, CREATED)
DT   01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE)
DT   01-FEB-1997 (REL. 35, LAST ANNOTATION UPDATE)
DE   GLYCEROL-3-PHOSPHATE DEHYDROGENASE (NAD+) 2 (EC 1.1.1.8).
GN   GPD2 OR GPD3 OR YOL059W OR O1222.
OS   SACCHAROMYCES CEREVISIAE (BAKER'S YEAST).
OC   EUKARYOTA; FUNGI; ASCOMYCOTINA; HEMIASCOMYCETES.
RN   [1]
RP   SEQUENCE OF 49-440 FROM N.A.
RX   MEDLINE; 96020665.
RA   ERIKSSON P., ANDRE L., ANSELL R., BLOMBERG A., ADLER L.;
RL   MOL. MICROBIOL. 17:95-107(1995).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   STRAIN=S288C / FY73;
RX   MEDLINE; 96381248.
RA   MANNHAUPT G., VETTER I., SCHWARZLOSE C., MITZEL S., FELDMANN H.;
RL   YEAST 12:67-76(1996).
CC   -!- CATALYTIC ACTIVITY: SN-GLYCEROL 3-PHOSPHATE + NAD(+) =
CC       GLYCERONE PHOSPHATE + NADH.
CC   -!- CAUTION: IT IS UNCERTAIN WHETHER MET-1 OR MET-49 IS THE INITIATOR.
DR   EMBL; Z35169; G511135; -.
DR   EMBL; X91067; G984182; -.
DR   EMBL; Z74801; E251866; -.
DR   SGD; L0000723; GPD2.
DR   SGD; L0003160; GPD3.
DR   PROSITE; PS00957; NAD_G3PDH.
KW   OXIDOREDUCTASE; NAD; MULTIGENE FAMILY.
FT   CONFLICT    411    440       LFEAVYQIVYNNVRMEDLPEMIEELDIDDE -> IIRGSLP
FT                                DSLQQRPHGRPTGDD (IN REF. 1).
SQ   SEQUENCE   440 AA;  49421 MW;  F3B4A1F1 CRC32;
     MLAVRRLTRY TFLKRTHPVL YTRRAYKILP SRSTFLRRSL LQTQLHSKMT AHTNIKQHKH
     CHEDHPIRRS DSAVSIVHLK RAPFKVTVIG SGNWGTTIAK VIAENTELHS HIFEPEVRMW
     VFDEKIGDEN LTDIINTRHQ NVKYLPNIDL PHNLVADPDL LHSIKGADIL VFNIPHQFLP
     NIVKQLQGHV APHVRAISCL KGFELGSKGV QLLSSYVTDE LGIQCGALSG ANLAPEVAKE
     HWSETTVAYQ LPKDYQGDGK DVDHKILKLL FHRPYFHVNV IDDVAGISIA GALKNVVALA
     CGFVEGMGWG NNASAAIQRL GLGEIIKFGR MFFPESKVET YYQESAGVAD LITTCSGGRN
     VKVATYMAKT GKSALEAEKE LLNGQSAQGI ITCREVHEWL QTCELTQEFP LFEAVYQIVY
     NNVRMEDLPE MIEELDIDDE
//
ID   GPDA_CAEEL     STANDARD;      PRT;   351 AA.
AC   P34517;
DT   01-FEB-1994 (REL. 28, CREATED)
DT   01-FEB-1994 (REL. 28, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   PROBABLE GLYCEROL-3-PHOSPHATE DEHYDROGENASE (NAD+), CYTOPLASMIC
DE   (EC 1.1.1.8).
GN   K11H3.1.
OS   CAENORHABDITIS ELEGANS.
OC   EUKARYOTA; METAZOA; ACOELOMATES; NEMATODA; SECERNENTEA; RHABDITIDA.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=BRISTOL N2;
RX   MEDLINE; 94150718.
RA   WILSON R., AINSCOUGH R., ANDERSON K., BAYNES C., BERKS M.,
RA   BONFIELD J., BURTON J., CONNELL M., COPSEY T., COOPER J., COULSON A.,
RA   CRAXTON M., DEAR S., DU Z., DURBIN R., FAVELLO A., FRASER A.,
RA   FULTON L., GARDNER A., GREEN P., HAWKINS T., HILLIER L., JIER M.,
RA   JOHNSTON L., JONES M., KERSHAW J., KIRSTEN J., LAISSTER N.,
RA   LATREILLE P., LIGHTNING J., LLOYD C., MORTIMORE B., O'CALLAGHAN M.,
RA   PARSONS J., PERCY C., RIFKEN L., ROOPRA A., SAUNDERS D., SHOWNKEEN R.,
RA   SIMS M., SMALDON N., SMITH A., SMITH M., SONNHAMMER E., STADEN R.,
RA   SULSTON J., THIERRY-MIEG J., THOMAS K., VAUDIN M., VAUGHAN K.,
RA   WATERSON R., WATSON A., WEINSTOCK L., WILKINSON-SPROAT J.,
RA   WOHLDMAN P.;
RL   NATURE 368:32-38(1994).
CC   -!- CATALYTIC ACTIVITY: SN-GLYCEROL 3-PHOSPHATE + NAD(+) =
CC       GLYCERONE PHOSPHATE + NADH.
CC   -!- SUBUNIT: HOMODIMER (BY SIMILARITY).
CC   -!- SUBCELLULAR LOCATION: CYTOPLASMIC (BY SIMILARITY).
DR   EMBL; Z22180; G297973; -.
DR   PIR; S40754; S40754.
DR   WORMPEP; K11H3.1; CE00505.
DR   PROSITE; PS00957; NAD_G3PDH.
KW   HYPOTHETICAL PROTEIN; OXIDOREDUCTASE; NAD.
SQ   SEQUENCE   351 AA;  38290 MW;  B3EA2980 CRC32;
     MSPKKVTIIG SGNWGSAIAR IVGSTTKSFP DEFDPTVRMW VFEEIVNGEK LSEVINNRHE
     NIKYLPGKVL PNNVVAVTDL VESCEGSNVL VFVVPHQFVK GICEKLVGKI PADTQAISLI
     KGVSTEKRGG LKLISEEIKE ILKIEVSVLM GANLAPEVAN DNFCEATIGC KRKAEDGPLL
     KKLFHTDNFR INVVEDAHTV ELCGALKNVV ACAAGFTDGL GYGDNTKAAV IRLGLMETTK
     FVEHYYPGSN LQTFFESCGI ADLITTCYGG RNRKVCEAFV KTGKSMAEVE KELLNGQSAQ
     GPLTAEEVYL MMHKTGLDAK FPLFTAVHKI CAGEMKPAEL VDCLRNHPEH M
//
ID   GPDA_CUPLA     STANDARD;      PRT;   372 AA.
AC   P52425;
DT   01-OCT-1996 (REL. 34, CREATED)
DT   01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   GLYCEROL-3-PHOSPHATE DEHYDROGENASE (NAD+) (EC 1.1.1.8).
GN   GPDH.
OS   CUPHEA LANCEOLATA.
OC   EUKARYOTA; PLANTA; EMBRYOPHYTA; ANGIOSPERMAE; DICOTYLEDONEAE;
OC   MYRTALES; LYTHRACEAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RA   HAUSMANN L., SCHELL J., TOEPFER R.;
RL   PLANT LIPID METAB. 1:534-536(1995).
CC   -!- CATALYTIC ACTIVITY: SN-GLYCEROL 3-PHOSPHATE + NAD(+) =
CC       GLYCERONE PHOSPHATE + NADH.
CC   -!- SUBUNIT: HOMODIMER (BY SIMILARITY).
CC   -!- SUBCELLULAR LOCATION: CYTOPLASMIC (BY SIMILARITY).
DR   EMBL; X79677; G840731; -.
KW   OXIDOREDUCTASE; NAD.
SQ   SEQUENCE   372 AA;  40811 MW;  6AD5A18B CRC32;
     MAPSELNCTH QNQHSSGYDG PRSRVTVVGS GNWGSVAAKL IATNTLKLPS FHDEVRMWVF
     EETLPSGEKL TDVINQTNEN VKYLPGIKLG RNVVADPDLE NAVKDANMLV FVTPHQFMEG
     ICKRLEGKIQ EGAQALSLIK GMEVKMEGPC MISSLISDLL GINCCVLMGA NIANEIAVEK
     FSEATVGFRE NRDIAEKWVQ LFSTPYFMVS AVEDVEGVEL CGTLKNIVAI AAGFVDGLEM
     GNNTKAAIMR IGLREMKAFS KLLFPSVKDT TFFESCGVAD LITTCLGGRN RKVAEAFAKN
     GGKRSFDDLE AEMLRGQKLQ GVSTAKEVYE VLGHRGWLEL FPLFSTVHEI STGRLPPSAI
     VEYSEQKTIF SW
//
ID   GPDA_DROME     STANDARD;      PRT;   350 AA.
AC   P13706;
DT   01-JAN-1990 (REL. 13, CREATED)
DT   01-FEB-1997 (REL. 35, LAST SEQUENCE UPDATE)
DT   01-FEB-1997 (REL. 35, LAST ANNOTATION UPDATE)
DE   GLYCEROL-3-PHOSPHATE DEHYDROGENASE (NAD+), CYTOPLASMIC (EC 1.1.1.8)
DE   (GPD-C) (GPDH-C).
GN   GPDH.
OS   DROSOPHILA MELANOGASTER (FRUIT FLY).
OC   EUKARYOTA; METAZOA; ARTHROPODA; INSECTA; DIPTERA.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 89296935.
RA   VON KALM L., WEAVER J., DEMARCO J., MACINTYRE R.J., SULLIVAN D.T.;
RL   PROC. NATL. ACAD. SCI. U.S.A. 86:5020-5024(1989).
RN   [2]
RP   SEQUENCE FROM N.A.
RC   STRAIN=CANTON-S;
RX   MEDLINE; 90067829.
RA   BEWLEY G.C., COOK J.L., KUSAKABE S., MUKAI T., RIGBY D.L.,
RA   CHAMBERS G.K.;
RL   NUCLEIC ACIDS RES. 17:8553-8567(1989).
RN   [3]
RP   SEQUENCE OF 298-350 FROM N.A.
RX   MEDLINE; 88273210.
RA   COOK J.L., BEWLEY G.C., SHAFFER J.B.;
RL   J. BIOL. CHEM. 263:10858-10864(1988).
CC   -!- CATALYTIC ACTIVITY: SN-GLYCEROL 3-PHOSPHATE + NAD(+) =
CC       GLYCERONE PHOSPHATE + NADH.
CC   -!- SUBUNIT: HOMODIMER.
CC   -!- SUBCELLULAR LOCATION: CYTOPLASMIC.
CC   -!- PATHWAY: THIS ENZYME IS ONE OF THE TWO ENZYMES CONSTITUTING THE
CC       ALPHA-GLYCEROPHOSPHATE CYCLE, IN WHICH THIS ENZYME OPERATES IN
CC       CONJUNCTION WITH A MITOCHONDRIAL ALPHA-GLYCEROPHOSPHATE OXIDASE.
CC       THE ALPHA-GLYCEROPHOSPHATE CYCLE IS ESSENTIAL FOR THE PRODUCTION
CC       OF ENERGY FOR FLIGHT IN INSECTS.
CC   -!- ALTERNATIVE PRODUCTS: 3 DIFERENT FORMS OF GPDH (GPDH-1, GPDH-2 AND
CC       GPDH-3) WHICH DIFFER IN THEIR C-TERMINALS ARE PRODUCED BY
CC       ALTERNATIVE SPLICING OF THE SAME GENE. GPDH-1 IS SHOWN HERE.
DR   EMBL; J04567; G157560; -.
DR   EMBL; J04567; G157561; -.
DR   EMBL; J04567; G157562; -.
DR   EMBL; X14179; G295744; -.
DR   EMBL; X14179; G295745; -.
DR   EMBL; X14179; G295746; -.
DR   EMBL; J03927; G157464; -.
DR   EMBL; J03927; G157465; -.
DR   EMBL; J03927; G157466; -.
DR   PIR; A28995; A28995.
DR   PIR; S06759; S06759.
DR   PIR; S06760; S06760.
DR   FLYBASE; FBGN0001128; GPDH.
DR   PROSITE; PS00957; NAD_G3PDH.
KW   OXIDOREDUCTASE; NAD; ALTERNATIVE SPLICING.
FT   VARSPLIC    320    350       FPLFTAIHKICTNQLKPNDLIDCIRNHPEHM -> DTSIMP
FT                                SPKL (IN GPDH-2).
FT   VARSPLIC    320    350       FPLFTAIHKICTNQLKPNDLIDCIRNHPEHM -> QNL
FT                                (IN GPDH-3).
SQ   SEQUENCE   350 AA;  38258 MW;  A0979D4A CRC32;
     MADKVNVCIV GSGNWGSAIA KIVGANAAAL PEFEERVTMF VYEELIDGKK LTEIINETHE
     NVKYLKGHKL PPNVVAVPDL VEAAKNADIL IFVVPHQFIP NFCKQLLGKI KPNAIAISLI
     KGFDKAEGGG IDLISHIITR HLKIPCAVLM GANLANEVAE GNFCETTIGC TDKKYGKVLR
     DLFQANHFRV VVVDDADAVE VCGALKNIVA CGAGFVDGLK LGDNTKAAVI RLGLMEMIRF
     VDVFYPGSKL STFFESCGVA DLITTCYGGR NRRVSEAFVT SGKTIEELEK EMLNGQKLQG
     PPTAEEVNYM LKNKGLEDKF PLFTAIHKIC TNQLKPNDLI DCIRNHPEHM
//
ID   GPDA_DROVI     STANDARD;      PRT;   352 AA.
AC   P07735;
DT   01-AUG-1988 (REL. 08, CREATED)
DT   01-AUG-1988 (REL. 08, LAST SEQUENCE UPDATE)
DT   01-FEB-1996 (REL. 33, LAST ANNOTATION UPDATE)
DE   GLYCEROL-3-PHOSPHATE DEHYDROGENASE (NAD+), CYTOPLASMIC (EC 1.1.1.8)
DE   (GPD-C) (GPDH-C).
GN   GPDH.
OS   DROSOPHILA VIRILIS (FRUIT FLY).
OC   EUKARYOTA; METAZOA; ARTHROPODA; INSECTA; DIPTERA.
RN   [1]
RP   SEQUENCE.
RA   ARAI K., TOMINAGA H., YOKOTE Y., NARISE S.;
RL   BIOCHIM. BIOPHYS. ACTA 953:6-13(1988).
CC   -!- CATALYTIC ACTIVITY: SN-GLYCEROL 3-PHOSPHATE + NAD(+) =
CC       GLYCERONE PHOSPHATE + NADH.
CC   -!- SUBUNIT: HOMODIMER.
CC   -!- SUBCELLULAR LOCATION: CYTOPLASMIC.
CC   -!- PATHWAY: THIS ENZYME IS ONE OF THE TWO ENZYMES CONSTITUTING THE
CC       ALPHA-GLYCEROPHOSPHATE CYCLE, IN WHICH THIS ENZYME OPERATES IN
CC       CONJUNCTION WITH A MITOCHONDRIAL ALPHA-GLYCEROPHOSPHATE OXIDASE.
CC       THE ALPHA-GLYCEROPHOSPHATE CYCLE IS ESSENTIAL FOR THE PRODUCTION
CC       OF ENERGY FOR FLIGHT IN INSECTS.
DR   PIR; JS0023; JS0023.
DR   FLYBASE; FBGN0013081; DVIR\GPDH.
DR   PROSITE; PS00957; NAD_G3PDH.
KW   OXIDOREDUCTASE; NAD.
FT   MOD_RES       1      1       BLOCKED.
SQ   SEQUENCE   352 AA;  38447 MW;  B699E7B0 CRC32;
     AEKVNVCIVG SGNNGSAIAK IVGANAAALP EFEERVTMFV YEEMIDGKKL TEIINETHEN
     VKYLKGHKLP TNVVAVPDLV EAAKNADILI FVVPHQFIPN FCKQLLGKIK PNAIAISLIK
     GFDKAEGGGI DLISHIITRH LKIPCAVLMG ANLANEVAEG NFCETTIGCT DKKYGKVLRD
     LFQANHFRVV VVEDADAVEV CGALKNIVAC GAGFVDGLKL GDNTKAAVIR LGLMEMIRFV
     DVFYPGSKLS TFFESCGVAD LITTCYGGRN RRVSEAFVTS GKTIEDLEKE MLNGQKLQGP
     PTAEEVNYML KNKGLEDKFP LFTAIHKICT NQLKPKDLID CIRNHPEHMQ TL
//
ID   GPDA_ECOLI     STANDARD;      PRT;   339 AA.
AC   P37606;
DT   01-OCT-1994 (REL. 30, CREATED)
DT   01-OCT-1994 (REL. 30, LAST SEQUENCE UPDATE)
DT   01-FEB-1997 (REL. 35, LAST ANNOTATION UPDATE)
DE   GLYCEROL-3-PHOSPHATE DEHYDROGENASE (NAD+) (EC 1.1.1.8).
GN   GPSA.
OS   ESCHERICHIA COLI.
OC   PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS;
OC   ENTEROBACTERIACEAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=K12 / MG1655;
RX   MEDLINE; 94316500.
RA   SOFIA H.J., BURLAND V., DANIELS D.L., PLUNKETT G. III, BLATTNER F.R.;
RL   NUCLEIC ACIDS RES. 22:2576-2586(1994).
CC   -!- CATALYTIC ACTIVITY: SN-GLYCEROL 3-PHOSPHATE + NAD(+) =
CC       GLYCERONE PHOSPHATE + NADH.
CC   -!- SUBCELLULAR LOCATION: CYTOPLASMIC (PROBABLE).
DR   EMBL; U00039; G466746; -.
DR   EMBL; AE000439; G1790037; -.
DR   ECOGENE; EG20091; GPSA.
DR   PROSITE; PS00957; NAD_G3PDH.
KW   OXIDOREDUCTASE; NAD.
SQ   SEQUENCE   339 AA;  36361 MW;  085E0E12 CRC32;
     MNQRNASMTV IGAGSYGTAL AITLARNGHE VVLWGHDPEH IATLERDRCN AAFLPDVPFP
     DTLHLESDLA TALAASRNIL VVVPSHVFGE VLRQIKPLMR PDARLVWATK GLEAETGRLL
     QDVAREALGD QIPLAVISGP TFAKELAAGL PTAISLASTD QTFADDLQQL LHCGKSFRVY
     SNPDFIGVQL GGAVKNVIAI GAGMSDGIGF GANARTALIT RGLAEMSRLG AALGADPATF
     MGMAGLGDLV LTCTDNQSRN RRFGMMLGQG MDVQSAQEKI GQVVEGYRNT KEVRELAHRF
     GVEMPITEEI YQVLYCGKNA REAALTLLGR ARKDERSSH
//
ID   GPDA_HAEIN     STANDARD;      PRT;   335 AA.
AC   P43798;
DT   01-NOV-1995 (REL. 32, CREATED)
DT   01-NOV-1995 (REL. 32, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   GLYCEROL-3-PHOSPHATE DEHYDROGENASE (NAD+) (EC 1.1.1.8).
GN   GPSA OR HI0605.
OS   HAEMOPHILUS INFLUENZAE.
OC   PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS;
OC   PASTEURELLACEAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=RD / KW20;
RX   MEDLINE; 95350630.
RA   FLEISCHMANN R.D., ADAMS M.D., WHITE O., CLAYTON R.A., KIRKNESS E.F.,
RA   KERLAVAGE A.R., BULT C.J., TOMB J.-F., DOUGHERTY B.A., MERRICK J.M.,
RA   MCKENNEY K., SUTTON G., FITZHUGH W., FIELDS C.A., GOCAYNE J.D.,
RA   SCOTT J.D., SHIRLEY R., LIU L.-I., GLODEK A., KELLEY J.M.,
RA   WEIDMAN J.F., PHILLIPS C.A., SPRIGGS T., HEDBLOM E., COTTON M.D.,
RA   UTTERBACK T.R., HANNA M.C., NGUYEN D.T., SAUDEK D.M., BRANDON R.C.,
RA   FINE L.D., FRITCHMAN J.L., FUHRMANN J.L., GEOGHAGEN N.S.M.,
RA   GNEHM C.L., MCDONALD L.A., SMALL K.V., FRASER C.M., SMITH H.O.,
RA   VENTER J.C.;
RL   SCIENCE 269:496-512(1995).
CC   -!- CATALYTIC ACTIVITY: SN-GLYCEROL 3-PHOSPHATE + NAD(+) =
CC       GLYCERONE PHOSPHATE + NADH.
CC   -!- SUBCELLULAR LOCATION: CYTOPLASMIC (PROBABLE).
DR   EMBL; U32743; G1573598; -.
DR   PROSITE; PS00957; NAD_G3PDH.
KW   OXIDOREDUCTASE; NAD.
SQ   SEQUENCE   335 AA;  36394 MW;  F4C329EE CRC32;
     MITSQTPITV LGAGSYGTAL AITFSRNGSP THLWGHNPAH IAQMQTERQN YRFLPDVIFP
     EDLHLESNLA QAMEYSQDIL IVVPSHAFGE ILIKIKPHLK AHHRLIWATK GLERNTGRLL
     QTVVEEQLGT QYPLAVLSGP TFAKELAQGL PSAITLAANN EQFAREFQSR IHCSKGFRVY
     INSDMTGVQL GGAIKNVIAI GAGISDGMGF GANARTALIT RGIAEITRLG ISLGANTNTF
     MGMSGLGDLV LTCTDNQSRN RRFGLMLGKG LDAQMAMENI GQVVEGFYNT KEAYLLAQRQ
     GVEMPITEQI YQMLFCGKSA QDVAISLLGR ACKGE
//
ID   GPDA_HUMAN     STANDARD;      PRT;   348 AA.
AC   P21695;
DT   01-MAY-1991 (REL. 18, CREATED)
DT   01-OCT-1996 (REL. 34, LAST SEQUENCE UPDATE)
DT   01-OCT-1996 (REL. 34, LAST ANNOTATION UPDATE)
DE   GLYCEROL-3-PHOSPHATE DEHYDROGENASE (NAD+), CYTOPLASMIC (EC 1.1.1.8)
DE   (GPD-C) (GPDH-C).
GN   GPD1.
OS   HOMO SAPIENS (HUMAN).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; PRIMATES.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   TISSUE=LIVER;
RX   MEDLINE; 95290502.
RA   MENAYA J., GONZALEZ-MANCHON C., PARRILLA R., AYUSO M.S.;
RL   BIOCHIM. BIOPHYS. ACTA 1262:91-94(1995).
RN   [2]
RP   SEQUENCE OF 1-13 FROM N.A.
RC   TISSUE=FETAL LIVER;
RX   MEDLINE; 90377214.
RA   GWYNN B., LYFORD K.L., BIRKENMEIER E.H.;
RL   MOL. CELL. BIOL. 10:5244-5256(1990).
CC   -!- CATALYTIC ACTIVITY: SN-GLYCEROL 3-PHOSPHATE + NAD(+) =
CC       GLYCERONE PHOSPHATE + NADH.
CC   -!- SUBUNIT: HOMODIMER.
CC   -!- SUBCELLULAR LOCATION: CYTOPLASMIC.
DR   EMBL; L34041; G508487; -.
DR   EMBL; M36917; G183487; -.
DR   MIM; 138420; -.
DR   PROSITE; PS00957; NAD_G3PDH.
KW   OXIDOREDUCTASE; NAD.
FT   INIT_MET      0      0       BY SIMILARITY.
SQ   SEQUENCE   348 AA;  37462 MW;  57274135 CRC32;
     ASKKVCIVGS GNWGSAIAKI VGGNAAQLAQ FDPRVTMWVF EEDIGGKKLT EIINTQHENV
     KYLPGHKLPP NVVAVPDVVQ AAEDADILIF VVPHQFIGKI CDQLKGHLKA NPTGISLIKG
     VDEGPNGLKL ISEVIGERLG IPMSVLMGAN IASEVADEKF CETTIGCKDP AQGQLLKELM
     QTPNFRITVV QEVDTVEICG ALKNVVAVGA GFCDGLGFGD NTKAAVIRLG LMEMIAFAKL
     FCSGPVSSAT FLESCGVADL ITTCYGGRNR KVAEAFARTG KSIEQLEKEL LNGQKLQGPE
     TARELYSILQ HKGLVDKFPL FMAVYKVCYE GQPVGEFIHC LQNHPEHM
//
ID   GPDA_MOUSE     STANDARD;      PRT;   348 AA.
AC   P13707;
DT   01-JAN-1990 (REL. 13, CREATED)
DT   01-FEB-1991 (REL. 17, LAST SEQUENCE UPDATE)
DT   01-FEB-1997 (REL. 35, LAST ANNOTATION UPDATE)
DE   GLYCEROL-3-PHOSPHATE DEHYDROGENASE (NAD+), CYTOPLASMIC (EC 1.1.1.8)
DE   (GPD-C) (GPDH-C).
GN   GPD1 OR GDC1 OR GDC-1.
OS   MUS MUSCULUS (MOUSE).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; RODENTIA.
RN   [1]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 87109336.
RA   DOBSON D.E., GROVES D.L., SPIEGELMAN B.M.;
RL   J. BIOL. CHEM. 262:1804-1809(1987).
RN   [2]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 86304311.
RA   IRELAND R.C., KOTARSKI M.A., JOHNSTON L.A., STADLER U.,
RA   BIRKENMEIER E., KOZAK L.P.;
RL   J. BIOL. CHEM. 261:11779-11785(1986).
RN   [3]
RP   SEQUENCE FROM N.A.
RX   MEDLINE; 86278164.
RA   PHILLIPS M., DJIAN P., GREEN H.;
RL   J. BIOL. CHEM. 261:10821-10827(1986).
CC   -!- CATALYTIC ACTIVITY: SN-GLYCEROL 3-PHOSPHATE + NAD(+) =
CC       GLYCERONE PHOSPHATE + NADH.
CC   -!- SUBUNIT: HOMODIMER.
CC   -!- SUBCELLULAR LOCATION: CYTOPLASMIC.
DR   EMBL; J02655; G309266; -.
DR   EMBL; M25558; G387177; -.
DR   EMBL; M13366; G387178; -.
DR   PIR; A26687; A26687.
DR   PIR; A25189; A25189.
DR   PIR; A25952; A25952.
DR   PROSITE; PS00957; NAD_G3PDH.
DR   MGD; MGI:95679; GDC1.
KW   OXIDOREDUCTASE; NAD.
FT   INIT_MET      0      0
FT   CONFLICT    245    245       T -> I (IN REF. 2).
FT   CONFLICT    300    300       Q -> L (IN REF. 1).
SQ   SEQUENCE   348 AA;  37441 MW;  107F7030 CRC32;
     AGKKVCIVGS GNWGSAIAKI VGSNAGRLAH FDPRVTMWVF EEDIGGRKLT EIINTQHENV
     KYLPGHKLPP NVVAIPDVVQ AATGADILVF VVPHQFIGKI CDQLKGHLKA NTIGISLIKG
     VDEGPNGLKL ISEVIGERLG IPMSVLMGAN IASEVAEEKF CETTIGCKDP AQGQLLKDLM
     QTPNFRITVV QEVDTVEICG ALKNIVAVGA GFCDGLGFGD NTKAAVIRLG LMEMIAFAKL
     FCSGTVSSAT FLESCGVADL ITTCYGGRNR KVAEAFARTG KSIEQLEKEM LNGQKLQGPQ
     TARELHSILQ HKGLVDKFPL FTAVYKVCYE GQPVGEFIRC LQNHPEHM
//
ID   GPDA_RABIT     STANDARD;      PRT;   348 AA.
AC   P08507;
DT   01-AUG-1988 (REL. 08, CREATED)
DT   01-AUG-1988 (REL. 08, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   GLYCEROL-3-PHOSPHATE DEHYDROGENASE (NAD+), CYTOPLASMIC (EC 1.1.1.8)
DE   (GPD-C) (GPDH-C).
GN   GPD1.
OS   ORYCTOLAGUS CUNICULUS (RABBIT).
OC   EUKARYOTA; METAZOA; CHORDATA; VERTEBRATA; TETRAPODA; MAMMALIA;
OC   EUTHERIA; LAGOMORPHA.
RN   [1]
RP   SECONDARY STRUCTURE PREDICTION.
RX   MEDLINE; 81003924.
RA   OTTO J., ARGOS P., ROSSMANN M.G.;
RL   EUR. J. BIOCHEM. 109:325-330(1980).
CC   -!- CATALYTIC ACTIVITY: SN-GLYCEROL 3-PHOSPHATE + NAD(+) =
CC       GLYCERONE PHOSPHATE + NADH.
CC   -!- SUBUNIT: HOMODIMER.
CC   -!- SUBCELLULAR LOCATION: CYTOPLASMIC.
DR   PIR; A32512; A32512.
DR   PROSITE; PS00957; NAD_G3PDH.
KW   OXIDOREDUCTASE; NAD.
SQ   SEQUENCE   348 AA;  37478 MW;  F9B96993 CRC32;
     AGKKVCIVGS GDWGSAIAKI VGGNAAQLAQ FDPRVTMWVF EEDIGGKKLT EIINTHQENV
     KYLPGHKLPP NVVAVPDVVK AAADADILIF VVPHQFIGKI CDEIKGHLKA NAIGISLIKG
     VNEGPKGLKL ISEVIGEHLG IPMSVLMGAN IASEVADEKF CETTIGCKDQ AQGQLLKQLM
     QTPNFRIVVT QEVNTVEICG ALKDLVAVGA GFCDGIGFGD NTKAAVIRLG LMEMIAFAKL
     FCSGPVSPAT FLESCGVADL ITTCYGGRNR KVAEAFARTG KSIEQLEKEM LNGQKLQGPE
     TARELHSILQ HKGLVDWFPL FMAVYKVCYQ GQPVGEFIRC LQNHPEHM
//
ID   GPDA_SALTY     STANDARD;      PRT;   171 AA.
AC   P40716;
DT   01-FEB-1995 (REL. 31, CREATED)
DT   01-FEB-1995 (REL. 31, LAST SEQUENCE UPDATE)
DT   01-NOV-1995 (REL. 32, LAST ANNOTATION UPDATE)
DE   GLYCEROL-3-PHOSPHATE DEHYDROGENASE (NAD+) (EC 1.1.1.8) (FRAGMENT).
GN   GPSA.
OS   SALMONELLA TYPHIMURIUM.
OC   PROKARYOTA; GRACILICUTES; SCOTOBACTERIA; FACULTATIVELY ANAEROBIC RODS;
OC   ENTEROBACTERIACEAE.
RN   [1]
RP   SEQUENCE FROM N.A.
RC   STRAIN=LT2;
RA   SIVAPRASAD A.V., KUCZEK E.S., BAWDEN C.S., ROGERS G.E.;
RL   SUBMITTED (MAY-1991) TO EMBL/GENBANK/DDBJ DATA BANKS.
RN   [2]
RP   CONCEPTUAL TRANSLATION.
RA   RUDD K.E.;
RL   UNPUBLISHED OBSERVATIONS (JAN-1995).
CC   -!- CATALYTIC ACTIVITY: SN-GLYCEROL 3-PHOSPHATE + NAD(+) =
CC       GLYCERONE PHOSPHATE + NADH.
CC   -!- SUBCELLULAR LOCATION: CYTOPLASMIC (PROBABLE).
CC   -!- CAUTION: THIS IS A CONCEPTUAL TRANSLATION; TWO FRAMESHIFTS HAD TO
CC       BE INTRODUCED TO PRODUCE THIS ORF.
DR   EMBL; X59594; -; NOT_ANNOTATED_CDS.
DR   STYGENE; SG10456; GPSA.
DR   PROSITE; PS00957; NAD_G3PDH.
KW   OXIDOREDUCTASE; NAD.
FT   NON_TER       1      1
SQ   SEQUENCE   171 AA;  18390 MW;  8A9F35E7 CRC32;
     DPQQLLHCGK SFRVYINADF IGVQLGGAVK NVIAIGAGMS DGIGFGANAR TALITRGLTE
     MSRLGARLGA DPATFMGMAG LGDLVLTCTD NQSRNRRFGM MLGQGIGLKA RQDKIGQVVE
     GYRNTKEVRE LAHRFGVEMP ITEEIYQVLY CGKNAREAAL TLLGRDPQGE S
//