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Database: UniProt
Entry: A0A2U3X4E1_ODORO
LinkDB: A0A2U3X4E1_ODORO
Original site: A0A2U3X4E1_ODORO 
ID   A0A2U3X4E1_ODORO        Unreviewed;       409 AA.
AC   A0A2U3X4E1;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE            EC=1.2.1.12 {ECO:0000256|RuleBase:RU361160};
GN   Name=GAPDHS {ECO:0000313|RefSeq:XP_004417148.1};
OS   Odobenus rosmarus divergens (Pacific walrus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC   Odobenus.
OX   NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004417148.1};
RN   [1] {ECO:0000313|RefSeq:XP_004417148.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- FUNCTION: May play an important role in regulating the switch between
CC       different pathways for energy production during spermiogenesis and in
CC       the spermatozoon. Required for sperm motility and male fertility.
CC       {ECO:0000256|ARBA:ARBA00037650}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-
CC         phospho-glyceroyl phosphate + H(+) + NADH; Xref=Rhea:RHEA:10300,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57604, ChEBI:CHEBI:57945, ChEBI:CHEBI:59776; EC=1.2.1.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00001810,
CC         ECO:0000256|RuleBase:RU361160};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5. {ECO:0000256|ARBA:ARBA00004869,
CC       ECO:0000256|RuleBase:RU361160}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|RuleBase:RU361160}.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00007406, ECO:0000256|RuleBase:RU000397}.
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DR   RefSeq; XP_004417148.1; XM_004417091.1.
DR   AlphaFoldDB; A0A2U3X4E1; -.
DR   STRING; 9708.A0A2U3X4E1; -.
DR   GeneID; 101369302; -.
DR   KEGG; oro:101369302; -.
DR   CTD; 26330; -.
DR   InParanoid; A0A2U3X4E1; -.
DR   OrthoDB; 275384at2759; -.
DR   UniPathway; UPA00109; UER00184.
DR   Proteomes; UP000245340; Unplaced.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
DR   InterPro; IPR020830; GlycerAld_3-P_DH_AS.
DR   InterPro; IPR020829; GlycerAld_3-P_DH_cat.
DR   InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
DR   InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR01534; GAPDH-I; 1.
DR   PANTHER; PTHR10836; GLYCERALDEHYDE 3-PHOSPHATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR10836:SF79; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE, TESTIS-SPECIFIC; 1.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   Pfam; PF00044; Gp_dh_N; 1.
DR   PRINTS; PR00078; G3PDHDRGNASE.
DR   SMART; SM00846; Gp_dh_N; 1.
DR   SUPFAM; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR   PROSITE; PS00071; GAPDH; 1.
PE   3: Inferred from homology;
KW   Glycolysis {ECO:0000256|RuleBase:RU361160};
KW   NAD {ECO:0000256|RuleBase:RU361160};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361160};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245340}.
FT   DOMAIN          77..225
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
FT   REGION          18..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..60
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   409 AA;  44879 MW;  E0631C3BDB5795F6 CRC64;
     MSKRDIVLTN VTVVQLLRQP CPVTRGPPPP EPKVETEREP QPEPEREPQP EPEPKPEPVK
     EESPLPQPTK PSVVQKLTVG INGFGRIGRL VLRACMEKGV KVVAVNDPFI DPEYMVYMFK
     YDSTHGRYKG SVEYRDGKLV VDNQEISVFQ CKQPRDVPWK SVGNPFVVES TGMYLSLQEA
     SDHIEAGATR VVISAPSPDA PIFVMGVNEK NYNPGSMKVV SNASCTTNCL APLAKVVHEQ
     FGIVEGLMTT VHSYTATQKT VDGPSKKAWR DGRGAHQNII PASTGAAKAV GKVIPDLKGK
     LTGMAFRVPT PDVSVVDLTC RLAQPTSYEA IKDAIKAAAQ GPMAGILAYT EDEVVSTDFV
     GDTHSSIFDA KAGIALNDNF VKLISWYDNE YGYSHRVVDL LRYMFSRHK
//
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