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Database: UniProt
Entry: G1RK80_NOMLE
LinkDB: G1RK80_NOMLE
Original site: G1RK80_NOMLE 
ID   G1RK80_NOMLE            Unreviewed;       409 AA.
AC   G1RK80;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 72.
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|Ensembl:ENSNLEP00000013637.1};
OS   Nomascus leucogenys (Northern white-cheeked gibbon) (Hylobates leucogenys).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC   Nomascus.
OX   NCBI_TaxID=61853 {ECO:0000313|Ensembl:ENSNLEP00000013637.1, ECO:0000313|Proteomes:UP000001073};
RN   [1] {ECO:0000313|Ensembl:ENSNLEP00000013637.1, ECO:0000313|Proteomes:UP000001073}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Gibbon Genome Sequencing Consortium;
RL   Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSNLEP00000013637.1}
RP   IDENTIFICATION.
RG   Ensembl;
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   EMBL; ADFV01122120; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003280087.1; XM_003280039.3.
DR   AlphaFoldDB; G1RK80; -.
DR   STRING; 61853.ENSNLEP00000013637; -.
DR   Ensembl; ENSNLET00000014314.2; ENSNLEP00000013637.1; ENSNLEG00000011203.2.
DR   GeneID; 100605071; -.
DR   KEGG; nle:100605071; -.
DR   CTD; 26330; -.
DR   eggNOG; KOG0657; Eukaryota.
DR   GeneTree; ENSGT00940000160272; -.
DR   HOGENOM; CLU_030140_0_3_1; -.
DR   InParanoid; G1RK80; -.
DR   OMA; ENMVKIM; -.
DR   OrthoDB; 275384at2759; -.
DR   TreeFam; TF300533; -.
DR   UniPathway; UPA00109; UER00184.
DR   Proteomes; UP000001073; Chromosome 10.
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:UP000001073}.
FT   DOMAIN          77..225
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
FT   REGION          18..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..68
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   409 AA;  44587 MW;  8C74F60603B5DC68 CRC64;
     MSKRDIVLTN VTVVQLLRQP CPVTRAPPPP EPKAEVEPQP QPQPTPVREE IKPPPPPPPP
     PRPATPPPKM VSVARELTVG INGFGRIGRL VLRACMEKGV KVVAVNDPFI DPEYMVYMFK
     YDSTHGRYKG SVEFRNGQLV VDNHEISVYQ CKEPKQIPWR AVGSPYVVES TGVYLSIEAA
     SDHISAGAQR VVISAPSPDA PTFVMGVNEN DYNPGSMNIV SNASCTTNCL APLAKVIHER
     FGIVEGLMTT VHSYTATQKT VDGPSRKSWR DGRGAHQNII PASTGAAKAV TKVIPELKGK
     LTGMAFRVPT PDVSVVDLTC RLAQPAPYSA IKEAVKAAAK GPMAGILAYT EDEVVSTDFL
     GDTHSSIFDA KAGIALNDNF VKLISWYDNE YGYSHRVVDL LRYMFSRDK
//
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