ID A0A2K6AQN5_MACNE Unreviewed; 406 AA.
AC A0A2K6AQN5;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
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:ENSMNEP00000001464.1};
OS Macaca nemestrina (Pig-tailed macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9545 {ECO:0000313|Ensembl:ENSMNEP00000001464.1, ECO:0000313|Proteomes:UP000233120};
RN [1] {ECO:0000313|Ensembl:ENSMNEP00000001464.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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 AlphaFoldDB; A0A2K6AQN5; -.
DR Ensembl; ENSMNET00000007164.1; ENSMNEP00000001464.1; ENSMNEG00000006546.1.
DR GeneTree; ENSGT00940000160272; -.
DR OMA; ENMVKIM; -.
DR UniPathway; UPA00109; UER00184.
DR Proteomes; UP000233120; Unplaced.
DR Bgee; ENSMNEG00000006546; Expressed in multicellular organism and 12 other cell types or tissues.
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:UP000233120}.
FT DOMAIN 77..225
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
FT REGION 18..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..73
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 406 AA; 44185 MW; CB5E6AFC2E540DFE CRC64;
MSKRDIVLTN VTVVQLLRQP CPVTRPPPPP EPKVEIEPQP QPEPTPVREE IKPPPPPSPP
PRPATPPPKM GPAPRELTVG INGFGRIGRL VLRACMEKGV KVVAVNDPFI DPEYMVYMFK
YDSTHGRYKG SVEFRNGQLV VDNHEISVYQ CKEPKQIPWR DVGSPYVVES TGVYLSIEAA
SNHISAGAQR VVISAPSPDA PTFVMGVNEN NYNPGSMNIV SNASCTTNCL APLAKVIHER
FGIVEGLMTT VHSYTATQKT VDGPSKKAWR DGRGAHQNII PASTGAAKAV TKGKAGAWPG
MAFRVPTPDV SVVDLTCRLA QPAPYSAIKE AIKAAAKGPM AGILAYTEDE VVSTDFVGDS
HSSIFDAKAG IALNDNFVKL ISWYDNEYGY SHRVVDLLRY MFSRDK
//
