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Database: UniProt
Entry: A0A0Q3PB69_AMAAE
LinkDB: A0A0Q3PB69_AMAAE
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ID   A0A0Q3PB69_AMAAE        Unreviewed;       421 AA.
AC   A0A0Q3PB69;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000256|RuleBase:RU361160};
DE            EC=1.2.1.12 {ECO:0000256|RuleBase:RU361160};
GN   ORFNames=AAES_117944 {ECO:0000313|EMBL:KQK78163.1};
OS   Amazona aestiva (Blue-fronted Amazon parrot).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Psittaciformes; Psittacidae; Amazona.
OX   NCBI_TaxID=12930 {ECO:0000313|EMBL:KQK78163.1, ECO:0000313|Proteomes:UP000051836};
RN   [1] {ECO:0000313|EMBL:KQK78163.1, ECO:0000313|Proteomes:UP000051836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FVVF132 {ECO:0000313|EMBL:KQK78163.1};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has both glyceraldehyde-3-phosphate dehydrogenase and
CC       nitrosylase activities, thereby playing a role in glycolysis and
CC       nuclear functions, respectively. Glyceraldehyde-3-phosphate
CC       dehydrogenase is a key enzyme in glycolysis that catalyzes the first
CC       step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P)
CC       into 3-phospho-D-glyceroyl phosphate (By similarity). Participates in
CC       nuclear events including transcription, RNA transport, DNA replication
CC       and apoptosis. Nuclear functions are probably due to the nitrosylase
CC       activity that mediates cysteine S-nitrosylation of nuclear target
CC       proteins such as SIRT1, HDAC2 and PRKDC.
CC       {ECO:0000256|ARBA:ARBA00025072}.
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-cysteinyl-[protein] + S-nitroso-L-cysteinyl-[GAPDH] = L-
CC         cysteinyl-[GAPDH] + S-nitroso-L-cysteinyl-[protein];
CC         Xref=Rhea:RHEA:66684, Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:17089,
CC         Rhea:RHEA-COMP:17090, Rhea:RHEA-COMP:17091, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:149494; Evidence={ECO:0000256|ARBA:ARBA00024287};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66685;
CC         Evidence={ECO:0000256|ARBA:ARBA00024287};
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   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000256|ARBA:ARBA00004245}. Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00007406, ECO:0000256|RuleBase:RU000397}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQK78163.1}.
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DR   EMBL; LMAW01002686; KQK78163.1; -; Genomic_DNA.
DR   STRING; 12930.A0A0Q3PB69; -.
DR   UniPathway; UPA00109; UER00184.
DR   Proteomes; UP000051836; Unassembled WGS sequence.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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:0035605; F:peptidyl-cysteine S-nitrosylase activity; IEA:RHEA.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
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:SF111; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; 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   Apoptosis {ECO:0000256|ARBA:ARBA00022703};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW   Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW   Glycolysis {ECO:0000256|RuleBase:RU361160};
KW   NAD {ECO:0000256|RuleBase:RU361160};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU361160};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051836};
KW   S-nitrosylation {ECO:0000256|ARBA:ARBA00022799};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          2..150
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
SQ   SEQUENCE   421 AA;  45498 MW;  C03EA745946CF6B8 CRC64;
     MVKVGVNGFG RIGRLVTRAA VLSGKVQVVA INDPFIDLNY MVYMFKYDST HGHFRGTVKA
     ENGKLVINGN AITIFQERDP SNIKWADAGA EYVVESTGVF TTMEXAGAHL KGGAKRVIIS
     APSADAPMFV MGVNHEKYDK SLKIVSNASC TTNCLAPLAK VIHDNFGIVE GLMTTVHAIT
     ATQKTVDGPS GKLWRDGRGA AQNIIPASTG AAKAVGKVIP ELNGKLTGMA FRVPTPNVSV
     VDLTCRLEKP AKYDDIKRVV KAAAEGPLKG ILAYTEDQVV SCDFNGDSHS STFDAGAGIA
     LNDHFVKLVS WYDNEYGYSN RVVDLMVHME SKESFWVIPN KRFSSAAMRR SPPYQVPDPD
     AVSSMKWMNR HNGANAVERE ARTXASMAPD CSSFNITCNS RVASTKFTLG CFTSSKTNCS
     I
//
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