G3P_DANRE
ID G3P_DANRE Reviewed; 333 AA.
AC Q5XJ10; Q1RM54;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P00355};
DE Short=GAPDH {ECO:0000250|UniProtKB:P00355};
DE EC=1.2.1.12 {ECO:0000250|UniProtKB:P04406};
DE AltName: Full=Peptidyl-cysteine S-nitrosylase GAPDH {ECO:0000305};
DE EC=2.6.99.- {ECO:0000250|UniProtKB:P04797};
GN Name=gapdh {ECO:0000312|ZFIN:ZDB-GENE-030115-1};
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1] {ECO:0000312|EMBL:AAH83506.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo {ECO:0000312|EMBL:AAH83506.2}, and
RC Ovary {ECO:0000312|EMBL:AAI15132.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (APR-2006) 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 (By similarity).
CC {ECO:0000250|UniProtKB:P04406, ECO:0000250|UniProtKB:P04797}.
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:0000250|UniProtKB:P04406, ECO:0000255|PROSITE-
CC ProRule:PRU10009};
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:0000250|UniProtKB:P04797};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66685;
CC Evidence={ECO:0000250|UniProtKB:P04797};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000250|UniProtKB:P00355}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P04406}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P04797}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P04797}. Nucleus {ECO:0000250|UniProtKB:P04797}.
CC -!- PTM: S-nitrosylation of Cys-150 leads to translocation to the nucleus.
CC {ECO:0000250|UniProtKB:P04797}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI15132.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC083506; AAH83506.2; -; mRNA.
DR EMBL; BC095386; AAH95386.2; -; mRNA.
DR EMBL; BC115131; AAI15132.1; ALT_INIT; mRNA.
DR RefSeq; NP_001108586.1; NM_001115114.1.
DR AlphaFoldDB; Q5XJ10; -.
DR SMR; Q5XJ10; -.
DR STRING; 7955.ENSDARP00000063799; -.
DR PaxDb; Q5XJ10; -.
DR PRIDE; Q5XJ10; -.
DR Ensembl; ENSDART00000063800; ENSDARP00000063799; ENSDARG00000043457.
DR Ensembl; ENSDART00000163606; ENSDARP00000134592; ENSDARG00000043457.
DR GeneID; 317743; -.
DR KEGG; dre:317743; -.
DR CTD; 2597; -.
DR ZFIN; ZDB-GENE-030115-1; gapdh.
DR eggNOG; KOG0657; Eukaryota.
DR GeneTree; ENSGT00940000153298; -.
DR HOGENOM; CLU_030140_0_3_1; -.
DR InParanoid; Q5XJ10; -.
DR OrthoDB; 945145at2759; -.
DR PhylomeDB; Q5XJ10; -.
DR TreeFam; TF300533; -.
DR Reactome; R-DRE-70171; Glycolysis.
DR Reactome; R-DRE-70263; Gluconeogenesis.
DR UniPathway; UPA00109; UER00184.
DR PRO; PR:Q5XJ10; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 16.
DR Bgee; ENSDARG00000043457; Expressed in muscle tissue and 36 other tissues.
DR ExpressionAtlas; Q5XJ10; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR GO; GO:0035605; F:peptidyl-cysteine S-nitrosylase activity; ISS:UniProtKB.
DR GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0051402; P:neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0035606; P:peptidyl-cysteine S-trans-nitrosylation; ISS:UniProtKB.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0032481; P:positive regulation of type I interferon production; ISS:UniProtKB.
DR GO; GO:0050821; P:protein stabilization; ISS:UniProtKB.
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 PANTHER; PTHR10836; PTHR10836; 1.
DR Pfam; PF02800; Gp_dh_C; 1.
DR Pfam; PF00044; Gp_dh_N; 1.
DR PIRSF; PIRSF000149; GAP_DH; 1.
DR PRINTS; PR00078; G3PDHDRGNASE.
DR SMART; SM00846; Gp_dh_N; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR01534; GAPDH-I; 1.
DR PROSITE; PS00071; GAPDH; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Cytoplasm; Cytoskeleton; Glycolysis; NAD; Nucleus;
KW Oxidoreductase; Reference proteome; S-nitrosylation; Transferase.
FT CHAIN 1..333
FT /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT /id="PRO_0000382469"
FT ACT_SITE 150
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P04406,
FT ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 11..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT BINDING 33
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT BINDING 78
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT BINDING 120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT BINDING 149..151
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT BINDING 180
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT BINDING 209..210
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT BINDING 232
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P22513"
FT BINDING 314
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT SITE 177
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250|UniProtKB:P04406"
FT MOD_RES 150
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:P04797"
FT CONFLICT 210
FT /note="G -> E (in Ref. 1; AAI15132)"
FT /evidence="ECO:0000305"
FT CONFLICT 318
FT /note="Y -> H (in Ref. 1; AAI15132)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 333 AA; 35784 MW; 206FC71AA4774526 CRC64;
MVKVGINGFG RIGRLVTRAA FLTKKVEIVA INDPFIDLDY MVYMFQYDST HGKYKGEVKA
EGGKLVIDGH AITVYSERDP ANIKWGDAGA TYVVESTGVF TTIEKASAHI KGGAKRVIIS
APSADAPMFV MGVNHEKYDN SLTVVSNASC TTNCLAPLAK VINDNFVIVE GLMSTVHAIT
ATQKTVDGPS GKLWRDGRGA SQNIIPASTG AAKAVGKVIP ELNGKLTGMA FRVPTPNVSV
VDLTVRLEKP AKYDEIKKVV KAAADGPMKG ILGYTEHQVV STDFNGDCRS SIFDAGAGIA
LNDHFVKLVT WYDNEFGYSN RVCDLMAHMA SKE
