G3P2_DANRE
ID G3P2_DANRE Reviewed; 335 AA.
AC Q5MJ86;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 2;
DE EC=1.2.1.12;
GN Name=gapdh-2; Synonyms=gapdh {ECO:0000303|PubMed:17239340};
GN ORFNames=zgc:76908;
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:0000305, ECO:0000312|EMBL:AAW28030.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=AB {ECO:0000312|EMBL:AAW28030.1};
RC TISSUE=Gastrula {ECO:0000269|PubMed:17239340};
RX PubMed=17239340; DOI=10.1016/j.ab.2006.12.005;
RA Pei D.-S., Sun Y.-H., Chen S.-P., Wang Y.-P., Hu W., Zhu Z.-Y.;
RT "Zebrafish GAPDH can be used as a reference gene for expression analysis in
RT cross-subfamily cloned embryos.";
RL Anal. Biochem. 363:291-293(2007).
RN [2] {ECO:0000312|EMBL:AAI54823.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney {ECO:0000312|EMBL:AAI54823.1};
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in
CC glycolysis that catalyzes the first step of the pathway by converting
CC D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl
CC phosphate. {ECO:0000250}.
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:Q64467, ECO:0000255|PROSITE-
CC ProRule:PRU10009};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000250|UniProtKB:Q64467}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q64467}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q64467}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000255}.
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DR EMBL; AY818346; AAW28030.1; -; mRNA.
DR EMBL; BC154822; AAI54823.1; -; mRNA.
DR RefSeq; NP_998259.1; NM_213094.2.
DR AlphaFoldDB; Q5MJ86; -.
DR SMR; Q5MJ86; -.
DR STRING; 7955.ENSDARP00000058383; -.
DR PaxDb; Q5MJ86; -.
DR GeneID; 406367; -.
DR KEGG; dre:406367; -.
DR CTD; 26330; -.
DR ZFIN; ZDB-GENE-020913-1; gapdhs.
DR eggNOG; KOG0657; Eukaryota.
DR InParanoid; Q5MJ86; -.
DR OrthoDB; 945145at2759; -.
DR PhylomeDB; Q5MJ86; -.
DR UniPathway; UPA00109; UER00184.
DR PRO; PR:Q5MJ86; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IBA:GO_Central.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
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; IBA:GO_Central.
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 Cytoplasm; Glycolysis; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..335
FT /note="Glyceraldehyde-3-phosphate dehydrogenase 2"
FT /id="PRO_0000382470"
FT ACT_SITE 152
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q64467,
FT ECO:0000255|PROSITE-ProRule:PRU10009"
FT BINDING 13..14
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q64467"
FT BINDING 34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q64467"
FT BINDING 79
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q64467"
FT BINDING 151..153
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:Q64467"
FT BINDING 182
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:Q64467"
FT BINDING 211..212
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:Q64467"
FT BINDING 234
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:Q64467"
FT BINDING 316
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:Q64467"
FT SITE 179
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250|UniProtKB:Q64467"
SQ SEQUENCE 335 AA; 36107 MW; 09EBADBE9AF19ECE CRC64;
MSELCVGING FGRIGRLVLR ACLQKGIKVT AINDPFIDLQ YMVYMFKYDS THGRYKGEVH
MEDGKLIVDG QAISVFQCMK PAEIPWGDAG ALYVVESTGV FLSIEKASAH IQGGAKRVVV
SAPSPDAPMF VMGVNQDKYD PSSMTIVSNA SCTTNCLAPL AKVIHDNFGI EEALMTTVHA
YTATQKTVDG PSAKAWRDGR GAHQNIIPAS TGAAKAVGKV IPELNGKLTG MAFRVPVADV
SVVDLTCRLT RPASYANIKE SVKKAAHGPM KGILGYTEDS VVSSDFVGDT HSSIFDAGAG
ISLNDNFVKL ISWYDNEFGY SHRVADLLMY MHSKE
