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Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (EC 1.2.1.12) (NAD-dependent glyceraldehyde-3-phosphate dehydrogenase)

 G3P_MYCPN               Reviewed;         337 AA.
P75358;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
07-JUN-2017, entry version 116.
RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P9WN83};
Short=GAPDH {ECO:0000250|UniProtKB:P9WN83};
EC=1.2.1.12 {ECO:0000250|UniProtKB:P9WN83};
AltName: Full=NAD-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P9WN83};
Name=gapA; Synonyms=gap; OrderedLocusNames=MPN_430; ORFNames=MP411;
Mycoplasma pneumoniae (strain ATCC 29342 / M129).
Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
NCBI_TaxID=272634;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29342 / M129;
PubMed=8948633; DOI=10.1093/nar/24.22.4420;
Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C.,
Herrmann R.;
"Complete sequence analysis of the genome of the bacterium Mycoplasma
pneumoniae.";
Nucleic Acids Res. 24:4420-4449(1996).
-!- FUNCTION: Catalyzes the oxidative phosphorylation of
glyceraldehyde 3-phosphate (G3P) to 1,3-bisphosphoglycerate (BPG)
using the cofactor NAD. The first reaction step involves the
formation of a hemiacetal intermediate between G3P and a cysteine
residue, and this hemiacetal intermediate is then oxidized to a
thioester, with concomitant reduction of NAD to NADH. The reduced
NADH is then exchanged with the second NAD, and the thioester is
attacked by a nucleophilic inorganic phosphate to produce BPG.
{ECO:0000250|UniProtKB:P9WN83}.
-!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate +
NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH.
{ECO:0000250|UniProtKB:P9WN83}.
-!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}.
-!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P54226}.
-!- INTERACTION:
P02679:FGG (xeno); NbExp=2; IntAct=EBI-2259469, EBI-1034422;
P02751:FN1 (xeno); NbExp=3; IntAct=EBI-2259469, EBI-1220319;
P02788:LTF (xeno); NbExp=3; IntAct=EBI-2259469, EBI-1058602;
P04004:VTN (xeno); NbExp=3; IntAct=EBI-2259469, EBI-1036653;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
-!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate
dehydrogenase family. {ECO:0000305}.
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EMBL; U00089; AAB96059.1; -; Genomic_DNA.
PIR; S73737; S73737.
RefSeq; NP_110118.1; NC_000912.1.
RefSeq; WP_010874786.1; NC_000912.1.
ProteinModelPortal; P75358; -.
SMR; P75358; -.
IntAct; P75358; 12.
PRIDE; P75358; -.
EnsemblBacteria; AAB96059; AAB96059; MPN_430.
GeneID; 876854; -.
KEGG; mpn:MPN430; -.
PATRIC; fig|272634.6.peg.465; -.
OMA; FTLENMV; -.
BioCyc; MetaCyc:MONOMER-548; -.
UniPathway; UPA00109; UER00184.
Proteomes; UP000000808; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:AgBase.
GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-EC.
GO; GO:0051287; F:NAD binding; IEA:InterPro.
GO; GO:0050661; F:NADP binding; IEA:InterPro.
GO; GO:0006006; P:glucose metabolic process; IEA:InterPro.
GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
GO; GO:0031639; P:plasminogen activation; IDA:AgBase.
GO; GO:0034394; P:protein localization to cell surface; IDA:AgBase.
InterPro; IPR020831; GlycerAld/Erythrose_P_DH.
InterPro; IPR020830; GlycerAld_3-P_DH_AS.
InterPro; IPR020829; GlycerAld_3-P_DH_cat.
InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd.
InterPro; IPR006424; Glyceraldehyde-3-P_DH_1.
InterPro; IPR016040; NAD(P)-bd_dom.
Pfam; PF02800; Gp_dh_C; 1.
Pfam; PF00044; Gp_dh_N; 1.
PIRSF; PIRSF000149; GAP_DH; 1.
PRINTS; PR00078; G3PDHDRGNASE.
SMART; SM00846; Gp_dh_N; 1.
SUPFAM; SSF51735; SSF51735; 1.
TIGRFAMs; TIGR01534; GAPDH-I; 1.
PROSITE; PS00071; GAPDH; 1.
1: Evidence at protein level;
Complete proteome; Cytoplasm; Glycolysis; NAD; Nucleotide-binding;
Oxidoreductase; Reference proteome.
CHAIN 1 337 Glyceraldehyde-3-phosphate dehydrogenase.
/FTId=PRO_0000145670.
NP_BIND 17 18 NAD. {ECO:0000250|UniProtKB:P00362}.
REGION 156 158 Glyceraldehyde 3-phosphate binding.
{ECO:0000250|UniProtKB:P00362}.
REGION 215 216 Glyceraldehyde 3-phosphate binding.
{ECO:0000250|UniProtKB:P00362}.
ACT_SITE 157 157 Nucleophile.
{ECO:0000250|UniProtKB:P00362}.
BINDING 39 39 NAD. {ECO:0000250|UniProtKB:P00362}.
BINDING 83 83 NAD; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P00362}.
BINDING 125 125 NAD. {ECO:0000250|UniProtKB:P00362}.
BINDING 187 187 Glyceraldehyde 3-phosphate.
{ECO:0000250|UniProtKB:P00362}.
BINDING 202 202 Glyceraldehyde 3-phosphate.
{ECO:0000250|UniProtKB:P00362}.
BINDING 238 238 Glyceraldehyde 3-phosphate.
{ECO:0000250|UniProtKB:P00362}.
BINDING 319 319 NAD. {ECO:0000250|UniProtKB:P00362}.
SITE 184 184 Activates thiol group during catalysis.
{ECO:0000250|UniProtKB:P00362}.
SEQUENCE 337 AA; 36806 MW; 550747A529ABCA83 CRC64;
MLAKSKTIRV AINGFGRIGR LVFRALLSQK NIEIVAVNDL THPDTLAHLL KYDSAHGEFK
KKVVAKDNTL MIDKKKVLVF SEKDPANLPW AEHNIDIVVE STGRFVSEEG ASLHLQAGAK
RVIISAPAKQ KTIKTVVYNV NHKIINAEDK IISAASCTTN CLAPMVHVLE KNFGILHGTM
VTVHAYTADQ RLQDAPHSDL RRARAAACNI VPTTTGAAKA IGLVVPEATG KLNGMALRVP
VLTGSIVELC VALEKDATVE QINQAMKKAA SASFRYCEDE IVSSDIVGSE HGSIFDSKLT
NIIEVDGNKL YKVYAWYDNE SSYVNQLVRV VNYCAKL


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