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Database: UniProt
Entry: I2BA89
LinkDB: I2BA89
Original site: I2BA89 
ID   G3P_SHIBC               Reviewed;         331 AA.
AC   I2BA89; P24749;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2012, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P0A9B2};
DE            Short=GAPDH {ECO:0000250|UniProtKB:P0A9B2};
DE            EC=1.2.1.12 {ECO:0000250|UniProtKB:P0A9B2};
DE   AltName: Full=NAD-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P0A9B2};
GN   Name=gapA; Synonyms=gap; OrderedLocusNames=EBL_c23540;
OS   Shimwellia blattae (strain ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 /
OS   CDC 9005-74) (Escherichia blattae).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shimwellia.
OX   NCBI_TaxID=630626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 / CDC 9005-74;
RX   PubMed=22843577; DOI=10.1128/jb.00829-12;
RA   Brzuszkiewicz E., Waschkowitz T., Wiezer A., Daniel R.;
RT   "Complete genome sequence of the B12-producing Shimwellia blattae strain
RT   DSM 4481, isolated from a cockroach.";
RL   J. Bacteriol. 194:4436-4436(2012).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 16-309.
RC   STRAIN=ATCC 29907 / DSM 4481 / JCM 1650 / NBRC 105725 / CDC 9005-74;
RX   PubMed=1955870; DOI=10.1099/00221287-137-8-1911;
RA   Lawrence J.G., Ochman H., Hartl D.L.;
RT   "Molecular and evolutionary relationships among enteric bacteria.";
RL   J. Gen. Microbiol. 137:1911-1921(1991).
CC   -!- FUNCTION: Catalyzes the oxidative phosphorylation of glyceraldehyde 3-
CC       phosphate (G3P) to 1,3-bisphosphoglycerate (BPG) using the cofactor
CC       NAD. The first reaction step involves the formation of a hemiacetal
CC       intermediate between G3P and a cysteine residue, and this hemiacetal
CC       intermediate is then oxidized to a thioester, with concomitant
CC       reduction of NAD to NADH. The reduced NADH is then exchanged with the
CC       second NAD, and the thioester is attacked by a nucleophilic inorganic
CC       phosphate to produce BPG. {ECO:0000250|UniProtKB:P0A9B2}.
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:P0A9B2};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P0A9B2}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; CP001560; AFJ47443.1; -; Genomic_DNA.
DR   EMBL; M63358; AAA23837.1; -; Genomic_DNA.
DR   PIR; I41220; I41220.
DR   RefSeq; WP_002440306.1; NZ_BAHA01000005.1.
DR   AlphaFoldDB; I2BA89; -.
DR   SMR; I2BA89; -.
DR   STRING; 630626.EBL_c23540; -.
DR   KEGG; ebt:EBL_c23540; -.
DR   PATRIC; fig|630626.3.peg.2276; -.
DR   eggNOG; COG0057; Bacteria.
DR   HOGENOM; CLU_030140_0_3_6; -.
DR   OrthoDB; 9803304at2; -.
DR   UniPathway; UPA00109; UER00184.
DR   Proteomes; UP000001955; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; ISS:UniProtKB.
DR   GO; GO:0051287; F:NAD binding; ISS:UniProtKB.
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:SF76; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE-RELATED; 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; 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   Cytoplasm; Glycolysis; NAD; Nucleotide-binding; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..331
FT                   /note="Glyceraldehyde-3-phosphate dehydrogenase"
FT                   /id="PRO_0000418985"
FT   ACT_SITE        150
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9B2"
FT   BINDING         12..13
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9B2"
FT   BINDING         34
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9B2"
FT   BINDING         78
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9B2"
FT   BINDING         120
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9B2"
FT   BINDING         149..151
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9B2"
FT   BINDING         180
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9B2"
FT   BINDING         209..210
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9B2"
FT   BINDING         232
FT                   /ligand="D-glyceraldehyde 3-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:59776"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9B2"
FT   BINDING         314
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9B2"
FT   SITE            177
FT                   /note="Activates thiol group during catalysis"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9B2"
SQ   SEQUENCE   331 AA;  35532 MW;  53212B9C4765B2B3 CRC64;
     MTIKVGINGF GRIGRIVFRA AQERSDIEIV AINDLLDAEY MAYMLKYDST HGRFNGTVEV
     KDGHLIVNGK KIRVTAERDP ANLKWNEAGV EVVAEATGLF LTDETARKHI TAGAKKVVMT
     GPSKDSTPMF VRGANFDTYA GQDIVSNASC TTNCLAPLAK VVNDNFGIVE ALMTTVHATT
     ATQKTVDGPS HKDWRGGRGA SQNIIPSSTG AAKAVGKVLP ELNGKLTGMA FRVPTPNVSV
     VDLTVRLAKP ATYEEIKKAM KAASEGAMKG VLGYTEDDVV STDFNGETCT SVFDAKAGIA
     LNDNFVKLVS WYDNETGYSH KVLDLIAHIS K
//
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