G3P2_BACCE
ID G3P2_BACCE Reviewed; 14 AA.
AC P83077;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 46.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 2 {ECO:0000250|UniProtKB:P00362};
DE Short=GAPDH 2 {ECO:0000250|UniProtKB:P00362};
DE EC=1.2.1.12 {ECO:0000250|UniProtKB:P09124};
DE Flags: Fragment;
GN Name=gap2;
OS Bacillus cereus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1396;
RN [1]
RP PROTEIN SEQUENCE.
RC STRAIN=DSM 626 / NCIMB 11796 / T;
RX PubMed=11872115; DOI=10.1046/j.1365-2672.2002.01541.x;
RA Browne N., Dowds B.C.A.;
RT "Acid stress in the food pathogen Bacillus cereus.";
RL J. Appl. Microbiol. 92:404-414(2002).
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:P00362}.
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:P09124};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000305}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P00362}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: Under acid-stress, this protein is expressed at a higher
CC level in wild-type B.cereus than in the acid-sensitive mutant strain
CC NB1. {ECO:0000269|PubMed:11872115}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {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 UniPathway; UPA00109; UER00184.
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:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Glycolysis; NAD; Nucleotide-binding;
KW Oxidoreductase.
FT CHAIN 1..>14
FT /note="Glyceraldehyde-3-phosphate dehydrogenase 2"
FT /id="PRO_0000271248"
FT BINDING 10..11
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00361"
FT NON_TER 14
FT /evidence="ECO:0000303|PubMed:11872115"
SQ SEQUENCE 14 AA; 1604 MW; 209872BB19F5E0C8 CRC64;
MKQGINGFAR RGRL