G3P1_BACCE
ID G3P1_BACCE Reviewed; 334 AA.
AC Q4MQ58; P83078;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase 1 {ECO:0000250|UniProtKB:P00362};
DE Short=GAPDH 1 {ECO:0000250|UniProtKB:P00362};
DE EC=1.2.1.12 {ECO:0000250|UniProtKB:P09124};
DE AltName: Full=NAD-dependent glyceraldehyde-3-phosphate dehydrogenase {ECO:0000250|UniProtKB:P00362};
GN Name=gap1; ORFNames=BCE_G9241_5218;
OS Bacillus cereus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1396;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=G9241;
RX PubMed=15155910; DOI=10.1073/pnas.0402414101;
RA Hoffmaster A.R., Ravel J., Rasko D.A., Chapman G.D., Chute M.D.,
RA Marston C.K., De B.K., Sacchi C.T., Fitzgerald C., Mayer L.W.,
RA Maiden M.C.J., Priest F.G., Barker M., Jiang L., Cer R.Z., Rilstone J.,
RA Peterson S.N., Weyant R.S., Galloway D.R., Read T.D., Popovic T.,
RA Fraser C.M.;
RT "Identification of anthrax toxin genes in a Bacillus cereus associated with
RT an illness resembling inhalation anthrax.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8449-8454(2004).
RN [2]
RP PROTEIN SEQUENCE OF 2-21, AND INDUCTION.
RC STRAIN=DSM 626 / NCIMB 11796 / T;
RX PubMed=11851817; DOI=10.1046/j.1365-2672.2001.01478.x;
RA Browne N., Dowds B.C.A.;
RT "Heat and salt stress in the food pathogen Bacillus cereus.";
RL J. Appl. Microbiol. 91:1085-1094(2001).
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.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P00362}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Repressed by salt stress. {ECO:0000269|PubMed:11851817}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; AAEK01000016; EAL14305.1; -; Genomic_DNA.
DR RefSeq; WP_000161236.1; NZ_WBPP01000004.1.
DR AlphaFoldDB; Q4MQ58; -.
DR SMR; Q4MQ58; -.
DR STRING; 1396.DJ87_4719; -.
DR PRIDE; Q4MQ58; -.
DR GeneID; 58159342; -.
DR GeneID; 67509763; -.
DR eggNOG; COG0057; Bacteria.
DR OMA; ATGVHRK; -.
DR OrthoDB; 944149at2; -.
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: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 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; PTHR43148; PTHR43148; 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 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Glycolysis; NAD; Nucleotide-binding;
KW Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11851817"
FT CHAIN 2..334
FT /note="Glyceraldehyde-3-phosphate dehydrogenase 1"
FT /id="PRO_0000271247"
FT ACT_SITE 151
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 11..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 33
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 77
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 150..152
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 181
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 182
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 196
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 209..210
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 232
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT BINDING 314
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P00362"
FT SITE 178
FT /note="Activates thiol group during catalysis"
FT /evidence="ECO:0000250|UniProtKB:Q6GIL8"
FT CONFLICT 13
FT /note="G -> R (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 334 AA; 35826 MW; D5E1F3F4C45BF23B CRC64;
MTKIGINGFG RIGRNVFRAA LNNSEVEVVA INDLTDAKTL AHLLKYDTVH GTLNAEVSAN
ENSIVVNGKE IKVIAERDPA QLPWSDYGVE VVVESTGRFT KKSDAEKHLG GSVKKVIISA
PASDEDITVV MGVNHEQYDA ANHNVVSNAS CTTNCLAPFA KVLNEKFGVK RGMMTTIHSY
TNDQQILDLP HKDLRRARAA AENMIPTSTG AAKAVALVLP ELKGKLNGGA VRVPTANVSL
VDLVVELDKE VTVEEVNAAF KAAAEGELKG ILGYSEEPLV SIDYNGCTAS STIDALSTMV
MEGNMVKVLS WYDNETGYSN RVVDLAAYMT SKGL
