ID   B0ZAS7_9BACI            Unreviewed;       212 AA.
AC   B0ZAS7;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) {ECO:0000256|ARBA:ARBA00013119};
DE            EC=1.2.1.12 {ECO:0000256|ARBA:ARBA00013119};
DE   Flags: Fragment;
GN   Name=gapA {ECO:0000313|EMBL:ACA04347.1};
OS   Peribacillus simplex.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX   NCBI_TaxID=1478 {ECO:0000313|EMBL:ACA04347.1};
RN   [1] {ECO:0000313|EMBL:ACA04347.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=I1c12o {ECO:0000313|EMBL:ACA04347.1};
RX   PubMed=18667574; DOI=10.1099/mic.0.2007/016105-0;
RA   Sikorski J., Brambilla E., Kroppenstedt R.M., Tindall B.J.;
RT   "The temperature-adaptive fatty acid content in Bacillus simplex strains
RT   from 'Evolution Canyon', Israel.";
RL   Microbiology 154:2416-2426(2008).
RN   [2] {ECO:0000313|EMBL:ACA04347.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=I1c12o {ECO:0000313|EMBL:ACA04347.1};
RX   PubMed=18272490; DOI=10.1073/pnas.0712205105;
RA   Koeppel A., Perry E.B., Sikorski J., Krizanc D., Warner A., Ward D.M.,
RA   Rooney A.P., Brambilla E., Connor N., Ratcliff R.M., Nevo E., Cohan F.M.;
RT   "Identifying the fundamental units of bacterial diversity: a paradigm shift
RT   to incorporate ecology into bacterial systematics.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:2504-2509(2008).
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 1/5. {ECO:0000256|ARBA:ARBA00004869}.
CC   -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC       family. {ECO:0000256|RuleBase:RU000397}.
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DR   EMBL; EU306055; ACA04347.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0ZAS7; -.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
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; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43148:SF11; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 1; 1.
DR   PANTHER; PTHR43148; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE 2; 1.
DR   Pfam; PF02800; Gp_dh_C; 1.
DR   Pfam; PF00044; Gp_dh_N; 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   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          1..83
FT                   /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT                   binding"
FT                   /evidence="ECO:0000259|SMART:SM00846"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ACA04347.1"
FT   NON_TER         212
FT                   /evidence="ECO:0000313|EMBL:ACA04347.1"
SQ   SEQUENCE   212 AA;  22951 MW;  B34385B2A0E83610 CRC64;
     HKVKVLAERD PAQLAWGELG VEVVVESTGR FTKRADAAKH LEAGAKKVII SAPASDEDIT
     IVMGVNEDKY DAANHHVISN ASCTTNCLAP FAKVLHEQFG IKRGMMTTVH SYTNDQQILD
     LPHKDYRRAR AAAENIIPTT TGAAKAVALV LPELKGKLNG MAMRVPTPNV SVVDLVVELE
     KDTTVEEVNA AFKKASEGEL KGILEYSELP LV
//