ID Q38Q10_9BACI Unreviewed; 217 AA.
AC Q38Q10;
DT 22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2005, sequence version 1.
DT 27-MAR-2024, entry version 62.
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:ABA41014.1};
OS Peribacillus simplex.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Peribacillus.
OX NCBI_TaxID=1478 {ECO:0000313|EMBL:ABA41014.1};
RN [1] {ECO:0000313|EMBL:ABA41014.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=I5c12s {ECO:0000313|EMBL:ABA41014.1};
RX PubMed=16249328; DOI=10.1073/pnas.0507944102;
RA Sikorski J., Nevo E.;
RT "Adaptation and incipient sympatric speciation of Bacillus simplex under
RT microclimatic contrast at "Evolution Canyons" I and II, Israel.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:15924-15929(2005).
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; DQ159343; ABA41014.1; -; Genomic_DNA.
DR AlphaFoldDB; Q38Q10; -.
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..88
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:ABA41014.1"
FT NON_TER 217
FT /evidence="ECO:0000313|EMBL:ABA41014.1"
SQ SEQUENCE 217 AA; 23407 MW; 44B5AB53EC1CAABE CRC64;
LVVDGHKVKV LAERDPAQLA WGELGVEVVV ESTGRFTKRA DAAKHLEAGA KKVIISAPAS
DEDITIVMGV NEDKYDAANH HVISNASCTT NCLAPFAKVL HEQFGIKRGM MTTVHSYTND
QQILDLPHKD YRRARAAAEN IIPTTTGAAK AVALVLPELK GKLNGMAMRV PTPNVSVVDL
VAELEKDTTV EEVNAAFKKA SEGELKGILE YSELPLV
//
