ID Q83R83_SHIFL Unreviewed; 250 AA.
AC Q83R83;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE SubName: Full=Glyceraldehyde-3-phosphate dehydrogenase A {ECO:0000313|EMBL:AAN43364.1};
GN OrderedLocusNames=SF1795 {ECO:0000313|EMBL:AAN43364.1};
OS Shigella flexneri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623 {ECO:0000313|EMBL:AAN43364.1, ECO:0000313|Proteomes:UP000001006};
RN [1] {ECO:0000313|EMBL:AAN43364.1, ECO:0000313|Proteomes:UP000001006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a {ECO:0000313|Proteomes:UP000001006};
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 1/5. {ECO:0000256|ARBA:ARBA00004869}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate dehydrogenase
CC family. {ECO:0000256|RuleBase:RU000397}.
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DR EMBL; AE005674; AAN43364.1; -; Genomic_DNA.
DR RefSeq; NP_707657.1; NC_004337.2.
DR AlphaFoldDB; Q83R83; -.
DR PaxDb; 198214-SF1795; -.
DR GeneID; 1024959; -.
DR KEGG; sfl:SF1795; -.
DR KEGG; sft:NCTC1_01931; -.
DR PATRIC; fig|198214.7.peg.2129; -.
DR HOGENOM; CLU_030140_0_1_6; -.
DR Proteomes; UP000001006; Chromosome.
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:SF6; GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASE; 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001006}.
FT DOMAIN 2..150
FT /note="Glyceraldehyde 3-phosphate dehydrogenase NAD(P)
FT binding"
FT /evidence="ECO:0000259|SMART:SM00846"
SQ SEQUENCE 250 AA; 26559 MW; 256424E6D9334179 CRC64;
MSKVGINGFG RIGRLVLRRL LEVKSNIDVV AINDLTSPKI LAYLLKHDSN YGPFPWSVDF
TEDSLIVDGK SIAVYAEKEA KNIPWKAKGA EIIVECTGFY TSADKSQAHL DAGAKKVLIS
APAGEMKTIV YNVNDDTLDG NDTIVSVASC TTNCLAPMAK ALHDSFGIEV GTMTTIHAYT
GTQSLVDGPR GKDLRASRAA AENIIPHTTG AAKAIGLVIP ELSGKLKGHA QRVPVKTGSV
TELVSILGKK
//
