ID Q87PX9_VIBPA Unreviewed; 200 AA.
AC Q87PX9;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Putative phosphoglycerate mutase family protein {ECO:0000313|EMBL:BAC59634.1};
GN OrderedLocusNames=VP1371 {ECO:0000313|EMBL:BAC59634.1};
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926 {ECO:0000313|EMBL:BAC59634.1, ECO:0000313|Proteomes:UP000002493};
RN [1] {ECO:0000313|EMBL:BAC59634.1, ECO:0000313|Proteomes:UP000002493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633 {ECO:0000313|Proteomes:UP000002493};
RX PubMed=12620739; DOI=10.1016/S0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; BA000031; BAC59634.1; -; Genomic_DNA.
DR RefSeq; NP_797750.1; NC_004603.1.
DR RefSeq; WP_005454893.1; NC_004603.1.
DR AlphaFoldDB; Q87PX9; -.
DR GeneID; 1188878; -.
DR KEGG; vpa:VP1371; -.
DR PATRIC; fig|223926.6.peg.1312; -.
DR eggNOG; COG0406; Bacteria.
DR HOGENOM; CLU_033323_9_1_6; -.
DR Proteomes; UP000002493; Chromosome 1.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR PANTHER; PTHR46517; FRUCTOSE-2,6-BISPHOSPHATASE TIGAR; 1.
DR PANTHER; PTHR46517:SF1; FRUCTOSE-2,6-BISPHOSPHATASE TIGAR; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR PIRSF; PIRSF000709; 6PFK_2-Ptase; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Reference proteome {ECO:0000313|Proteomes:UP000002493}.
FT ACT_SITE 10
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 89
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 9..16
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 200 AA; 23058 MW; 5405B5A7082534F9 CRC64;
MTRRIFVLRH GETEFNADKK LQGHCNSSLT SKGSDQARRV GTTLKQYVEN RLFRVYSSTL
GRALQTSQIV CEELNYSYEN LNKEPRLKEF SLGEWEQRTI PSLEQEIPNL LAQNDWYLQA
PNCETYESVR ERLSSWLSDV AHDEDIVVVS HGLTGIVLRG LLLGMDYTQV WQQDLPQDAF
FIIEDSRITR VNCVDAVEVV
//
