ID A0A0H2VIJ2_STAES Unreviewed; 196 AA.
AC A0A0H2VIJ2;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) {ECO:0000256|ARBA:ARBA00012028};
DE EC=5.4.2.11 {ECO:0000256|ARBA:ARBA00012028};
GN OrderedLocusNames=SE_2364 {ECO:0000313|EMBL:AAO06007.1};
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280 {ECO:0000313|EMBL:AAO06007.1, ECO:0000313|Proteomes:UP000001411};
RN [1] {ECO:0000313|EMBL:AAO06007.1, ECO:0000313|Proteomes:UP000001411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200 {ECO:0000313|Proteomes:UP000001411};
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.Q., Ren S.X., Li H.L., Wang Y.X., Fu G., Yang J., Qin Z.Q.,
RA Miao Y.G., Wang W.Y., Chen R.S., Shen Y., Chen Z., Yuan Z.H., Zhao G.P.,
RA Qu D., Danchin A., Wen Y.M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.11; Evidence={ECO:0000256|ARBA:ARBA00000380};
CC -!- SIMILARITY: Belongs to the phosphoglycerate mutase family. BPG-
CC dependent PGAM subfamily. {ECO:0000256|ARBA:ARBA00006717}.
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DR EMBL; AE015929; AAO06007.1; -; Genomic_DNA.
DR RefSeq; NP_765919.1; NC_004461.1.
DR RefSeq; WP_002485681.1; NZ_WBME01000004.1.
DR AlphaFoldDB; A0A0H2VIJ2; -.
DR KEGG; sep:SE_2364; -.
DR PATRIC; fig|176280.10.peg.2304; -.
DR eggNOG; COG0406; Bacteria.
DR HOGENOM; CLU_033323_8_5_9; -.
DR OrthoDB; 9782128at2; -.
DR Proteomes; UP000001411; Chromosome.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
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 InterPro; IPR005952; Phosphogly_mut1.
DR PANTHER; PTHR11931; PHOSPHOGLYCERATE MUTASE; 1.
DR PANTHER; PTHR11931:SF0; PHOSPHOGLYCERATE MUTASE; 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 3: Inferred from homology;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235}.
FT ACT_SITE 8
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 85
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 7..14
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 62
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT SITE 158
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-3"
SQ SEQUENCE 196 AA; 23715 MW; AB9014CEF5FEF69F CRC64;
MEIYLVRHGE SQSNYDNKHG YLYFCGQLDV PLTERGIKSA KELSVYFKNK YIDNIYLSDL
KRTRQTYEEL FPYDIPTIYT KTLRERSLGV FEGENKEEVC KDKRFEKYFR DPNYKYFRHS
FSQKAPQGES YQDVYDRVVT FIENELNQQQ KRVVIVAHQV VIRCFFVYFK MITKEEALAT
EIHNCYPYLI KKEMKF
//
