ID Q49UT4_STAS1 Unreviewed; 192 AA.
AC Q49UT4;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 97.
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=SSP2337 {ECO:0000313|EMBL:BAE19482.1};
OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS 20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=342451 {ECO:0000313|EMBL:BAE19482.1, ECO:0000313|Proteomes:UP000006371};
RN [1] {ECO:0000313|EMBL:BAE19482.1, ECO:0000313|Proteomes:UP000006371}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41
RC {ECO:0000313|Proteomes:UP000006371};
RX PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT pathogenesis of uncomplicated urinary tract infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP008934; BAE19482.1; -; Genomic_DNA.
DR RefSeq; WP_011303934.1; NZ_MTGA01000035.1.
DR AlphaFoldDB; Q49UT4; -.
DR KEGG; ssp:SSP2337; -.
DR PATRIC; fig|342451.11.peg.2326; -.
DR eggNOG; COG0406; Bacteria.
DR HOGENOM; CLU_033323_8_5_9; -.
DR OrthoDB; 9782128at2; -.
DR Proteomes; UP000006371; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000006371}.
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 SITE 158
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-3"
SQ SEQUENCE 192 AA; 22387 MW; A73B4D1FC8825174 CRC64;
MKIYLVRHGE SQSNYDKKQG KNYFCGQLDV PLTERGTWSA QLLQSYFDKK AIDHIYISDL
LRTRQTYNAI FDKSIPASVT PLLRERSLGV FEGKIVEAVE QNSSYTRYFE DQNYLEFRHS
FTQKAPEGES YADVMERVKQ FFENEIDDSL DSIAIVAHQV VIRCCFVYLG YDSEATVIDR
KIENCVPYEL EK
//
