GPMI_CLOD6
ID GPMI_CLOD6 Reviewed; 510 AA.
AC Q181T7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase {ECO:0000255|HAMAP-Rule:MF_01038};
DE Short=BPG-independent PGAM {ECO:0000255|HAMAP-Rule:MF_01038};
DE Short=Phosphoglyceromutase {ECO:0000255|HAMAP-Rule:MF_01038};
DE Short=iPGM {ECO:0000255|HAMAP-Rule:MF_01038};
DE EC=5.4.2.12 {ECO:0000255|HAMAP-Rule:MF_01038};
GN Name=gpmI {ECO:0000255|HAMAP-Rule:MF_01038}; OrderedLocusNames=CD630_31710;
OS Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Clostridioides.
OX NCBI_TaxID=272563;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=630;
RX PubMed=16804543; DOI=10.1038/ng1830;
RA Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT mobile, mosaic genome.";
RL Nat. Genet. 38:779-786(2006).
CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and 3-
CC phosphoglycerate. {ECO:0000255|HAMAP-Rule:MF_01038}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate;
CC Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289;
CC EC=5.4.2.12; Evidence={ECO:0000255|HAMAP-Rule:MF_01038};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01038};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_01038};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC glyceraldehyde 3-phosphate: step 3/5. {ECO:0000255|HAMAP-
CC Rule:MF_01038}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01038}.
CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase
CC family. {ECO:0000255|HAMAP-Rule:MF_01038}.
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; AM180355; CAJ70068.1; -; Genomic_DNA.
DR RefSeq; WP_011861866.1; NC_009089.1.
DR RefSeq; YP_001089688.1; NC_009089.1.
DR AlphaFoldDB; Q181T7; -.
DR SMR; Q181T7; -.
DR STRING; 272563.CD630_31710; -.
DR EnsemblBacteria; CAJ70068; CAJ70068; CD630_31710.
DR KEGG; cdf:CD630_31710; -.
DR PATRIC; fig|272563.8.peg.3322; -.
DR eggNOG; COG0696; Bacteria.
DR OMA; FMDGRDT; -.
DR PhylomeDB; Q181T7; -.
DR BioCyc; PDIF272563:G12WB-3337-MON; -.
DR UniPathway; UPA00109; UER00186.
DR Proteomes; UP000001978; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006007; P:glucose catabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR CDD; cd16010; iPGM; 1.
DR Gene3D; 3.40.1450.10; -; 1.
DR Gene3D; 3.40.720.10; -; 1.
DR HAMAP; MF_01038; GpmI; 1.
DR InterPro; IPR017850; Alkaline_phosphatase_core_sf.
DR InterPro; IPR011258; BPG-indep_PGM_N.
DR InterPro; IPR006124; Metalloenzyme.
DR InterPro; IPR036646; PGAM_B_sf.
DR InterPro; IPR005995; Pgm_bpd_ind.
DR PANTHER; PTHR31637; PTHR31637; 1.
DR Pfam; PF06415; iPGM_N; 1.
DR Pfam; PF01676; Metalloenzyme; 1.
DR PIRSF; PIRSF001492; IPGAM; 1.
DR SUPFAM; SSF53649; SSF53649; 1.
DR SUPFAM; SSF64158; SSF64158; 1.
DR TIGRFAMs; TIGR01307; pgm_bpd_ind; 1.
PE 3: Inferred from homology;
KW Glycolysis; Isomerase; Manganese; Metal-binding; Reference proteome.
FT CHAIN 1..510
FT /note="2,3-bisphosphoglycerate-independent phosphoglycerate
FT mutase"
FT /id="PRO_1000063955"
FT ACT_SITE 62
FT /note="Phosphoserine intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 12
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 62
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 121
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 151..152
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 183
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 189
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 258..261
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 331
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 398
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 402
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 439
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 440
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
FT BINDING 458
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01038"
SQ SEQUENCE 510 AA; 56374 MW; 5AD88452945333F0 CRC64;
MMKKPVALII MDGFGYNKDV KGNAIAESKT PNLDRIKKEY PNTLINASGL DVGLPDGQMG
NSEVGHTNIG AGRIVYQDLT RITKSIKDGD FFTNKVLCEA MDNAKENSLH VMGLLSDGGV
HSHIDHLKAI IKMAKDKGVQ KVYVHAFTDG RDTDPQSALE YAKEVQASMD EIGVGEFATV
SGRYYAMDRD KRWERVELAY NAMVRGIGEK ANSIEEAIQN SYDDGKNDEF IMPTVIMKDD
KPVGSIKEND SIIFFNFRPD RARQITRALV CEEFDGFKRE DIKNFFVCLT EYDITIENVH
IAFGPQSLAN TLGEYLAKNG KTQLRAAETE KYAHVTFFFN GGVEEPNKGE ERLLIPSPKV
ATYDLKPEMS AYELTDKALD KLGEDKFDFI VLNFANPDMV GHTGSIEAAI KAVETVDTCV
GKLIDKIVEL GGSAIITADH GNAEYMLDPE TGKTVTAHSI NPVPFIVVGQ EYESAKLLDG
GRLSDIAPTI LDMMKLEKPE EMTGHSLISK
