ID A0A160F8I7_9BACI Unreviewed; 207 AA.
AC A0A160F8I7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=phosphoglycerate mutase (2,3-diphosphoglycerate-dependent) {ECO:0000256|ARBA:ARBA00012028};
DE EC=5.4.2.11 {ECO:0000256|ARBA:ARBA00012028};
GN ORFNames=GFC29_1173 {ECO:0000313|EMBL:ANB62987.1};
OS Anoxybacillus sp. B7M1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=1490057 {ECO:0000313|EMBL:ANB62987.1, ECO:0000313|Proteomes:UP000076753};
RN [1] {ECO:0000313|EMBL:ANB62987.1, ECO:0000313|Proteomes:UP000076753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=b7m1 {ECO:0000313|Proteomes:UP000076753};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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; CP015436; ANB62987.1; -; Genomic_DNA.
DR RefSeq; WP_044746438.1; NZ_CP015436.1.
DR AlphaFoldDB; A0A160F8I7; -.
DR KEGG; anl:GFC29_1173; -.
DR PATRIC; fig|1490057.3.peg.1342; -.
DR OrthoDB; 9782128at2; -.
DR Proteomes; UP000076753; Chromosome.
DR GO; GO:0016868; F:intramolecular phosphotransferase activity; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; 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 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:UP000076753}.
FT ACT_SITE 9
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 82
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 8..15
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 207 AA; 23897 MW; 13BCFB0BE199EA23 CRC64;
MLTLYVTRHG ETEWNIEKRL QGWNDSPLTK KGREDALRLG KRMEKIDLTA IYTSTSGRAL
ETAKLIRGER LIPMYEDERW REIHLGDWEG RTHEEIQKFD AVRFHHFWNE PHVYQPARGE
AFSDVQQRAF AALESIIERH ASGDILIVTH AVVLKALTTL LKNAPLERLW DPPYIYGTSV
TTIQVENGVM TLLSEGDASH IEEVKHV
//
