ID A4J5S6_DESRM Unreviewed; 208 AA.
AC A4J5S6;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Phosphoglycerate mutase {ECO:0000313|EMBL:ABO50429.1};
DE EC=5.4.2.- {ECO:0000313|EMBL:ABO50429.1};
GN OrderedLocusNames=Dred_1908 {ECO:0000313|EMBL:ABO50429.1};
OS Desulforamulus reducens (strain ATCC BAA-1160 / DSM 100696 / MI-1)
OS (Desulfotomaculum reducens).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=349161 {ECO:0000313|EMBL:ABO50429.1, ECO:0000313|Proteomes:UP000001556};
RN [1] {ECO:0000313|EMBL:ABO50429.1, ECO:0000313|Proteomes:UP000001556}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MI-1 {ECO:0000313|EMBL:ABO50429.1,
RC ECO:0000313|Proteomes:UP000001556};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Sims D., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Kim E., Tebo B.M., Richardson P.;
RT "Complete sequence of Desulfotomaculum reducens MI-1.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000612; ABO50429.1; -; Genomic_DNA.
DR RefSeq; WP_011878241.1; NC_009253.1.
DR AlphaFoldDB; A4J5S6; -.
DR STRING; 349161.Dred_1908; -.
DR KEGG; drm:Dred_1908; -.
DR eggNOG; COG0406; Bacteria.
DR HOGENOM; CLU_033323_8_4_9; -.
DR OrthoDB; 9781415at2; -.
DR Proteomes; UP000001556; Chromosome.
DR GO; GO:0043755; F:alpha-ribazole phosphatase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:InterPro.
DR GO; GO:0006003; P:fructose 2,6-bisphosphate metabolic process; IEA:InterPro.
DR CDD; cd07067; HP_PGM_like; 1.
DR Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR InterPro; IPR003094; 6Pfruct_kin.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR001345; PG/BPGM_mutase_AS.
DR InterPro; IPR017578; Ribazole_CobC.
DR NCBIfam; TIGR03162; ribazole_cobC; 1.
DR PANTHER; PTHR48100; BROAD-SPECIFICITY PHOSPHATASE YOR283W-RELATED; 1.
DR PANTHER; PTHR48100:SF1; PHOSPHOGLYCERATE MUTASE PMU1-RELATED; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR PIRSF; PIRSF000709; 6PFK_2-Ptase; 1.
DR PRINTS; PR00991; 6PFRUCTKNASE.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000313|EMBL:ABO50429.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001556}.
FT ACT_SITE 11
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 84
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 10..17
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 60
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT SITE 152
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-3"
SQ SEQUENCE 208 AA; 23755 MW; B4F54B18493E535E CRC64;
MKKTRMYLVR HGETQWNADG RFQGHSDVPL SVLGRSQVET LTTKLSQLKI DAFYSSDLSR
AMETAEILAK KHQCQIYYLP DLREINFGEW EGLTFEEIAQ NYGELSSQWW ANPFTTQIPS
GESLQDVAER CAKAVHEIID RHAGKTVVVA AHGGVIRMIV AHALGMDFQH YWKLRLDNVS
LTIVEYHGYE KAILELYNDT CHLKNTPS
//
