ID A7HE66_ANADF Unreviewed; 251 AA.
AC A7HE66;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Phosphoglycerate mutase {ECO:0000313|EMBL:ABS27012.1};
GN OrderedLocusNames=Anae109_2812 {ECO:0000313|EMBL:ABS27012.1};
OS Anaeromyxobacter sp. (strain Fw109-5).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=404589 {ECO:0000313|EMBL:ABS27012.1, ECO:0000313|Proteomes:UP000006382};
RN [1] {ECO:0000313|EMBL:ABS27012.1, ECO:0000313|Proteomes:UP000006382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fw109-5 {ECO:0000313|EMBL:ABS27012.1,
RC ECO:0000313|Proteomes:UP000006382};
RX PubMed=25614562; DOI=10.1128/genomeA.01449-14;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T.,
RA Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C.,
RA Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J.,
RA Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A.,
RA Loeffler F.E., Fields M.W.;
RT "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic,
RT metal-reducing bacterium isolated from a contaminated subsurface
RT environment.";
RL Genome Announc. 3:0-0(2015).
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DR EMBL; CP000769; ABS27012.1; -; Genomic_DNA.
DR AlphaFoldDB; A7HE66; -.
DR STRING; 404589.Anae109_2812; -.
DR KEGG; afw:Anae109_2812; -.
DR eggNOG; COG0406; Bacteria.
DR HOGENOM; CLU_033323_9_4_7; -.
DR Proteomes; UP000006382; Chromosome.
DR GO; GO:0003824; F:catalytic activity; 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 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 SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR PROSITE; PS00175; PG_MUTASE; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000006382}.
FT REGION 27..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 58
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 132
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT BINDING 57..64
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 107
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 132..135
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 251 AA; 27146 MW; 1EDE28922B923C63 CRC64;
MRDVHPPRRR RARAPWHNRC HFATRRAGSA PRRWRSRPGR VNVPPMAPTE RHLLLVRHGE
TDWNAAGRWQ GQTDVPLNAT GRAQAAALAA RLRPEGVRAI ATSDLCRARG TAEIVGEALG
LRIAFVDADL RERAYGLWEG LTRGECEARF PEEWARHVSD PRAPPPAGES TDALLARVLP
AIERAAGRLE SPAVLVTHGG VMRAFLAAAL GACPGPAQVA PPRFIPNGGV WRVRLVAGRV
VGAAALHGDA P
//
