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Database: UniProt
Entry: C4L115_EXISA
LinkDB: C4L115_EXISA
Original site: C4L115_EXISA 
ID   C4L115_EXISA            Unreviewed;       199 AA.
AC   C4L115;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Phosphoglycerate mutase {ECO:0000313|EMBL:ACQ70978.1};
GN   OrderedLocusNames=EAT1b_2055 {ECO:0000313|EMBL:ACQ70978.1};
OS   Exiguobacterium sp. (strain ATCC BAA-1283 / AT1b).
OC   Bacteria; Bacillota; Bacilli; Bacillales;
OC   Bacillales Family XII. Incertae Sedis; Exiguobacterium.
OX   NCBI_TaxID=360911 {ECO:0000313|EMBL:ACQ70978.1, ECO:0000313|Proteomes:UP000000716};
RN   [1] {ECO:0000313|EMBL:ACQ70978.1, ECO:0000313|Proteomes:UP000000716}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1283 / AT1b {ECO:0000313|Proteomes:UP000000716};
RX   PubMed=21460088; DOI=10.1128/JB.00303-11;
RA   Vishnivetskaya T.A., Lucas S., Copeland A., Lapidus A., Glavina Del Rio T.,
RA   Dalin E., Tice H., Bruce D.C., Goodwin L.A., Pitluck S., Saunders E.,
RA   Brettin T., Detter C., Han C., Larimer F., Land M.L., Hauser L.J.,
RA   Kyrpides N.C., Ovchinnikova G., Kathariou S., Ramaley R.F., Rodrigues D.F.,
RA   Hendrix C., Richardson P., Tiedje J.M.;
RT   "Complete genome sequence of the Thermophilic Bacterium Exiguobacterium sp.
RT   AT1b.";
RL   J. Bacteriol. 193:2880-2881(2011).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC       Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; CP001615; ACQ70978.1; -; Genomic_DNA.
DR   RefSeq; WP_015880537.1; NC_012673.1.
DR   AlphaFoldDB; C4L115; -.
DR   STRING; 360911.EAT1b_2055; -.
DR   KEGG; eat:EAT1b_2055; -.
DR   eggNOG; COG0406; Bacteria.
DR   HOGENOM; CLU_033323_8_4_9; -.
DR   OrthoDB; 9782128at2; -.
DR   Proteomes; UP000000716; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; PTHR46517; FRUCTOSE-2,6-BISPHOSPHATASE TIGAR; 1.
DR   PANTHER; PTHR46517:SF1; FRUCTOSE-2,6-BISPHOSPHATASE TIGAR; 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   Cytoplasm {ECO:0000256|ARBA:ARBA00022490}.
FT   ACT_SITE        9
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         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   199 AA;  22152 MW;  6F1DD91E2AF4903D CRC64;
     MTELCLVRHG QTDWNRLEII QGREDNPLNA LGRQQAEESA TFLSQEKWDV IVSSPLSRAV
     HTAQAIATAC GIEHKAILLD ERFIEREFGA ASGQPVKGIY EAVQADDQNQ IPGLETEDEM
     RTRVLEGMNH LVDTYSGKRI IVVCHSHAIK AALSAIDGAY TFRHAMRNAC SNYITHQQGQ
     FEVKAVNVAD HITDPTIMK
//
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