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Database: UniProt
Entry: B1Y8E3_LEPCP
LinkDB: B1Y8E3_LEPCP
Original site: B1Y8E3_LEPCP 
ID   B1Y8E3_LEPCP            Unreviewed;       240 AA.
AC   B1Y8E3;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   SubName: Full=Phosphoglycerate mutase {ECO:0000313|EMBL:ACB36209.1};
GN   OrderedLocusNames=Lcho_3955 {ECO:0000313|EMBL:ACB36209.1};
OS   Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix
OS   discophora (strain SP-6)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Sphaerotilaceae; Leptothrix.
OX   NCBI_TaxID=395495 {ECO:0000313|EMBL:ACB36209.1, ECO:0000313|Proteomes:UP000001693};
RN   [1] {ECO:0000313|EMBL:ACB36209.1, ECO:0000313|Proteomes:UP000001693}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51168 / LMG 8142 / SP-6
RC   {ECO:0000313|Proteomes:UP000001693};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Lykidis A., Emerson D., Richardson P.;
RT   "Complete sequence of Leptothrix cholodnii SP-6.";
RL   Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP001013; ACB36209.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1Y8E3; -.
DR   STRING; 395495.Lcho_3955; -.
DR   KEGG; lch:Lcho_3955; -.
DR   eggNOG; COG0406; Bacteria.
DR   HOGENOM; CLU_033323_9_5_4; -.
DR   OrthoDB; 9783269at2; -.
DR   Proteomes; UP000001693; Chromosome.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
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   PANTHER; PTHR48100:SF34; BROAD-SPECIFICITY PHOSPHATASE YOR283W; 1.
DR   PANTHER; PTHR48100; BROAD-SPECIFICITY PHOSPHATASE YOR283W-RELATED; 1.
DR   Pfam; PF00300; His_Phos_1; 1.
DR   SMART; SM00855; PGAM; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE   4: Predicted;
KW   Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001693}.
FT   ACT_SITE        14
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        87
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         13..20
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         63
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         114..115
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ   SEQUENCE   240 AA;  25629 MW;  3CFA95189869C24F CRC64;
     MPYSDVTRVL AIRHGETAWN RDARIQGQID IPLNDAGLAQ ARSLAQALAE DALAAVYSSD
     LLRAHQTAEA VAAAQGLVVQ ADVGLRERHF GDFEGRTYHE IDADLPELAQ RWRRRDPDFG
     PPGGEVLKAF FARSVSAIER IAASHRGQTI AVVCHGGVLD CLYRAATRLS LNAPRTWTVA
     NASINRLLFT DDGCTLVGWG DTQHLDGSDH APLDSRSAHA GHTAIAAAPP LDEGSDGGAA
//
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