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Database: UniProt
Entry: A0A0R0C4X5_9GAMM
LinkDB: A0A0R0C4X5_9GAMM
Original site: A0A0R0C4X5_9GAMM 
ID   A0A0R0C4X5_9GAMM        Unreviewed;       214 AA.
AC   A0A0R0C4X5;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Phosphoglycerate mutase {ECO:0000313|EMBL:KRG64549.1};
GN   ORFNames=ABB26_08005 {ECO:0000313|EMBL:KRG64549.1};
OS   Stenotrophomonas humi.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=405444 {ECO:0000313|EMBL:KRG64549.1, ECO:0000313|Proteomes:UP000050864};
RN   [1] {ECO:0000313|EMBL:KRG64549.1, ECO:0000313|Proteomes:UP000050864}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18929 {ECO:0000313|EMBL:KRG64549.1,
RC   ECO:0000313|Proteomes:UP000050864};
RA   Patil P.P., Midha S., Patil P.B.;
RT   "Genome sequencing and analysis of members of genus Stenotrophomonas.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KRG64549.1}.
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DR   EMBL; LDJI01000013; KRG64549.1; -; Genomic_DNA.
DR   RefSeq; WP_057633146.1; NZ_LDJI01000013.1.
DR   AlphaFoldDB; A0A0R0C4X5; -.
DR   STRING; 405444.ABB26_08005; -.
DR   PATRIC; fig|405444.3.peg.608; -.
DR   OrthoDB; 9781415at2; -.
DR   Proteomes; UP000050864; Unassembled WGS sequence.
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;
FT   ACT_SITE        8
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         7..14
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         57
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ   SEQUENCE   214 AA;  23564 MW;  EB676993E7ABE15F CRC64;
     MRILLARHGE TPWNAEGRYQ GQIDIPLSPV GEAQAKALGE RLADVQITRA VASPLSRAQS
     TAKAALGSNR ESMLLTEPDL QEIAHGEWEG LLASEINDKD PARLRAWREE PDTVLMPGGE
     SLRQVLDRSW RGLAKAAEGL GEEDTLLVVA HDAVNRVILC KILGLPISKL WTFRQAPTTL
     NLLEGPDVEH LEVVRLNDCA HHTPFFGEAK HRAL
//
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