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Database: UniProt
Entry: D9WRP1_9ACTN
LinkDB: D9WRP1_9ACTN
Original site: D9WRP1_9ACTN 
ID   D9WRP1_9ACTN            Unreviewed;       217 AA.
AC   D9WRP1;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Phosphoglycerate mutase {ECO:0000313|EMBL:EFL26161.1};
GN   ORFNames=SSOG_05875 {ECO:0000313|EMBL:EFL26161.1};
OS   Streptomyces himastatinicus ATCC 53653.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces violaceusniger group.
OX   NCBI_TaxID=457427 {ECO:0000313|EMBL:EFL26161.1, ECO:0000313|Proteomes:UP000003963};
RN   [1] {ECO:0000313|EMBL:EFL26161.1, ECO:0000313|Proteomes:UP000003963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53653 {ECO:0000313|EMBL:EFL26161.1,
RC   ECO:0000313|Proteomes:UP000003963};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA   Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces hygroscopicus strain ATCC 53653.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; GG657754; EFL26161.1; -; Genomic_DNA.
DR   AlphaFoldDB; D9WRP1; -.
DR   STRING; 457427.SSOG_05875; -.
DR   HOGENOM; CLU_033323_9_5_11; -.
DR   OrthoDB; 9781415at2; -.
DR   Proteomes; UP000003963; 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:SF68; GLUCOSYL-3-PHOSPHOGLYCERATE PHOSPHATASE; 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        17
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        90
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         16..23
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         66
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ   SEQUENCE   217 AA;  23508 MW;  AB12A9D35F73B9DC CRC64;
     MNGTMSGRGR RIVLWRHGQT AWNIERRFQG SLDIELTDTG VAQAHRAARL LAGLRPDAII
     ASDLKRVMAT AAELATVTGL TVDHYAGLRE TYAGDWQGLT HEEIIERFGE QYAAWKRGEP
     VRRGGGELES EVADRAAPVV LEATEKLPDG GTLVVVSHGG TIRTTIGRLL GLEPHTWEAL
     GGLSNCCWSV LGEGARGWRL LEHNAGSLPE PVLGDDD
//
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