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Database: UniProt
Entry: A0A069K7M4_9ACTN
LinkDB: A0A069K7M4_9ACTN
Original site: A0A069K7M4_9ACTN 
ID   A0A069K7M4_9ACTN        Unreviewed;       219 AA.
AC   A0A069K7M4;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Phosphoglycerate mutase {ECO:0000313|EMBL:KDQ69912.1};
GN   ORFNames=DT87_22775 {ECO:0000313|EMBL:KDQ69912.1};
OS   Streptomyces sp. NTK 937.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1487711 {ECO:0000313|EMBL:KDQ69912.1, ECO:0000313|Proteomes:UP000027475};
RN   [1] {ECO:0000313|EMBL:KDQ69912.1, ECO:0000313|Proteomes:UP000027475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NTK 937 {ECO:0000313|EMBL:KDQ69912.1,
RC   ECO:0000313|Proteomes:UP000027475};
RA   Olano C., Cano-Prieto C., Losada A., Mendez C., Salas J.A.;
RT   "Draft genome sequence of marine actinomycete Streptomyces sp. NTK 937,
RT   producer of the benzoxazol antibiotic caboxamycin.";
RL   Submitted (APR-2014) 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:KDQ69912.1}.
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DR   EMBL; JJOB01000001; KDQ69912.1; -; Genomic_DNA.
DR   RefSeq; WP_028441191.1; NZ_JJOB01000001.1.
DR   AlphaFoldDB; A0A069K7M4; -.
DR   OrthoDB; 5449373at2; -.
DR   Proteomes; UP000027475; 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; PTHR46192; BROAD-RANGE ACID PHOSPHATASE DET1; 1.
DR   PANTHER; PTHR46192:SF11; BROAD-RANGE ACID PHOSPHATASE DET1; 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        12
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   ACT_SITE        92
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT   BINDING         11..18
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT   BINDING         67
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ   SEQUENCE   219 AA;  25812 MW;  9ED1B1814F567E53 CRC64;
     MARPQRIVLV RHGESVGNAD DSVYEREPDH ALRLTARGLR QARETGAELR EVFGQERISV
     YVSPYRRTHE TLRSFALAPE RVRVREEPRL REQDWGNWQD RDDVRLQKTY RDAYGHFFYR
     FPQGESGADV YDRVDAFLES LHRSFESPDH PQNVLLVTHG LTMRLFCMRW FHWSVAEFES
     LSNPGNGETR MLLLGADGRY TLDRPFRQWR TPEPYGRTG
//
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