ID Q9ADA1_STRCO Unreviewed; 228 AA.
AC Q9ADA1;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE SubName: Full=Phosphatase {ECO:0000313|EMBL:CAC36369.1};
GN OrderedLocusNames=SCO1666 {ECO:0000313|EMBL:CAC36369.1};
GN ORFNames=SCI52.08c {ECO:0000313|EMBL:CAC36369.1};
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226 {ECO:0000313|EMBL:CAC36369.1, ECO:0000313|Proteomes:UP000001973};
RN [1] {ECO:0000313|EMBL:CAC36369.1, ECO:0000313|Proteomes:UP000001973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145
RC {ECO:0000313|Proteomes:UP000001973};
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.H.,
RA Kieser T., Larke L., Murphy L., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
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DR EMBL; AL939109; CAC36369.1; -; Genomic_DNA.
DR RefSeq; NP_625941.1; NC_003888.3.
DR RefSeq; WP_003977159.1; NZ_VNID01000018.1.
DR AlphaFoldDB; Q9ADA1; -.
DR STRING; 100226.gene:17759259; -.
DR PaxDb; 100226-SCO1666; -.
DR PATRIC; fig|100226.15.peg.1683; -.
DR eggNOG; COG0406; Bacteria.
DR HOGENOM; CLU_033323_8_0_11; -.
DR InParanoid; Q9ADA1; -.
DR OrthoDB; 4120859at2; -.
DR PhylomeDB; Q9ADA1; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
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; IPR022492; Phosphomutase_MSMEG4193_put.
DR NCBIfam; TIGR03848; MSMEG_4193; 1.
DR PANTHER; PTHR48100; BROAD-SPECIFICITY PHOSPHATASE YOR283W-RELATED; 1.
DR PANTHER; PTHR48100:SF2; CONSERVED PROTEIN; 1.
DR Pfam; PF00300; His_Phos_1; 1.
DR SMART; SM00855; PGAM; 1.
DR SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001973}.
FT REGION 207..228
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 9
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-1"
FT ACT_SITE 84
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 59
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
FT BINDING 84..87
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR613078-2"
SQ SEQUENCE 228 AA; 24439 MW; 25CF888D301850F6 CRC64;
MPTLILVRHG RSTANTEGLL AGWTPGVALD ERGAAQAAAL PGRLAGLPLS EIVTSPLQRC
QETLRPLLDA RPELRAHTDE RIGECHYGDW SGRKLAELGN EPLMEVVQAH PSAAAFPGGE
SMRAMQTRAA EAVREWNARV ERDHGPDAVY LMCSHGDIIK SLVAEALGLH LDLFQRISVE
PCSVTAIRYT RLRPFLVRLG DTGDFASLAP REEPSGDEAP VGGGAGAP
//