(data stored in SCRATCH zone)

SWISSPROT: B1VRT6_STRGG

ID   B1VRT6_STRGG            Unreviewed;       253 AA.
AC   B1VRT6;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   08-MAY-2019, entry version 64.
DE   RecName: Full=2-phosphosulfolactate phosphatase {ECO:0000256|SAAS:SAAS00873693};
DE            EC=3.1.3.71 {ECO:0000256|SAAS:SAAS00873693};
GN   OrderedLocusNames=SGR_675 {ECO:0000313|EMBL:BAG17504.1};
OS   Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=455632 {ECO:0000313|EMBL:BAG17504.1, ECO:0000313|Proteomes:UP000001685};
RN   [1] {ECO:0000313|EMBL:BAG17504.1, ECO:0000313|Proteomes:UP000001685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4626 / NBRC 13350 {ECO:0000313|Proteomes:UP000001685};
RX   PubMed=18375553; DOI=10.1128/JB.00204-08;
RA   Ohnishi Y., Ishikawa J., Hara H., Suzuki H., Ikenoya M., Ikeda H.,
RA   Yamashita A., Hattori M., Horinouchi S.;
RT   "Genome sequence of the streptomycin-producing microorganism
RT   Streptomyces griseus IFO 13350.";
RL   J. Bacteriol. 190:4050-4060(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-O-phospho-3-sulfolactate + H2O = (R)-3-sulfolactate
CC         + phosphate; Xref=Rhea:RHEA:23416, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15597, ChEBI:CHEBI:43474, ChEBI:CHEBI:58738;
CC         EC=3.1.3.71; Evidence={ECO:0000256|SAAS:SAAS01115611};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00873701};
CC   -!- SIMILARITY: Belongs to the ComB family.
CC       {ECO:0000256|SAAS:SAAS00873703}.
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DR   EMBL; AP009493; BAG17504.1; -; Genomic_DNA.
DR   STRING; 455632.SGR_675; -.
DR   EnsemblBacteria; BAG17504; BAG17504; SGR_675.
DR   KEGG; sgr:SGR_675; -.
DR   eggNOG; COG2045; LUCA.
DR   HOGENOM; HOG000232676; -.
DR   KO; K05979; -.
DR   OMA; ACAQYIA; -.
DR   Proteomes; UP000001685; Chromosome.
DR   GO; GO:0050532; F:2-phosphosulfolactate phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   Gene3D; 3.90.1560.10; -; 1.
DR   InterPro; IPR005238; ComB-like.
DR   InterPro; IPR036702; ComB-like_sf.
DR   PANTHER; PTHR37311; PTHR37311; 1.
DR   Pfam; PF04029; 2-ph_phosp; 1.
DR   SUPFAM; SSF142823; SSF142823; 1.
PE   3: Inferred from homology;
DR   PRODOM; B1VRT6.
DR   SWISS-2DPAGE; B1VRT6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001685};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00873692};
KW   Magnesium {ECO:0000256|SAAS:SAAS00873702}.
SQ   SEQUENCE   253 AA;  26080 MW;  A60154A13CC87592 CRC64;
     MTTGQPLGDH GRMEARFLGI AELAETPSVA VVVDVMRAFT VAAWAFGRGA EKIVLAESPD
     DVLALKAGNP GWVALKDGPP APGFDAVNSP GLLRSLDLRG RTVVQKTTAG TVGALAVKEA
     SLVLCAGFVV AGATARLLRQ QGCDAVTFVV TGEEGRAEED LACAQYIARR ADGSAGDATA
     FLRRAAGSRA AAELTEGVRL GSHPDDVALC LELDRFPFAM VAAVEEASMV LRPRAVPAPA
     PVPVPVPGDE TSP
//

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