COMB_THEMA
ID COMB_THEMA Reviewed; 227 AA.
AC Q9WZQ4;
DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Probable 2-phosphosulfolactate phosphatase;
DE EC=3.1.3.71;
GN Name=comB; OrderedLocusNames=TM_0797;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2R)-O-phospho-3-sulfolactate + H2O = (2R)-3-sulfolactate +
CC phosphate; Xref=Rhea:RHEA:23416, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15597, ChEBI:CHEBI:43474, ChEBI:CHEBI:58738; EC=3.1.3.71;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the ComB family. {ECO:0000305}.
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DR EMBL; AE000512; AAD35879.1; -; Genomic_DNA.
DR PIR; F72334; F72334.
DR RefSeq; NP_228606.1; NC_000853.1.
DR RefSeq; WP_004080870.1; NZ_CP011107.1.
DR PDB; 2YYV; X-ray; 1.65 A; A/B=1-227.
DR PDB; 2YZO; X-ray; 1.85 A; A/B=1-227.
DR PDBsum; 2YYV; -.
DR PDBsum; 2YZO; -.
DR AlphaFoldDB; Q9WZQ4; -.
DR SMR; Q9WZQ4; -.
DR STRING; 243274.THEMA_00665; -.
DR EnsemblBacteria; AAD35879; AAD35879; TM_0797.
DR KEGG; tma:TM0797; -.
DR eggNOG; COG2045; Bacteria.
DR InParanoid; Q9WZQ4; -.
DR OMA; RLFMSTT; -.
DR OrthoDB; 1617556at2; -.
DR EvolutionaryTrace; Q9WZQ4; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0050532; F:2-phosphosulfolactate phosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050545; F:sulfopyruvate decarboxylase activity; IBA:GO_Central.
DR Gene3D; 3.90.1560.10; -; 1.
DR HAMAP; MF_00490; ComB; 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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Magnesium; Reference proteome.
FT CHAIN 1..227
FT /note="Probable 2-phosphosulfolactate phosphatase"
FT /id="PRO_0000081477"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:2YYV"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:2YYV"
FT TURN 22..24
FT /evidence="ECO:0007829|PDB:2YYV"
FT HELIX 25..34
FT /evidence="ECO:0007829|PDB:2YYV"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:2YYV"
FT HELIX 46..51
FT /evidence="ECO:0007829|PDB:2YYV"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:2YYV"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:2YYV"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:2YYV"
FT STRAND 89..93
FT /evidence="ECO:0007829|PDB:2YYV"
FT HELIX 97..103
FT /evidence="ECO:0007829|PDB:2YYV"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:2YYV"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:2YYV"
FT HELIX 117..124
FT /evidence="ECO:0007829|PDB:2YYV"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:2YYV"
FT HELIX 143..156
FT /evidence="ECO:0007829|PDB:2YYV"
FT HELIX 163..173
FT /evidence="ECO:0007829|PDB:2YYV"
FT HELIX 178..185
FT /evidence="ECO:0007829|PDB:2YYV"
FT HELIX 187..194
FT /evidence="ECO:0007829|PDB:2YYV"
FT HELIX 198..204
FT /evidence="ECO:0007829|PDB:2YYV"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:2YYV"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:2YYV"
SQ SEQUENCE 227 AA; 24857 MW; ED32447E6140D9F8 CRC64;
MVDVVMAPCS PVECRTAVVI DVLRATSTIV TALSNGASGV IPVKTIEEAL EKKKEGVLIC
GERNAQKPKG FNLGNSPLEY RKEKISGKTI VLTTTNGTQV IEKIRSEEII AASFLNLSAV
VEYLKSKEDI LLVCAGTNGR FSLEDFLLAG AIVKRLKRND LGDGAHAAER YFESVENTRE
EIKKHSSHAK RLISLGFEND IEFCTTEDLF KTVPALVNGV FILKEFP