ID   COMB_CLOAB              Reviewed;         235 AA.
AC   Q97E82;
DT   05-DEC-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 111.
DE   RecName: Full=Probable 2-phosphosulfolactate phosphatase;
DE            EC=3.1.3.71;
GN   Name=comB; OrderedLocusNames=CA_C3233;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK81168.1; -; Genomic_DNA.
DR   PIR; E97297; E97297.
DR   RefSeq; NP_349828.1; NC_003030.1.
DR   RefSeq; WP_010966508.1; NC_003030.1.
DR   PDB; 1VR0; X-ray; 2.49 A; A/B/C=1-235.
DR   PDBsum; 1VR0; -.
DR   AlphaFoldDB; Q97E82; -.
DR   SMR; Q97E82; -.
DR   STRING; 272562.CA_C3233; -.
DR   DrugBank; DB02334; (R)-2-Hydroxy-3-Sulfopropanoic Acid.
DR   EnsemblBacteria; AAK81168; AAK81168; CA_C3233.
DR   GeneID; 44999730; -.
DR   KEGG; cac:CA_C3233; -.
DR   PATRIC; fig|272562.8.peg.3411; -.
DR   eggNOG; COG2045; Bacteria.
DR   HOGENOM; CLU_070028_0_0_9; -.
DR   OMA; RLFMSTT; -.
DR   OrthoDB; 1617556at2; -.
DR   BRENDA; 3.1.3.71; 1452.
DR   EvolutionaryTrace; Q97E82; -.
DR   Proteomes; UP000000814; 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   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..235
FT                   /note="Probable 2-phosphosulfolactate phosphatase"
FT                   /id="PRO_0000081465"
FT   STRAND          1..6
FT                   /evidence="ECO:0007829|PDB:1VR0"
FT   HELIX           9..11
FT                   /evidence="ECO:0007829|PDB:1VR0"
FT   HELIX           14..16
FT                   /evidence="ECO:0007829|PDB:1VR0"
FT   TURN            17..19
FT                   /evidence="ECO:0007829|PDB:1VR0"
FT   STRAND          20..25
FT                   /evidence="ECO:0007829|PDB:1VR0"
FT   TURN            27..29
FT                   /evidence="ECO:0007829|PDB:1VR0"
FT   HELIX           30..39
FT                   /evidence="ECO:0007829|PDB:1VR0"
FT   STRAND          44..47
FT                   /evidence="ECO:0007829|PDB:1VR0"
FT   HELIX           51..61
FT                   /evidence="ECO:0007829|PDB:1VR0"
FT   HELIX           62..64
FT                   /evidence="ECO:0007829|PDB:1VR0"
FT   STRAND          65..69
FT                   /evidence="ECO:0007829|PDB:1VR0"
FT   HELIX           85..87
FT                   /evidence="ECO:0007829|PDB:1VR0"
FT   HELIX           90..93
FT                   /evidence="ECO:0007829|PDB:1VR0"
FT   STRAND          97..101
FT                   /evidence="ECO:0007829|PDB:1VR0"
FT   HELIX           105..111
FT                   /evidence="ECO:0007829|PDB:1VR0"
FT   TURN            112..114
FT                   /evidence="ECO:0007829|PDB:1VR0"
FT   STRAND          115..121
FT                   /evidence="ECO:0007829|PDB:1VR0"
FT   HELIX           126..136
FT                   /evidence="ECO:0007829|PDB:1VR0"
FT   STRAND          140..144
FT                   /evidence="ECO:0007829|PDB:1VR0"
FT   HELIX           153..169
FT                   /evidence="ECO:0007829|PDB:1VR0"
FT   STRAND          173..175
FT                   /evidence="ECO:0007829|PDB:1VR0"
FT   HELIX           177..187
FT                   /evidence="ECO:0007829|PDB:1VR0"
FT   HELIX           193..196
FT                   /evidence="ECO:0007829|PDB:1VR0"
FT   HELIX           200..207
FT                   /evidence="ECO:0007829|PDB:1VR0"
FT   HELIX           211..217
FT                   /evidence="ECO:0007829|PDB:1VR0"
FT   STRAND          228..230
FT                   /evidence="ECO:0007829|PDB:1VR0"
FT   STRAND          233..235
FT                   /evidence="ECO:0007829|PDB:1VR0"
SQ   SEQUENCE   235 AA;  26144 MW;  A8BFB7DF07161EBD CRC64;
     MKIDLIISAD DIKEEKVKNK TAVVIDMLRA TSVITTALNN GCKRVVPVLT VEEALKKVKE
     YGKDAILGGE RKGLKIEGFD FSNSPMEYTE DVVKGKTLIM TTTNGTRAIK GSETARDILI
     GSVLNGEAVA EKIVELNNDV VIVNAGTYGE FSIDDFICSG YIINCVMDRM KKLELTDAAT
     TAQYVYKTNE DIKGFVKYAK HYKRIMELGL KKDFEYCCKK DIVKLVPQYT NGEIL