COMB_THET8
ID COMB_THET8 Reviewed; 237 AA.
AC Q5SID6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Probable 2-phosphosulfolactate phosphatase {ECO:0000255|HAMAP-Rule:MF_00490};
DE EC=3.1.3.71 {ECO:0000255|HAMAP-Rule:MF_00490};
GN Name=comB {ECO:0000255|HAMAP-Rule:MF_00490}; OrderedLocusNames=TTHA1438;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_00490};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00490};
CC -!- SIMILARITY: Belongs to the ComB family. {ECO:0000255|HAMAP-
CC Rule:MF_00490}.
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DR EMBL; AP008226; BAD71261.1; -; Genomic_DNA.
DR RefSeq; WP_008632942.1; NC_006461.1.
DR RefSeq; YP_144704.1; NC_006461.1.
DR PDB; 2Z0J; X-ray; 1.50 A; A/B/C/D/E/F/G/H=1-237.
DR PDBsum; 2Z0J; -.
DR AlphaFoldDB; Q5SID6; -.
DR SMR; Q5SID6; -.
DR STRING; 300852.55772820; -.
DR EnsemblBacteria; BAD71261; BAD71261; BAD71261.
DR GeneID; 3168156; -.
DR KEGG; ttj:TTHA1438; -.
DR PATRIC; fig|300852.9.peg.1412; -.
DR eggNOG; COG2045; Bacteria.
DR HOGENOM; CLU_070028_0_0_0; -.
DR OMA; RLFMSTT; -.
DR EvolutionaryTrace; Q5SID6; -.
DR Proteomes; UP000000532; 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..237
FT /note="Probable 2-phosphosulfolactate phosphatase"
FT /id="PRO_1000014477"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:2Z0J"
FT STRAND 16..22
FT /evidence="ECO:0007829|PDB:2Z0J"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:2Z0J"
FT HELIX 27..36
FT /evidence="ECO:0007829|PDB:2Z0J"
FT STRAND 40..44
FT /evidence="ECO:0007829|PDB:2Z0J"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:2Z0J"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:2Z0J"
FT HELIX 79..84
FT /evidence="ECO:0007829|PDB:2Z0J"
FT STRAND 90..95
FT /evidence="ECO:0007829|PDB:2Z0J"
FT HELIX 99..107
FT /evidence="ECO:0007829|PDB:2Z0J"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:2Z0J"
FT HELIX 121..131
FT /evidence="ECO:0007829|PDB:2Z0J"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:2Z0J"
FT HELIX 149..164
FT /evidence="ECO:0007829|PDB:2Z0J"
FT HELIX 172..183
FT /evidence="ECO:0007829|PDB:2Z0J"
FT HELIX 187..192
FT /evidence="ECO:0007829|PDB:2Z0J"
FT HELIX 195..202
FT /evidence="ECO:0007829|PDB:2Z0J"
FT HELIX 208..212
FT /evidence="ECO:0007829|PDB:2Z0J"
FT STRAND 222..228
FT /evidence="ECO:0007829|PDB:2Z0J"
FT STRAND 231..236
FT /evidence="ECO:0007829|PDB:2Z0J"
SQ SEQUENCE 237 AA; 24738 MW; 94DE9D1855C9A6BE CRC64;
MRLRVDVIPG EHLAYPDVVL VVDVIRATTT AAAFLEAGAE ALYWTPSLES ALAFKDEDVV
LAGETGGLKP PRFDLGNSPR EALSAQVAGR VVVMSTTNGT KAAHAAARTA KHVLLASLYN
AHAAARLARE LATEEVAILC AGKEGRAGLD DLYTAGVLAE YLGFLGEVEP EDGARVALAV
KRAYPDPLEA LSLSAAALAL KQVGLEADVP FCAQVAKSAA VPVLRGRVGE ALIFKRA
