ID   B2RGN5_PORG3            Unreviewed;       256 AA.
AC   B2RGN5;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   10-JUN-2026, entry version 84.
DE   RecName: Full=Probable 2-phosphosulfolactate phosphatase {ECO:0000256|ARBA:ARBA00021948};
DE            EC=3.1.3.71 {ECO:0000256|ARBA:ARBA00012953};
GN   OrderedLocusNames=PGN_0011 {ECO:0000313|EMBL:BAG32530.1};
OS   Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM
OS   12257 / NCTC 11834 / 2561).
OC   Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales;
OC   Porphyromonadaceae; Porphyromonas.
OX   NCBI_TaxID=431947 {ECO:0000313|EMBL:BAG32530.1, ECO:0000313|Proteomes:UP000008842};
RN   [1] {ECO:0000313|EMBL:BAG32530.1, ECO:0000313|Proteomes:UP000008842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 /
RC   2561 {ECO:0000313|Proteomes:UP000008842};
RX   PubMed=18524787; DOI=10.1093/dnares/dsn013;
RA   Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H.,
RA   Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T.,
RA   Nakayama K.;
RT   "Determination of the genome sequence of Porphyromonas gingivalis strain
RT   ATCC 33277 and genomic comparison with strain W83 revealed extensive genome
RT   rearrangements in P. gingivalis.";
RL   DNA Res. 15:215-225(2008).
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:0000256|ARBA:ARBA00033711};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the ComB family.
CC       {ECO:0000256|ARBA:ARBA00009997}.
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DR   EMBL; AP009380; BAG32530.1; -; Genomic_DNA.
DR   RefSeq; WP_012457168.1; NC_010729.1.
DR   AlphaFoldDB; B2RGN5; -.
DR   GeneID; 29255272; -.
DR   KEGG; pgn:PGN_0011; -.
DR   eggNOG; COG2045; Bacteria.
DR   HOGENOM; CLU_070028_0_1_10; -.
DR   OrthoDB; 4913at2; -.
DR   BioCyc; PGIN431947:G1G2V-12-MONOMER; -.
DR   Proteomes; UP000008842; Chromosome.
DR   GO; GO:0050532; F:2-phosphosulfolactate phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0050545; F:sulfopyruvate decarboxylase activity; IEA:TreeGrafter.
DR   Gene3D; 3.90.1560.10; ComB-like; 1.
DR   InterPro; IPR005238; ComB-like.
DR   InterPro; IPR036702; ComB-like_sf.
DR   PANTHER; PTHR37311; 2-PHOSPHOSULFOLACTATE PHOSPHATASE-RELATED; 1.
DR   PANTHER; PTHR37311:SF1; 2-PHOSPHOSULFOLACTATE PHOSPHATASE-RELATED; 1.
DR   Pfam; PF04029; 2-ph_phosp; 1.
DR   SUPFAM; SSF142823; ComB-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008842}.
SQ   SEQUENCE   256 AA;  28017 MW;  DF3B5F6E032BBA16 CRC64;
     MLQISLCPSP VLYPYYKTEQ EEYTVVIVDI FRAGTTITTA LMNGAVGIIP IATVEEAEIY
     AGNGFLVGGE RGTKRLPFAR FGNAPEEYTR QAVEGKQLVL STTNGTRAAD IAAGALHVII
     GAFINLEAVA RYCIAKQKPV MVLASGWQNR MSTEDCLFAG ALAATIVRLG EEVICEDGAS
     VFQELWGNYN THEKLTAYLN GRDHYERLRA NKLERSVPYC TSLNLTEIVP ELTFKISAAS
     TDCPANRLFL PVTPPF
//