ID   PSLS_XANP2              Reviewed;         303 AA.
AC   Q9AF21; A7IQF4;
DT   21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 2.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Phosphosulfolactate synthase;
DE            EC=4.4.1.19;
DE   AltName: Full=(2R)-phospho-3-sulfolactate synthase;
DE            Short=PSL synthase;
GN   Name=xecG; OrderedLocusNames=Xaut_5052;
OS   Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2).
OG   Plasmid pXAUT01, and Plasmid pEK1.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Xanthobacteraceae; Xanthobacter.
OX   NCBI_TaxID=78245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pEK1;
RX   PubMed=11244054; DOI=10.1128/jb.183.7.2172-2177.2001;
RA   Krum J.G., Ensign S.A.;
RT   "Evidence that a linear megaplasmid encodes enzymes of aliphatic alkene and
RT   epoxide metabolism and coenzyme M (2-mercaptoethanesulfonate) biosynthesis
RT   in Xanthobacter strain Py2.";
RL   J. Bacteriol. 183:2172-2177(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1158 / Py2; PLASMID=pXAUT01;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA   Israni S., Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Tapia R., Brainard J., Schmutz J., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Kim E., Ensigns S.A., Richardson P.;
RT   "Complete sequence of plasmid pXAUT01 of Xanthobacter autotrophicus Py2.";
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the addition of sulfite to phosphoenolpyruvate
CC       (PEP) to yield (2R)-phospho-3-sulfolactate (PSL). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-O-phospho-3-sulfolactate = H(+) + phosphoenolpyruvate +
CC         sulfite; Xref=Rhea:RHEA:22784, ChEBI:CHEBI:15378, ChEBI:CHEBI:15597,
CC         ChEBI:CHEBI:17359, ChEBI:CHEBI:58702; EC=4.4.1.19;
CC   -!- PATHWAY: Cofactor biosynthesis; coenzyme M biosynthesis;
CC       sulfoacetaldehyde from phosphoenolpyruvate and sulfite: step 1/4.
CC   -!- MISCELLANEOUS: In Xanthobacter strain Py2 coenzyme M plays a role in
CC       epoxide carboxylation by serving as the nucleophile for epoxide ring
CC       opening and the carrier of the C3 unit that is ultimately carboxylated
CC       to acetoacetate.
CC   -!- SIMILARITY: Belongs to the phosphosulfolactate synthase family.
CC       {ECO:0000305}.
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DR   EMBL; AY024334; AAG61256.1; -; Genomic_DNA.
DR   EMBL; CP000782; ABS70250.1; -; Genomic_DNA.
DR   RefSeq; WP_011993153.1; NC_009717.1.
DR   AlphaFoldDB; Q9AF21; -.
DR   SMR; Q9AF21; -.
DR   STRING; 78245.Xaut_5052; -.
DR   EnsemblBacteria; ABS70250; ABS70250; Xaut_5052.
DR   KEGG; xau:Xaut_5052; -.
DR   eggNOG; COG1809; Bacteria.
DR   HOGENOM; CLU_062679_2_0_5; -.
DR   OrthoDB; 1319510at2; -.
DR   PhylomeDB; Q9AF21; -.
DR   BRENDA; 4.4.1.19; 1641.
DR   UniPathway; UPA00355; UER00469.
DR   Proteomes; UP000002417; Plasmid pXAUT01.
DR   GO; GO:0043817; F:phosphosulfolactate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019295; P:coenzyme M biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR003830; ComA_synth.
DR   InterPro; IPR036112; ComA_synth_sf.
DR   Pfam; PF02679; ComA; 1.
DR   SUPFAM; SSF102110; SSF102110; 1.
PE   3: Inferred from homology;
KW   Coenzyme M biosynthesis; Lyase; Plasmid; Reference proteome.
FT   CHAIN           1..303
FT                   /note="Phosphosulfolactate synthase"
FT                   /id="PRO_0000080833"
FT   REGION          273..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..303
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        1..3
FT                   /note="MSA -> M (in Ref. 1; AAG61256)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        7..8
FT                   /note="AK -> SD (in Ref. 1; AAG61256)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        21
FT                   /note="I -> L (in Ref. 1; AAG61256)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        26..27
FT                   /note="TQ -> SR (in Ref. 1; AAG61256)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        46
FT                   /note="L -> M (in Ref. 1; AAG61256)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        50
FT                   /note="D -> A (in Ref. 1; AAG61256)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        100
FT                   /note="V -> I (in Ref. 1; AAG61256)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        113..114
FT                   /note="EE -> RD (in Ref. 1; AAG61256)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        118
FT                   /note="T -> S (in Ref. 1; AAG61256)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   303 AA;  33182 MW;  843B461FC5943963 CRC64;
     MSAQARAKRP WRGVLALDAA IDRRVTQPRK RGITMVIDKG IGPAALADID AVAAPYIDHW
     KLAFGTSALM PPQVLADKLA FLRERGVLTY PGGTLLEAAV VQQHCRVFMQ RAEELGFTAV
     EISDGTIDLP RDRRRRIIDC AREAGLVVIT EVGKKDPQCQ PEAAELAEQA LDDLKWGSSF
     VIVEARESGR GIGIYDKTGE LRSSFLEEIA NLLGDKIDQL IWEAPQKEQQ AALVARFGAN
     VSLGNVAVNE VLALEALRAG LRFETLAAVA DREKASGQWD PDMPEPDEGP ATRESARQEL
     RHD