ID   SUYB_PARPN              Reviewed;         393 AA.
AC   Q58Y43;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 31.
DE   RecName: Full=(2R)-sulfolactate sulfo-lyase subunit beta;
DE            EC=4.4.1.24 {ECO:0000269|PubMed:15758220};
DE   AltName: Full=Sulfolactate sulfo-lyase B;
DE   Flags: Precursor;
GN   Name=suyB;
OS   Paracoccus pantotrophus (Thiosphaera pantotropha).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=82367;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 3-22; 117-128 AND
RP   240-259, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=DSM 12449 / NKNCYSA;
RX   PubMed=15758220; DOI=10.1099/mic.0.27548-0;
RA   Rein U., Gueta R., Denger K., Ruff J., Hollemeyer K., Cook A.M.;
RT   "Dissimilation of cysteate via 3-sulfolactate sulfo-lyase and a sulfate
RT   exporter in Paracoccus pantotrophus NKNCYSA.";
RL   Microbiology 151:737-747(2005).
CC   -!- FUNCTION: Together with SuyA, desulfonates sulfolactate to pyruvate and
CC       sulfite. {ECO:0000269|PubMed:15758220}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-3-sulfolactate = H(+) + pyruvate + sulfite;
CC         Xref=Rhea:RHEA:21428, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17359, ChEBI:CHEBI:58738; EC=4.4.1.24;
CC         Evidence={ECO:0000269|PubMed:15758220};
CC   -!- SUBUNIT: (2R)-sulfolactate sulfo-lyase is composed of a SuyA and a SuyB
CC       subunit. {ECO:0000305|PubMed:15758220}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:15758220}.
CC   -!- SIMILARITY: Belongs to the UxaA family. {ECO:0000305}.
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DR   EMBL; AY704413; AAW23059.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q58Y43; -.
DR   SMR; Q58Y43; -.
DR   KEGG; ag:AAW23059; -.
DR   BioCyc; MetaCyc:MON-15874; -.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0034010; F:sulfolactate sulfo-lyase activity; IDA:UniProtKB.
DR   InterPro; IPR007392; Gal/Altron_deHydtase_C.
DR   Pfam; PF04295; GD_AH_C; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Lyase.
FT   PROPEP          1..2
FT                   /evidence="ECO:0000269|PubMed:15758220"
FT                   /id="PRO_0000418745"
FT   CHAIN           3..393
FT                   /note="(2R)-sulfolactate sulfo-lyase subunit beta"
FT                   /id="PRO_0000418746"
FT   CONFLICT        13
FT                   /note="W -> A (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        17..19
FT                   /note="NGR -> EGG (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   393 AA;  42452 MW;  0F5E34B6FAA91905 CRC64;
     MALDFSNATV KAWRRENGRV GVRNHVLILP VDDISNAACE AVANNVKGTL AIPHAYGRLQ
     FGEDLELHFR TIIGTGANPN VAAVVVIGIE PEWTQVIVDG IAKTGKPVTG FSIEQKGDFE
     TIRQAGWKAK EYVHWASELQ KEDCPISDLW ISTKCGESDT TTGLSSCPTV GNMYDKLLPQ
     GIYGCFGETS EITGAEHICE KRAANPETAR KFKEIWQAYS DDVIFAHQTD DLSDSQPTKG
     NILGGLTTIE EKALGNLEKI GRTSTYIDAM GPAETPSKGP GLYFMDSSSA AAECVTLMAA
     GGYVIHTFPT GQGNVVGNPI VPVIKISGNP RTLRTMSEHI DVDVTGVLTR EMTIDQAGDA
     LIEMIIRTAN GRMTAAEALG HREFSMTKLY RSA