ID   CUYA_ROSNI              Reviewed;         338 AA.
AC   A3SQG3;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 61.
DE   RecName: Full=L-cysteate sulfo-lyase {ECO:0000303|PubMed:19581363};
DE            EC=4.4.1.25 {ECO:0000269|PubMed:19581363};
GN   Name=cuyA {ECO:0000303|PubMed:19581363};
GN   ORFNames=ISM_09626 {ECO:0000312|EMBL:EAP75372.1};
OS   Roseovarius nubinhibens (strain ATCC BAA-591 / DSM 15170 / ISM).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseovarius.
OX   NCBI_TaxID=89187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-591 / DSM 15170 / ISM;
RA   Moran M.A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA   Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL   Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND INDUCTION.
RC   STRAIN=ATCC BAA-591 / DSM 15170 / ISM;
RX   PubMed=19581363; DOI=10.1128/jb.00569-09;
RA   Denger K., Mayer J., Buhmann M., Weinitschke S., Smits T.H., Cook A.M.;
RT   "Bifurcated degradative pathway of 3-sulfolactate in Roseovarius
RT   nubinhibens ISM via sulfoacetaldehyde acetyltransferase and (S)-cysteate
RT   sulfolyase.";
RL   J. Bacteriol. 191:5648-5656(2009).
CC   -!- FUNCTION: Catalyzes the desulfonation and deamination of L-cysteate,
CC       yielding pyruvate, sulphite and ammonium. Involved in sulfolactate
CC       degradation. {ECO:0000269|PubMed:19581363}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-cysteate = H(+) + NH4(+) + pyruvate + sulfite;
CC         Xref=Rhea:RHEA:13441, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:58090; EC=4.4.1.25;
CC         Evidence={ECO:0000269|PubMed:19581363};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13442;
CC         Evidence={ECO:0000269|PubMed:19581363};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:Q5LL69};
CC   -!- INDUCTION: Induced during growth on sulfolactate or cysteate.
CC       {ECO:0000269|PubMed:19581363}.
CC   -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase
CC       family. {ECO:0000305}.
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DR   EMBL; AALY01000003; EAP75372.1; -; Genomic_DNA.
DR   RefSeq; WP_009813935.1; NZ_CH724156.1.
DR   AlphaFoldDB; A3SQG3; -.
DR   SMR; A3SQG3; -.
DR   STRING; 89187.ISM_09626; -.
DR   eggNOG; COG2515; Bacteria.
DR   HOGENOM; CLU_048897_1_0_5; -.
DR   OrthoDB; 1714795at2; -.
DR   BioCyc; MetaCyc:MON-15910; -.
DR   Proteomes; UP000005954; Unassembled WGS sequence.
DR   GO; GO:0034011; F:L-cysteate sulfo-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR027278; ACCD_DCysDesulf.
DR   InterPro; IPR005966; D-Cys_desShydrase.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   PANTHER; PTHR43780; PTHR43780; 1.
DR   Pfam; PF00291; PALP; 1.
DR   PIRSF; PIRSF006278; ACCD_DCysDesulf; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR01275; ACC_deam_rel; 1.
PE   1: Evidence at protein level;
KW   Lyase; Pyridoxal phosphate; Reference proteome.
FT   CHAIN           1..338
FT                   /note="L-cysteate sulfo-lyase"
FT                   /id="PRO_0000446000"
FT   MOD_RES         49
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q7M523"
SQ   SEQUENCE   338 AA;  36103 MW;  4DE01C1D22FDCB0E CRC64;
     MHLARFPRRF IAHLPTPLER LDRLSAELGG PEIWIKRDDC TGLSTGGNKT RKLEFLMAEA
     ELQGAEIVMT QGATQSNHAR QTAAFAAKLG MKCHILLEDR TGSNEANYNH NGNVLLDHLH
     GATTEKRPGG GDMNAEMEKL ADEWRADGKK VYTIPGGGSN PTGALGYVNC AFELLAQAND
     GGLKIDHIVH ATGSAGTQAG LITGLKAMNA QIPLLGIGVR APKPKQEENV YNLACATAEK
     LGCPGVVARE DVVANTDYVG QGYGIPTESG MEAIKMFAEL ESILLDPVYS AKGAAGFIDL
     IRKGHFKKGE RVVFLHTGGA AALFGYDGAF DFSSRWVG