ID   CUYA_RUEPO              Reviewed;         339 AA.
AC   Q5LL69;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=L-cysteate sulfo-lyase;
DE            EC=4.4.1.25 {ECO:0000269|PubMed:16302849};
GN   Name=cuyA; OrderedLocusNames=SPOA0158;
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS   pomeroyi).
OG   Plasmid megaplasmid Spo.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA   Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT   environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
RN   [3]
RP   PROTEIN SEQUENCE OF 1-7, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP   BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY, GENE NAME, SUBUNIT,
RP   AND INDUCTION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=16302849; DOI=10.1042/bj20051311;
RA   Denger K., Smits T.H., Cook A.M.;
RT   "L-cysteate sulpho-lyase, a widespread pyridoxal 5'-phosphate-coupled
RT   desulphonative enzyme purified from Silicibacter pomeroyi DSS-3(T).";
RL   Biochem. J. 394:657-664(2006).
CC   -!- FUNCTION: Catalyzes the desulfonation and deamination of L-cysteate,
CC       yielding pyruvate, sulphite and ammonium. Is involved in a L-cysteate
CC       degradation pathway that allows Silicibacter pomeroyi to grow on L-
CC       cysteate as the sole source of carbon and energy. To a lesser extent,
CC       can also act on D-cysteine in vitro, leading to the production of
CC       pyruvate, sulfide and ammonium. L-cysteine, L-cysteine sulfinate, and
CC       1-aminocyclopropane-1-carboxylate (ACC) are not substrates for the
CC       enzyme. {ECO:0000269|PubMed:16302849}.
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:16302849};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:16302849};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=11.7 mM for L-cysteate {ECO:0000269|PubMed:16302849};
CC       pH dependence:
CC         Optimum pH is 8.8-9.0. {ECO:0000269|PubMed:16302849};
CC   -!- SUBUNIT: Homomultimer, maybe a homotrimer.
CC       {ECO:0000269|PubMed:16302849}.
CC   -!- INDUCTION: Expressed in cells grown on L-cysteate, but not on acetate
CC       or taurine. Cotranscribed with cuyZ, with which it is likely to form an
CC       operon. {ECO:0000269|PubMed:16302849}.
CC   -!- SIMILARITY: Belongs to the ACC deaminase/D-cysteine desulfhydrase
CC       family. {ECO:0000305}.
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DR   EMBL; CP000032; AAV97294.1; -; Genomic_DNA.
DR   RefSeq; WP_011241939.1; NC_006569.1.
DR   AlphaFoldDB; Q5LL69; -.
DR   SMR; Q5LL69; -.
DR   STRING; 246200.SPOA0158; -.
DR   EnsemblBacteria; AAV97294; AAV97294; SPOA0158.
DR   KEGG; sil:SPOA0158; -.
DR   eggNOG; COG2515; Bacteria.
DR   HOGENOM; CLU_048897_1_0_5; -.
DR   OMA; LVQEKWV; -.
DR   OrthoDB; 1714795at2; -.
DR   BioCyc; MetaCyc:MON-15876; -.
DR   Proteomes; UP000001023; Plasmid megaplasmid Spo.
DR   GO; GO:0034011; F:L-cysteate sulfo-lyase activity; IDA:UniProtKB.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR   GO; GO:0000098; P:sulfur amino acid catabolic process; IDA:UniProtKB.
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   Direct protein sequencing; Lyase; Plasmid; Pyridoxal phosphate;
KW   Reference proteome.
FT   CHAIN           1..339
FT                   /note="L-cysteate sulfo-lyase"
FT                   /id="PRO_0000418826"
FT   MOD_RES         49
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   339 AA;  36533 MW;  316A3658EB4BFFF0 CRC64;
     MHLARYPRRF IAHLPTPLER LDRLTAELGG PEIWIKRDDC TGLSTGGNKT RKLEFLMAEA
     ELQGADMVMT QGATQSNHAR QTAAFAAKLG MDCHILLEDR TGSNNANYNN NGNVLLDHLH
     GATTEKRPGS GLDMNAEMEK VAEKFRADGR KVYTIPGGGS NPTGALGYVN CAFEMLNQFN
     ERGLKVDHIV HATGSAGTQA GLITGLQAMN AQIPLLGIGV RAPKPKQEEN VYNLACATAE
     KLGCPGVVAR EDVVANTDYV GEGYGIPTES GLEAIRMFAE LEAILLDPVY SAKGAAGFID
     LIRKGHFKKG ERVVFLHTGG AVALFGYDNA FDYSGRWVA