ID   Q9PFQ4_XYLFA            Unreviewed;       456 AA.
AC   Q9PFQ4;
DT   01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2000, sequence version 1.
DT   27-MAR-2024, entry version 125.
DE   RecName: Full=cysteine synthase {ECO:0000256|ARBA:ARBA00012681};
DE            EC=2.5.1.47 {ECO:0000256|ARBA:ARBA00012681};
GN   OrderedLocusNames=XF_0603 {ECO:0000313|EMBL:AAF83413.1};
OS   Xylella fastidiosa (strain 9a5c).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=160492 {ECO:0000313|EMBL:AAF83413.1, ECO:0000313|Proteomes:UP000000812};
RN   [1] {ECO:0000313|EMBL:AAF83413.1, ECO:0000313|Proteomes:UP000000812}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9a5c {ECO:0000313|EMBL:AAF83413.1,
RC   ECO:0000313|Proteomes:UP000000812};
RX   PubMed=10910347; DOI=10.1038/35018003;
RA   Simpson A.J., Reinach F.C., Arruda P., Abreu F.A., Acencio M.,
RA   Alvarenga R., Alves L.M., Araya J.E., Baia G.S., Baptista C.S.,
RA   Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.,
RA   Bueno M.R., Camargo A.A., Camargo L.E., Carraro D.M., Carrer H.,
RA   Colauto N.B., Colombo C., Costa F.F., Costa M.C., Costa-Neto C.M.,
RA   Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H.,
RA   Facincani A.P., Ferreira A.J., Ferreira V.C., Ferro J.A., Fraga J.S.,
RA   Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H.,
RA   Goldman M.H., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D.,
RA   Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E.,
RA   Laigret F., Lambais M.R., Leite L.C., Lemos E.G., Lemos M.V., Lopes S.A.,
RA   Lopes C.R., Machado J.A., Machado M.A., Madeira A.M., Madeira H.M.,
RA   Marino C.L., Marques M.V., Martins E.A., Martins E.M., Matsukuma A.Y.,
RA   Menck C.F., Miracca E.C., Miyaki C.Y., Monteriro-Vitorello C.B., Moon D.H.,
RA   Nagai M.A., Nascimento A.L., Netto L.E., Nhani A.Jr., Nobrega F.G.,
RA   Nunes L.R., Oliveira M.A., de Oliveira M.C., de Oliveira R.C.,
RA   Palmieri D.A., Paris A., Peixoto B.R., Pereira G.A., Pereira H.A.Jr.,
RA   Pesquero J.B., Quaggio R.B., Roberto P.G., Rodrigues V., de M Rosa A.J.,
RA   de Rosa V.E.Jr., de Sa R.G., Santelli R.V., Sawasaki H.E., da Silva A.C.,
RA   da Silva A.M., da Silva F.R., da Silva W.A.Jr., da Silveira J.F.,
RA   Silvestri M.L., Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F.,
RA   Truffi D., Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A.,
RA   Verjovski-Almeida S., Vettore A.L., Zago M.A., Zatz M., Meidanis J.,
RA   Setubal J.C.;
RT   "The genome sequence of the plant pathogen Xylella fastidiosa.";
RL   Nature 406:151-159(2000).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hydrogen sulfide + O-acetyl-L-serine = acetate + L-cysteine;
CC         Xref=Rhea:RHEA:14829, ChEBI:CHEBI:29919, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:35235, ChEBI:CHEBI:58340; EC=2.5.1.47;
CC         Evidence={ECO:0000256|ARBA:ARBA00000298};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-cysteine biosynthesis; L-cysteine
CC       from L-serine: step 2/2. {ECO:0000256|ARBA:ARBA00004962}.
CC   -!- SIMILARITY: Belongs to the cysteine synthase/cystathionine beta-
CC       synthase family. {ECO:0000256|ARBA:ARBA00007103}.
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DR   EMBL; AE003849; AAF83413.1; -; Genomic_DNA.
DR   PIR; G82784; G82784.
DR   RefSeq; WP_010893128.1; NC_002488.3.
DR   AlphaFoldDB; Q9PFQ4; -.
DR   STRING; 160492.XF_0603; -.
DR   KEGG; xfa:XF_0603; -.
DR   PATRIC; fig|160492.11.peg.644; -.
DR   eggNOG; COG0031; Bacteria.
DR   eggNOG; COG0517; Bacteria.
DR   HOGENOM; CLU_021018_0_0_6; -.
DR   Proteomes; UP000000812; Chromosome.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:UniProt.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR   CDD; cd01561; CBS_like; 1.
DR   CDD; cd04608; CBS_pair_CBS; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   Gene3D; 3.10.580.10; CBS-domain; 1.
DR   InterPro; IPR046353; CBS_C.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR001216; P-phosphate_BS.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   PANTHER; PTHR10314; CYSTATHIONINE BETA-SYNTHASE; 1.
DR   PANTHER; PTHR10314:SF191; CYSTATHIONINE BETA-SYNTHASE; 1.
DR   Pfam; PF00571; CBS; 1.
DR   Pfam; PF00291; PALP; 1.
DR   SMART; SM00116; CBS; 1.
DR   SUPFAM; SSF54631; CBS-domain pair; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS51371; CBS; 1.
DR   PROSITE; PS00901; CYS_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   CBS domain {ECO:0000256|PROSITE-ProRule:PRU00703};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT   DOMAIN          339..396
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
SQ   SEQUENCE   456 AA;  50010 MW;  51D51CF683C0B8E5 CRC64;
     MVIHSSVLEL IGNTPIVKAQ RLDTGLCDLF LKLESANPGG SIKDRVGLSM IEAAECRGHI
     KPGATLVDGA ASSTSMGLAF VARQKGYRLI LVVPDNMAWE KISNLKAMGA EVILTRSDVS
     KGHPEHYQDL AEKLAAETPG AYFINQFGNA DNPAAHEFGT GPEILKQMGD HVDAVVLGCD
     SAGTITGLSR AFDSVASDVE LILADPVGSI LTQYINEGTC SDKSGTWLVE GIGSDCLPPI
     SDFRRIKKTY AISDAESFHT ARELLSKEGI LGGSSTGTLL AAALKYCREQ IERKRVLVFV
     CDTGNKYLLN MYNDDWMLDN GFLKRPHYGD LRDLILHPYS QRHTVVVDPN DLLTVAYQRM
     KRYGVSQLPV IEDGQLVGIL DESDVLLHVY GDETRFCDPV STAMVSKLHR LDVKSPIEGL
     LPVFERGQVA IVMEDAQFLG LITRIDLLNY LRRRMQ
//