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Database: UniProt
Entry: B0SR34_LEPBP
LinkDB: B0SR34_LEPBP
Original site: B0SR34_LEPBP 
ID   B0SR34_LEPBP            Unreviewed;       333 AA.
AC   B0SR34;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 85.
DE   SubName: Full=Cysteine synthase B {ECO:0000313|EMBL:ABZ97735.1};
DE            EC=2.5.1.47 {ECO:0000313|EMBL:ABZ97735.1};
GN   Name=cysM {ECO:0000313|EMBL:ABZ97735.1};
GN   OrderedLocusNames=LEPBI_I1628 {ECO:0000313|EMBL:ABZ97735.1};
OS   Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=456481 {ECO:0000313|EMBL:ABZ97735.1, ECO:0000313|Proteomes:UP000001847};
RN   [1] {ECO:0000313|EMBL:ABZ97735.1, ECO:0000313|Proteomes:UP000001847}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Patoc 1 / ATCC 23582 / Paris
RC   {ECO:0000313|Proteomes:UP000001847};
RX   PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA   Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA   Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA   Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA   Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT   "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT   into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL   PLoS ONE 3:E1607-E1607(2008).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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DR   EMBL; CP000786; ABZ97735.1; -; Genomic_DNA.
DR   RefSeq; WP_012388613.1; NC_010602.1.
DR   AlphaFoldDB; B0SR34; -.
DR   STRING; 456481.LEPBI_I1628; -.
DR   KEGG; lbi:LEPBI_I1628; -.
DR   HOGENOM; CLU_021018_1_0_12; -.
DR   OMA; GIRRWPE; -.
DR   OrthoDB; 356755at2; -.
DR   BioCyc; LBIF456481:LEPBI_RS08040-MONOMER; -.
DR   Proteomes; UP000001847; Chromosome I.
DR   GO; GO:0004124; F:cysteine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006535; P:cysteine biosynthetic process from serine; IEA:InterPro.
DR   CDD; cd01561; CBS_like; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
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:SF162; CYSTEINE SYNTHASE B; 1.
DR   Pfam; PF00291; PALP; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00901; CYS_SYNTHASE; 1.
PE   4: Predicted;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001847};
KW   Transferase {ECO:0000313|EMBL:ABZ97735.1}.
FT   DOMAIN          42..315
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
SQ   SEQUENCE   333 AA;  36583 MW;  7FD41EAAC4BC30DF CRC64;
     MIDPISKGID DFGNSLLQAL NNVQGIFGKE LSVAKPIKDN VLQLIGNTPL IRLNRIGSEY
     SGVQFYLKAE FLNPTGSAKD RTAIAMVLDA EKRGKLKKGM PIILSGAGSS SVSFTWIGKV
     KGYPVYCLVP LTTPPERVQL LRSYGAEVTV TNESDIVKLT ELAEEKAKKM GGYLPDELEN
     PANPNFHFKT TGPEIWRDLQ GKVGAVISAP GSGGAITGIG RYLKSQDRRV KVIIAGKQNS
     AFMEYGKTDN PKERERIRLP AVYDPKLIDH YFHVTKDEAL HLQADLYEKE GIFAGLTTGT
     VITGALRFSE TLSESEKNER NPFNIVILSP DRD
//
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