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
//