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Database: UniProt/TrEMBL
Entry: Q8E7L5_STRA3
LinkDB: Q8E7L5_STRA3
Original site: Q8E7L5_STRA3 
ID   Q8E7L5_STRA3            Unreviewed;       410 AA.
AC   Q8E7L5;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   01-MAY-2013, entry version 70.
DE   RecName: Full=Cysteine desulfurase;
DE            EC=2.8.1.7;
GN   OrderedLocusNames=gbs0139;
OS   Streptococcus agalactiae serotype III (strain NEM316).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=211110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEM316;
RX   PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA   Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L.,
RA   Msadek T., Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P.,
RA   Kunst F.;
RT   "Genome sequence of Streptococcus agalactiae, a pathogen causing
RT   invasive neonatal disease.";
RL   Mol. Microbiol. 45:1499-1513(2002).
CC   -!- CATALYTIC ACTIVITY: L-cysteine + acceptor = L-alanine + S-
CC       sulfanyl-acceptor.
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
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DR   EMBL; AL766844; CAD45784.1; -; Genomic_DNA.
DR   RefSeq; NP_734609.1; NC_004368.1.
DR   HSSP; P77444; 1KMJ.
DR   ProteinModelPortal; Q8E7L5; -.
DR   STRING; 211110.gbs0139; -.
DR   EnsemblBacteria; CAD45784; CAD45784; CAD45784.
DR   GeneID; 1031215; -.
DR   KEGG; san:gbs0139; -.
DR   PATRIC; 19636019; VBIStrAga3577_0141.
DR   GenoList; gbs0139; -.
DR   HOGENOM; HOG000017511; -.
DR   KO; K11717; -.
DR   OMA; QACERTG; -.
DR   ProtClustDB; CLSK572165; -.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006534; P:cysteine metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR000192; Aminotrans_V/Cys_dSase.
DR   InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR   InterPro; IPR010970; Cys_dSase_SufS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR   TIGRFAMs; TIGR01979; sufS; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Pyridoxal phosphate; Transferase.
SQ   SEQUENCE   410 AA;  45553 MW;  2F67D945519BBA00 CRC64;
     MTLLDSYKLK QDFPILNQLV NDEPLIYLDN AATTQKPNQV LETLRAYYQN DNANVHRGVH
     TLAERATAQY ETAREKARQF LNAKSSKEIL FTRGTTTGLN WVAKFAESIL ERGDEVLISI
     MEHHSNIIPW QQACERTGAK LVYAYLKDGS LDLEDFYNKL SSKTKFVSLA HISNVLGCIT
     PVKAIAERVH QVGAYMVVDG AQSAPHMAID VQDLDCDFFA LSGHKMLGPT GIGVLYGKES
     ILDKMPPVEF GGEMIDFVYE QSATWKELPW KFEAGTPNIA GAIAFGEALD YLTDVGMDEI
     HQYEQSLVSY VLPKLQAIDG LTIYGPSDAE SHVGVIAFNL EGLHPHDVAT AMDYEGVAVR
     AGHHCAQPLI NHLGIHSAVR ASFYFYNTKE DCDKLVDAIQ KTKEFFNGTL
//
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