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Database: UniProt/TrEMBL
Entry: F4DKH4_CHLPE
LinkDB: F4DKH4_CHLPE
Original site: F4DKH4_CHLPE 
ID   F4DKH4_CHLPE            Unreviewed;       406 AA.
AC   F4DKH4;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   03-APR-2013, entry version 14.
DE   RecName: Full=Cysteine desulfurase;
DE            EC=2.8.1.7;
GN   OrderedLocusNames=G5S_0359;
OS   Chlamydophila pecorum (strain ATCC VR-628 / E58).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=331635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-628 / E58;
RX   PubMed=21571992; DOI=10.1128/JB.00454-11;
RA   Mojica S., Huot Creasy H., Daugherty S., Read T.D., Kim T.,
RA   Kaltenboeck B., Bavoil P., Myers G.S.;
RT   "Genome sequence of the obligate intracellular animal pathogen
RT   Chlamydia pecorum E58.";
RL   J. Bacteriol. 193:3690-3690(2011).
CC   -!- CATALYTIC ACTIVITY: L-cysteine + acceptor = L-alanine + S-
CC       sulfanyl-acceptor.
CC   -!- COFACTOR: Pyridoxal phosphate (By similarity).
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DR   EMBL; CP002608; AEB41359.1; -; Genomic_DNA.
DR   RefSeq; YP_004377062.1; NC_015408.1.
DR   EnsemblBacteria; AEB41359; AEB41359; G5S_0359.
DR   GeneID; 10448012; -.
DR   KEGG; cpm:G5S_0359; -.
DR   PATRIC; 54466738; VBIChlPec99706_0327.
DR   KO; K11717; -.
DR   BioCyc; CPEC331635:GHCA-339-MONOMER; -.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW.
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   Aminotransferase; Complete proteome; Pyridoxal phosphate; Transferase.
SQ   SEQUENCE   406 AA;  44341 MW;  15801102549A0D3C CRC64;
     MREIKKDFPI FASKEKNGES FVYLDSAATT HKPQDVLDAL IKFYTTSYAS VGRSIYSSSR
     EASQEFSLVR QKIRDWLGAA FEEEIVFTRG TTAGLNTLAI AVNDLWSSGG VVLVSETEHH
     ANVISWEIAC RRRGSSVKKI SVLDSGLIDL NHLEDLLKEG ANLVSIPGIH NVSGGIQPIK
     EIAALVHRYH AWLAVDGAQS MGHQSVDVRS WDVDFYVFSS HKVYGPTGLG VLYGKKELLE
     LLPPVEGGGG MVEIYDPQDP KYLPSPLKFE AGTPHVAGVV GLGAALDYLN KLSPEAIYSH
     EAELIAYMHE QLVKNIPGLH VLGPELGFPR GGLLSMKIDQ AHPLDLGVLL DLQGIAVRTG
     HLCSQPSMAR WGTGHVLRAS LGVYNDKHDI DTFICALQDA VAQLRR
//
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