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Database: UniProt
Entry: A0A0G0ESC2_9BACT
LinkDB: A0A0G0ESC2_9BACT
Original site: A0A0G0ESC2_9BACT 
ID   A0A0G0ESC2_9BACT        Unreviewed;       425 AA.
AC   A0A0G0ESC2;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   28-FEB-2018, entry version 12.
DE   RecName: Full=Cysteine desulfurase {ECO:0000256|SAAS:SAAS00645443};
DE            EC=2.8.1.7 {ECO:0000256|SAAS:SAAS00645443};
GN   ORFNames=UR67_C0001G0146 {ECO:0000313|EMBL:KKP70237.1};
OS   candidate division CPR3 bacterium GW2011_GWF2_35_18.
OC   Bacteria; candidate division CPR3.
OX   NCBI_TaxID=1618350 {ECO:0000313|EMBL:KKP70237.1, ECO:0000313|Proteomes:UP000034581};
RN   [1] {ECO:0000313|EMBL:KKP70237.1, ECO:0000313|Proteomes:UP000034581}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a
RT   large radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- CATALYTIC ACTIVITY: L-cysteine + acceptor = L-alanine + S-
CC       sulfanyl-acceptor. {ECO:0000256|SAAS:SAAS00645449}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|SAAS:SAAS00645451};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|SAAS:SAAS00645453}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KKP70237.1}.
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DR   EMBL; LBQB01000001; KKP70237.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKP70237; KKP70237; UR67_C0001G0146.
DR   PATRIC; fig|1618350.3.peg.153; -.
DR   Proteomes; UP000034581; Unassembled WGS sequence.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-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; -; 2.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR010970; Cys_dSase_SufS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR01979; sufS; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000034581};
KW   Pyridoxal phosphate {ECO:0000256|SAAS:SAAS00645444};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034581};
KW   Transferase {ECO:0000256|SAAS:SAAS00645445}.
FT   DOMAIN       22    395       Aminotran_5. {ECO:0000259|Pfam:PF00266}.
SQ   SEQUENCE   425 AA;  48088 MW;  23BEB6B72C9E970D CRC64;
     MLNTTKIKSD FPIFKNQLNL TYLDSTATSL KPQSVIDKLN EYYTQYSSNI FRGLYPISQK
     ATEEHEATRE IVTKFIGAKH PEEVIFTKNT SESLNLLMYT LGDKIVQKDD NVIISIAEHH
     SNFVPWQMLC LKKEAEFRVL GINKEGTVKL DELEQQVDSR TKIIALTYIS NVLGTVNPIE
     KIVKIAKKKN PNVIIIIDAA QAAPHLKLEV RKLGADFVAF SSHKMLGPTG VGILWGKKEL
     FEEMPPFMFG GEMIEKVSVE KTTFDKLPHK FEAGTPAIGE IIALKEAVKY LEKIGLKNIE
     KHEKELTNYA LERLNNEFGN DFQVIGPNDY KLKTGIIAFV FKDYHPHDIA DILGNQGICI
     RAGHHCAAPL HEKANISASS RMSFYLYNNQ EDVEKIINGL KKVDQILKMG FHERSTNSKF
     KQPCC
//
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