GenomeNet

Database: UniProt
Entry: C3G982_BACTU
LinkDB: C3G982_BACTU
Original site: C3G982_BACTU 
ID   C3G982_BACTU            Unreviewed;       380 AA.
AC   C3G982;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Cysteine desulfurase {ECO:0000313|EMBL:EEM69548.1};
GN   ORFNames=bthur0009_44030 {ECO:0000313|EMBL:EEM69548.1};
OS   Bacillus thuringiensis serovar andalousiensis BGSC 4AW1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=527032 {ECO:0000313|EMBL:EEM69548.1};
RN   [1] {ECO:0000313|EMBL:EEM69548.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGSC 4AW1 {ECO:0000313|EMBL:EEM69548.1};
RX   PubMed=22645259; DOI=10.1101/gr.134437.111;
RA   Zwick M.E., Joseph S.J., Didelot X., Chen P.E., Bishop-Lilly K.A.,
RA   Stewart A.C., Willner K., Nolan N., Lentz S., Thomason M.K.,
RA   Sozhamannan S., Mateczun A.J., Du L., Read T.D.;
RT   "Genomic characterization of the Bacillus cereus sensu lato species:
RT   Backdrop to the evolution of Bacillus anthracis.";
RL   Genome Res. 22:1512-1524(2012).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EEM69548.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; ACNG01000100; EEM69548.1; -; Genomic_DNA.
DR   RefSeq; WP_000638961.1; NZ_CM000754.1.
DR   AlphaFoldDB; C3G982; -.
DR   HOGENOM; CLU_003433_0_2_9; -.
DR   Proteomes; UP000001380; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR016454; Cysteine_dSase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11601:SF50; CYSTEINE DESULFURASE ISCS 2-RELATED; 1.
DR   PANTHER; PTHR11601; CYSTEINE DESULFURYLASE FAMILY MEMBER; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF005572; NifS; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   4: Predicted;
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT   DOMAIN          2..364
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   380 AA;  41707 MW;  5B2964C634B5F075 CRC64;
     MIYFDNSATT KPYPEALQSY VTVAGKYFGN PSSIHSLGGE AERLLTQSRT IAAQLLHVKP
     SEIIFTSGGT EGNNLAIKGI AMRNRSRGKH IITTNIEHAS VFEAYKQLED LGFDVTYLPV
     NEHGVVSVED VKRALREDTI LVSIIHVNNE TGAIQPVAEI GTLLSNYPKI RFHVDHVQGI
     GKVPLNLYAS HIDLCSISGH KFHSVKGTGL LYVRDGVRLD PILSGGQQEL KYRSGTENLP
     GIVAMVKALR MTMEQVKEKV AHLHSLQAEL VRFFKEMEDV TINTSLAYAA PHILNVSFVG
     LKPEVVVHAL EEHGVYVSTK SACSSKANEV SRVLVSMGVP HAAAASAIRI SLAPENTMEE
     VKQFEGIVKE TMPKLYEVMR
//
DBGET integrated database retrieval system