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Database: UniProt
Entry: A0A268E1K8_9BACI
LinkDB: A0A268E1K8_9BACI
Original site: A0A268E1K8_9BACI 
ID   A0A268E1K8_9BACI        Unreviewed;       378 AA.
AC   A0A268E1K8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 14.
DE   SubName: Full=Cysteine desulfurase {ECO:0000313|EMBL:PAD67005.1};
DE            EC=2.8.1.7 {ECO:0000313|EMBL:PAD67005.1};
GN   ORFNames=CHH83_21155 {ECO:0000313|EMBL:PAD67005.1};
OS   Bacillus sp. 7586-K.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2021690 {ECO:0000313|EMBL:PAD67005.1, ECO:0000313|Proteomes:UP000216230};
RN   [1] {ECO:0000313|EMBL:PAD67005.1, ECO:0000313|Proteomes:UP000216230}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=7586-K {ECO:0000313|EMBL:PAD67005.1,
RC   ECO:0000313|Proteomes:UP000216230};
RA   Kalinowski J., Ahrens B., Al-Dilaimi A., Winkler A., Wibberg D.,
RA   Schleenbecker U., Ruckert C., Wolfel R., Grass G.;
RT   "Isolation and whole genome analysis of endospore-forming bacteria from
RT   heroin.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU004504};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. NifS/IscS subfamily.
CC       {ECO:0000256|ARBA:ARBA00006490}.
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:PAD67005.1}.
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DR   EMBL; NPCL01000110; PAD67005.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A268E1K8; -.
DR   OrthoDB; 9808002at2; -.
DR   Proteomes; UP000216230; Unassembled WGS sequence.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.260.50; -; 1.
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; IPR020578; Aminotrans_V_PyrdxlP_BS.
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:SF36; CYSTEINE DESULFURASE NIFS-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.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000216230};
KW   Transferase {ECO:0000313|EMBL:PAD67005.1}.
FT   DOMAIN          2..365
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   378 AA;  41750 MW;  A8619A154E439353 CRC64;
     MIYLDYAATT PISDQALTIY GKAAKSAFGN SNSLHDIGGT SSQLLESSRR VIAKLINGDE
     KGLFFTGSGS EANILTIQSL LNGLNDSKKH LITSQIEHSS LYHLFKKLER EGYKVTYLIP
     NKQGHIEINQ VEKALRDDTG LVSIQHGNSE IGVVQNIKKI GELLKQKNIV FHSDCVQTFG
     KLPIDVEEFG LDAISISSHK IYGPKGIGAA YIKPSTFWNP VIPGTTHESG FRPGTVDVPA
     VAAFATASME ICGKIAENMN HYEQLRRIFI DSFSPHQKLI TIINDSQHCI LPNIIPLQIK
     GIEGQYVMLE CNRYGYAVST GSACQVGMQE PSRTLLSIGY TKQIAKQYIR ISLGTQTTHE
     QIENFAKVLI NVVKDYYK
//
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