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Database: UniProt
Entry: A0A433RRY7_9BACL
LinkDB: A0A433RRY7_9BACL
Original site: A0A433RRY7_9BACL 
ID   A0A433RRY7_9BACL        Unreviewed;       380 AA.
AC   A0A433RRY7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Cysteine desulfurase {ECO:0000313|EMBL:RUS54383.1};
GN   ORFNames=QI30_13270 {ECO:0000313|EMBL:RUS54383.1};
OS   Kurthia sp. 3B1D.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Kurthia.
OX   NCBI_TaxID=1562256 {ECO:0000313|EMBL:RUS54383.1, ECO:0000313|Proteomes:UP000288623};
RN   [1] {ECO:0000313|EMBL:RUS54383.1, ECO:0000313|Proteomes:UP000288623}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3B1D {ECO:0000313|EMBL:RUS54383.1,
RC   ECO:0000313|Proteomes:UP000288623};
RA   Lawson J.N., Gonzalez J.E., Rinauldi L., Xuan Z., Firman A., Shaddox L.,
RA   Trudeau A., Shah S., Reiman D.;
RT   "Genome sequence and analysis of novel Kurthia sp.";
RL   Submitted (NOV-2014) 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:RUS54383.1}.
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DR   EMBL; JTFC01000032; RUS54383.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A433RRY7; -.
DR   OrthoDB; 9808002at2; -.
DR   Proteomes; UP000288623; 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:SF34; CYSTEINE DESULFURASE, MITOCHONDRIAL; 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:UP000288623}.
FT   DOMAIN          4..366
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   380 AA;  41276 MW;  B8ACDE3D3E1C0849 CRC64;
     MTEIYLDHAA TSPMHPEVID AMVAVMNDVY GNPSSIHGIG RHARKYLDNA RGFIARSIGA
     KDHEIVLTSG GSEADNLAIF GTAYAHQNEG RHIITTQVEH HAVLRACERL EKEGFDVTYL
     PVDKHGMIAI DDFKRALRDD TILVTIMYGN NEVGTKQPIA EIGALLKDHT ATFHTDAVQA
     FGLEKIDVDA LGVDLLSTSA HKLNGPKGIG FLYERPKAHL QSLIVGGDQE RKRRASTENV
     PAVVGFAKAV ELAQSSMEEK ATEYARYRQM LLSAFDEAGI AYHVNGDALH ALPHVLNVSF
     NGMDVESFLI NLDIEGIAVS SGSACTAGSL EPSHVLLAMY GKGAEELRNS IRFSFGYGLD
     SAQIKRAAQT VIGIVKRLTK
//
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