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Database: UniProt
Entry: L7FDR2_9ACTN
LinkDB: L7FDR2_9ACTN
Original site: L7FDR2_9ACTN 
ID   L7FDR2_9ACTN            Unreviewed;       385 AA.
AC   L7FDR2;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Putative cysteine desulfurase {ECO:0000313|EMBL:ELP69221.1};
DE   Flags: Fragment;
GN   ORFNames=STRTUCAR8_07697 {ECO:0000313|EMBL:ELP69221.1};
OS   Streptomyces turgidiscabies Car8.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=698760 {ECO:0000313|EMBL:ELP69221.1, ECO:0000313|Proteomes:UP000010931};
RN   [1] {ECO:0000313|EMBL:ELP69221.1, ECO:0000313|Proteomes:UP000010931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Car8 {ECO:0000313|EMBL:ELP69221.1,
RC   ECO:0000313|Proteomes:UP000010931};
RX   PubMed=21087627; DOI=10.1016/j.plasmid.2010.11.002;
RA   Huguet-Tapia J.C., Badger J.H., Loria R., Pettis G.S.;
RT   "Streptomyces turgidiscabies Car8 contains a modular pathogenicity island
RT   that shares virulence genes with other actinobacterial plant pathogens.";
RL   Plasmid 65:118-124(2011).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
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:ELP69221.1}.
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DR   EMBL; AEJB01000161; ELP69221.1; -; Genomic_DNA.
DR   RefSeq; WP_006375550.1; NZ_AEJB01000161.1.
DR   AlphaFoldDB; L7FDR2; -.
DR   STRING; 85558.T45_05918; -.
DR   Proteomes; UP000010931; 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   GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
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; 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.
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:UP000010931}.
FT   DOMAIN          3..370
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
FT   NON_TER         385
FT                   /evidence="ECO:0000313|EMBL:ELP69221.1"
SQ   SEQUENCE   385 AA;  40108 MW;  50D2BEA7E89B4318 CRC64;
     MAYLDHAATT PMLPEAVEAM TAQLAVTGNA SSLHAAGRRA RRTVEEARET LAESLGARPS
     EVVFTAGGTE ADNLAVKGLY WARRDADPAR VRVLASPVEH HAVLDAVHWL GEHEGAVVEY
     LPVDAYGRVH PDALREAVAR DPDSVALATV MWANNEIGTI MPVRELADVA NEFGVPLHAD
     AVQAYGQVPV SFADSGLAAM TVSGHKIGGP YGIGALLLGR EYRPVPVLHG GGQERHVRSG
     TLDVPAVASF AVAGRLAAEQ QGWFAREIGA LRDALVAAVR TAVPDAILGG DPVDRLPANA
     HFTFPGCEGD SLLLLLDAQG IECSTGSACT AGVAQPSHVL LAVGTDPDLA RGTLRFSLGH
     TSTEADVEAV AKVIAPVVER ARAAG
//
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