ID A0A0C5FVG4_9ACTN Unreviewed; 459 AA.
AC A0A0C5FVG4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Cysteine desulfurase {ECO:0000313|EMBL:AJP01688.1};
GN ORFNames=TU94_09375 {ECO:0000313|EMBL:AJP01688.1};
OS Streptomyces cyaneogriseus subsp. noncyanogenus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=477245 {ECO:0000313|EMBL:AJP01688.1, ECO:0000313|Proteomes:UP000032234};
RN [1] {ECO:0000313|EMBL:AJP01688.1, ECO:0000313|Proteomes:UP000032234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NMWT 1 {ECO:0000313|EMBL:AJP01688.1,
RC ECO:0000313|Proteomes:UP000032234};
RA Wang H., Li C., Xiang W., Wang X.;
RT "Genome sequence of thermotolerant Streptomyces cyaneogriseus subsp.
RT Noncyanogenus NMWT1, the producer of nematocidal antibiotics nemadectin.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-
CC alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-
CC COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:64428; EC=2.8.1.7;
CC Evidence={ECO:0000256|ARBA:ARBA00001357};
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 -!- SIMILARITY: Belongs to the sulfur carrier protein TusA family.
CC {ECO:0000256|ARBA:ARBA00008984}.
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DR EMBL; CP010849; AJP01688.1; -; Genomic_DNA.
DR RefSeq; WP_044381091.1; NZ_CP010849.1.
DR AlphaFoldDB; A0A0C5FVG4; -.
DR STRING; 477245.TU94_09375; -.
DR KEGG; scw:TU94_09375; -.
DR PATRIC; fig|477245.3.peg.2008; -.
DR HOGENOM; CLU_003433_0_0_11; -.
DR OrthoDB; 9808002at2; -.
DR Proteomes; UP000032234; Chromosome.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
DR CDD; cd00291; SirA_YedF_YeeD; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.30.110.40; TusA-like domain; 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 InterPro; IPR001455; TusA-like.
DR InterPro; IPR036868; TusA-like_sf.
DR PANTHER; PTHR11601:SF34; CYSTEINE DESULFURASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11601; CYSTEINE DESULFURYLASE FAMILY MEMBER; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR Pfam; PF01206; TusA; 1.
DR PIRSF; PIRSF005572; NifS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR SUPFAM; SSF64307; SirA-like; 1.
DR PROSITE; PS01148; UPF0033; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000032234}.
FT DOMAIN 390..414
FT /note="UPF0033"
FT /evidence="ECO:0000259|PROSITE:PS01148"
FT COILED 242..269
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 459 AA; 47807 MW; 9FAE9344F904FE1A CRC64;
MSYFDAASAA PLHSVARQAL LASLDEGWAD PARLYREGRR ARMLLDAARE AAAEAVGCRP
DELVFTPSGT RAVHEGVAGA LAGRRRTGRH LIVSAVEHSS VLHAAEVHEA GGGTVTQVAV
DRTGAVDPAA YAGALRADTA LACLQSANHE VGTEQPVAEV AEACRAAGVP LLVDAAQSLG
WGPVAGGWSL LTASAHKWGG PSGVGLLAVR KGVRFAPQGP ADERESGRAP GFENIPAIVA
AAASLRAVRA EAAREAARLR ELTDRIRARV PAVVPDVEVV GDPARRLPGI VTFSCLYVDG
ETLLHELDRA GFSVSSGSSC TSSTLTPSHV LKAMGVLSEG NVRVSLPPGT RAEDVERFLE
VLPEAVAGVR EKLGAPAPAA RSRQEDAIVV DAVGRRCPVP VIELAKVIGD VPVGGTVRVL
ADDEAARLDI PAWCEMRGQE YVGEEPADRG AAYVVRRVS
//