ID I7JEX4_9RICK Unreviewed; 399 AA.
AC I7JEX4;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Cysteine desulfurase {ECO:0000256|ARBA:ARBA00013558};
GN ORFNames=wOo_07870 {ECO:0000313|EMBL:CCF78345.1};
OS Wolbachia endosymbiont of Onchocerca ochengi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC Anaplasmataceae; Wolbachieae; Wolbachia.
OX NCBI_TaxID=100901 {ECO:0000313|EMBL:CCF78345.1, ECO:0000313|Proteomes:UP000007516};
RN [1] {ECO:0000313|EMBL:CCF78345.1, ECO:0000313|Proteomes:UP000007516}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Adamawa_Cameroon {ECO:0000313|Proteomes:UP000007516};
RX PubMed=22919073; DOI=10.1101/gr.138420.112;
RA Darby A.C., Armstrong S.D., Bah G.S., Kaur G., Hughes M.A., Kay S.M.,
RA Koldkaer P., Rainbow L., Radford A.D., Blaxter M.L., Tanya V.N.,
RA Trees A.J., Cordaux R., Wastling J.M., Makepeace B.L.;
RT "Analysis of gene expression from the Wolbachia genome of a filarial
RT nematode supports both metabolic and defensive roles within the
RT symbiosis.";
RL Genome Res. 22:2467-2477(2012).
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 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}.
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DR EMBL; HE660029; CCF78345.1; -; Genomic_DNA.
DR AlphaFoldDB; I7JEX4; -.
DR STRING; 100901.wOo_07870; -.
DR KEGG; woo:wOo_07870; -.
DR PATRIC; fig|100901.6.peg.643; -.
DR eggNOG; COG1104; Bacteria.
DR HOGENOM; CLU_003433_0_0_5; -.
DR Proteomes; UP000007516; Chromosome.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
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 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
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:UP000007516}.
FT DOMAIN 30..381
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 399 AA; 43494 MW; B50395E2A1B43084 CRC64;
MYSFNDKRSL YNSVTNKPLS SFFLENSNYI YADYNATSPI SDGVRKSILE VLSKQILNPS
SLHRKGQETR KILQDARDAV CGIIDVSSDK EIVFTSGATE ANNLVMRGVT GFQYVVSAIE
HPSILNSAHN PHIIPVNQEG IIDLLELEKI LSKLKGNKVI VSVMMANNET GVVQPIREIA
EIAHKFGAIC HTDAAQSVGK IKVNMENLGV DLLTLSAHKF GGIAGSGVLV FNKNLTIKPI
IVGGGQEKGL RGGTENVVAI AGLSAALQSV PDLLSKMNEI KKLRDQLESK LLNLVSSIKI
FGKNSKRLPN TSFVYMPGVK SDVQLMHFDL NNIAVSNGSA CSSGKIEPSY VLLAMGATKE
QANCSVRISI GPQNKPQDIK KIVDCWYDIY KKNTLNMYK
//