ID A3SPJ6_ROSNI Unreviewed; 347 AA.
AC A3SPJ6;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=Cysteine desulfurase {ECO:0000256|ARBA:ARBA00013558};
GN ORFNames=ISM_16010 {ECO:0000313|EMBL:EAP76386.1};
OS Roseovarius nubinhibens (strain ATCC BAA-591 / DSM 15170 / ISM).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=89187 {ECO:0000313|EMBL:EAP76386.1, ECO:0000313|Proteomes:UP000005954};
RN [1] {ECO:0000313|EMBL:EAP76386.1, ECO:0000313|Proteomes:UP000005954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-591 / DSM 15170 / ISM
RC {ECO:0000313|Proteomes:UP000005954};
RA Moran M.A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (DEC-2005) 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 -!- 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:EAP76386.1}.
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DR EMBL; AALY01000002; EAP76386.1; -; Genomic_DNA.
DR RefSeq; WP_009815211.1; NZ_CH724156.1.
DR AlphaFoldDB; A3SPJ6; -.
DR STRING; 89187.ISM_16010; -.
DR eggNOG; COG1104; Bacteria.
DR HOGENOM; CLU_003433_0_0_5; -.
DR OrthoDB; 9808002at2; -.
DR Proteomes; UP000005954; 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:0008483; F:transaminase activity; 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; 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; 2.
DR PIRSF; PIRSF005572; NifS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW Aminotransferase {ECO:0000313|EMBL:EAP76386.1};
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:UP000005954};
KW Transferase {ECO:0000313|EMBL:EAP76386.1}.
FT DOMAIN 4..79
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT DOMAIN 122..331
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 347 AA; 35970 MW; AF0404FD5554DCAD CRC64;
MTRVYLDHNA TAPLRPEARA AMLAAMDLVG NPSSVHAEGR AAKSLMERAR GQVAAALGAE
GADVIFTSGA TEAAALACAG RGLLGAGVEH DAVREWIDET LAVDAAGQVT VNEPGQSALQ
LANSETGVVQ TLPQGLAVCD MTQGFGKLPL AFNWAGCEMA LISAHKIGGP KGIGALVIKR
GTDLAAQIRG GGQEMGRRSG TENLIGIAGF GAAAEAAARD LADGAWQQVE EFRNILENAL
VESSKETIFV GKSGPRLPNT SCFVTDGWKG ETQVMALDLA GFAVSAGSAC SSGKTRASHV
LRCMGLSESQ AGCALRVSLG PGITEDEIYR FAETWAKLRE RHRARAA
//
