ID A0A1M7FYB1_9RHOB Unreviewed; 348 AA.
AC A0A1M7FYB1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Cysteine desulfurase {ECO:0000256|ARBA:ARBA00013558};
GN ORFNames=SAMN05444389_103311 {ECO:0000313|EMBL:SHM08976.1};
OS Paracoccus solventivorans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=53463 {ECO:0000313|EMBL:SHM08976.1, ECO:0000313|Proteomes:UP000184444};
RN [1] {ECO:0000313|EMBL:SHM08976.1, ECO:0000313|Proteomes:UP000184444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6637 {ECO:0000313|EMBL:SHM08976.1,
RC ECO:0000313|Proteomes:UP000184444};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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}.
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DR EMBL; FRCK01000003; SHM08976.1; -; Genomic_DNA.
DR RefSeq; WP_073064493.1; NZ_FRCK01000003.1.
DR AlphaFoldDB; A0A1M7FYB1; -.
DR STRING; 53463.SAMN05444389_103311; -.
DR OrthoDB; 9808002at2; -.
DR Proteomes; UP000184444; 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; 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 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}.
FT DOMAIN 4..80
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
FT DOMAIN 125..331
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 348 AA; 36030 MW; EABB92AECC285048 CRC64;
MNRVYLDWNA TAPLRPEARA AMADALDIIG NPSSVHAEGR AAKMLLERSR EQLAEALGAA
QADIVFTSGA TEAAALALSG RGLACTGIEH DCVRAWCDET LATGPDGQVT PPDPASATLQ
LANSETGVIQ TLPQGLAASD LTQGFGKVPF AFDWLGIRAG MVSAHKLGGP RGIGALVLAA
GEDREALLRG GGQESGRRAG TENLAAIAGF AAAAGAAQRD LAGGMAERLA EMRDHLLDRL
ENAEGITMFP GRESPRLPQT LSILTPGWKG ETQVMQMDLA GFAVSAGSAC SSGKVRESGV
LRAMGVAGPD AGCALRVSFG GTTTLEDLDR FADAWLAARA RWQGKQGR
//
