ID A0A142M942_AMIAI Unreviewed; 387 AA.
AC A0A142M942;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Cysteine desulfurase {ECO:0000256|ARBA:ARBA00013558};
GN ORFNames=FHS67_001014 {ECO:0000313|EMBL:MBB3704711.1};
OS Aminobacter aminovorans (Chelatobacter heintzii).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Aminobacter.
OX NCBI_TaxID=83263 {ECO:0000313|EMBL:MBB3704711.1, ECO:0000313|Proteomes:UP000577697};
RN [1] {ECO:0000313|EMBL:MBB3704711.1, ECO:0000313|Proteomes:UP000577697}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10368 {ECO:0000313|EMBL:MBB3704711.1,
RC ECO:0000313|Proteomes:UP000577697};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (AUG-2020) 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:MBB3704711.1}.
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DR EMBL; JACICB010000003; MBB3704711.1; -; Genomic_DNA.
DR RefSeq; WP_067962695.1; NZ_JACICB010000003.1.
DR AlphaFoldDB; A0A142M942; -.
DR STRING; 83263.AA2016_3944; -.
DR OrthoDB; 9808002at2; -.
DR Proteomes; UP000577697; 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; 1.
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};
KW Transferase {ECO:0000313|EMBL:MBB3704711.1}.
FT DOMAIN 7..369
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 387 AA; 39809 MW; B9AA39E40B339845 CRC64;
MAGPRAYLDY NASAPLLPAA RAAVVAALEV GANPSSVHSE GRAARKIIED ARRDVAALVG
ARPEHVVFTS GATEAATTLL SPDWRMGRGA VRMSRLYVTE ADHPCVLNGG RFPAERLTRL
GVDGDGIVDL VGLEAALAAH DKSEGLPLVA IHAANNETGV IQPIRAIAEL VKVAGGVLVL
DAVQAAGRIP LDMSEGYADY LILSSHKIGG PKGAGAIVAQ ADLMMPAPLV TGGGQEKGHR
GGTENLPAIS GFGAAARTAL DGLAGIGEVR ALRDRLEETV LRLVSDAEIF GKAVERLANT
TFFAIPGVKA ETAQIAFDLA GVALSAGSAC SSGKVGPSHV LKAMGFADNL GALRVSIGRQ
TSEADVEKFE TALAALLSRR TDRTKAA
//
