ID A0A0S8KZV9_9PROT Unreviewed; 382 AA.
AC A0A0S8KZV9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Cysteine desulfurase {ECO:0000313|EMBL:KPL27434.1};
GN ORFNames=AMJ72_08935 {ECO:0000313|EMBL:KPL27434.1};
OS Acidithiobacillales bacterium SM1_46.
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales.
OX NCBI_TaxID=1703384 {ECO:0000313|EMBL:KPL27434.1, ECO:0000313|Proteomes:UP000052054};
RN [1] {ECO:0000313|EMBL:KPL27434.1, ECO:0000313|Proteomes:UP000052054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM1_46 {ECO:0000313|EMBL:KPL27434.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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}.
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:KPL27434.1}.
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DR EMBL; LJVB01000075; KPL27434.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8KZV9; -.
DR PATRIC; fig|1703384.3.peg.2506; -.
DR Proteomes; UP000052054; 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; 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}.
FT DOMAIN 3..362
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 382 AA; 40467 MW; CD015DFA2753BB8B CRC64;
MPVYLDHNAT TPLDAAVLDT MMPFLREQFG NPSSPHRFGR RTRAAIDAAR EQVAALVKVH
ASQVIFTSGG TESNNLAIKG VAAADEPGIL AIGATEHPSV IEPARALAAH GWRVREITVD
REGRVHPELF RETIAARPRL VSLMYANNET GVIQDVPALA SVARSQGVVF HTDAVQAAGK
LALDFPSSGV HLMSLSAHKL NGPQGVGALV VDKAIECRPL LHGGGQERDR RSGTENVAGI
VGFGAAASLA IDQMGVRTAH FMALRTRLES ALRAIGGVTI FGAGANRLPN TVYFGLRDID
GETLILGLDR KGFACASGSA CGSVRHEPSH VLRAMQVESD LAIGAIRVSF GAGNNERDVD
DFAAALAAEI QRLRPPSRRR AV
//
