ID A0A1W9K641_9PROT Unreviewed; 366 AA.
AC A0A1W9K641;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Cysteine desulfurase {ECO:0000313|EMBL:OQW79616.1};
GN ORFNames=BVN35_01940 {ECO:0000313|EMBL:OQW79616.1};
OS Proteobacteria bacterium ST_bin11.
OC Bacteria; Pseudomonadota.
OX NCBI_TaxID=1978759 {ECO:0000313|EMBL:OQW79616.1, ECO:0000313|Proteomes:UP000192691};
RN [1] {ECO:0000313|EMBL:OQW79616.1, ECO:0000313|Proteomes:UP000192691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ST_bin11 {ECO:0000313|EMBL:OQW79616.1};
RX PubMed=28390307; DOI=10.1016/j.watres.2017.03.042;
RA Wang Y., Ma L., Mao Y., Jiang X., Xia Y., Yu K., Li B., Zhang T.;
RT "Comammox in drinking water systems.";
RL Water Res. 116:332-341(2017).
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:OQW79616.1}.
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DR EMBL; MSXO01000003; OQW79616.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9K641; -.
DR STRING; 1978759.BVN35_01940; -.
DR Proteomes; UP000192691; 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}.
FT DOMAIN 2..356
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 366 AA; 39222 MW; 8D899D089CDFA2D8 CRC64;
MIYLDHNATT RCDERVVEAM LPYLNTMYGN PSSLYKLGRI ARSAIDTARE QISALIDAAG
ARIVFTSGGT EANALALANA RHRGLAVSAI EHPSIFENAA YYKHWFRDLQ TIEVNGDGLV
SLPLEKTSWQ TGDMVSVMLA NNETGVIQDL AAISEALAER GLNLHTDAVQ ALGKIPVSFK
TLGVNLMSLS SHKIYGPKGC GALVVSEDFV LKPSQRGGDQ EHGWRAGTEN VAAIVGFGKA
ADLAKSELGS RQTRMLALRT RLEQSLRTIP GLVIFAEKAK RIPNTVQFGI PGISGEMLLM
QLDQRNIAVS SGSACSASSG EISPVLTAMG VDVRLARSAI RVSLGKDNNE SEIDQFVDVL
KASIAN
//
