ID A0A0G1DW06_9BACT Unreviewed; 399 AA.
AC A0A0G1DW06;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN ORFNames=UV79_C0005G0014 {ECO:0000313|EMBL:KKT01768.1};
OS candidate division TM6 bacterium GW2011_GWF2_43_17.
OC Bacteria; Candidatus Dependentiae.
OX NCBI_TaxID=1619085 {ECO:0000313|EMBL:KKT01768.1, ECO:0000313|Proteomes:UP000034620};
RN [1] {ECO:0000313|EMBL:KKT01768.1, ECO:0000313|Proteomes:UP000034620}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(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. Csd subfamily.
CC {ECO:0000256|ARBA:ARBA00010447}.
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:KKT01768.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LCFV01000005; KKT01768.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1DW06; -.
DR STRING; 1619085.UV79_C0005G0014; -.
DR PATRIC; fig|1619085.3.peg.190; -.
DR Proteomes; UP000034620; Unassembled WGS sequence.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006534; P:cysteine metabolic process; IEA:InterPro.
DR CDD; cd06453; SufS_like; 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; IPR010970; Cys_dSase_SufS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR PANTHER; PTHR43586:SF27; CYSTEINE DESULFURASE 1, CHLOROPLASTIC; 1.
DR Pfam; PF00266; Aminotran_5; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT DOMAIN 18..388
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 399 AA; 43854 MW; BAFCFD8382357EF8 CRC64;
MKGIKESFPI FSRYPDLVYL DSAATSQKPY AVVDRLASFY SFENASVHRS FYQLAEQATQ
NYEYVRTQAA EFFGARESSE IVFTSGATAG CNAVAFGWLQ HVLRPGDEIV ISALEHHSTF
LPMVEVARAC GALVRFMPLD TEGQLLLEIA EAAITSKTRL VVCSAGSNVV GVATPLEFIV
QKARSVGAAV FVDAAQVAPR RRLQVAAMGI DFLVCSAHKM CGPTGLGVLY VSKKRHSECH
PWVLGGSMVH EVHTDRWSPT CLPAMWEAGT PPIAQVIGFG ETLSFLQRLD FEALRAHEAA
LCRVFIEELA GLPELVIVGN KDLLASQGHL VSFYINNFHA HDVAAYLAQY QICVRSGYHC
AQPLHEALNI PQTVRASWYM YTSLDDVRAC AAHLRKLSQ
//
