ID A0A0G0J8L2_9BACT Unreviewed; 410 AA.
AC A0A0G0J8L2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN ORFNames=US49_C0002G0034 {ECO:0000313|EMBL:KKQ33139.1};
OS candidate division TM6 bacterium GW2011_GWF2_37_49.
OC Bacteria; Candidatus Dependentiae.
OX NCBI_TaxID=1619083 {ECO:0000313|EMBL:KKQ33139.1, ECO:0000313|Proteomes:UP000033926};
RN [1] {ECO:0000313|EMBL:KKQ33139.1, ECO:0000313|Proteomes:UP000033926}
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 -!- 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:KKQ33139.1}.
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DR EMBL; LBTE01000002; KKQ33139.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0J8L2; -.
DR PATRIC; fig|1619083.3.peg.413; -.
DR Proteomes; UP000033926; Unassembled WGS sequence.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
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; 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 NCBIfam; TIGR01979; sufS; 1.
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.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT DOMAIN 20..397
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 410 AA; 45345 MW; EAEDF8CB6816C4A5 CRC64;
MDFKKTKNDF PIFRQSKHLV YLDNSATTQK PQVVIDAVSK FYSEQNSNVH RGLYDHGEIA
TTLYESARQK IASFINAKHV EEIVFTSGTT ESINFVANGW GLSHLRPGDE ILITQAEHHA
NMLPWQYIAG KTGAVLKFIE INPATYLFND PERFLTSRTK LIAVTHHSNV LGPVWGNNCE
NLKKLISSAQ KQGVKVLIDA AQIFAHQKFD VQALNADFVA FSGHKMFGPT GVGVLFIKKD
LHEEVNPFMF GGGMVNSVSW ESAKWAPAPH KFEAGTPPIS SAIGLAAAVD YIQSNFDFNE
LKTHQAELCK TLVEQLNCIS QVRIVGNIQL IESEGHLVSF AVEGIHAHDI AGFVGSKGIA
VRAGHHCAQP LVKHLGFESL VRVSFAAYNT IYDVEVFVKE LKSAITIFKK
//
