ID A0A174GVL9_9BACE Unreviewed; 403 AA.
AC A0A174GVL9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN Name=sufS {ECO:0000313|EMBL:CUO66772.1};
GN ORFNames=ERS852494_00462 {ECO:0000313|EMBL:CUO66772.1};
OS Bacteroides caccae.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=47678 {ECO:0000313|EMBL:CUO66772.1, ECO:0000313|Proteomes:UP000095657};
RN [1] {ECO:0000313|EMBL:CUO66772.1, ECO:0000313|Proteomes:UP000095657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2789STDY5834880 {ECO:0000313|EMBL:CUO66772.1,
RC ECO:0000313|Proteomes:UP000095657};
RG Pathogen Informatics;
RL Submitted (SEP-2015) 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. Csd subfamily.
CC {ECO:0000256|ARBA:ARBA00010447}.
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DR EMBL; CZAI01000001; CUO66772.1; -; Genomic_DNA.
DR RefSeq; WP_055170056.1; NZ_CZAI01000001.1.
DR AlphaFoldDB; A0A174GVL9; -.
DR STRING; 47678.ERS852494_00462; -.
DR Proteomes; UP000095657; 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; IPR016454; Cysteine_dSase.
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 PIRSF; PIRSF005572; NifS; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000095657};
KW Transferase {ECO:0000313|EMBL:CUO66772.1}.
FT DOMAIN 23..392
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 403 AA; 44887 MW; 9280F46E652BE9E1 CRC64;
MDIQKIREDF PILSRTVYGK PLVYFDNGAT TQKPRLVVDA LVDEYYSVNA NVHRGVHYLS
QQATELHEAS RETVRQFINA RSTSEVVFTR GTTESINLLV SSFGDEFMQE GDEVILSVME
HHSNIVPWQL LAARKGIAIK VIPMNDKGEL LLDEYEKLFS ERTKIVSVVH VSNVLGTVNP
VKEMIATAHA HGVPCLIDAA QSIPHMKVDV QDLDADFLVF SAHKIYGPTG VGVLYGKEEW
LDRLPPYQGG GEMIQHVSFE KTTFNELPFK FEAGTPDYIG TTGLARALDY VNGIGLEQIA
AHEHELTTYA LQRLKEIPTM RIFGEVADHG AVISFLVGDI HHFDLGTLLD RLGIAVRTGH
HCAQPLMQRL GIEGTVRASF AMYNTKSEID ILVAGIERVS KMF
//
