ID B2TRV5_CLOBB Unreviewed; 379 AA.
AC B2TRV5; U4PHJ3;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN OrderedLocusNames=CLL_A2340 {ECO:0000313|EMBL:ACD22865.1};
OS Clostridium botulinum (strain Eklund 17B / Type B).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=935198 {ECO:0000313|EMBL:ACD22865.1, ECO:0000313|Proteomes:UP000001195};
RN [1] {ECO:0000313|Proteomes:UP000001195}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Eklund 17B / Type B {ECO:0000313|Proteomes:UP000001195};
RA Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA Smith T.J., Sutton G., Brettin T.S.;
RT "Complete sequence of Clostridium botulinum strain Eklund.";
RL Submitted (APR-2008) 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 ECO:0000256|RuleBase:RU004504};
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; CP001056; ACD22865.1; -; Genomic_DNA.
DR AlphaFoldDB; B2TRV5; -.
DR KEGG; cbk:CLL_A2340; -.
DR PATRIC; fig|935198.13.peg.2297; -.
DR HOGENOM; CLU_003433_2_4_9; -.
DR Proteomes; UP000001195; Chromosome.
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; IPR010969; Cys_dSase-rel_unknwn_funct.
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; TIGR01977; am_tr_V_EF2568; 1.
DR PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR PANTHER; PTHR43586:SF4; ISOPENICILLIN N EPIMERASE; 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 Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898}.
FT DOMAIN 2..368
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 379 AA; 41758 MW; C64F42C12B2C68CA CRC64;
MIYLDNAATS FPKPSQVYEE VLNCMRNYAA NPGRGSYEIS IKAALKIMET REEICQLFNI
PSPFNLIFTC NATEALNIGI KGVLKRGDHV ISTMIEHNSV LRPLHSLSED GVEVTLVSVD
KAGYVNIKDI KEEIKESTKM IIINHASNVL GSIQDIKNIG NLSKSKGIIF MVDASQSAGV
IPIDVERDNI DLLAFSGHKG LLGPQGTGGL FIRNGIKLKN FREGGTGSNS HFMIQPDFMP
DQFESGTLNI PGIAGLCEGV KFIKKVGIRT IEKHEEELMS YLLKELKKLS YIKIYGSNSV
KQRSSVISFN VEGVDASIVG EQLNEEGIAV RTGYHCAPLI HDVIDTEYAG TVRVSPGYFN
TLDDIDKLLV TIMKIYKVR
//
