ID Q97FD5_CLOAB Unreviewed; 414 AA.
AC Q97FD5;
DT 01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN OrderedLocusNames=CA_C2805 {ECO:0000313|EMBL:AAK80749.1};
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562 {ECO:0000313|EMBL:AAK80749.1, ECO:0000313|Proteomes:UP000000814};
RN [1] {ECO:0000313|EMBL:AAK80749.1, ECO:0000313|Proteomes:UP000000814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
RC {ECO:0000313|Proteomes:UP000000814};
RX PubMed=11466286; DOI=10.1128/JB.183.16.4823-4838.2001;
RA Nolling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK80749.1; -; Genomic_DNA.
DR PIR; B97245; B97245.
DR RefSeq; NP_349409.1; NC_003030.1.
DR RefSeq; WP_010966090.1; NC_003030.1.
DR AlphaFoldDB; Q97FD5; -.
DR STRING; 272562.CA_C2805; -.
DR GeneID; 44999290; -.
DR KEGG; cac:CA_C2805; -.
DR PATRIC; fig|272562.8.peg.2992; -.
DR eggNOG; COG0520; Bacteria.
DR HOGENOM; CLU_003433_2_0_9; -.
DR OrthoDB; 9804366at2; -.
DR Proteomes; UP000000814; Chromosome.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; 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 Lyase {ECO:0000313|EMBL:AAK80749.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000814}.
FT DOMAIN 15..404
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 414 AA; 47085 MW; CE1DE3CF5A44FBB5 CRC64;
MDYRKYFEKL KSDYVYLDNA ATTPPLKSVM KKALEFLENY SSIHRGTGYL AKMSTDSYEN
SRRVIGEYLH ATKDDVVVFT ANTTDSINKF ALLYPFMGNE GVLISDIEHS SNMLPWFKNS
GRVKMFNTGK SNKINPYSIE EELYRNPQIK IVSICGASNL TGYLTPLRDI YKICKKYGVY
LLVDASQIAP HFKITLDDCD FIAFSGHKMY APFGAGVLAG RKDVLSHIGL APTGGGNIVY
IGKRGEVIYK EPPLSLEAGT PNGLGAVTVA EAMRVLNEDI GWENMNQHNK RINEIGYKYL
SDLSNIKLYY PKDQDIRINR TPTFVFDFKN VGTKVGCDIL KENKIGVRCG TFCLYRLIEK
VKNIDEYERK RLYRNYIVPN RELPERYSLV RASAGLMTTE EDFLRLRAAI KKVE
//
