ID C9XZI5_CROTZ Unreviewed; 401 AA.
AC C9XZI5;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN Name=csdA {ECO:0000313|EMBL:CBA33335.1};
GN OrderedLocusNames=Ctu_33610 {ECO:0000313|EMBL:CBA33335.1};
OS Cronobacter turicensis (strain DSM 18703 / CCUG 55852 / LMG 23827 / z3032).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=693216 {ECO:0000313|EMBL:CBA33335.1, ECO:0000313|Proteomes:UP000002069};
RN [1] {ECO:0000313|Proteomes:UP000002069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18703 / CCUG 55852 / LMG 23827 / z3032
RC {ECO:0000313|Proteomes:UP000002069};
RX PubMed=21037008; DOI=10.1128/JB.01162-10;
RA Stephan R., Lehner A., Tischler P., Rattei T.;
RT "Complete genome sequence of Cronobacter turicensis LMG 23827, a food-borne
RT pathogen causing deaths in neonates.";
RL J. Bacteriol. 193:309-310(2011).
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; FN543093; CBA33335.1; -; Genomic_DNA.
DR AlphaFoldDB; C9XZI5; -.
DR KEGG; ctu:CTU_33610; -.
DR PATRIC; fig|693216.3.peg.3182; -.
DR HOGENOM; CLU_003433_2_5_6; -.
DR Proteomes; UP000002069; Chromosome.
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 GO; GO:0016226; P:iron-sulfur cluster assembly; 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; IPR022471; Cys_desulphurase_CdsA.
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; TIGR03392; FeS_syn_CsdA; 1.
DR PANTHER; PTHR43586; CYSTEINE DESULFURASE; 1.
DR PANTHER; PTHR43586:SF26; CYSTEINE DESULFURASE CSDA; 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};
KW Transferase {ECO:0000313|EMBL:CBA33335.1}.
FT DOMAIN 21..388
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 401 AA; 42757 MW; 7CB027999BBC85E3 CRC64;
MKVFSPAHFR AQFPALRDAG VYLDSAATAL KPQPVIEASQ QFYSLSAGNV HRSQFAEARR
LTERYEAARG SVASLLNAPD SRDIVWTRGT TESINIIAQC YARPRLKPGD EIIVSEAEHH
ANLVPWLMVA EQTGAKVVKL PLGADRLPDL ALLPTLIKER TFLLALGQMS NVTGGCPDLA
DAIAKAHVAG AVVVVDGAQG VVHCPPDVQQ LDIDFYAFSG HKLYGPTGIG VLYGKTDLLA
QMSPWLGGGK MVTEVTFDGF KTQPVPYRFE AGTPNVAGVT GLSAALAWLE NIDLAKAESY
SRGLATLAEA ELAKRPGFRS FRCQDSSLLA FDFAGVHHSD LVTLLAESGI ALRAGQHCAQ
PLLAALGVSG TLRASFAPYN TQGDVEALIA AIDRALDILV D
//
