ID F4CJD0_PSEUX Unreviewed; 473 AA.
AC F4CJD0;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN OrderedLocusNames=Psed_2680 {ECO:0000313|EMBL:AEA24882.1};
OS Pseudonocardia dioxanivorans (strain ATCC 55486 / DSM 44775 / JCM 13855 /
OS CB1190).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=675635 {ECO:0000313|EMBL:AEA24882.1, ECO:0000313|Proteomes:UP000007809};
RN [1] {ECO:0000313|EMBL:AEA24882.1, ECO:0000313|Proteomes:UP000007809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55486 / DSM 44775 / JCM 13855 / CB1190
RC {ECO:0000313|Proteomes:UP000007809};
RX PubMed=21725009; DOI=10.1128/JB.00415-11;
RA Sales C.M., Mahendra S., Grostern A., Parales R.E., Goodwin L.A., Woyke T.,
RA Nolan M., Lapidus A., Chertkov O., Ovchinnikova G., Sczyrba A.,
RA Alvarez-Cohen L.;
RT "Genome sequence of the 1,4-dioxane-degrading Pseudonocardia dioxanivorans
RT strain CB1190.";
RL J. Bacteriol. 193:4549-4550(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; CP002593; AEA24882.1; -; Genomic_DNA.
DR RefSeq; WP_013674806.1; NC_015312.1.
DR AlphaFoldDB; F4CJD0; -.
DR STRING; 675635.Psed_2680; -.
DR KEGG; pdx:Psed_2680; -.
DR eggNOG; COG0520; Bacteria.
DR HOGENOM; CLU_003433_2_0_11; -.
DR Proteomes; UP000007809; Chromosome.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
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 Reference proteome {ECO:0000313|Proteomes:UP000007809};
KW Transferase {ECO:0000313|EMBL:AEA24882.1}.
FT DOMAIN 54..421
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 473 AA; 48245 MW; C2417095EA9AEFF3 CRC64;
MSVVLQAARP TAPTVPADVA AHALPAPAAS CLPALVGTGL PVPLVDGTTV AHANLDLAAS
APALRSVADR VAALLPYHAS VHRGAGYAST VCTAALEWAR TTVGRFVGAR SDDVVVFTRN
TTDALNLLAG AVPGAVLCLD VEHHANLLAW RGGEHRVLRA AATVDATLAQ LRAALEARPT
ALVAITGASN VTGEVLPLAE IADLAHSHGA RLVVDAAQLA PHRRVDIAAT GIDYVALSGH
KLYAPYGTGA LVGRRDWLDV ATPYLAGGGA VVRVDAVGDG SPAEVTWTAA PHRHEAGTPN
VPGAVALATA CEALDAVIDE AAPAHERALS ERLDAGLADI PGVRTLRIWH DAPDRVGVHS
LTVDGYPAAL VAAYLSAEHG ISVRDGKFCA HPLLARLTGW AEGAVRASLG LGTTAADVDR
LLAALRTLVT DGPGVAYECV DGRWLPTADG RDTDPLGLGI GDEVTGAGRG CGH
//
