ID A0A0P8WBR7_9CLOT Unreviewed; 447 AA.
AC A0A0P8WBR7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN Name=sufS_1 {ECO:0000313|EMBL:KPU46091.1};
GN ORFNames=OXPF_02010 {ECO:0000313|EMBL:KPU46091.1};
OS Oxobacter pfennigii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Oxobacter.
OX NCBI_TaxID=36849 {ECO:0000313|EMBL:KPU46091.1, ECO:0000313|Proteomes:UP000050326};
RN [1] {ECO:0000313|EMBL:KPU46091.1, ECO:0000313|Proteomes:UP000050326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3222 {ECO:0000313|EMBL:KPU46091.1,
RC ECO:0000313|Proteomes:UP000050326};
RA Poehlein A., Bengelsdorf F.R., Schiel-Bengelsdorf B., Duerre P., Daniel R.;
RT "Genome sequence of Oxobacter pfennigii DSM 3222.";
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 ECO:0000256|RuleBase:RU004504};
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. Csd subfamily.
CC {ECO:0000256|ARBA:ARBA00010447}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPU46091.1}.
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DR EMBL; LKET01000014; KPU46091.1; -; Genomic_DNA.
DR RefSeq; WP_054873356.1; NZ_LKET01000014.1.
DR AlphaFoldDB; A0A0P8WBR7; -.
DR STRING; 36849.OXPF_02010; -.
DR PATRIC; fig|36849.3.peg.222; -.
DR OrthoDB; 9804366at2; -.
DR Proteomes; UP000050326; Unassembled WGS sequence.
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:UP000050326};
KW Transferase {ECO:0000313|EMBL:KPU46091.1}.
FT DOMAIN 32..421
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 447 AA; 50346 MW; 971960A5DEE2575D CRC64;
MYFGNLDKGY RSLIMGADTK VPIENGRFVT AINFDNAATT PPFVSVINEV NKFAPWYSSV
HRGSGYKSRL SSDLFESARL RVLNFVNADP EKYTAIFVKN TTEALNKLSY CFYNNHKDCV
ILSSYMEHHS NDLPWRDKFK VEYIDITEEG RLQVSDLEKR LIKHKGKVKL VTITGASNVT
GYKNPIHEIA ALSHKYGAQI CVDGAQLIPH SSIDMMPHTP LENIDFLAFS AHKMYAPFGT
GVLIGPKDMF ERGDPDYKGG GTVKIVTKDF VIWDEAPYRE EAGSPNIIGV VALLAAINTL
EAVSMENIES YEQELTGYAA EKIRHIPDIT VYGDSYSKDD KVGIISFNIK GLHHEIVAEA
LSREVGIAVR NGCFCAQPYI QKILNLTSGD IKNIIDNAYF PRPGMVRISF GLYNSFEEID
KAINALQWIT AHRYRYTEKY ASFRRSR
//
