ID A0A1I4C6P3_9FIRM Unreviewed; 383 AA.
AC A0A1I4C6P3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN ORFNames=SAMN05216390_103178 {ECO:0000313|EMBL:SFK76814.1};
OS Lachnospiraceae bacterium KH1T2.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1855374 {ECO:0000313|EMBL:SFK76814.1, ECO:0000313|Proteomes:UP000198626};
RN [1] {ECO:0000313|EMBL:SFK76814.1, ECO:0000313|Proteomes:UP000198626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH1T2 {ECO:0000313|EMBL:SFK76814.1,
RC ECO:0000313|Proteomes:UP000198626};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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. NifS/IscS subfamily.
CC {ECO:0000256|ARBA:ARBA00006490}.
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DR EMBL; FOSY01000003; SFK76814.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4C6P3; -.
DR STRING; 1855374.SAMN05216390_103178; -.
DR OrthoDB; 9808002at2; -.
DR Proteomes; UP000198626; Unassembled WGS sequence.
DR GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.10.260.50; -; 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; IPR016454; Cysteine_dSase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR11601:SF34; CYSTEINE DESULFURASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11601; CYSTEINE DESULFURYLASE FAMILY MEMBER; 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 Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000198626}.
FT DOMAIN 4..364
FT /note="Aminotransferase class V"
FT /evidence="ECO:0000259|Pfam:PF00266"
SQ SEQUENCE 383 AA; 42150 MW; F6D09A1FA39CD954 CRC64;
MECYLDNSAT TRVLPEAAEL MNKIFLEDYG NPSSLHNKGF DAEKYIRSAR DSFASFLKCG
KNDIIFTSGG TESNNTAILG AAIHYGSRGH HMITTRIEHA AVSEPMKFLE SKGWQIDYLD
VDSTGRVSLD QLKELLRKDT VLVSVMHVNN EIGTIQPIAE IGELIHNTAP DCLFHVDDIQ
GFGKLPLIPS KLHIDLLSAS SHKIHGPKGV GLLYVSPRTH ISPIIFGGGH QNGMRSGTEN
VPGVAGFALA ASEMYKHMDE NHKHFEELHE YFVSEISQLE DVTINGSKEF GAPYIISLTV
KNVRAEVLLH ALEDKGIYVS AGSACSSNKP SISATLKAID VPRYALDSTV RLSFSAHTTM
EELEYAINAL KELVPTLRKF TRK
//