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Database: UniProt
Entry: A0A1I4C6P3_9FIRM
LinkDB: A0A1I4C6P3_9FIRM
Original site: A0A1I4C6P3_9FIRM 
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
//
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