ID   A0A1Y4NGD3_9FIRM        Unreviewed;       378 AA.
AC   A0A1Y4NGD3;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Cysteine desulfurase {ECO:0000313|EMBL:OUP79111.1};
GN   ORFNames=B5F09_00600 {ECO:0000313|EMBL:OUP79111.1};
OS   Erysipelatoclostridium sp. An173.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Coprobacillaceae; Thomasclavelia.
OX   NCBI_TaxID=1965571 {ECO:0000313|EMBL:OUP79111.1, ECO:0000313|Proteomes:UP000196550};
RN   [1] {ECO:0000313|Proteomes:UP000196550}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An173 {ECO:0000313|Proteomes:UP000196550};
RA   Medvecky M., Cejkova D., Polansky O., Karasova D., Kubasova T., Cizek A.,
RA   Rychlik I.;
RT   "Function of individual gut microbiota members based on whole genome
RT   sequencing of pure cultures obtained from chicken caecum.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:OUP79111.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; NFKR01000001; OUP79111.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y4NGD3; -.
DR   Proteomes; UP000196550; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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:SF50; CYSTEINE DESULFURASE ISCS 2-RELATED; 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   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196550}.
FT   DOMAIN          2..363
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   378 AA;  42968 MW;  9AED3FD82F837717 CRC64;
     MIYLDYVATT PLNQDVLNTY HNLLSKYFYN ADSMYDKGIE VNRLMEHSRK LISDYLNVKE
     DEVIFTSCGS EANNMAIKGV AFQYQNRGKH IITTAIEHSS VYETCKELEE VFGFEVTYLP
     VDNRGCISLE QLENSIRDDT ILVSIMYVNN EIGVINPIEK IKKIVKKHDR VKLHFDMVQA
     LGKLPIDLND VDLASFSAHK IYGLKGSGLL FKRRSTTIVP LISGGQQEFG LRGGTSNGCT
     NIVFAKTLRL ALENFDKKSA HIKKINQYCR QCLKEIDGVV INSDEKVCID TIINFSCLGY
     KPEVILHDLE TKEIYLSTRS ACSSKTSNIS RIMKQLNLDE AISSSALRIS FSEHTSKEDI
     DKFCYYLQDS MARLKKQR
//