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Database: UniProt
Entry: A0A0D2I552_9EURO
LinkDB: A0A0D2I552_9EURO
Original site: A0A0D2I552_9EURO 
ID   A0A0D2I552_9EURO        Unreviewed;       515 AA.
AC   A0A0D2I552;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=cysteine desulfurase {ECO:0000256|ARBA:ARBA00012239};
DE            EC=2.8.1.7 {ECO:0000256|ARBA:ARBA00012239};
GN   ORFNames=Z520_11974 {ECO:0000313|EMBL:KIX92366.1};
OS   Fonsecaea multimorphosa CBS 102226.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIX92366.1, ECO:0000313|Proteomes:UP000053411};
RN   [1] {ECO:0000313|EMBL:KIX92366.1, ECO:0000313|Proteomes:UP000053411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 102226 {ECO:0000313|EMBL:KIX92366.1,
RC   ECO:0000313|Proteomes:UP000053411};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL   Submitted (JAN-2015) 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}.
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DR   EMBL; KN848106; KIX92366.1; -; Genomic_DNA.
DR   RefSeq; XP_016626489.1; XM_016782461.1.
DR   AlphaFoldDB; A0A0D2I552; -.
DR   STRING; 1442371.A0A0D2I552; -.
DR   GeneID; 27717720; -.
DR   VEuPathDB; FungiDB:Z520_11974; -.
DR   OrthoDB; 212394at2759; -.
DR   Proteomes; UP000053411; Unassembled WGS sequence.
DR   GO; GO:0031071; F:cysteine desulfurase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0044571; P:[2Fe-2S] cluster assembly; IEA:InterPro.
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   HAMAP; MF_00331; Cys_desulf_IscS; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR020578; Aminotrans_V_PyrdxlP_BS.
DR   InterPro; IPR010240; Cys_deSase_IscS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   NCBIfam; TIGR02006; IscS; 1.
DR   PANTHER; PTHR11601:SF34; CYSTEINE DESULFURASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11601; CYSTEINE DESULFURYLASE FAMILY MEMBER; 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   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:UP000053411}.
FT   DOMAIN          116..480
FT                   /note="Aminotransferase class V"
FT                   /evidence="ECO:0000259|Pfam:PF00266"
SQ   SEQUENCE   515 AA;  56292 MW;  5EACB65B49245C2D CRC64;
     MPGPTSSVIR QASRACTRGL SNNAILSPSR SGTASIASSR FVGRRSYVSE SRPANAQVAD
     VESAIKADQK KFIQESGNLP SQVKMPGTEI TADTMLSPQA GILKHATIMD QGTRPIYLDA
     QATTPVDPRV LDAMLPFLTG LFGNPHSRTH AYGWESEKAS EQAREHVAKL IGADPKEIIF
     TSGATESNNM SIKGVARFFG RSGKKKHIIT SQTEHKCVLD SCRHLQDEGF EVTYLPVDSS
     GLINLQQLEE AIRPETALVS IMTVNNEIGV IQPMKEIGQL CRSKKVYFHT DGAQAVGKIP
     ISVNDWNVDL MSISSHKIYG PKGIGACYVR RRPRVRLDPI ISGGGQERGL RSGTLAPHLV
     VGFGEACRIA KEEMEYDSKR INFLSKRLVD GLLAMEHTSL NGDPTRRYPG CVNVSFAYVE
     GESLLMALKD IALSSGSACT SASLEPSYVL RALGNSDESA HSSIRFGIGR FTTTSEIDYV
     LKAVRERVTF LRELSPLWEL VQEGIDLNTI EWSQH
//
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