ID   NFS1_ARTBC              Reviewed;         503 AA.
AC   P0DN31; D4ANC7;
DT   11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT   11-NOV-2015, sequence version 1.
DT   03-AUG-2022, entry version 24.
DE   RecName: Full=Cysteine desulfurase, mitochondrial {ECO:0000250|UniProtKB:P25374};
DE            EC=2.8.1.7 {ECO:0000250|UniProtKB:P25374};
DE   Flags: Precursor;
GN   ORFNames=ARB_05732-2;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371;
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
CC   -!- FUNCTION: Catalyzes the removal of elemental sulfur from cysteine to
CC       produce alanine (By similarity). It supplies the inorganic sulfur for
CC       iron-sulfur (Fe-S) clusters (By similarity). Plays a role in both tRNA-
CC       processing and mitochondrial metabolism (By similarity). Involved in
CC       the 2-thio-modification of both 5-carboxymethylaminomethyl-2-
CC       thiouridine in mitochondrial tRNAs and 5-methoxycarbonylmethyl-2-
CC       thiouridine (mcm5s2U) in cytoplasmic tRNAs (By similarity).
CC       {ECO:0000250|UniProtKB:P25374}.
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:0000250|UniProtKB:P25374};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P0A6B9};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250|UniProtKB:P25374}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. NifS/IscS subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EFE35688.1; Type=Erroneous gene model prediction; Note=The predicted gene ARB_05732 has been split into 2 genes: ARB_05732-1 and ARB_05732-2.; Evidence={ECO:0000305};
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; ABSU01000003; EFE35688.1; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_003016333.1; XM_003016287.1.
DR   AlphaFoldDB; P0DN31; -.
DR   SMR; P0DN31; -.
DR   STRING; 663331.P0DN31; -.
DR   EnsemblFungi; EFE35688; EFE35688; ARB_05732.
DR   GeneID; 9521816; -.
DR   KEGG; abe:ARB_05732; -.
DR   eggNOG; KOG1549; Eukaryota.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
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   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 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   PANTHER; PTHR11601:SF34; PTHR11601:SF34; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR02006; IscS; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Iron; Iron-sulfur; Metal-binding; Mitochondrion; Pyridoxal phosphate;
KW   Reference proteome; Transferase; Transit peptide; tRNA processing.
FT   TRANSIT         1..27
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           28..503
FT                   /note="Cysteine desulfurase, mitochondrial"
FT                   /id="PRO_5003054138"
FT   REGION          34..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        427
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B7"
FT   BINDING         172..173
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT   BINDING         254
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:O29689"
FT   BINDING         282
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT   BINDING         302..304
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT   BINDING         342
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT   BINDING         427
FT                   /ligand="[2Fe-2S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:190135"
FT                   /note="via persulfide group"
FT                   /evidence="ECO:0000250|UniProtKB:O29689"
FT   MOD_RES         305
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
SQ   SEQUENCE   503 AA;  54691 MW;  B611C86109692AB7 CRC64;
     MSNIAPQVLR HASRACSRRL SLSASLVRPA YSARTVTGSG SGGRRYVSGS QRHNAQAQTT
     VESAVKTEQK ASVPGTAVTG DALANPSAGI LKQATIMDEG NRPIYLDMQA TTPTDPRVLD
     AMLPFLTGLY GNPHSRTHAY GWETEKATEQ ARSHVATLIG ADPKEIIFTS GATESNNMSI
     KGVARFFGRS GKKKHIITTQ TEHKCVLDSC RHLQDEGFEV TYLPVQSNGL IKIEDLEAAI
     RPETALVSIM TVNNEIGVIQ PMKEIGALCR SKKVFFHTDA AQAVGKIPVD VNEWNVDLMS
     ISGHKLYGPK GIGACYVRRR PRVRIDPLIT GGGQERGLRS GTLAPPLVVG FGEACRLAKE
     EMEYDSKRIS ALSQRLLTSL LALEHTTLNG DPNRHYPGCV NVSFAYVEGE SLLMALKDIA
     LSSGSACTSA SLEPSYVLRA LGNSDESAHS SIRFGIGRFT TESEIDYVIK AVKERVTFLR
     ELSPLWELVQ EGVDLNTIEW SQH