ID   NFS1_ENCCU              Reviewed;         432 AA.
AC   Q8SQS2;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Cysteine desulfurase, mitosomal {ECO:0000250|UniProtKB:P25374};
DE            EC=2.8.1.7 {ECO:0000250|UniProtKB:P25374};
GN   Name=NFS1 {ECO:0000250|UniProtKB:P25374}; OrderedLocusNames=ECU11_1770;
OS   Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC   Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC   Encephalitozoon.
OX   NCBI_TaxID=284813;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GB-M1;
RX   PubMed=11719806; DOI=10.1038/35106579;
RA   Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA   Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA   Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA   Vivares C.P.;
RT   "Genome sequence and gene compaction of the eukaryote parasite
RT   Encephalitozoon cuniculi.";
RL   Nature 414:450-453(2001).
RN   [2]
RP   SUBCELLULAR LOCATION, AND FUNCTION.
RX   PubMed=18311129; DOI=10.1038/nature06606;
RA   Goldberg A.V., Molik S., Tsaousis A.D., Neumann K., Kuhnke G., Delbac F.,
RA   Vivares C.P., Hirt R.P., Lill R., Embley T.M.;
RT   "Localization and functionality of microsporidian iron-sulphur cluster
RT   assembly proteins.";
RL   Nature 452:624-628(2008).
CC   -!- FUNCTION: Catalyzes the removal of elemental sulfur from cysteine to
CC       produce alanine. It supplies the inorganic sulfur for iron-sulfur (Fe-
CC       S) clusters in mitosomes. {ECO:0000269|PubMed:18311129}.
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: Mitosome {ECO:0000269|PubMed:18311129}.
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. NifS/IscS subfamily. {ECO:0000305}.
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DR   EMBL; AL590450; CAD26087.1; -; Genomic_DNA.
DR   RefSeq; NP_586483.1; NM_001042316.1.
DR   AlphaFoldDB; Q8SQS2; -.
DR   SMR; Q8SQS2; -.
DR   STRING; 284813.Q8SQS2; -.
DR   GeneID; 860137; -.
DR   KEGG; ecu:ECU11_1770; -.
DR   VEuPathDB; MicrosporidiaDB:ECU11_1770; -.
DR   HOGENOM; CLU_003433_0_2_1; -.
DR   InParanoid; Q8SQS2; -.
DR   OMA; KGLYWAR; -.
DR   OrthoDB; 664730at2759; -.
DR   Proteomes; UP000000819; Chromosome XI.
DR   GO; GO:0032047; C:mitosome; 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   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; 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; PTHR11601:SF34; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   PIRSF; PIRSF005572; NifS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE   3: Inferred from homology;
KW   Iron; Iron-sulfur; Metal-binding; Mitosome; Pyridoxal phosphate;
KW   Reference proteome; Transferase.
FT   CHAIN           1..432
FT                   /note="Cysteine desulfurase, mitosomal"
FT                   /id="PRO_0000382928"
FT   ACT_SITE        357
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B7"
FT   BINDING         102..103
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT   BINDING         212
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT   BINDING         232..234
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT   BINDING         272
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT   BINDING         357
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         235
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0A6B9"
SQ   SEQUENCE   432 AA;  47016 MW;  3C414E5CA3FCEF5E CRC64;
     MIGGLKSCIE QPSLPKPSTL LPQDKACDTG GKRIFLDVQS TTPVDPRVLD AMLPFYTTVF
     GNPHSRTHRY GWQAEAAVEK ARSQVASLIG CDPKEIIFTS GATESNNLAL KGVSGFKLKE
     GKAAHIITLQ TEHKCILDTC RNLEENGVEV TYLPVGNDGV VDIDDVKKSI KENTVLVSIG
     AVNSEIGTVQ PLKEIGMLCK ERGVLFHTDA AQGVGKIQID VNEMNIDLLS MCAHKIYGPK
     GIGALYVRRR PRVRMVPLIN GGGQERGLRS GTVASPLVVG FGKAAEICSK EMKRDFEHIK
     ELSKKLKNMF KKNIEGVIIN GSEKGFPGCV NVSFPFVEGE SLLMHLKDIA LSSGSACTSA
     SLEPSYVLRA LGRDDELAHS SIRFGIGRFT MAKEIDIVAN KTVEAVQKLR EMSPLYEMVK
     EGIDLSKISW TS