NFS1_TRAHO
ID NFS1_TRAHO Reviewed; 441 AA.
AC B0YLW6; L7JZX4;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 53.
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}; ORFNames=THOM_0306;
OS Trachipleistophora hominis (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Pleistophoridae;
OC Trachipleistophora.
OX NCBI_TaxID=72359;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, FUNCTION, AND
RP INTERACTION WITH ISD11.
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23133373; DOI=10.1371/journal.ppat.1002979;
RA Heinz E., Williams T.A., Nakjang S., Noel C.J., Swan D.C., Goldberg A.V.,
RA Harris S.R., Weinmaier T., Markert S., Becher D., Bernhardt J., Dagan T.,
RA Hacker C., Lucocq J.M., Schweder T., Rattei T., Hall N., Hirt R.P.,
RA Embley T.M.;
RT "The genome of the obligate intracellular parasite Trachipleistophora
RT hominis: new insights into microsporidian genome dynamics and reductive
RT evolution.";
RL PLoS Pathog. 8:E1002979-E1002979(2012).
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 -!- SUBUNIT: Interacts with ISD11. {ECO:0000269|PubMed:18311129}.
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; EF571313; ABS58597.1; -; Genomic_DNA.
DR EMBL; JH993832; ELQ76591.1; -; Genomic_DNA.
DR AlphaFoldDB; B0YLW6; -.
DR SMR; B0YLW6; -.
DR STRING; 72359.B0YLW6; -.
DR EnsemblFungi; ELQ76591; ELQ76591; THOM_0306.
DR VEuPathDB; MicrosporidiaDB:THOM_0306; -.
DR HOGENOM; CLU_003433_0_2_1; -.
DR OMA; KGLYWAR; -.
DR Proteomes; UP000011185; Unassembled WGS sequence.
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 1: Evidence at protein level;
KW Iron; Iron-sulfur; Metal-binding; Mitosome; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..441
FT /note="Cysteine desulfurase, mitosomal"
FT /id="PRO_0000382929"
FT ACT_SITE 367
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0A6B7"
FT BINDING 107..108
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 189
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O29689"
FT BINDING 217
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 237..239
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 277
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 367
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 240
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
SQ SEQUENCE 441 AA; 48744 MW; A749533D79CCE73B CRC64;
MPLPNQIATS NVETKNFASL KRSDEPIAIA QASRTPAKIY FDFQATTPVD PRVLDAMLPY
FTKKYGNPHS RTHSFGWESE KAVETARKQV ADLIGAHEKE IIFTSGATES NNLAIKGAVD
WKAQDGNPVH VITTQVEHKC VLDSMRFLEE KGARVTYMKV NKDGVIDLEE LKRSISDDTV
LVSIMGVNNE IGTVQPLEEI GKICKERNVL FHCDAAQMFG KLKIDVNKMN IDLLSISGHK
IYGPKGVGAL YVRRRPRVRL VPLFSGGGQE RGLRSGTLPT PLIVGLGKAA AVCQEEMQRD
LSWIESLSKK LYTCLKENIP NVIKNGSLQT NPLRWFPGCL NLSFPHVEGE GLLMALKNIA
LSSGSACTSA SLEPSYVLRA LGNDDELAHS SIRFGIGRFT TPCEIKEVAK QTTSAVKKLR
DMSPLYEMEQ EGIDLKTIKW T
