NFS1_ASHGO
ID NFS1_ASHGO Reviewed; 490 AA.
AC O60028;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Cysteine desulfurase, mitochondrial {ECO:0000250|UniProtKB:P25374};
DE EC=2.8.1.7 {ECO:0000250|UniProtKB:P25374};
DE AltName: Full=tRNA-splicing protein SPL1 {ECO:0000250|UniProtKB:P25374};
DE Flags: Precursor;
GN Name=NFS1 {ECO:0000250|UniProtKB:P25374};
GN Synonyms=SPL1 {ECO:0000250|UniProtKB:P25374}; OrderedLocusNames=AAL013W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RA Mohr C., Philippsen P.;
RT "Isolation of the Ashbya gossypii LEU2 gene and its use as a marker gene in
RT transformation experiments.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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. Plays a role in both tRNA-processing and mitochondrial
CC metabolism. Involved in the 2-thio-modification of both 5-
CC carboxymethylaminomethyl-2-thiouridine in mitochondrial tRNAs and 5-
CC methoxycarbonylmethyl-2-thiouridine (mcm5s2U) in cytoplasmic tRNAs.
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}.
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DR EMBL; AJ006406; CAA07007.1; -; Genomic_DNA.
DR EMBL; AE016814; AAS50353.1; -; Genomic_DNA.
DR RefSeq; NP_982529.1; NM_207882.1.
DR AlphaFoldDB; O60028; -.
DR SMR; O60028; -.
DR STRING; 33169.AAS50353; -.
DR EnsemblFungi; AAS50353; AAS50353; AGOS_AAL013W.
DR GeneID; 4618565; -.
DR KEGG; ago:AGOS_AAL013W; -.
DR eggNOG; KOG1549; Eukaryota.
DR HOGENOM; CLU_003433_0_2_1; -.
DR InParanoid; O60028; -.
DR OMA; KGLYWAR; -.
DR Proteomes; UP000000591; Chromosome I.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:1990221; C:L-cysteine desulfurase complex; IEA:EnsemblFungi.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031071; F:cysteine desulfurase activity; IBA:GO_Central.
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:0006879; P:cellular iron ion homeostasis; IEA:EnsemblFungi.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IBA:GO_Central.
DR GO; GO:0070903; P:mitochondrial tRNA thio-modification; IEA:EnsemblFungi.
DR GO; GO:0002143; P:tRNA wobble position uridine thiolation; IEA:EnsemblFungi.
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.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..490
FT /note="Cysteine desulfurase, mitochondrial"
FT /id="PRO_0000001300"
FT ACT_SITE 414
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0A6B7"
FT BINDING 161..162
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 241
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O29689"
FT BINDING 269
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 289..291
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 329
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 414
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 292
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
SQ SEQUENCE 490 AA; 54436 MW; FDA56512E59365B7 CRC64;
MLRQVLRRSL SDSRRPLRSV GSISCSARAS GIGMRAYSSQ IFKEGMQLET HTDIQSAARE
QAQERMGSEA LASNNSVLKH AYQESVDHGT RPIYLDMQAT TPTDPRVVDT MLKFYTGLYG
NPHSNTHSYG WETSQEVEKA RKNVADVIKA DPKEIIFTSG ATESNNMALK GVARFYKKRK
NHIITTRTEH KCVLEAARSM KDEGFDVTFL NVNEDGLVSL EELEQAIRPE TSLVSVMSVN
NEIGVVQPIK EIGAICRRHK VFFHSDAAQA YGKIPIDVDE MNIDLLSISS HKIYGPKGIG
ALYVRRRPRV RMEPLLSGGG QERGFRSGTL PPPLVVGLGH AAKLMVEEYE YDSAHVRRLS
DRLLKGLLSI EQTTLNGSAD HRYPGCVNVS FAFVEGESLL MALRDIALSS GSACTSASLE
PSYVLHAIGR DDALAHSSIR FGIGRFTTEA EVDYVIKAIT ERVEFLRELS PLWEMYKDGI
DLNTIEWSGH
