NFS1_CANAL
ID NFS1_CANAL Reviewed; 488 AA.
AC P87185; A0A1D8PQK2; Q3MPU0; Q5AFI7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 129.
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; Synonyms=SPL1 {ECO:0000303|PubMed:9544248};
GN OrderedLocusNames=CAALFM_C700390WA; ORFNames=CaJ7.0052, CaO19.7081;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9544248;
RX DOI=10.1002/(sici)1097-0061(199802)14:3<287::aid-yea213>3.0.co;2-u;
RA Plant E.P., Becher D., Poulter R.T.M.;
RT "The SPL1 tRNA splicing gene of Candida maltosa and Candida albicans.";
RL Yeast 14:287-295(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15937140; DOI=10.1534/genetics.104.034652;
RA Chibana H., Oka N., Nakayama H., Aoyama T., Magee B.B., Magee P.T.,
RA Mikami Y.;
RT "Sequence finishing and gene mapping for Candida albicans chromosome 7 and
RT syntenic analysis against the Saccharomyces cerevisiae genome.";
RL Genetics 170:1525-1537(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [6]
RP INDUCTION.
RX PubMed=15387822; DOI=10.1111/j.1365-2958.2004.04214.x;
RA Lan C.Y., Rodarte G., Murillo L.A., Jones T., Davis R.W., Dungan J.,
RA Newport G., Agabian N.;
RT "Regulatory networks affected by iron availability in Candida albicans.";
RL Mol. Microbiol. 53:1451-1469(2004).
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 -!- INDUCTION: Expression is up-regulated at high-iron conditions.
CC {ECO:0000269|PubMed:15387822}.
CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC aminotransferase family. NifS/IscS subfamily. {ECO:0000305}.
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DR EMBL; AF000120; AAC49940.1; -; Genomic_DNA.
DR EMBL; AP006852; BAE44570.1; -; Genomic_DNA.
DR EMBL; CP017629; AOW30418.1; -; Genomic_DNA.
DR RefSeq; XP_720372.1; XM_715279.1.
DR AlphaFoldDB; P87185; -.
DR SMR; P87185; -.
DR STRING; 237561.P87185; -.
DR GeneID; 3638035; -.
DR KEGG; cal:CAALFM_C700390WA; -.
DR CGD; CAL0000182012; SPL1.
DR VEuPathDB; FungiDB:C7_00390W_A; -.
DR eggNOG; KOG1549; Eukaryota.
DR HOGENOM; CLU_003433_0_2_1; -.
DR InParanoid; P87185; -.
DR OMA; KGLYWAR; -.
DR OrthoDB; 664730at2759; -.
DR Proteomes; UP000000559; Chromosome 7.
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:0004123; F:cystathionine gamma-lyase activity; NAS:CGD.
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 PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 2: Evidence at transcript level;
KW Iron; Iron-sulfur; Metal-binding; Mitochondrion; Pyridoxal phosphate;
KW Reference proteome; Transferase; Transit peptide; tRNA processing.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..488
FT /note="Cysteine desulfurase, mitochondrial"
FT /id="PRO_0000001301"
FT REGION 25..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 412
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0A6B7"
FT BINDING 157..158
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 237
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O29689"
FT BINDING 265
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 285..287
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 325
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 412
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 288
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
SQ SEQUENCE 488 AA; 53489 MW; C4A0693459EC3EB0 CRC64;
MYKSIFKTTG RLGKTVSSRN FVTTLPKPLA TSSSPATNAP NKTSNPKTGE LHVSTPVDTA
KISIEPPEGS SISLKSASRD ASLFGTRPIY LDVQATTPVD PRVLDKMLEF YTGLYGNPHS
STHAYGWETD KEVEKARTYI ADVINADPKE IIFTSGATET NNMAIKGVPR FYKKTKKHII
TTQTEHKCVL DSARHMQDEG FEVTYLPVSS EGLINLDDLK KAIRKDTVLV SIMAVNNEIG
VIQPLKEIGK ICRENKVFFH TDAAQAYGKI PIDVNEMNID LLSISSHKIY GPKGIGACYV
RRRPRVRLDP IITGGGQERG LRSGTLAPPL VAGFGEAARL MKQESSFDKR HIEKLSSKLK
NGLLSIPSTQ FNGCNDAKSQ YPGCVNVSFA YIEGESLLMA LKDIALSSGS ACTSASLEPS
YVLHALGADD ALAHSSIRFG IGRFTTEAEV DYVIQAINER VDFLRKMSPL WEMVQEGIDL
NTIEWSGH
