NFS1_CANMA
ID NFS1_CANMA Reviewed; 484 AA.
AC P87187; P87188; P87189;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 95.
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:0000303|PubMed:9544248};
DE Flags: Precursor;
GN Name=SPL1 {ECO:0000303|PubMed:9544248};
OS Candida maltosa (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=5479;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CHAU1, and L4;
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).
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; AF000115; AAC49935.1; -; Genomic_DNA.
DR EMBL; AF000116; AAC49936.1; -; Genomic_DNA.
DR EMBL; AF000117; AAC49937.1; -; Genomic_DNA.
DR EMBL; AF000118; AAC49938.1; -; Genomic_DNA.
DR AlphaFoldDB; P87187; -.
DR SMR; P87187; -.
DR PRIDE; P87187; -.
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 PROSITE; PS00595; AA_TRANSFER_CLASS_5; 1.
PE 3: Inferred from homology;
KW Iron; Iron-sulfur; Metal-binding; Mitochondrion; Pyridoxal phosphate;
KW Transferase; Transit peptide; tRNA processing.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..484
FT /note="Cysteine desulfurase, mitochondrial"
FT /id="PRO_0000001302"
FT REGION 29..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 408
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0A6B7"
FT BINDING 153..154
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 233
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:O29689"
FT BINDING 261
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 281..283
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 321
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT BINDING 408
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 284
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P0A6B9"
FT VARIANT 374
FT /note="T -> A (in strain: CHAU1)"
FT CONFLICT 155
FT /note="E -> A (in Ref. 1; AAC49936)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="Missing (in Ref. 1; AAC49936)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 484 AA; 53124 MW; AAE3D2E33370CF8C CRC64;
MYKTVLKNSG RIQRNFIFRN VSSTLQRSLA TSASTSSSTT TSNAETGELH VSTPLDSPSV
HPPDGSSISL KSATRDASLF GTRPIYLDVQ ATTPVDPRVL DKMLEFYTGL YGNPHSSTHA
YGWETDKEVE KARGYIADVI NADPKEIIFT SGATETNNMA IKGVPRFYKK TKKHIITTQT
EHKCVLDSAR HMQDEGFDIT YLPVNSEGLI NLDDLKKAIR KDTVLVSVMA VNNEIGVIQP
LKEIGQICRE NKIFFHTDAA QAYGKIPIDV NEMNIDLLSI SSHKIYGPKG IGACYVRRRP
RVRLDPIITG GGQERGLRSG TLAPPLVAGF GEAARLMKQE SAFDKKHIEK LSTKLKNGLL
SIPSTQFNGC NNPTYQYPGC VNVSFAYIEG ESLLMALKDI ALSSGSACTS ASLEPSYVLH
ALGADDALAH SSIRFGIGRF TTEAEVDYVI QAINERVDFL RKMSPLWEMV QGGIDLNSIE
WSGH
