NFU1_YEAST
ID NFU1_YEAST Reviewed; 256 AA.
AC P32860; D6VXP6;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=NifU-like protein, mitochondrial;
DE Flags: Precursor;
GN Name=NFU1; Synonyms=NUB1; OrderedLocusNames=YKL040C; ORFNames=YKL253;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8154189; DOI=10.1002/yea.320091212;
RA Purnelle B., Tettelin H., van Dyck L., Skala J., Goffeau A.;
RT "The sequence of a 17.5 kb DNA fragment on the left arm of yeast chromosome
RT XI identifies the protein kinase gene ELM1, the DNA primase gene PRI2, a
RT new gene encoding a putative histone and seven new open reading frames.";
RL Yeast 9:1379-1384(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8196765; DOI=10.1038/369371a0;
RA Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V.,
RA Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P.,
RA Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L.,
RA Daignan-Fornier B., del Rey F., Dion C., Domdey H., Duesterhoeft A.,
RA Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H.,
RA Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L.,
RA Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M.,
RA Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H.,
RA Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J.,
RA Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H.,
RA Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J.,
RA Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S.,
RA Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F.,
RA Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R.,
RA Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W.,
RA Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M.,
RA Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C.,
RA Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H.,
RA Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L.,
RA van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S.,
RA von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M.,
RA Becker I., Mewes H.-W.;
RT "Complete DNA sequence of yeast chromosome XI.";
RL Nature 369:371-378(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-229.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=1481573; DOI=10.1002/yea.320081108;
RA Purnelle B., Skala J., van Dyck L., Goffeau A.;
RT "The sequence of a 12 kb fragment on the left arm of yeast chromosome XI
RT reveals five new open reading frames, including a zinc finger protein and a
RT homolog of the UDP-glucose pyrophosphorylase from potato.";
RL Yeast 8:977-986(1992).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10468587; DOI=10.1073/pnas.96.18.10206;
RA Schilke B., Voisine C., Beinert H., Craig E.;
RT "Evidence for a conserved system for iron metabolism in the mitochondria of
RT Saccharomyces cerevisiae.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:10206-10211(1999).
RN [7]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH BOL3, SUBUNIT, DOMAIN, AND
RP MUTAGENESIS OF GLY-194 AND 196-CYS--CYS-199.
RX PubMed=27532773; DOI=10.7554/elife.15991;
RA Melber A., Na U., Vashisht A., Weiler B.D., Lill R., Wohlschlegel J.A.,
RA Winge D.R.;
RT "Role of Nfu1 and Bol3 in iron-sulfur cluster transfer to mitochondrial
RT clients.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: Involved in iron homeostasis within the mitochondrion where
CC it is involved in the assembly of iron-sulfur proteins
CC (PubMed:10468587, PubMed:27532773). Together with BOL3, required during
CC the last step of iron-sulfur protein assembly when the iron-sulfur
CC cluster is inserted into the target protein (PubMed:27532773). Required
CC for protecting iron sulfur clusters from oxidative damage
CC (PubMed:27532773). {ECO:0000269|PubMed:10468587,
CC ECO:0000269|PubMed:27532773}.
CC -!- SUBUNIT: Homodimer; in absence of BOL3, probably bridged by an iron-
CC sulfure cluster (PubMed:27532773). Interacts with BOL3
CC (PubMed:27532773). Interacts with apo-target proteins, such as ACO1,
CC LYS4, ACO2 and SDH2 (PubMed:27532773). {ECO:0000269|PubMed:27532773}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:10468587}.
CC -!- DOMAIN: The CxxC motif may bind a [4Fe-4S] cluster.
CC {ECO:0000305|PubMed:27532773}.
CC -!- DISRUPTION PHENOTYPE: Cells are impaired in growth on synthetic
CC complete medium with acetate as a carbon source due to defects in
CC mitochondrial [4Fe-4S] cluster formation.
CC {ECO:0000269|PubMed:27532773}.
CC -!- MISCELLANEOUS: Present with 11300 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the NifU family. {ECO:0000305}.
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DR EMBL; X71621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z28040; CAA81875.1; -; Genomic_DNA.
DR EMBL; AY557904; AAS56230.1; -; Genomic_DNA.
DR EMBL; X69584; CAA49299.1; -; Genomic_DNA.
DR EMBL; BK006944; DAA09116.1; -; Genomic_DNA.
DR PIR; S37861; S37861.
DR RefSeq; NP_012884.3; NM_001179606.3.
DR PDB; 2LTL; NMR; -; A=17-124.
DR PDBsum; 2LTL; -.
DR AlphaFoldDB; P32860; -.
DR BMRB; P32860; -.
DR SMR; P32860; -.
DR BioGRID; 34092; 206.
DR IntAct; P32860; 2.
DR MINT; P32860; -.
DR STRING; 4932.YKL040C; -.
DR iPTMnet; P32860; -.
DR MaxQB; P32860; -.
DR PaxDb; P32860; -.
DR PRIDE; P32860; -.
DR DNASU; 853826; -.
DR EnsemblFungi; YKL040C_mRNA; YKL040C; YKL040C.
DR GeneID; 853826; -.
DR KEGG; sce:YKL040C; -.
DR SGD; S000001523; NFU1.
DR VEuPathDB; FungiDB:YKL040C; -.
DR eggNOG; KOG2358; Eukaryota.
DR GeneTree; ENSGT00390000011296; -.
DR HOGENOM; CLU_060555_0_2_1; -.
DR InParanoid; P32860; -.
DR OMA; GDIQYRG; -.
DR BioCyc; YEAST:G3O-31841-MON; -.
DR PRO; PR:P32860; -.
DR Proteomes; UP000002311; Chromosome XI.
DR RNAct; P32860; protein.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central.
DR GO; GO:0005506; F:iron ion binding; IBA:GO_Central.
DR GO; GO:0006880; P:intracellular sequestering of iron ion; IMP:SGD.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:SGD.
DR GO; GO:0106035; P:protein maturation by [4Fe-4S] cluster transfer; IMP:SGD.
DR GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IMP:SGD.
DR Gene3D; 3.30.1370.70; -; 1.
DR Gene3D; 3.30.300.130; -; 1.
DR InterPro; IPR034904; FSCA_dom_sf.
DR InterPro; IPR014824; Nfu/NifU_N.
DR InterPro; IPR036498; Nfu/NifU_N_sf.
DR InterPro; IPR035433; NFU1-like.
DR InterPro; IPR001075; NIF_FeS_clus_asmbl_NifU_C.
DR Pfam; PF08712; Nfu_N; 1.
DR Pfam; PF01106; NifU; 1.
DR PIRSF; PIRSF036773; HIRIP5; 1.
DR SMART; SM00932; Nfu_N; 1.
DR SUPFAM; SSF110836; SSF110836; 1.
DR SUPFAM; SSF117916; SSF117916; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Mitochondrion; Reference proteome; Transit peptide.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN ?..256
FT /note="NifU-like protein, mitochondrial"
FT /id="PRO_0000019702"
FT MOTIF 196..199
FT /note="CxxC motif"
FT /evidence="ECO:0000305|PubMed:27532773"
FT MUTAGEN 194
FT /note="G->C: Dominant negative mutant; cells show a severe
FT synthetic sick phenotype on glycerol/lactate medium."
FT /evidence="ECO:0000269|PubMed:27532773"
FT MUTAGEN 196..199
FT /note="CTSC->ATSA: Loss of function. Abolished
FT homodimerization."
FT /evidence="ECO:0000269|PubMed:27532773"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:2LTL"
FT STRAND 32..39
FT /evidence="ECO:0007829|PDB:2LTL"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:2LTL"
FT HELIX 60..65
FT /evidence="ECO:0007829|PDB:2LTL"
FT HELIX 67..75
FT /evidence="ECO:0007829|PDB:2LTL"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:2LTL"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:2LTL"
FT HELIX 99..116
FT /evidence="ECO:0007829|PDB:2LTL"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:2LTL"
SQ SEQUENCE 256 AA; 29174 MW; 4EF11EFD9C438BB5 CRC64;
MFKSVAKLGK SPIFYLNSQR LIHIKTLTTP NENALKFLST DGEMLQTRGS KSIVIKNTDE
NLINHSKLAQ QIFLQCPGVE SLMIGDDFLT INKDRMVHWN SIKPEIIDLL TKQLAYGEDV
ISKEFHAVQE EEGEGGYKIN MPKFELTEED EEVSELIEEL IDTRIRPAIL EDGGDIDYRG
WDPKTGTVYL RLQGACTSCS SSEVTLKYGI ESMLKHYVDE VKEVIQIMDP EQEIALKEFD
KLEKKLESSK NTSHEK
