ADRX_YEAST
ID ADRX_YEAST Reviewed; 172 AA.
AC Q12184; D6W3B9;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Adrenodoxin homolog, mitochondrial;
DE AltName: Full=Mitochondrial ferredoxin;
DE Flags: Precursor;
GN Name=YAH1; OrderedLocusNames=YPL252C;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169875;
RA Bussey H., Storms R.K., Ahmed A., Albermann K., Allen E., Ansorge W.,
RA Araujo R., Aparicio A., Barrell B.G., Badcock K., Benes V., Botstein D.,
RA Bowman S., Brueckner M., Carpenter J., Cherry J.M., Chung E.,
RA Churcher C.M., Coster F., Davis K., Davis R.W., Dietrich F.S., Delius H.,
RA DiPaolo T., Dubois E., Duesterhoeft A., Duncan M., Floeth M., Fortin N.,
RA Friesen J.D., Fritz C., Goffeau A., Hall J., Hebling U., Heumann K.,
RA Hilbert H., Hillier L.W., Hunicke-Smith S., Hyman R.W., Johnston M.,
RA Kalman S., Kleine K., Komp C., Kurdi O., Lashkari D., Lew H., Lin A.,
RA Lin D., Louis E.J., Marathe R., Messenguy F., Mewes H.-W., Mirtipati S.,
RA Moestl D., Mueller-Auer S., Namath A., Nentwich U., Oefner P., Pearson D.,
RA Petel F.X., Pohl T.M., Purnelle B., Rajandream M.A., Rechmann S.,
RA Rieger M., Riles L., Roberts D., Schaefer M., Scharfe M., Scherens B.,
RA Schramm S., Schroeder M., Sdicu A.-M., Tettelin H., Urrestarazu L.A.,
RA Ushinsky S., Vierendeels F., Vissers S., Voss H., Walsh S.V., Wambutt R.,
RA Wang Y., Wedler E., Wedler H., Winnett E., Zhong W.-W., Zollner A.,
RA Vo D.H., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.";
RL Nature 387:103-105(1997).
RN [2]
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 [3]
RP IDENTIFICATION, AND SUBCELLULAR LOCATION.
RX PubMed=10375636; DOI=10.1016/s0378-1119(99)00137-7;
RA Barros M.H., Nobrega F.G.;
RT "YAH1 of Saccharomyces cerevisiae: a new essential gene that codes for a
RT protein homologous to human adrenodoxin.";
RL Gene 233:197-203(1999).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10655482; DOI=10.1073/pnas.97.3.1050;
RA Lange H., Kaut A., Kispal G., Lill R.;
RT "A mitochondrial ferredoxin is essential for biogenesis of cellular iron-
RT sulfur proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:1050-1055(2000).
RN [5]
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).
CC -!- FUNCTION: Required for Fe-S cluster incorporation into mitochondrial
CC and cytosolic apoproteins. May be part of a novel electron transport
CC chain. {ECO:0000269|PubMed:10655482}.
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000269|PubMed:10375636, ECO:0000269|PubMed:10655482}.
CC -!- MISCELLANEOUS: Present with 14800 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the adrenodoxin/putidaredoxin family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z73608; CAA97975.1; -; Genomic_DNA.
DR EMBL; Z67751; CAA91592.1; -; Genomic_DNA.
DR EMBL; BK006949; DAA11185.1; -; Genomic_DNA.
DR PIR; S61012; S61012.
DR RefSeq; NP_015071.1; NM_001184066.1.
DR PDB; 2MJD; NMR; -; A=58-172.
DR PDB; 2MJE; NMR; -; A=58-172.
DR PDBsum; 2MJD; -.
DR PDBsum; 2MJE; -.
DR AlphaFoldDB; Q12184; -.
DR BMRB; Q12184; -.
DR SMR; Q12184; -.
DR BioGRID; 35911; 12.
DR ComplexPortal; CPX-392; Mitochondrial NIAUFX iron-sulfur cluster assembly complex.
DR DIP; DIP-5027N; -.
DR IntAct; Q12184; 2.
DR STRING; 4932.YPL252C; -.
DR MaxQB; Q12184; -.
DR PaxDb; Q12184; -.
DR PRIDE; Q12184; -.
DR EnsemblFungi; YPL252C_mRNA; YPL252C; YPL252C.
DR GeneID; 855824; -.
DR KEGG; sce:YPL252C; -.
DR SGD; S000006173; YAH1.
DR VEuPathDB; FungiDB:YPL252C; -.
DR eggNOG; KOG3309; Eukaryota.
DR GeneTree; ENSGT00940000161143; -.
DR HOGENOM; CLU_082632_0_2_1; -.
DR InParanoid; Q12184; -.
DR OMA; CQVIMTK; -.
DR BioCyc; MetaCyc:G3O-34137-MON; -.
DR BioCyc; YEAST:G3O-34137-MON; -.
DR Reactome; R-SCE-1362409; Mitochondrial iron-sulfur cluster biogenesis.
DR Reactome; R-SCE-2395516; Electron transport from NADPH to Ferredoxin.
DR PRO; PR:Q12184; -.
DR Proteomes; UP000002311; Chromosome XVI.
DR RNAct; Q12184; protein.
DR GO; GO:1990229; C:iron-sulfur cluster assembly complex; IC:ComplexPortal.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:InterPro.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016653; F:oxidoreductase activity, acting on NAD(P)H, heme protein as acceptor; IMP:SGD.
DR GO; GO:0022900; P:electron transport chain; IBA:GO_Central.
DR GO; GO:0006784; P:heme A biosynthetic process; IMP:SGD.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IDA:UniProtKB.
DR GO; GO:0140647; P:P450-containing electron transport chain; IEA:InterPro.
DR GO; GO:0051353; P:positive regulation of oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IMP:SGD.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR001055; Adrenodoxin.
DR InterPro; IPR018298; Adrenodoxin_Fe-S_BS.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR PANTHER; PTHR23426; PTHR23426; 1.
DR Pfam; PF00111; Fer2; 1.
DR PRINTS; PR00355; ADRENODOXIN.
DR SUPFAM; SSF54292; SSF54292; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00814; ADX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Electron transport; Iron; Iron-sulfur; Metal-binding;
KW Mitochondrion; Reference proteome; Transit peptide; Transport.
FT TRANSIT 1..?
FT /note="Mitochondrion"
FT CHAIN ?..172
FT /note="Adrenodoxin homolog, mitochondrial"
FT /id="PRO_0000000994"
FT DOMAIN 61..163
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 98
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 104
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 107
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 144
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:2MJD"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:2MJD"
FT HELIX 83..90
FT /evidence="ECO:0007829|PDB:2MJD"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:2MJD"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:2MJD"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:2MJD"
FT TURN 124..127
FT /evidence="ECO:0007829|PDB:2MJD"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:2MJD"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:2MJD"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:2MJD"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:2MJD"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:2MJE"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:2MJD"
SQ SEQUENCE 172 AA; 18932 MW; D7DB9CFACBED1BFC CRC64;
MLKIVTRAGH TARISNIAAH LLRTSPSLLT RTTTTTRFLP FSTSSFLNHG HLKKPKPGEE
LKITFILKDG SQKTYEVCEG ETILDIAQGH NLDMEGACGG SCACSTCHVI VDPDYYDALP
EPEDDENDML DLAYGLTETS RLGCQIKMSK DIDGIRVALP QMTRNVNNND FS
