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Database: UniProt
Entry: E6ZZA7_SPORE
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ID   E6ZZA7_SPORE            Unreviewed;       274 AA.
AC   E6ZZA7;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   13-SEP-2023, entry version 55.
DE   RecName: Full=NADH-ubiquinone oxidoreductase chain 3 {ECO:0000256|ARBA:ARBA00021007, ECO:0000256|RuleBase:RU003640};
DE            EC=7.1.1.2 {ECO:0000256|RuleBase:RU003640};
GN   ORFNames=sr17110 {ECO:0000313|EMBL:CBQ72564.1};
OS   Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OG   Mitochondrion {ECO:0000313|EMBL:CBQ72564.1}.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX   NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ72564.1, ECO:0000313|Proteomes:UP000008867};
RN   [1] {ECO:0000313|EMBL:CBQ72564.1, ECO:0000313|Proteomes:UP000008867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX   PubMed=21148393; DOI=10.1126/science.1195330;
RA   Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA   Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA   Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA   Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA   Kahmann R.;
RT   "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL   Science 330:1546-1548(2010).
CC   -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC       NADH dehydrogenase (Complex I) which catalyzes electron transfer from
CC       NADH through the respiratory chain, using ubiquinone as an electron
CC       acceptor. Essential for the catalytic activity of complex I.
CC       {ECO:0000256|RuleBase:RU003640}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) +
CC         NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC         COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00000766,
CC         ECO:0000256|RuleBase:RU003640};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC       {ECO:0000256|RuleBase:RU003640}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU003640}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 3 family.
CC       {ECO:0000256|ARBA:ARBA00008472, ECO:0000256|RuleBase:RU003640}.
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DR   EMBL; FQ311469; CBQ72564.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6ZZA7; -.
DR   EnsemblFungi; CBQ72564; CBQ72564; sr17110.
DR   VEuPathDB; FungiDB:sr17110; -.
DR   eggNOG; KOG4662; Eukaryota.
DR   HOGENOM; CLU_1016253_0_0_1; -.
DR   OrthoDB; 1561354at2759; -.
DR   Proteomes; UP000008867; Mitochondrion.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.20.58.1610; NADH:ubiquinone/plastoquinone oxidoreductase, chain 3; 1.
DR   InterPro; IPR000440; NADH_UbQ/plastoQ_OxRdtase_su3.
DR   InterPro; IPR038430; NDAH_ubi_oxred_su3_sf.
DR   PANTHER; PTHR11058; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 3; 1.
DR   PANTHER; PTHR11058:SF9; NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 3; 1.
DR   Pfam; PF00507; Oxidored_q4; 1.
PE   3: Inferred from homology;
KW   Electron transport {ECO:0000256|RuleBase:RU003640};
KW   Endonuclease {ECO:0000313|EMBL:CBQ72564.1};
KW   Hydrolase {ECO:0000313|EMBL:CBQ72564.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU003640};
KW   Mitochondrion {ECO:0000256|RuleBase:RU003640, ECO:0000313|EMBL:CBQ72564.1};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU003640};
KW   Nuclease {ECO:0000313|EMBL:CBQ72564.1};
KW   Respiratory chain {ECO:0000256|RuleBase:RU003640};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU003640};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU003640};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU003640};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU003640};
KW   Ubiquinone {ECO:0000256|RuleBase:RU003640, ECO:0000313|EMBL:CBQ72564.1}.
FT   TRANSMEM        6..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003640"
FT   TRANSMEM        57..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003640"
FT   TRANSMEM        89..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU003640"
FT   REGION          133..159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   274 AA;  30747 MW;  442211927401F681 CRC64;
     MNTITLFFIF IPILAVILLF ANLLLAVHRP DSEKVTPYEC GFSPVYGQTR NPFSIQFYLV
     GILFLVFDIE LLMTYPFAVN LYQTSAYGFW IFVIFFLVLT IGFVYEFGTG ALYFTDKRSS
     INNVDVIKSD TSPFTNQKRS YSTSSKNSKS ETNNNEVEKK KKSTYLADAY EKDLGQSTEN
     VHLKAQRHIQ SGNPTDHTTI NEVPPHSISI TQEELDKLVS ISPSTILLSD SISEIRKAFQ
     AIVGVGRSKL DTKKRVCGVY VFTNLVTGVG AARN
//
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