ID A0A150GFK9_GONPE Unreviewed; 197 AA.
AC A0A150GFK9;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 13-SEP-2023, entry version 26.
DE RecName: Full=NADH-ubiquinone oxidoreductase chain 3 {ECO:0000256|ARBA:ARBA00021007};
DE AltName: Full=NADH dehydrogenase subunit 3 {ECO:0000256|ARBA:ARBA00031029};
GN ORFNames=GPECTOR_26g534 {ECO:0000313|EMBL:KXZ48631.1};
OS Gonium pectorale (Green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Gonium.
OX NCBI_TaxID=33097 {ECO:0000313|EMBL:KXZ48631.1, ECO:0000313|Proteomes:UP000075714};
RN [1] {ECO:0000313|Proteomes:UP000075714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-2863 {ECO:0000313|Proteomes:UP000075714};
RX PubMed=27102219; DOI=10.1038/ncomms11370;
RA Hanschen E.R., Marriage T.N., Ferris P.J., Hamaji T., Toyoda A.,
RA Fujiyama A., Neme R., Noguchi H., Minakuchi Y., Suzuki M.,
RA Kawai-Toyooka H., Smith D.R., Sparks H., Anderson J., Bakaric R., Luria V.,
RA Karger A., Kirschner M.W., Durand P.M., Michod R.E., Nozaki H., Olson B.J.;
RT "The Gonium pectorale genome demonstrates co-option of cell cycle
RT regulation during the evolution of multicellularity.";
RL Nat. Commun. 7:11370-11370(2016).
CC -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC NADH dehydrogenase (Complex I) that is believed to belong to the
CC minimal assembly required for catalysis. Complex I functions in the
CC transfer of electrons from NADH to the respiratory chain. The immediate
CC electron acceptor for the enzyme is believed to be ubiquinone.
CC {ECO:0000256|ARBA:ARBA00003257}.
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 -!- SUBCELLULAR LOCATION: Mitochondrion membrane
CC {ECO:0000256|ARBA:ARBA00004225}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004225}.
CC -!- SIMILARITY: Belongs to the complex I subunit 3 family.
CC {ECO:0000256|ARBA:ARBA00008472}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KXZ48631.1}.
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DR EMBL; LSYV01000027; KXZ48631.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A150GFK9; -.
DR STRING; 33097.A0A150GFK9; -.
DR OrthoDB; 5487322at2759; -.
DR Proteomes; UP000075714; Unassembled WGS sequence.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000075714};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 85..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 197 AA; 21551 MW; 94392C3077564373 CRC64;
MPSSSLLAAA AKASGAAPLL PRRPLRRAML PGLAGMGLAP GLTMTQLRGY NAWSPAQRYF
VEGDHVVAAE ANRTFQFTGL DSGSFYPYIV ATAIATAIST VFIVLPLVIA PSRVDLDKSS
AYECGFDAFG EARQTFSVSF YLVSIMYLLF DIEIAYLFPY AMTHASLPMY WTMNLFLAIL
VAGFAYEWGM GALEWRE
//