NDUV1_BOVIN
ID NDUV1_BOVIN Reviewed; 464 AA.
AC P25708; Q148I2;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial;
DE EC=7.1.1.2;
DE AltName: Full=Complex I-51kD;
DE Short=CI-51kD;
DE AltName: Full=NADH dehydrogenase flavoprotein 1;
DE AltName: Full=NADH-ubiquinone oxidoreductase 51 kDa subunit;
DE Flags: Precursor;
GN Name=NDUFV1; Synonyms=UQOR1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=2034666; DOI=10.1073/pnas.88.10.4225;
RA Patel S.D., Aebersold R., Attardi G.;
RT "cDNA-derived amino acid sequence of the NADH-binding 51-kDa subunit of the
RT bovine respiratory NADH dehydrogenase reveals striking similarities to a
RT bacterial NAD(+)-reducing hydrogenase.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:4225-4229(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1900194; DOI=10.1021/bi00222a021;
RA Pilkington S.J., Skehel J.M., Gennis R.B., Walker J.E.;
RT "Relationship between mitochondrial NADH-ubiquinone reductase and a
RT bacterial NAD-reducing hydrogenase.";
RL Biochemistry 30:2166-2175(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PARTIAL PROTEIN SEQUENCE, SUBUNIT, IDENTIFICATION IN COMPLEX I, FUNCTION,
RP AND SUBCELLULAR LOCATION.
RX PubMed=10852722; DOI=10.1021/bi000335t;
RA Sazanov L.A., Peak-Chew S.Y., Fearnley I.M., Walker J.E.;
RT "Resolution of the membrane domain of bovine complex I into subcomplexes:
RT implications for the structural organization of the enzyme.";
RL Biochemistry 39:7229-7235(2000).
RN [5]
RP SUBUNIT, IDENTIFICATION IN COMPLEX I, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18721790; DOI=10.1016/j.ab.2008.07.029;
RA Lemma-Gray P., Valusova E., Carroll C.A., Weintraub S.T., Musatov A.,
RA Robinson N.C.;
RT "Subunit analysis of bovine heart complex I by reversed-phase high-
RT performance liquid chromatography, electrospray ionization-tandem mass
RT spectrometry, and matrix-assisted laser desorption/ionization-time-of-
RT flight mass spectrometry.";
RL Anal. Biochem. 382:116-121(2008).
RN [6]
RP SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=25209663; DOI=10.1038/nature13686;
RA Vinothkumar K.R., Zhu J., Hirst J.;
RT "Architecture of mammalian respiratory complex I.";
RL Nature 515:80-84(2014).
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. {ECO:0000269|PubMed:10852722, ECO:0000269|PubMed:18721790}.
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 -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000305};
CC Note=Binds 1 FMN. {ECO:0000305};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000305};
CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
CC -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC I) which is composed of 45 different subunits (PubMed:10852722,
CC PubMed:18721790). This is a component of the flavoprotein-sulfur (FP)
CC fragment of the enzyme (PubMed:10852722, PubMed:18721790). Interacts
CC with RAB5IF (By similarity). {ECO:0000250|UniProtKB:P49821,
CC ECO:0000269|PubMed:10852722, ECO:0000269|PubMed:18721790}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:10852722, ECO:0000269|PubMed:18721790,
CC ECO:0000269|PubMed:25209663}; Peripheral membrane protein
CC {ECO:0000305|PubMed:25209663}; Matrix side
CC {ECO:0000305|PubMed:25209663}.
CC -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA30661.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M58607; AAA30450.1; -; mRNA.
DR EMBL; M63009; AAA30661.1; ALT_INIT; mRNA.
DR EMBL; BC118304; AAI18305.1; -; mRNA.
DR PIR; A39362; A39362.
DR RefSeq; NP_777233.1; NM_174808.1.
DR PDB; 5LC5; EM; 4.35 A; F=1-464.
DR PDB; 5LDW; EM; 4.27 A; F=21-464.
DR PDB; 5LDX; EM; 5.60 A; F=21-464.
DR PDB; 5O31; EM; 4.13 A; F=1-464.
DR PDB; 7QSD; EM; 3.10 A; F=1-464.
DR PDBsum; 5LC5; -.
DR PDBsum; 5LDW; -.
DR PDBsum; 5LDX; -.
DR PDBsum; 5O31; -.
DR PDBsum; 7QSD; -.
DR AlphaFoldDB; P25708; -.
DR SMR; P25708; -.
DR CORUM; P25708; -.
DR DIP; DIP-38805N; -.
DR IntAct; P25708; 3.
DR STRING; 9913.ENSBTAP00000029026; -.
DR BindingDB; P25708; -.
DR ChEMBL; CHEMBL614865; -.
DR TCDB; 3.D.1.6.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
DR PaxDb; P25708; -.
DR PeptideAtlas; P25708; -.
DR PRIDE; P25708; -.
DR GeneID; 287014; -.
DR KEGG; bta:287014; -.
DR CTD; 4723; -.
DR eggNOG; KOG2658; Eukaryota.
DR HOGENOM; CLU_014881_0_1_1; -.
DR InParanoid; P25708; -.
DR OrthoDB; 549172at2759; -.
DR TreeFam; TF300381; -.
DR PRO; PR:P25708; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005743; C:mitochondrial inner membrane; IDA:UniProtKB.
DR GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IBA:GO_Central.
DR Gene3D; 1.20.1440.230; -; 1.
DR Gene3D; 3.40.50.11540; -; 1.
DR InterPro; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS.
DR InterPro; IPR011537; NADH-UbQ_OxRdtase_suF.
DR InterPro; IPR011538; Nuo51_FMN-bd.
DR InterPro; IPR037225; Nuo51_FMN-bd_sf.
DR InterPro; IPR019575; Nuop51_4Fe4S-bd.
DR InterPro; IPR037207; Nuop51_4Fe4S-bd_sf.
DR InterPro; IPR019554; Soluble_ligand-bd.
DR Pfam; PF01512; Complex1_51K; 1.
DR Pfam; PF10589; NADH_4Fe-4S; 1.
DR Pfam; PF10531; SLBB; 1.
DR SMART; SM00928; NADH_4Fe-4S; 1.
DR SUPFAM; SSF140490; SSF140490; 1.
DR SUPFAM; SSF142019; SSF142019; 1.
DR TIGRFAMs; TIGR01959; nuoF_fam; 1.
DR PROSITE; PS00644; COMPLEX1_51K_1; 1.
DR PROSITE; PS00645; COMPLEX1_51K_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; 4Fe-4S; Acetylation; Direct protein sequencing;
KW Electron transport; Flavoprotein; FMN; Iron; Iron-sulfur; Membrane;
KW Metal-binding; Methylation; Mitochondrion; Mitochondrion inner membrane;
KW NAD; Oxidoreductase; Reference proteome; Respiratory chain;
KW Transit peptide; Translocase; Transport; Ubiquinone.
FT TRANSIT 1..20
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 21..464
FT /note="NADH dehydrogenase [ubiquinone] flavoprotein 1,
FT mitochondrial"
FT /id="PRO_0000019975"
FT BINDING 87..96
FT /ligand="NADH"
FT /ligand_id="ChEBI:CHEBI:57945"
FT /evidence="ECO:0000250"
FT BINDING 199..247
FT /ligand="FMN"
FT /ligand_id="ChEBI:CHEBI:58210"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 382
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 385
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT BINDING 425
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255"
FT MOD_RES 81
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91YT0"
FT MOD_RES 81
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q91YT0"
FT MOD_RES 104
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91YT0"
FT MOD_RES 257
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q91YT0"
FT MOD_RES 375
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q91YT0"
FT CONFLICT 413
FT /note="W -> C (in Ref. 2; AAA30450)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 464 AA; 50652 MW; 8ACEC256E026B317 CRC64;
MLAARRLLGG SLPARVSVRF SGDTTAPKKT SFGSLKDEDR IFTNLYGRHD WRLKGAQSRG
DWYKTKEILL KGPDWILGEV KTSGLRGRGG AGFPTGLKWS FMNKPSDGRP KYLVVNADEG
EPGTCKDREI IRHDPHKLVE GCLVGGRAMG ARAAYIYIRG EFYNEASNLQ VAIREAYEAG
LIGKNACGSG YDFDVFVVRG AGAYICGEET ALIESIEGKQ GKPRLKPPFP ADVGVFGCPT
TVANVETVAV SPTICRRGGA WFASFGRERN SGTKLFNISG HVNNPCTVEE EMSVPLKELI
EKHAGGVTGG WDNLLAVIPG GSSTPLIPKS VCETVLMDFD ALIQAQTGLG TAAVIVMDRS
TDIVKAIARL IEFYKHESCG QCTPCREGVD WMNKVMARFV RGDARPAEID SLWEISKQIE
GHTICALGDG AAWPVQGLIR HFRPELEERM QQFAQQHQAR QAAF
