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NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial (EC 1.6.5.3) (EC 1.6.99.3) (Complex I-51kD) (CI-51kD) (NADH dehydrogenase flavoprotein 1) (NADH-ubiquinone oxidoreductase 51 kDa subunit)

 NDUV1_BOVIN             Reviewed;         464 AA.
P25708; Q148I2;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 2.
28-MAR-2018, entry version 141.
RecName: Full=NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial;
EC=1.6.5.3;
EC=1.6.99.3;
AltName: Full=Complex I-51kD;
Short=CI-51kD;
AltName: Full=NADH dehydrogenase flavoprotein 1;
AltName: Full=NADH-ubiquinone oxidoreductase 51 kDa subunit;
Flags: Precursor;
Name=NDUFV1; Synonyms=UQOR1;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=2034666; DOI=10.1073/pnas.88.10.4225;
Patel S.D., Aebersold R., Attardi G.;
"cDNA-derived amino acid sequence of the NADH-binding 51-kDa subunit
of the bovine respiratory NADH dehydrogenase reveals striking
similarities to a bacterial NAD(+)-reducing hydrogenase.";
Proc. Natl. Acad. Sci. U.S.A. 88:4225-4229(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1900194; DOI=10.1021/bi00222a021;
Pilkington S.J., Skehel J.M., Gennis R.B., Walker J.E.;
"Relationship between mitochondrial NADH-ubiquinone reductase and a
bacterial NAD-reducing hydrogenase.";
Biochemistry 30:2166-2175(1991).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Hereford; TISSUE=Basal ganglia;
NIH - Mammalian Gene Collection (MGC) project;
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
[4]
PARTIAL PROTEIN SEQUENCE, SUBUNIT, AND IDENTIFICATION IN COMPLEX I.
PubMed=10852722; DOI=10.1021/bi000335t;
Sazanov L.A., Peak-Chew S.Y., Fearnley I.M., Walker J.E.;
"Resolution of the membrane domain of bovine complex I into
subcomplexes: implications for the structural organization of the
enzyme.";
Biochemistry 39:7229-7235(2000).
[5]
SUBUNIT, AND IDENTIFICATION IN COMPLEX I.
PubMed=18721790; DOI=10.1016/j.ab.2008.07.029;
Lemma-Gray P., Valusova E., Carroll C.A., Weintraub S.T., Musatov A.,
Robinson N.C.;
"Subunit analysis of bovine heart complex I by reversed-phase high-
performance liquid chromatography, electrospray ionization-tandem mass
spectrometry, and matrix-assisted laser desorption/ionization-time-of-
flight mass spectrometry.";
Anal. Biochem. 382:116-121(2008).
-!- FUNCTION: Core subunit of the mitochondrial membrane respiratory
chain NADH dehydrogenase (Complex I) that is believed to belong to
the minimal assembly required for catalysis. Complex I functions
in the transfer of electrons from NADH to the respiratory chain.
The immediate electron acceptor for the enzyme is believed to be
ubiquinone.
-!- CATALYTIC ACTIVITY: NADH + ubiquinone + 5 H(+)(In) = NAD(+) +
ubiquinol + 4 H(+)(Out).
-!- CATALYTIC ACTIVITY: NADH + acceptor = NAD(+) + reduced acceptor.
-!- COFACTOR:
Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000305};
Note=Binds 1 FMN. {ECO:0000305};
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000305};
Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305};
-!- SUBUNIT: Complex I is composed of 45 different subunits. This is a
component of the flavoprotein-sulfur (FP) fragment of the enzyme.
{ECO:0000269|PubMed:10852722, ECO:0000269|PubMed:18721790}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane; Peripheral
membrane protein; Matrix side.
-!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA30661.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M58607; AAA30450.1; -; mRNA.
EMBL; M63009; AAA30661.1; ALT_INIT; mRNA.
EMBL; BC118304; AAI18305.1; -; mRNA.
PIR; A39362; A39362.
RefSeq; NP_777233.1; NM_174808.1.
UniGene; Bt.4072; -.
PDB; 5LC5; EM; 4.35 A; F=1-464.
PDB; 5LDW; EM; 4.27 A; F=21-464.
PDB; 5LDX; EM; 5.60 A; F=21-464.
PDB; 5O31; EM; 4.13 A; F=1-464.
PDBsum; 5LC5; -.
PDBsum; 5LDW; -.
PDBsum; 5LDX; -.
PDBsum; 5O31; -.
ProteinModelPortal; P25708; -.
SMR; P25708; -.
CORUM; P25708; -.
DIP; DIP-38805N; -.
IntAct; P25708; 3.
STRING; 9913.ENSBTAP00000029026; -.
BindingDB; P25708; -.
ChEMBL; CHEMBL614865; -.
TCDB; 3.D.1.6.1; the h(+) or na(+)-translocating nadh dehydrogenase (ndh) family.
PaxDb; P25708; -.
PeptideAtlas; P25708; -.
PRIDE; P25708; -.
Ensembl; ENSBTAT00000029026; ENSBTAP00000029026; ENSBTAG00000021776.
GeneID; 287014; -.
KEGG; bta:287014; -.
CTD; 4723; -.
VGNC; VGNC:31974; NDUFV1.
eggNOG; KOG2658; Eukaryota.
eggNOG; COG1894; LUCA.
GeneTree; ENSGT00390000010641; -.
HOGENOM; HOG000251534; -.
HOVERGEN; HBG006542; -.
InParanoid; P25708; -.
KO; K03942; -.
OMA; SGMKWSF; -.
OrthoDB; EOG091G05AF; -.
TreeFam; TF300381; -.
Reactome; R-BTA-611105; Respiratory electron transport.
Reactome; R-BTA-6799198; Complex I biogenesis.
PRO; PR:P25708; -.
Proteomes; UP000009136; Chromosome 29.
Bgee; ENSBTAG00000021776; -.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005747; C:mitochondrial respiratory chain complex I; IDA:UniProtKB.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0010181; F:FMN binding; IEA:InterPro.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0051287; F:NAD binding; IEA:InterPro.
GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
GO; GO:0042775; P:mitochondrial ATP synthesis coupled electron transport; IEA:Ensembl.
Gene3D; 1.20.1440.230; -; 1.
Gene3D; 3.40.50.11540; -; 1.
InterPro; IPR001949; NADH-UbQ_OxRdtase_51kDa_CS.
InterPro; IPR011537; NADH-UbQ_OxRdtase_suF.
InterPro; IPR011538; Nuo51_FMN-bd.
InterPro; IPR037225; Nuo51_FMN-bd_sf.
InterPro; IPR019575; Nuop51_4Fe4S-bd.
InterPro; IPR037207; Nuop51_4Fe4S-bd_sf.
InterPro; IPR019554; Soluble_ligand-bd.
Pfam; PF01512; Complex1_51K; 1.
Pfam; PF10589; NADH_4Fe-4S; 1.
Pfam; PF10531; SLBB; 1.
SMART; SM00928; NADH_4Fe-4S; 1.
SUPFAM; SSF140490; SSF140490; 1.
SUPFAM; SSF142019; SSF142019; 1.
TIGRFAMs; TIGR01959; nuoF_fam; 1.
PROSITE; PS00644; COMPLEX1_51K_1; 1.
PROSITE; PS00645; COMPLEX1_51K_2; 1.
1: Evidence at protein level;
3D-structure; 4Fe-4S; Acetylation; Complete proteome;
Direct protein sequencing; Electron transport; Flavoprotein; FMN;
Iron; Iron-sulfur; Membrane; Metal-binding; Methylation;
Mitochondrion; Mitochondrion inner membrane; NAD; Oxidoreductase;
Reference proteome; Respiratory chain; Transit peptide; Transport;
Ubiquinone.
TRANSIT 1 20 Mitochondrion.
CHAIN 21 464 NADH dehydrogenase [ubiquinone]
flavoprotein 1, mitochondrial.
/FTId=PRO_0000019975.
NP_BIND 87 96 NAD(H). {ECO:0000250}.
NP_BIND 199 247 FMN. {ECO:0000250}.
METAL 379 379 Iron-sulfur (4Fe-4S). {ECO:0000255}.
METAL 382 382 Iron-sulfur (4Fe-4S). {ECO:0000255}.
METAL 385 385 Iron-sulfur (4Fe-4S). {ECO:0000255}.
METAL 425 425 Iron-sulfur (4Fe-4S). {ECO:0000255}.
MOD_RES 81 81 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q91YT0}.
MOD_RES 81 81 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:Q91YT0}.
MOD_RES 104 104 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q91YT0}.
MOD_RES 257 257 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:Q91YT0}.
MOD_RES 375 375 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q91YT0}.
CONFLICT 413 413 W -> C (in Ref. 2; AAA30450).
{ECO:0000305}.
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


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