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 24-JAN-2024, entry version 169. DE RecName: Full=NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial; DE Short=NDUFV1 {ECO:0000303|PubMed:27509854}; DE EC=7.1.1.2 {ECO:0000269|PubMed:10852722, ECO:0000269|PubMed:18721790, ECO:0000269|PubMed:25209663, ECO:0000269|PubMed:27509854}; 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 {ECO:0000250|UniProtKB:P49821}; DE Flags: Precursor; GN Name=NDUFV1 {ECO:0000250|UniProtKB:P49821}; 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 CATALYTIC ACTIVITY, 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, CATALYTIC ACTIVITY, AND RP 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 FUNCTION, CATALYTIC ACTIVITY, 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). RN [7] {ECO:0007744|PDB:5LC5, ECO:0007744|PDB:5LDW, ECO:0007744|PDB:5LDX} RP STRUCTURE BY ELECTRON MICROSCOPY (4.27 ANGSTROMS) OF 21-464, FUNCTION, RP CATALYTIC ACTIVITY, AND COFACTOR. RX PubMed=27509854; DOI=10.1038/nature19095; RA Zhu J., Vinothkumar K.R., Hirst J.; RT "Structure of mammalian respiratory complex I."; RL Nature 536:354-358(2016). 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. Part of the peripheral arm of the enzyme, where the electrons CC from NADH are accepted by flavin mononucleotide (FMN) and then passed CC along a chain of iron-sulfur clusters by electron tunnelling to the CC final acceptor ubiquinone. Contains FMN, which is the initial electron CC acceptor. {ECO:0000269|PubMed:10852722, ECO:0000269|PubMed:18721790, CC ECO:0000269|PubMed:25209663, ECO:0000269|PubMed:27509854}. 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:0000305|PubMed:10852722, ECO:0000305|PubMed:18721790, CC ECO:0000305|PubMed:25209663, ECO:0000305|PubMed:27509854}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29092; CC Evidence={ECO:0000305|PubMed:10852722, ECO:0000305|PubMed:18721790, CC ECO:0000305|PubMed:25209663, ECO:0000305|PubMed:27509854}; CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000269|PubMed:27509854}; CC Note=Binds 1 FMN. {ECO:0000269|PubMed:27509854}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000269|PubMed:27509854}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:27509854}; 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}; 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; 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; 7DGQ; EM; 5.00 A; 8=21-464. DR PDB; 7DGR; EM; 4.60 A; 8=21-464. DR PDB; 7DGS; EM; 7.80 A; 8=21-464. DR PDB; 7DGZ; EM; 3.80 A; 8=21-464. DR PDB; 7DH0; EM; 4.20 A; 8=21-464. DR PDB; 7DKF; EM; 8.30 A; 82=21-464. DR PDB; 7QSD; EM; 3.10 A; F=1-464. DR PDB; 7QSK; EM; 2.84 A; F=1-464. DR PDB; 7QSL; EM; 2.76 A; F=1-464. DR PDB; 7QSM; EM; 2.30 A; F=1-464. DR PDB; 7QSN; EM; 2.81 A; F=1-464. DR PDB; 7QSO; EM; 3.02 A; F=1-464. DR PDB; 7R41; EM; 2.30 A; F=1-464. DR PDB; 7R42; EM; 2.30 A; F=1-464. DR PDB; 7R43; EM; 2.40 A; F=1-464. DR PDB; 7R44; EM; 2.40 A; F=1-464. DR PDB; 7R45; EM; 2.40 A; F=1-464. DR PDB; 7R46; EM; 2.40 A; F=1-464. DR PDB; 7R47; EM; 2.30 A; F=1-464. DR PDB; 7R48; EM; 2.30 A; F=1-464. DR PDB; 7R4C; EM; 2.30 A; F=1-464. DR PDB; 7R4D; EM; 2.30 A; F=1-464. DR PDB; 7R4F; EM; 2.40 A; F=1-464. DR PDB; 7R4G; EM; 2.50 A; F=1-464. DR PDBsum; 5LC5; -. DR PDBsum; 5LDW; -. DR PDBsum; 5LDX; -. DR PDBsum; 5O31; -. DR PDBsum; 7DGQ; -. DR PDBsum; 7DGR; -. DR PDBsum; 7DGS; -. DR PDBsum; 7DGZ; -. DR PDBsum; 7DH0; -. DR PDBsum; 7DKF; -. DR PDBsum; 7QSD; -. DR PDBsum; 7QSK; -. DR PDBsum; 7QSL; -. DR PDBsum; 7QSM; -. DR PDBsum; 7QSN; -. DR PDBsum; 7QSO; -. DR PDBsum; 7R41; -. DR PDBsum; 7R42; -. DR PDBsum; 7R43; -. DR PDBsum; 7R44; -. DR PDBsum; 7R45; -. DR PDBsum; 7R46; -. DR PDBsum; 7R47; -. DR PDBsum; 7R48; -. DR PDBsum; 7R4C; -. DR PDBsum; 7R4D; -. DR PDBsum; 7R4F; -. DR PDBsum; 7R4G; -. DR AlphaFoldDB; P25708; -. DR EMDB; EMD-14251; -. DR EMDB; EMD-14256; -. DR EMDB; EMD-14261; -. DR EMDB; EMD-14266; -. DR EMDB; EMD-14272; -. DR EMDB; EMD-14277; -. DR EMDB; EMD-14282; -. DR EMDB; EMD-14287; -. DR EMDB; EMD-14292; -. DR EMDB; EMD-14297; -. DR EMDB; EMD-14302; -. DR EMDB; EMD-14307; -. DR SMR; P25708; -. DR CORUM; P25708; -. DR DIP; DIP-38805N; -. DR IntAct; P25708; 3. DR STRING; 9913.ENSBTAP00000070140; -. DR BindingDB; P25708; -. DR ChEMBL; CHEMBL614865; -. DR TCDB; 3.D.1.6.1; the h+ or na+-translocating nadh dehydrogenase (ndh) family. DR PaxDb; 9913-ENSBTAP00000029026; -. DR PeptideAtlas; 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 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; IDA:UniProtKB. DR GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; IDA:UniProtKB. DR Gene3D; 3.10.20.600; -; 1. DR Gene3D; 3.40.50.11540; NADH-ubiquinone oxidoreductase 51kDa subunit; 1. DR Gene3D; 1.20.1440.230; NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain; 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 NCBIfam; TIGR01959; nuoF_fam; 1. DR PANTHER; PTHR11780:SF10; NADH DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN 1, MITOCHONDRIAL; 1. DR PANTHER; PTHR11780; NADH-UBIQUINONE OXIDOREDUCTASE FLAVOPROTEIN 1 NDUFV1; 1. 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; SSF142019; Nqo1 FMN-binding domain-like; 1. DR SUPFAM; SSF142984; Nqo1 middle domain-like; 1. DR SUPFAM; SSF140490; Nqo1C-terminal domain-like; 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:0000269|PubMed:27509854, FT ECO:0007744|PDB:5LC5, ECO:0007744|PDB:5LDW, FT ECO:0007744|PDB:5LDX" FT BINDING 382 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000269|PubMed:27509854, FT ECO:0007744|PDB:5LC5, ECO:0007744|PDB:5LDW, FT ECO:0007744|PDB:5LDX" FT BINDING 385 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000269|PubMed:27509854, FT ECO:0007744|PDB:5LC5, ECO:0007744|PDB:5LDW, FT ECO:0007744|PDB:5LDX" FT BINDING 425 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000269|PubMed:27509854, FT ECO:0007744|PDB:5LC5, ECO:0007744|PDB:5LDW, FT ECO:0007744|PDB:5LDX" 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" FT HELIX 37..39 FT /evidence="ECO:0007829|PDB:7QSM" FT TURN 43..46 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 53..58 FT /evidence="ECO:0007829|PDB:7QSM" FT TURN 59..62 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 65..70 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 73..83 FT /evidence="ECO:0007829|PDB:7QSM" FT STRAND 88..91 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 95..99 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 100..102 FT /evidence="ECO:0007829|PDB:7QSM" FT STRAND 112..117 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 126..133 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 135..149 FT /evidence="ECO:0007829|PDB:7QSM" FT STRAND 152..158 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 163..178 FT /evidence="ECO:0007829|PDB:7QSM" FT STRAND 181..183 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 186..188 FT /evidence="ECO:0007829|PDB:7QSM" FT STRAND 193..199 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 204..207 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 209..216 FT /evidence="ECO:0007829|PDB:7QSM" FT STRAND 226..228 FT /evidence="ECO:0007829|PDB:7QSM" FT TURN 230..232 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 235..237 FT /evidence="ECO:0007829|PDB:7QSM" FT STRAND 240..244 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 245..257 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 259..263 FT /evidence="ECO:0007829|PDB:7QSM" FT STRAND 265..267 FT /evidence="ECO:0007829|PDB:7QSM" FT STRAND 272..284 FT /evidence="ECO:0007829|PDB:7QSM" FT STRAND 286..291 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 296..303 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 311..313 FT /evidence="ECO:0007829|PDB:7QSM" FT STRAND 314..318 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 329..332 FT /evidence="ECO:0007829|PDB:7QSM" FT STRAND 336..338 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 339..344 FT /evidence="ECO:0007829|PDB:7QSM" FT STRAND 353..358 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 363..377 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 383..401 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 407..419 FT /evidence="ECO:0007829|PDB:7QSM" FT STRAND 422..425 FT /evidence="ECO:0007829|PDB:7QSM" FT HELIX 427..457 FT /evidence="ECO:0007829|PDB:7QSM" 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 //