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NDUV1_PONPY
ID   NDUV1_PONPY             Reviewed;         464 AA.
AC   Q0MQI4;
DT   03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 81.
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-ubiquinone oxidoreductase 51 kDa subunit;
DE   Flags: Precursor;
GN   Name=NDUFV1;
OS   Pongo pygmaeus (Bornean orangutan).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16828987; DOI=10.1016/j.gene.2006.03.015;
RA   Mishmar D., Ruiz-Pesini E., Mondragon-Palomino M., Procaccio V., Gaut B.,
RA   Wallace D.C.;
RT   "Adaptive selection of mitochondrial complex I subunits during primate
RT   radiation.";
RL   Gene 378:11-18(2006).
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:0000250|UniProtKB:P25708}.
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 (By similarity). This is
CC       a component of the flavoprotein-sulfur (FP) fragment of the enzyme (By
CC       similarity). Interacts with RAB5IF (By similarity).
CC       {ECO:0000250|UniProtKB:P49821}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P25708}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:P25708}; Matrix side
CC       {ECO:0000250|UniProtKB:P25708}.
CC   -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC       {ECO:0000305}.
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DR   EMBL; DQ885650; ABH12159.1; -; mRNA.
DR   AlphaFoldDB; Q0MQI4; -.
DR   SMR; Q0MQI4; -.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0045271; C:respiratory chain complex I; IEA:UniProt.
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   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   Pfam; PF01512; Complex1_51K; 1.
DR   Pfam; PF10589; NADH_4Fe-4S; 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   2: Evidence at transcript level;
KW   4Fe-4S; Acetylation; Electron transport; Flavoprotein; FMN; Iron;
KW   Iron-sulfur; Membrane; Metal-binding; Methylation; Mitochondrion;
KW   Mitochondrion inner membrane; NAD; Oxidoreductase; 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_0000251878"
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"
SQ   SEQUENCE   464 AA;  50727 MW;  7F0B1F0440B1C4BA CRC64;
     MLAARRLLGW SLPARVSVRF SGDTTAPKKT SFGSLKDEDR IFTNLYGRHD WRLKGALSRG
     DWYKTKEILL KGPDWILGEI KTSGLRGRGG AGFPTGLKWS FMNKPSDGRP KYLVVNADEG
     EPGTCKDREI IRHDPHKLVE GCLVGGRAMG ARAAYIYIRG EFYNEASNLQ VAIREAYEAG
     LIGKNACGSG YDFDVFVVRG AGAYICGEET ALIESIEGKQ GKPRLKPPFP ADVGVFGCPT
     TVANVETVAV SPTICRRGGT WFAGFGRERN SGTKLFNISG HVNYPCTVEE EMSVPLKELI
     EKHAGGVTGG WDNLLAVIPG GSSTPLIPKS VCETVLMDFD ALVQAQTGLG TAAVIVMDRS
     TDIVKAIARL IEFYKHESCG QCTPCREGVD WMNKVMARFV RGDAQPAEID SLWEISKQIE
     GHTICALGDG AAWPVQGLIR HFRPELEERM QRFAQQHQAQ QAAS
 
 
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