ID A0A0J9X8N6_GEOCN Unreviewed; 503 AA.
AC A0A0J9X8N6;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 13-SEP-2023, entry version 28.
DE RecName: Full=NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial {ECO:0000256|RuleBase:RU364066};
DE EC=7.1.1.2 {ECO:0000256|RuleBase:RU364066};
GN ORFNames=BN980_GECA04s04729g {ECO:0000313|EMBL:CDO53127.1};
OS Geotrichum candidum (Oospora lactis) (Dipodascus geotrichum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Geotrichum.
OX NCBI_TaxID=1173061 {ECO:0000313|EMBL:CDO53127.1, ECO:0000313|Proteomes:UP000242525};
RN [1] {ECO:0000313|EMBL:CDO53127.1, ECO:0000313|Proteomes:UP000242525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 918 {ECO:0000313|EMBL:CDO53127.1,
RC ECO:0000313|Proteomes:UP000242525};
RA Casaregola S.;
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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. Essential for the catalytic activity and assembly of complex
CC I. {ECO:0000256|RuleBase:RU364066}.
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|RuleBase:RU364066};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917,
CC ECO:0000256|RuleBase:RU364066};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966,
CC ECO:0000256|RuleBase:RU364066};
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000256|RuleBase:RU364066}; Peripheral membrane protein
CC {ECO:0000256|RuleBase:RU364066}; Matrix side
CC {ECO:0000256|RuleBase:RU364066}.
CC -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00007523, ECO:0000256|RuleBase:RU364066}.
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DR EMBL; CCBN010000004; CDO53127.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J9X8N6; -.
DR STRING; 1173061.A0A0J9X8N6; -.
DR OrthoDB; 5483539at2759; -.
DR Proteomes; UP000242525; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0045271; C:respiratory chain complex I; IEA:UniProt.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC.
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 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU364066};
KW Electron transport {ECO:0000256|RuleBase:RU364066};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|RuleBase:RU364066};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|RuleBase:RU364066};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU364066};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU364066};
KW Membrane {ECO:0000256|RuleBase:RU364066};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU364066};
KW Mitochondrion {ECO:0000256|RuleBase:RU364066};
KW Mitochondrion inner membrane {ECO:0000256|RuleBase:RU364066};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU364066};
KW Respiratory chain {ECO:0000256|RuleBase:RU364066};
KW Transit peptide {ECO:0000256|RuleBase:RU364066};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transport {ECO:0000256|RuleBase:RU364066};
KW Ubiquinone {ECO:0000313|EMBL:CDO53127.1}.
FT DOMAIN 382..427
FT /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT sulphur binding"
FT /evidence="ECO:0000259|SMART:SM00928"
SQ SEQUENCE 503 AA; 54951 MW; 5DCF687FCBF66DBE CRC64;
MLSRRLSALN ALKSTSQKHT SIALSSLRIS HSRRQFATVQ DGTPRRYGGL KDQDRIFQNV
YGTYGHDLKS AKRMGDWYKT KEIILKGYDW IINEMKKSGL RGRGGAGFPS GLKWSFMNPP
GWEKNEGPRY LVVNADEGEP GTCKDREIIR KDPHKLIEGC LLAGRGMNAS AAYIYIRGEF
YNEAVILQNA INEAYADGLI GKNACGSGYD FDVYIHRGMG AYICGEETAL IESIEGKAGK
PRLKPPFPAG VGLFGRPTTV ANVETVAVAP TILRRGGDWF ASFGRERNQG TKLFCISGNV
NEPCTVEEEM SIPLRELLEK HCGGIKGGWD NLLGVIPGGS SVPILTKDVC NDVLMDYDAL
KDVGSGLGTA AVIVLDRSAD IVRAIQRFSY FYKHESCGQC TPCREGTTWL LKVMDRFRAG
QGSAREIDML FELTKEIEGH TICALGDAAA WPVQGLIKNF RPEMEARFKK FEEEVGSVSV
GGWTSGAGIA GGKVVGGNVP SSH
//
