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Database: UniProt
Entry: A0A0Q5VDX0_9CAUL
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Original site: A0A0Q5VDX0_9CAUL 
ID   A0A0Q5VDX0_9CAUL        Unreviewed;       438 AA.
AC   A0A0Q5VDX0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=NADH-quinone oxidoreductase subunit F {ECO:0000256|RuleBase:RU364066};
DE            EC=7.1.1.- {ECO:0000256|RuleBase:RU364066};
GN   ORFNames=ASG17_07885 {ECO:0000313|EMBL:KQS55961.1};
OS   Brevundimonas sp. Leaf363.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=1736353 {ECO:0000313|EMBL:KQS55961.1, ECO:0000313|Proteomes:UP000051182};
RN   [1] {ECO:0000313|EMBL:KQS55961.1, ECO:0000313|Proteomes:UP000051182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf363 {ECO:0000313|EMBL:KQS55961.1,
RC   ECO:0000313|Proteomes:UP000051182};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQS55961.1, ECO:0000313|Proteomes:UP000051182}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf363 {ECO:0000313|EMBL:KQS55961.1,
RC   ECO:0000313|Proteomes:UP000051182};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC       (Fe-S) centers, to quinones in the respiratory chain.
CC       {ECO:0000256|RuleBase:RU364066}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a quinone + 5 H(+)(in) + NADH = a quinol + 4 H(+)(out) +
CC         NAD(+); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124;
CC         Evidence={ECO:0000256|ARBA:ARBA00000100,
CC         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   -!- SIMILARITY: Belongs to the complex I 51 kDa subunit family.
CC       {ECO:0000256|ARBA:ARBA00007523, ECO:0000256|RuleBase:RU364066}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KQS55961.1}.
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DR   EMBL; LMPZ01000002; KQS55961.1; -; Genomic_DNA.
DR   RefSeq; WP_056101478.1; NZ_LMPZ01000002.1.
DR   AlphaFoldDB; A0A0Q5VDX0; -.
DR   STRING; 1736353.ASG17_07885; -.
DR   OrthoDB; 9761899at2; -.
DR   Proteomes; UP000051182; Unassembled WGS sequence.
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:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:UniProtKB-KW.
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   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   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   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   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU364066};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU364066};
KW   Oxidoreductase {ECO:0000313|EMBL:KQS55961.1};
KW   Quinone {ECO:0000256|RuleBase:RU364066};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051182}.
FT   DOMAIN          334..379
FT                   /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT                   sulphur binding"
FT                   /evidence="ECO:0000259|SMART:SM00928"
SQ   SEQUENCE   438 AA;  48231 MW;  620EE8B277AEDA73 CRC64;
     MTGVLQDKDR IFTNLYGLHD WGLEGAKNRG CWNATKDILD LGRDWIITNT KNSGLRGRGG
     AGFSTGLKWS FMPKEVKDGR PHYLVVNADE SEPGTCKDRE IMRHDPHLLI EGCLIASFAM
     QAHACYIYLR GEYVLERERM EAAVKQAYEA KLIGKNNAHG WDFDVYIHHG AGAYICGEET
     ALLESLEGKK GQPRLKPPFP AGAGLYGCPT TVNNVESIAV VGTILRRGAD WFAGFGRPNN
     TGTKLMSISG HVNKPCNIEE AMSIPMKQLL EEHCGGIRGG WDNLKAVIPG GVSVPLITRD
     MAETALMDFD SLREMRSGLG TAAVIVMDQS TDLVKAIARI SYFYKHESCG QCTPCREGTG
     WMWRVLERMA IGEADPTEID LLLDVAGQVE GHTICALGDA AAWPVQGLIR HFRHEIEDRI
     ASYRSRRANF AGHAIAAE
//
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