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Database: UniProt
Entry: A0A0T0PX24_9SPHN
LinkDB: A0A0T0PX24_9SPHN
Original site: A0A0T0PX24_9SPHN 
ID   A0A0T0PX24_9SPHN        Unreviewed;       441 AA.
AC   A0A0T0PX24;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=NADH-quinone oxidoreductase subunit F {ECO:0000256|RuleBase:RU364066};
DE            EC=7.1.1.- {ECO:0000256|RuleBase:RU364066};
GN   ORFNames=ASG29_06130 {ECO:0000313|EMBL:KQT33598.1};
OS   Sphingomonas sp. Leaf412.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1736370 {ECO:0000313|EMBL:KQT33598.1, ECO:0000313|Proteomes:UP000051178};
RN   [1] {ECO:0000313|EMBL:KQT33598.1, ECO:0000313|Proteomes:UP000051178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf412 {ECO:0000313|EMBL:KQT33598.1,
RC   ECO:0000313|Proteomes:UP000051178};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQT33598.1, ECO:0000313|Proteomes:UP000051178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf412 {ECO:0000313|EMBL:KQT33598.1,
RC   ECO:0000313|Proteomes:UP000051178};
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:KQT33598.1}.
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DR   EMBL; LMQP01000002; KQT33598.1; -; Genomic_DNA.
DR   RefSeq; WP_055981718.1; NZ_LMQP01000002.1.
DR   AlphaFoldDB; A0A0T0PX24; -.
DR   STRING; 1736370.ASG29_06130; -.
DR   OrthoDB; 9761899at2; -.
DR   Proteomes; UP000051178; 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   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   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:KQT33598.1};
KW   Quinone {ECO:0000256|RuleBase:RU364066};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051178};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT   DOMAIN          337..382
FT                   /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT                   sulphur binding"
FT                   /evidence="ECO:0000259|SMART:SM00928"
SQ   SEQUENCE   441 AA;  48085 MW;  599C537F560E85A4 CRC64;
     MSAITSLTDK DRIFTNLYGY QSWRLDAARM RGDWDDTKAL LALGQDAIID VVKASGLRGR
     GGAGFPTGTK WSFMPKEPKP DRPNFLVINA DESEPGSCKD REIIRHDPHK LIEGALVAGF
     AMRARAAYIY IRGEYIREAE TLFAAVQEAY DAGLVGKNAC GSGYDFDVFV HRGAGAYICG
     EETAMLESLE GKKGQPRLKP PFPAGAGLYG CPTTVNNVES IAVAPTILRR GAAWFSSFGA
     ENNKGTKLFQ ISGHVDRPTV VEEAMSITFR ELIEKHCGGI RGGWDNLLAV IPGGSSVPLV
     PAREIIDCPM DFDGLKGVGS GLGTAAIIVM DKSTDIVRAI SRISYFYKHE SCGQCTPCRE
     GTGWMWRVME RLRTGDAEIG EIDMLQQVTK QVEGHSICAL GDAAAWPIQG LIKHFRPELE
     RRIHERVGTP ADMAPMQEAA E
//
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