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Database: UniProt
Entry: A0A512RR12_9BACT
LinkDB: A0A512RR12_9BACT
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ID   A0A512RR12_9BACT        Unreviewed;       424 AA.
AC   A0A512RR12;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   18-JUN-2025, entry version 16.
DE   RecName: Full=NADH-quinone oxidoreductase subunit F {ECO:0000256|RuleBase:RU364066};
DE            EC=7.1.1.- {ECO:0000256|RuleBase:RU364066};
GN   ORFNames=CCY01nite_44190 {ECO:0000313|EMBL:GEP98159.1};
OS   Chitinophaga cymbidii.
OC   Bacteria; Pseudomonadati; Bacteroidota; Chitinophagia; Chitinophagales;
OC   Chitinophagaceae; Chitinophaga.
OX   NCBI_TaxID=1096750 {ECO:0000313|EMBL:GEP98159.1, ECO:0000313|Proteomes:UP000321436};
RN   [1] {ECO:0000313|EMBL:GEP98159.1, ECO:0000313|Proteomes:UP000321436}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 109752 {ECO:0000313|EMBL:GEP98159.1,
RC   ECO:0000313|Proteomes:UP000321436};
RA   Hosoyama A., Uohara A., Ohji S., Ichikawa N.;
RT   "Whole genome shotgun sequence of Chitinophaga cymbidii NBRC 109752.";
RL   Submitted (JUL-2019) 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 + NADH + 5 H(+)(in) = a quinol + NAD(+) + 4
CC         H(+)(out); Xref=Rhea:RHEA:57888, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:132124; Evidence={ECO:0000256|ARBA:ARBA00047712,
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:GEP98159.1}.
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DR   EMBL; BKAU01000005; GEP98159.1; -; Genomic_DNA.
DR   RefSeq; WP_146866414.1; NZ_BKAU01000005.1.
DR   AlphaFoldDB; A0A512RR12; -.
DR   OrthoDB; 9761899at2; -.
DR   Proteomes; UP000321436; Unassembled WGS sequence.
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   FunFam; 3.40.50.11540:FF:000001; NADH dehydrogenase [ubiquinone] flavoprotein 1, mitochondrial; 1.
DR   FunFam; 1.20.1440.230:FF:000002; NADH-quinone oxidoreductase subunit F; 1.
DR   Gene3D; 3.10.20.600; -; 1.
DR   Gene3D; 6.10.250.1450; -; 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   NCBIfam; NF010120; PRK13596.1; 1.
DR   PANTHER; PTHR43578; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR   PANTHER; PTHR43578:SF3; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 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; 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   Quinone {ECO:0000256|RuleBase:RU364066};
KW   Reference proteome {ECO:0000313|Proteomes:UP000321436};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT   DOMAIN          325..370
FT                   /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT                   sulphur binding"
FT                   /evidence="ECO:0000259|SMART:SM00928"
SQ   SEQUENCE   424 AA;  46479 MW;  C4C8B9A7E55BDBCF CRC64;
     MERPLTQHIT FPPLGLRQYE AVGGYQAARK AIRHMTPPEV TALVKESNLK GRGGAGFSTG
     MKWSFVPMDV SGPKYLVANA DEMEPGTFKD RWLLEGNPHQ LIEGMIVSAF AIQATESFVF
     LRWAYKAAAE EIRKAIQEAY DAGYLGKNIL GSDYSLDMHL HTGVGRYMCG EETALLNSLE
     GKRATPRAKP PFPQVSGLFG KPTIVNNVET LSYIPHIVNK GAAWFQSLSH TADGGTKIYG
     VSGKVNKPGA WELPMGVTMR ELIEEHAGGM KNGYRFRGVL PGGASTDFLV EEHMDVKMDF
     AGVAAAGSRL GTGTMVVLDD QTCPVGFVHN LEHFFAQESC GFCTPCREGL PWTEKLLWAI
     EQGQGREEDL ALLASHATLL GPGNTFCALA PGAMEPLQSA LKYFRDDFER HIKEQKCPYG
     DHIH
//
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