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Database: UniProt
Entry: A0A136MWV5_9BACT
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ID   A0A136MWV5_9BACT        Unreviewed;       427 AA.
AC   A0A136MWV5;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=NADH-quinone oxidoreductase subunit F {ECO:0000256|RuleBase:RU364066};
DE            EC=7.1.1.- {ECO:0000256|RuleBase:RU364066};
GN   Name=nuoF {ECO:0000313|EMBL:KXK38318.1};
GN   ORFNames=UZ16_OP3001000883 {ECO:0000313|EMBL:KXK38318.1};
OS   Candidatus Hinthialibacteria bacterium OLB16.
OC   Bacteria; Candidatus Hinthialibacterota.
OX   NCBI_TaxID=1617433 {ECO:0000313|EMBL:KXK38318.1, ECO:0000313|Proteomes:UP000070296};
RN   [1] {ECO:0000313|EMBL:KXK38318.1, ECO:0000313|Proteomes:UP000070296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB16 {ECO:0000313|EMBL:KXK38318.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Genome based microbial ecology of anammox granules in a full-scale
RT   wastewater treatment system.";
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|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:KXK38318.1}.
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DR   EMBL; LMZT01000043; KXK38318.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136MWV5; -.
DR   STRING; 1617433.UZ16_OP3001000883; -.
DR   PATRIC; fig|1617433.3.peg.952; -.
DR   Proteomes; UP000070296; 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; 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   PANTHER; PTHR43578; NADH-QUINONE OXIDOREDUCTASE SUBUNIT F; 1.
DR   PANTHER; PTHR43578:SF1; 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   Oxidoreductase {ECO:0000313|EMBL:KXK38318.1};
KW   Quinone {ECO:0000256|RuleBase:RU364066};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT   DOMAIN          331..376
FT                   /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT                   sulphur binding"
FT                   /evidence="ECO:0000259|SMART:SM00928"
SQ   SEQUENCE   427 AA;  46877 MW;  56DDD78919F61AB2 CRC64;
     MIDRPLTKNI DLSREPFSIK EYEAAGGYQG VHKALKEFTD PKSIVDLVKN AGLKGRGGAG
     FSTGLKWSFV PMGPDAPRPR YLVCNGDEME PGTFKDRLLL EGDPHSLIEG MICTAYAIQA
     EVAYIFLRWG YTLAEQRLSK AIAEAYQAGY LGKSILGTGF NLDLHLHISA GRYICGEETA
     LLNSLEGKRA NPRTKPPFPQ VSGLFGKPTI VQNVETLCNV HHILVHGVDW YKGLSRCEDG
     GTKLYGVSGK VKKPGVWELP MGVTVREILE DHAGGMRDGL KLKGFLPGGA STDFLVEEHL
     DLKMDYATIG KAGSRMGTGT MIILDDQTCP VGMVLNLTRF FAQESCGWCT PCRDGLPWSV
     KLLEAIEKGE GKPEDLDRLA AQCRFMGPGN TFCALAPGAA EPIQSSLKYF KEDFERHLAE
     KRCPWRS
//
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