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Database: UniProt
Entry: W0L8Z2_9GAMM
LinkDB: W0L8Z2_9GAMM
Original site: W0L8Z2_9GAMM 
ID   W0L8Z2_9GAMM            Unreviewed;       450 AA.
AC   W0L8Z2;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=NADH-quinone oxidoreductase subunit F {ECO:0000256|ARBA:ARBA00019901, ECO:0000256|RuleBase:RU364066};
DE            EC=7.1.1.- {ECO:0000256|RuleBase:RU364066};
GN   ORFNames=Z042_03295 {ECO:0000313|EMBL:AHG18742.1};
OS   Chania multitudinisentens RB-25.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Chania.
OX   NCBI_TaxID=1441930 {ECO:0000313|EMBL:AHG18742.1, ECO:0000313|Proteomes:UP000019030};
RN   [1] {ECO:0000313|EMBL:AHG18742.1, ECO:0000313|Proteomes:UP000019030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RB-25 {ECO:0000313|EMBL:AHG18742.1,
RC   ECO:0000313|Proteomes:UP000019030};
RA   Robson E.H.J.;
RT   "Isolation of Serratia multitudinisentens RB-25 from Ex-Landfill site.";
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AHG18742.1, ECO:0000313|Proteomes:UP000019030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RB-25 {ECO:0000313|EMBL:AHG18742.1,
RC   ECO:0000313|Proteomes:UP000019030};
RA   Chan K.-G.;
RL   Submitted (MAR-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}.
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DR   EMBL; CP007044; AHG18742.1; -; Genomic_DNA.
DR   RefSeq; WP_024911402.1; NZ_JAJC01000008.1.
DR   AlphaFoldDB; W0L8Z2; -.
DR   STRING; 1441930.Z042_03295; -.
DR   KEGG; sfo:Z042_03295; -.
DR   PATRIC; fig|1441930.4.peg.664; -.
DR   eggNOG; COG1894; Bacteria.
DR   HOGENOM; CLU_014881_0_1_6; -.
DR   OrthoDB; 9805533at2; -.
DR   Proteomes; UP000019030; Chromosome.
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   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   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:AHG18742.1};
KW   Quinone {ECO:0000256|RuleBase:RU364066};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019030}.
FT   DOMAIN          339..384
FT                   /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT                   sulphur binding"
FT                   /evidence="ECO:0000259|SMART:SM00928"
SQ   SEQUENCE   450 AA;  49436 MW;  3BFBB2AA771405E9 CRC64;
     MMIDIKRTAE MHPLTWRLRD DEQPVWLDEY RSKNGYAGAE KALKGMAPDE IVNLVKDAGL
     KGRGGAGFST GLKWSLMPKD ESMNIRYLLC NADEMEPGTY KDRLLMEQLP HLLVEGMLIS
     AFALKAYRGY IFLRGEYIEA AVHLRRAIAE ATEAGWLGKN IQGSGFDFEL IVHTGAGRYI
     CGEETALINS LEGRRANPRS KPPFPASAGV WGKPTCVNNV ETLCNVPAIL EHGVDWYKGI
     SAGKSNDAGT KLMGFSGRVK NPGLWELPFG TTAREILEDY AGGMRDGLKF KAWQPGGAGT
     DFLTADHLDL PMDFESIAKA GSRLGTALAM AVDHEIGMVS LVRNLEEFFA RESCGWCTPC
     RDGLPWSVKI LRALENGEGQ PGDIETLEQL CRSLGPGKTF CAHAPGAVEP LQSAIKYFRD
     EFEAGIATQY FGNIQAIGGI QPNNLLKQRW
//
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