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Database: UniProt
Entry: A0A0L7TB34_9GAMM
LinkDB: A0A0L7TB34_9GAMM
Original site: A0A0L7TB34_9GAMM 
ID   A0A0L7TB34_9GAMM        Unreviewed;       446 AA.
AC   A0A0L7TB34;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
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=NG42_02125 {ECO:0000313|EMBL:KOC92573.1}, NG43_14325
GN   {ECO:0000313|EMBL:KOC92019.1};
OS   Erwinia iniecta.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=1560201 {ECO:0000313|EMBL:KOC92573.1, ECO:0000313|Proteomes:UP000037088};
RN   [1] {ECO:0000313|Proteomes:UP000036851, ECO:0000313|Proteomes:UP000037088}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B120 {ECO:0000313|EMBL:KOC92573.1,
RC   ECO:0000313|Proteomes:UP000037088}, and B149
RC   {ECO:0000313|EMBL:KOC92019.1, ECO:0000313|Proteomes:UP000036851};
RX   PubMed=26198254;
RA   Campillo T., Luna E., Portier P., Fischer-Le Saux M., Lapitan N.,
RA   Tisserat N.A., Leach J.E.;
RT   "Erwinia iniecta sp. nov., isolated from Russian wheat aphids (Diuraphis
RT   noxia).";
RL   Int. J. Syst. Evol. Microbiol. 0:0-0(2015).
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:KOC92573.1}.
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DR   EMBL; JRXF01000022; KOC92019.1; -; Genomic_DNA.
DR   EMBL; JRXE01000002; KOC92573.1; -; Genomic_DNA.
DR   RefSeq; WP_052897298.1; NZ_JRXF01000022.1.
DR   AlphaFoldDB; A0A0L7TB34; -.
DR   STRING; 1560201.NG42_02125; -.
DR   PATRIC; fig|1560201.3.peg.452; -.
DR   OrthoDB; 9805533at2; -.
DR   Proteomes; UP000036851; Unassembled WGS sequence.
DR   Proteomes; UP000037088; 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   NCBIfam; TIGR01959; nuoF_fam; 1.
DR   PANTHER; PTHR43578:SF3; HYDROGENASE SUBUNIT; 1.
DR   PANTHER; PTHR43578; 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:KOC92573.1};
KW   Quinone {ECO:0000256|RuleBase:RU364066};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037088}.
FT   DOMAIN          336..381
FT                   /note="NADH-ubiquinone oxidoreductase 51kDa subunit iron-
FT                   sulphur binding"
FT                   /evidence="ECO:0000259|SMART:SM00928"
SQ   SEQUENCE   446 AA;  48896 MW;  B8B137527DC94D6E CRC64;
     MKQIIRTAEM HPLTWRMRED KQPVWLDEYR SKNGYAGAEK ALKGMAPDEI VALVKDSGLK
     GRGGAGFSTG LKWSLMPKDE SMNIRYLLCN ADEMEPGTYK DRLLMEQMPH QLVEGMLISA
     FALKAYRGYI FLRGEYIEAA VNLRRAIAEA TEAGLLGKNI LGSGFDFELI VHTGAGRYIC
     GEETALINSL EGRRANPRSK PPFPASAGAW GKPTCVNNVE TLSNVPAILA NGVEWYKGIS
     NSDDAGTKMM GFSGRVKNPG VWELPFGTTA REILEDYAGG MRDGLKFKAW QPGGAGTDFL
     TDQHLDLPME FASIGKAGSR LGTALAMAVD HEINMVSLVR NLEEFFARES CGWCTPCRDG
     LPWSVKILRA LEQGKGQPGD IETLEQLCRQ LGPGKTFCAH APGAVEPLQS AIKYFREEFE
     AGIAPQVFGN ARAISGIQPN LLKARW
//
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