ID W0BCM9_9GAMM Unreviewed; 497 AA.
AC W0BCM9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=NADH-quinone oxidoreductase {ECO:0000256|RuleBase:RU003525};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU003525};
GN ORFNames=Loa_02722 {ECO:0000313|EMBL:AHE68253.1};
OS Legionella oakridgensis ATCC 33761 = DSM 21215.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=1268635 {ECO:0000313|EMBL:AHE68253.1, ECO:0000313|Proteomes:UP000018838};
RN [1] {ECO:0000313|EMBL:AHE68253.1, ECO:0000313|Proteomes:UP000018838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OR-10, ATCC 33761 {ECO:0000313|Proteomes:UP000018838};
RX PubMed=23932911; DOI=10.1016/j.ijmm.2013.07.003;
RA Brzuszkiewicz E., Schulz T., Rydzewski K., Daniel R., Gillmaier N.,
RA Dittmann C., Holland G., Schunder E., Lautner M., Eisenreich W., Luck C.,
RA Heuner K.;
RT "Legionella oakridgensis ATCC 33761 genome sequence and phenotypic
RT characterization reveals its replication capacity in amoebae.";
RL Int. J. Med. Microbiol. 303:514-528(2013).
CC -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC (Fe-S) centers, to quinones in the respiratory chain. Couples the redox
CC reaction to proton translocation (for every two electrons transferred,
CC four hydrogen ions are translocated across the cytoplasmic membrane),
CC and thus conserves the redox energy in a proton gradient.
CC {ECO:0000256|RuleBase:RU003525}.
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:RU003525};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|RuleBase:RU003525};
CC Note=Binds 1 [2Fe-2S] cluster per subunit.
CC {ECO:0000256|RuleBase:RU003525};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966,
CC ECO:0000256|RuleBase:RU003525};
CC -!- SUBUNIT: Composed of 13 different subunits. Subunits NuoCD, E, F, and G
CC constitute the peripheral sector of the complex.
CC {ECO:0000256|ARBA:ARBA00026021}.
CC -!- SIMILARITY: Belongs to the complex I 75 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00005404, ECO:0000256|RuleBase:RU003525}.
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DR EMBL; CP004006; AHE68253.1; -; Genomic_DNA.
DR AlphaFoldDB; W0BCM9; -.
DR STRING; 1268635.Loa_02722; -.
DR KEGG; lok:Loa_02722; -.
DR PATRIC; fig|1268635.3.peg.2793; -.
DR eggNOG; COG1034; Bacteria.
DR HOGENOM; CLU_000422_11_0_6; -.
DR Proteomes; UP000018838; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0048038; F:quinone binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR000283; NADH_UbQ_OxRdtase_75kDa_su_CS.
DR InterPro; IPR010228; NADH_UbQ_OxRdtase_Gsu.
DR InterPro; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR NCBIfam; TIGR01973; NuoG; 1.
DR PANTHER; PTHR43105:SF13; NADH-UBIQUINONE OXIDOREDUCTASE 75 KDA SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51839; 4FE4S_HC3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00641; COMPLEX1_75K_1; 1.
DR PROSITE; PS00642; COMPLEX1_75K_2; 1.
DR PROSITE; PS00643; COMPLEX1_75K_3; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|RuleBase:RU003525};
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|RuleBase:RU003525};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003525};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU003525};
KW Metal-binding {ECO:0000256|RuleBase:RU003525};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU003525};
KW Oxidoreductase {ECO:0000313|EMBL:AHE68253.1};
KW Quinone {ECO:0000256|RuleBase:RU003525};
KW Reference proteome {ECO:0000313|Proteomes:UP000018838};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU003525}.
FT DOMAIN 1..78
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 78..117
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 215..271
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 497 AA; 55614 MW; 16C693F02BBC9E6B CRC64;
MATIEIDGKT LEAENGKMII EVADEAGIYI PRFCYHKKLS VAANCRMCLV EVENGRKPVP
ACATPITNGM KVFTKSEGTI RSQQAVMEFL LINHPLDCPI CDQGGECELQ DISMGFGHDS
SDYEESKRAV ADENLGPLIA TEMTRCIHCT RCVRFGDEIA GLRELGATGR GEHMEIGTYV
KHSMVSEVSG NVIDLCPVGA LTSKPYRFTA RAWELMQHDS LAPHDCLGSN VFLHVRRNQL
MRAVPKENET INETWLSDRD RFSYLGLNSK DRAGNPMIKR DGQWETVDWE TALKFTAEGM
SRIIKQHGPE QLAVFASPSS TLEEFYLLQK LMRELGVQNL DHRLQQTDFR DQEGQKVMPL
GSISYAELES QANILLVGCN IDREVPLAGV RTRKAFRNGA KIYAINPVDY DYRFDLTKKI
VVTPQEMLIQ LACLVRAMVE HVDGLPEEVQ KLLIGLEPDE RICAMAAALR EPKAVIVTGA
IFENHPHASL LRTLIFC
//
