ID A0A249L308_9ACTN Unreviewed; 783 AA.
AC A0A249L308;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=NADH-quinone oxidoreductase {ECO:0000256|RuleBase:RU003525};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU003525};
GN ORFNames=B1sIIB91_00385 {ECO:0000313|EMBL:ASY23397.1};
OS Candidatus Nanopelagicus abundans.
OC Bacteria; Actinomycetota; Actinomycetes; Candidatus Nanopelagicales;
OC Candidatus Nanopelagicaceae; Nanopelagicus.
OX NCBI_TaxID=1884916 {ECO:0000313|EMBL:ASY23397.1, ECO:0000313|Proteomes:UP000217210};
RN [1] {ECO:0000313|EMBL:ASY23397.1, ECO:0000313|Proteomes:UP000217210}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMS-IIB-91 {ECO:0000313|EMBL:ASY23397.1};
RA Neuenschwander S.M., Salcher M., Ghai R., Pernthaler J.;
RT "High microdiversification within the ubiquitous acI lineage of
RT Actinobacteria.";
RL Submitted (JUL-2016) 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. 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 -!- 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; CP016779; ASY23397.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A249L308; -.
DR KEGG; nab:B1sIIB91_00385; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000217210; Chromosome.
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:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
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; 2.40.40.20; -; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.740; -; 2.
DR Gene3D; 2.20.25.90; ADC-like domains; 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; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
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:SF12; NADH-QUINONE OXIDOREDUCTASE SUBUNIT G; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 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; SSF50692; ADC-like; 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|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003525}; NAD {ECO:0000256|RuleBase:RU003525};
KW Quinone {ECO:0000256|RuleBase:RU003525};
KW Reference proteome {ECO:0000313|Proteomes:UP000217210};
KW Translocase {ECO:0000256|RuleBase:RU003525}.
FT DOMAIN 15..97
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 99..138
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 237..293
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 783 AA; 84571 MW; 5AD6CD9D2E8ED795 CRC64;
MSIQELSTDQ EVAVEMITCV IDGFEITVPK GTLVIRAAEK LGIQIPRFCD HPLLEPAGAC
RQCLVDIEIN GRAFPKPQAS CTIPVENGMI VKTQLTSAVA DKAQKGVMEL LLINHPLDCP
VCDKGGECPL QNQAMSTGRS ESRFEGIKRT FEKPVAISSQ VLLDRERCVL CARCTRFSEQ
IAGDPFITLN ERGALQQVGI YEDEPFDSYY SGNTVQICPV GALTGTSYRF RARPFDLVST
SSACEHCASG CDMRTDVRRG KTLRRLAGDD ADVNEEWNCD KGRWAFKYEV AKNRLTAPMI
RDSSGQLQEV SWPEALAAAA AGLRDAKAGV LVGGRSTIED AYGYSKFARV ALGTNNIDFR
SRVHSNEELD FLASAPLTAT YKDIDKADHV VLINFEPEDE SPIIFLRIYK QTHKRSIKVT
TIAPFASRGS EKLKANLIKC AAGNEISAIS SLTGLTKKTV VLVGERLSET PGALSAVLQL
INQSGAKLGW VPRRAGERGA IAAGASGNLL PGNRLVSDSA ARVDIATVWS SSSLPTDSGM
NTLEIINSDL QAVLVGAVDP MDISPDAKIK LSKKFIVSLE IRHSDITDIA SVVLPVAAVV
EKSGSFMDWQ GNVRKFEAAV AQSLNRSDVR ILSMLADEIG KPINLPTVKA ARVEFDSIGN
WDGAKNTFKS VAPVANKNVS SDEAILTSWR NLLDKGSLQD GEDNLAGTAR KSVVVMSADR
AKKLGVKESE LVRVSNEYGA ITLPCQIADI EEASVWLPRN SASSQLIRNL GVVSNSIVKV
AKA
//
