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Database: UniProt
Entry: Q473T7_CUPPJ
LinkDB: Q473T7_CUPPJ
Original site: Q473T7_CUPPJ 
ID   Q473T7_CUPPJ            Unreviewed;       791 AA.
AC   Q473T7;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   24-JAN-2024, entry version 115.
DE   RecName: Full=NADH-quinone oxidoreductase {ECO:0000256|RuleBase:RU003525};
DE            EC=7.1.1.- {ECO:0000256|RuleBase:RU003525};
GN   OrderedLocusNames=Reut_A0967 {ECO:0000313|EMBL:AAZ60346.1};
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198 {ECO:0000313|EMBL:AAZ60346.1};
RN   [1] {ECO:0000313|EMBL:AAZ60346.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JMP134 {ECO:0000313|EMBL:AAZ60346.1};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J.,
RA   Larimer F., Land M., Lykidis A., Richardson P.;
RT   "Complete sequence of Chromosome1 of Ralstonia eutropha JMP134.";
RL   Submitted (AUG-2005) 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; CP000090; AAZ60346.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q473T7; -.
DR   STRING; 264198.Reut_A0967; -.
DR   KEGG; reu:Reut_A0967; -.
DR   eggNOG; COG1034; Bacteria.
DR   HOGENOM; CLU_000422_11_6_4; -.
DR   OMA; HKNVGPL; -.
DR   OrthoDB; 7376058at2; -.
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   CDD; cd02772; MopB_NDH-1_NuoG2; 1.
DR   Gene3D; 3.10.20.740; -; 1.
DR   Gene3D; 3.30.70.20; -; 1.
DR   Gene3D; 3.40.50.740; -; 2.
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; 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; 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   Oxidoreductase {ECO:0000313|EMBL:AAZ60346.1};
KW   Quinone {ECO:0000256|RuleBase:RU003525};
KW   Translocase {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          216..272
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   791 AA;  83805 MW;  84C88214C4F30D62 CRC64;
     MVELEIDGKK VEVAEGSLVM EAARKLGTYI PHFCYHRKLS IAANCRMCLV EVEKAPKALP
     ACATPVTPGM KVFTNSEKAV KAQKSVMEFL LINHPLDCPI CDQGGECQLQ DLAVGYGASE
     SRYKEEKRVV FHKNVGPLIS MEEMTRCIHC TRCVRFGQEV AGVMELGMLN RGEHSEITTF
     VGQTVDSELS GNMIDLCPVG ALTSKPFRYS ARTWELARRK SVSPHDGLGA NLVVQSKNQR
     VMRVLPLENE DVNECWISDK DRFSYEGLNS ADRLTRPLLK QGGQWIETDW QTALEYVANG
     LSSIKRDHGA DQIAALASPH STLEELYLLG KLMRGIGSDN VDFRLRQSDF SAALKGAPWL
     GMPVADVSTL QRVLVIGSSL RKDHPLLASR LRQAGKKGAR VAVLGAGGED LLMPLAARID
     VAPSGWTAAL AGIARAVATA KGVAAPAGTE GFDGGDAARA AADALLSGER RAVFLGNEAV
     RHPQFAALHA LAQWIATEAG ATLGFLTEAA NTVGGYVAGA LPKQGGANAQ AMLESPRKAY
     VLLNTEPEFD AADPRKALAA LAQAGTVVVL SPFRSEAAMQ YADVILPVTP FTETAGTFVN
     CEGLPQSFNG VVRALGESRP AWKVLRVLGN LLDVAGFDYD SAEAVRAEVL ANPVAPQLSN
     ATDAPIRVSA AAANGIERIA DVPIYHADPI VRRAESLQLT AAARRAQQVA LSADLFAGLG
     IQSGDPVRVT QGEGSVVLPG VLENTLPANT VRVPAATPAA MSLGAMFGTV KVEKAVDLSA
     GQKAAATAGA A
//
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