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Database: UniProt
Entry: V4JTB2_9GAMM
LinkDB: V4JTB2_9GAMM
Original site: V4JTB2_9GAMM 
ID   V4JTB2_9GAMM            Unreviewed;       800 AA.
AC   V4JTB2;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=NADH-quinone oxidoreductase {ECO:0000256|RuleBase:RU003525};
DE            EC=7.1.1.- {ECO:0000256|RuleBase:RU003525};
GN   ORFNames=N838_08405 {ECO:0000313|EMBL:ESQ15525.1};
OS   Thiohalocapsa sp. PB-PSB1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thiohalocapsa.
OX   NCBI_TaxID=1385625 {ECO:0000313|EMBL:ESQ15525.1, ECO:0000313|Proteomes:UP000017935};
RN   [1] {ECO:0000313|EMBL:ESQ15525.1, ECO:0000313|Proteomes:UP000017935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Wilbanks E.G., Jaekel U., Salman V., Humphrey P.T., Eisen J.A.,
RA   Facciotti M.T., Buckley D.H., Zinder S.H., Druschel G.K., Fike D.A.,
RA   Orphan V.J.;
RT   "A sulfurous symbiosis: microscale sulfur cycling in the pink berry
RT   consortia of the Sippewissett salt marsh.";
RL   Submitted (AUG-2013) 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   -!- FUNCTION: NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur
CC       (Fe-S) centers, to quinones in the respiratory chain. The immediate
CC       electron acceptor for the enzyme in this species is believed to be
CC       ubiquinone. Couples the redox reaction to proton translocation (for
CC       every two electrons transferred, four hydrogen ions are translocated
CC       across the cytoplasmic membrane), and thus conserves the redox energy
CC       in a proton gradient. {ECO:0000256|ARBA:ARBA00002378}.
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}.
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:ESQ15525.1}.
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DR   EMBL; AVFR01000382; ESQ15525.1; -; Genomic_DNA.
DR   AlphaFoldDB; V4JTB2; -.
DR   PATRIC; fig|1385625.5.peg.2668; -.
DR   Proteomes; UP000017935; Unassembled WGS sequence.
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; 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: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; PF01568; Molydop_binding; 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   Quinone {ECO:0000256|RuleBase:RU003525};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017935};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Translocase {ECO:0000256|RuleBase:RU003525}.
SQ   SEQUENCE   800 AA;  85211 MW;  7CC9B087AA1A525D CRC64;
     MSDKITIELD GRACEAVPGE MIIAVADREG IAIPRFCYHQ KLSIAANCRM CLVEAEQGGR
     PFPKPVPACA TPVGNGMKVQ TRSHKALEAQ RGTMEFLLIN HPLDCPICDQ GGECELQDVS
     MGYGSDVSRF TERKRVVKDE NLGPLIATDM TRCIHCTRCV RFGAEIAGSR ELGATGRGEE
     MRIGTFVEHT VAHELSGNII DLCPVGALTS KPYRFTARAW ELSREEGIAA HDAVGSNLYL
     HVRGGRVMRV HPRDNEAVNE TWISDRDRFS YEGLASETRL RSPLVKRDGI WHEVDWQSAL
     QLAAGGLRGV DADQIGWLMA ANATLEELYL AQKLVRGIGG LHIDTRVRQQ DFRGDESDPP
     VPWLGLPIAQ LEKQTALLLI GSDIRQEQPL LAHRIRKAAL AGGSVFVVNP YQLALTHPAS
     QFTAPPGDLP LELAAIAKVL GQTGTAATAE LIHQAQPTDA HTAAAQALRD AGADDAGIVL
     LGALAEAGPD YALIKSLAYA IADAAGCRIG FLPRAANSVG AALAGALPHL DAGGRSTSAP
     GLNALAMLTE PRAAYVLWGL DPAMDLLDPS LALSVLGESG LVIACSAFRH PSLDSVANLM
     LPIASFAETS GTFVNASGDW QRFQGAVAPP GQARPGWKVL RVLGNLLELD GFDYASARQV
     HDEVKRTCNG IMPDNNPRGT YDHAAPTSLP ADGATTLMRV GNVPIYSVDQ LVRAAPSLQR
     TPSAGSLAIF LHPDQAAKVG VKDGDTVEVA QGRARARMDV RYDDSLAIGC ARIPAAVTGS
     EELGAQIGPI TLFKTHGESA
//
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