ID A0A0B0HEQ3_SOVGS Unreviewed; 782 AA.
AC A0A0B0HEQ3;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=NADH-quinone oxidoreductase {ECO:0000256|RuleBase:RU003525};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU003525};
GN Name=ndhG {ECO:0000313|EMBL:KHF25926.1};
GN ORFNames=JV46_20340 {ECO:0000313|EMBL:KHF25926.1};
OS Solemya velum gill symbiont.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts.
OX NCBI_TaxID=2340 {ECO:0000313|EMBL:KHF25926.1, ECO:0000313|Proteomes:UP000030856};
RN [1] {ECO:0000313|EMBL:KHF25926.1, ECO:0000313|Proteomes:UP000030856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH {ECO:0000313|EMBL:KHF25926.1,
RC ECO:0000313|Proteomes:UP000030856};
RX PubMed=25342549; DOI=10.1186/1471-2164-15-924;
RA Dmytrenko O., Russell S.L., Loo W.T., Fontanez K.M., Liao L., Roeselers G.,
RA Sharma R., Stewart F.J., Newton I.L., Woyke T., Wu D., Lang J.M.,
RA Eisen J.A., Cavanaugh C.M.;
RT "The genome of the intracellular bacterium of the coastal bivalve, Solemya
RT velum: a blueprint for thriving in and out of symbiosis.";
RL BMC Genomics 15:924-924(2014).
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}.
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:KHF25926.1}.
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DR EMBL; JRAA01000001; KHF25926.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B0HEQ3; -.
DR STRING; 2340.JV46_20340; -.
DR PATRIC; fig|2340.3.peg.438; -.
DR eggNOG; COG1034; Bacteria.
DR Proteomes; UP000030856; Unassembled WGS sequence.
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; 3.30.200.210; -; 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:KHF25926.1};
KW Quinone {ECO:0000256|RuleBase:RU003525};
KW Reference proteome {ECO:0000313|Proteomes:UP000030856};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU003525}.
FT DOMAIN 7..85
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 85..124
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 222..278
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 782 AA; 84214 MW; 926A25D94F89F490 CRC64;
MAMSEEQTIT IEVDGNQLPA KPGQMLIEVT DAAGITVPRF CYHKNLSISA NCRMCLVEVE
NAPKPLPACA TPCADGMKVF TKSPLARAAQ KGTMEFLLIN HPLDCPICDQ GGECELQDVA
IGYGNDVSRF AENKRVVADP DIGPLVATEM TRCIHCTRCV RFGDEIAGLR ELGATGRGEH
TKIGTYVKHA MTSELSGNVI DLCPVGALTS KPFRYTARAW EVTQQETIAP HDSVGSNLYA
HVRRGKVMRI VPRENDAINQ SWISDRDRFG YEGLDHEERL TQPMVREGGS LKTVSWDDAL
TKAAESLAKV KTQPDEVMTL VSPSATLEEM YLAQKLVRDM GSNNIDHRLR QIDFRGDSAD
PQVSWLGVTL DDLENSDAVL LVGSNVRKEQ PMINHRLRLA ANRGASVMSI NPLSTNANYT
AGPSLVVKPS EMVKTLQALA SAVGAGDEDM PVSDEIRAIA ENLRSAADAV VLLGNIAVSH
PDYSIVRDTA ARVAEATGCA LGIIPEAANS VGAWIAGAVP NRLPGGKPVS ASGRSVNEMM
TPPPQCALLI GVEPMADVAR GRALVNSLRG TESVIAVSAY MSDALMEVAD VVLPMTPFSE
TSGTYVNAQR DMQSFNGLVK PKGESRPGWK ILRVLGNFLD LEGFDYESSE DVCNELIQQC
DDSLPEMKVG QSGASESKTE AGGVEATPYV PAYSVDAVVR RSEPLQSTED ARCVFRMHPQ
TASAHGLSDG NWAILKQGEN HCSAKVVTDD ELCEDVLVYA SQSGDLIWGN SMIEKADTGV
IV
//
