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Database: UniProt
Entry: A0A370G2U8_GLULI
LinkDB: A0A370G2U8_GLULI
Original site: A0A370G2U8_GLULI 
ID   A0A370G2U8_GLULI        Unreviewed;       688 AA.
AC   A0A370G2U8;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=NADH-quinone oxidoreductase {ECO:0000256|RuleBase:RU003525};
DE            EC=7.1.1.- {ECO:0000256|RuleBase:RU003525};
GN   ORFNames=C7453_104138 {ECO:0000313|EMBL:RDI38197.1}, HLH32_09035
GN   {ECO:0000313|EMBL:MBB2186530.1};
OS   Gluconacetobacter liquefaciens (Acetobacter liquefaciens).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconacetobacter.
OX   NCBI_TaxID=89584 {ECO:0000313|EMBL:RDI38197.1, ECO:0000313|Proteomes:UP000254958};
RN   [1] {ECO:0000313|EMBL:RDI38197.1, ECO:0000313|Proteomes:UP000254958}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5603 {ECO:0000313|EMBL:RDI38197.1,
RC   ECO:0000313|Proteomes:UP000254958};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:MBB2186530.1, ECO:0000313|Proteomes:UP000562982}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 1382 {ECO:0000313|EMBL:MBB2186530.1,
RC   ECO:0000313|Proteomes:UP000562982};
RA   Sombolestani A.;
RT   "Description of novel Gluconacetobacter.";
RL   Submitted (APR-2020) 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}.
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:RDI38197.1}.
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DR   EMBL; JABEQI010000004; MBB2186530.1; -; Genomic_DNA.
DR   EMBL; QQAW01000004; RDI38197.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A370G2U8; -.
DR   OrthoDB; 9816402at2; -.
DR   Proteomes; UP000254958; Unassembled WGS sequence.
DR   Proteomes; UP000562982; 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: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; cd02773; MopB_Res-Cmplx1_Nad11; 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   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   InterPro; IPR015405; NDUFS1-like_C.
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   Pfam; PF09326; NADH_dhqG_C; 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; PS00642; COMPLEX1_75K_2; 1.
DR   PROSITE; PS00643; COMPLEX1_75K_3; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:MBB2186530.1};
KW   Quinone {ECO:0000256|RuleBase:RU003525};
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   688 AA;  73793 MW;  0202E35EDA1FD4D5 CRC64;
     MVKVTVDGIV VDVPNGSSAL QACEAAGKEI PRFCFHERLS VAGNCRMCLV QVVRAPKPVA
     SCGFPVAEGM EILTDTEIVR KARRAVMEFL LINHPLDCPI CDQGGECDLQ DQAFGYGADH
     SRYQEAKRAV KDKYLGPLVK TVMTRCIQCT RCIRFATEIA GVPELGAVSR GENMEVTNYV
     EKALTSELSG NLIDICPVGA LTSKPYAFTA RPWELKRTDS IDVSDAVGAN ISLHVRGSAV
     LRAVPRVNDA VNEEWLADKG RFSVDGLKHR RLDRPWVRVH GKLQAVSWQD AFVAIGRRLD
     GVPGDRIGAI AGDLCDAESL LALKDLMTAL GSPNIDCRQD GAEYDLSHRA YYTFGTSIAG
     IEDADALLIV GAIPRQEAPV LNARIRKRFL SAGRGGFPIG LIGAPTADPT YKADLLGEGP
     DVLAALRDGT HPFAETLKAA KKPMIIVGHG ALMRPDARAI LASTWALAVE TGAVAAGWNG
     FNVLHRAASR VAGLDLGLVP GKGGRSAAGM MSGGVDVLWL LGADEFHTAQ IGPQTFVIYQ
     GHHGDAAAAR ADVILPGATY AEKSGTYVNT EGRVQRSFRA IMPPGDARED WRILRAFSEV
     VGHTLPYDTM EVLRERLATV NPVFRVIGGL DAVDVSVLPG PAGGGAVSPV PFRPVFDDYY
     QTDPICRASP TMGECSRIYV HPRTVAAE
//
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