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Database: UniProt
Entry: A0A1Q4GTQ9_9PROT
LinkDB: A0A1Q4GTQ9_9PROT
Original site: A0A1Q4GTQ9_9PROT 
ID   A0A1Q4GTQ9_9PROT        Unreviewed;       788 AA.
AC   A0A1Q4GTQ9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=NADH-quinone oxidoreductase {ECO:0000256|RuleBase:RU003525};
DE            EC=7.1.1.- {ECO:0000256|RuleBase:RU003525};
GN   ORFNames=BGP21_13080 {ECO:0000313|EMBL:OJZ19010.1};
OS   Thiobacillus sp. 65-29.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=1895862 {ECO:0000313|EMBL:OJZ19010.1, ECO:0000313|Proteomes:UP000186483};
RN   [1] {ECO:0000313|EMBL:OJZ19010.1, ECO:0000313|Proteomes:UP000186483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=65-29 {ECO:0000313|EMBL:OJZ19010.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-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}.
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:OJZ19010.1}.
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DR   EMBL; MKWN01000023; OJZ19010.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q4GTQ9; -.
DR   STRING; 1895862.BGP21_13080; -.
DR   Proteomes; UP000186483; 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; cd02772; MopB_NDH-1_NuoG2; 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   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|RuleBase:RU003525};
KW   Quinone {ECO:0000256|RuleBase:RU003525};
KW   Translocase {ECO:0000256|RuleBase:RU003525}.
FT   DOMAIN          2..80
FT                   /note="2Fe-2S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51085"
FT   DOMAIN          80..119
FT                   /note="4Fe-4S His(Cys)3-ligated-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51839"
FT   DOMAIN          217..273
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
SQ   SEQUENCE   788 AA;  83804 MW;  C296832F04384C37 CRC64;
     MSLLNIEIDG QPLQIESGKT IMDAAGRLGI TIPYFCYHKK LSIAASCRMC LVEVEKAPKP
     LPACATPVAE GMKVHTRSQY AINAQKGVME FLLINHPLDC PICDQGGECT LQDIAVGYGA
     SASRYGEAKR VVIEKNLGPL IATDMTRCIH CSRCVRFGVE IGGIMELGMP GRGEHTEVMS
     FLESQVASEI SGNVIDLCPV GALTSKPFRY SARSWELARR PSISPHDSLG ANIEVQVKND
     RVMRVLPRDN EAVNECWIAD RDRFAYEGLN SAERLTRPMV KREGQWLEVS WQDALDYVVA
     RLKLIPAAQI GALAAPHRTV EELYLLQKLM RELGAGNVDH RLRQTDFGLD GQARGSFWLG
     LPVAELSGLD RALVIGSNPR KDHPLLAQRL RAAVRAGGEI SLVGVSGEDF LARVHARSTV
     APSQLPAALA GVCAALATLK GEGVPALAAA QLGTGAPDAA AQRMAASLAS GERRAVLLGN
     LAQHHPAYAQ LHALAQEIAR LAGASFGVLG EAANSVGAAV AGAVPHHGPL GQPAVQGLNA
     GQMLAQHLRA YVLLDVEMEL DTHDPVLALT SLQNAECVVA LSSYTGRALD YADVLLPVAP
     WTETSGTFVN TEGRVQSFAA VVKPLGETRP AWKVLRVLGN LLGLAGFDQD DTREVLREAL
     GETAEAGVRA ALDNRVAGVT PAAVPAAAGI ERIAEVPIYQ TDPTVRRAPA LQRTADAALP
     VAHMHGSLIA HLGLEENGRA SVRQTASALT LKVERDDNLP DGCIRIPAGH PLTASLGPMF
     GPVAVERV
//
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