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
//