ID A0A0S8DK94_9PROT Unreviewed; 798 AA.
AC A0A0S8DK94;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=NADH-quinone oxidoreductase {ECO:0000256|RuleBase:RU003525};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU003525};
GN ORFNames=AMJ66_00755 {ECO:0000313|EMBL:KPK35595.1};
OS Betaproteobacteria bacterium SG8_40.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1703389 {ECO:0000313|EMBL:KPK35595.1, ECO:0000313|Proteomes:UP000051602};
RN [1] {ECO:0000313|EMBL:KPK35595.1, ECO:0000313|Proteomes:UP000051602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_40 {ECO:0000313|EMBL:KPK35595.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK35595.1}.
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DR EMBL; LJTS01000007; KPK35595.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8DK94; -.
DR PATRIC; fig|1703389.3.peg.1300; -.
DR Proteomes; UP000051602; 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 CDD; cd02775; MopB_CT; 1.
DR CDD; cd02772; MopB_NDH-1_NuoG2; 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; 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; 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};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU003525};
KW Oxidoreductase {ECO:0000313|EMBL:KPK35595.1};
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 216..272
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 798 AA; 85840 MW; 2DCCE8E23BAF0BAD CRC64;
MITLEIDGKT VEVAEHSTVM DAANKLGIYV PHFCYHKKLS IAANCRMCLV QVEKAPKPLP
ACATPVTEGM KVWTHSELAI NAQKAVMEFL LINHPLDCPI CDQGGECQLQ DLAVGYGGSS
SRFHEGKRVV GHKDLGPLVS AEEMSRCIHC TRCVRFGQEI AGIMELGMAG RGEHSEIMAF
VGHTVDSELS GNMIDVCPVG ALTSKPFRYS ARTWELSRRR SVSPHDSLGS NLVVQVKQNR
VMRVLPRENE DVNECWLSDR DRFSYEGLTS KERLTTPMVK RDGRWQEVDW ATALEYVTSE
LSRLREAHGP AALGALATAQ ATSEEFFLLQ KLLRSMGSDN VDFRLRQLDF SGDVPGAGIP
WLGMKVADLN NLDRVLLIGS NVRKEHPLLA QRIRQAVRKN GSHLNVINSV GDDLLVRTHG
RAIVAPGRIA DTIAAVAKAA AERAGVSIAP QIAQAVVDDN ARQIAESLAG GDNKAILLGN
LAQQHPQWSH IRSLANLLAS IVGGRVGVLV DGANTMGGYL CGAVPGGASS SSNSSGRNAR
DMISSPLKAY ILLHAEPELD MALPGAALAA MQSAELVVAM SPYKHRALDY ARVLLPVSPF
TETAGTFVNL EGRTQHFNGV VPPLGDTRPA WKVLRVMGNL LQLDGFDYET IDDVRQQMAD
AIGSVEGRLD NKSHAAPDVS AGAVSATNPD AIERIGEVPA YHADGIVRRA GSLQQTRDAD
VGHAWMNARL IERLALSAGD RVRVSQDGGE AILTVARDDR LPDGCVRVAA ANAATSQLGS
PFGTVSVERL AAVAEVDS
//
