ID A0A1T0CKV2_9GAMM Unreviewed; 1033 AA.
AC A0A1T0CKV2;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=NADH-quinone oxidoreductase {ECO:0000256|RuleBase:RU003525};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU003525};
GN ORFNames=B0682_00820 {ECO:0000313|EMBL:OOS22791.1};
OS Moraxella lincolnii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=90241 {ECO:0000313|EMBL:OOS22791.1, ECO:0000313|Proteomes:UP000191094};
RN [1] {ECO:0000313|EMBL:OOS22791.1, ECO:0000313|Proteomes:UP000191094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 9405 {ECO:0000313|EMBL:OOS22791.1,
RC ECO:0000313|Proteomes:UP000191094};
RA Salva-Serra F., Engstrom-Jakobsson H., Thorell K., Jaen-Luchoro D.,
RA Gonzales-Siles L., Karlsson R., Yazdan S., Boulund F., Johnning A.,
RA Engstrand L., Kristiansson E., Moore E.;
RT "Draft genome sequence of Moraxella lincolnii CCUG 9405T type strain.";
RL Submitted (FEB-2017) 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 -!- 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:OOS22791.1}.
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DR EMBL; MUYT01000001; OOS22791.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T0CKV2; -.
DR STRING; 90241.B0682_00820; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000191094; 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 Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.200.210; -; 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; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 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 Quinone {ECO:0000256|RuleBase:RU003525};
KW Reference proteome {ECO:0000313|Proteomes:UP000191094};
KW Translocase {ECO:0000256|ARBA:ARBA00022967, ECO:0000256|RuleBase:RU003525}.
FT DOMAIN 1..86
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 86..125
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 224..280
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 1033 AA; 115588 MW; F57B7E48502FDEA5 CRC64;
MAVIHIDGKT YDVDGSDNLL SACLSLGIDV PYFCYHPALG SVGSCRQCAV KQYNNAEDYQ
AGKGRLVMSC MVAPSDDMYI SVDDDEAKAF RKSIVEYLMT NHPHDCPTCE EGGHCHLQDM
TYMSGHHRRR YRFTKRTHHN QELGPFIAHE MNRCIACYRC VRFYQDYAGG DDLGVYASNN
RVYFGRPEDG QFDSEFSGNL TEVCPTGVFT DKTHSERYNR KWDMQYAPSI CHGCSAGCNI
SAGERYGELR RIENRYNHDV NGYFLCDRGR FGYGYVNRAD RPTQAIERIN DKQVKINIDY
ALDETVKRLK GKKIIGIGSA RASLETNFSL KKLVGSDNFS TGLNATQQHL VQGVIDILQD
SNTHNVSMRE IETHDAVWVI GEDITQTSPR IALAVRQAAK NKAKKLANDV QAQQWLAEPV
KRVAQNQLSP VYITDVHDTK LSDISKLSLS ATPDDLLALV QAVIEQINTV TMDKQVLQNE
HDEGKLWQQL QENNQHSQQN NTNTNTNTNT NASHDEMQKT LAILIAHDLL MAQKPLIVSG
VSLGDDRLLT ASQHLVRVLT DKRMMLNTVK QPSNQSAQPT SLVQPTKDKE LTAKPNHQLD
EQADNKHQNQ TLRQDMPIDE HMLRMQYQAS IYLVVPEVNS VGVVLLGGQD IDTLLATDFE
AVVVVENQLT DAIGDIALKK LLTDNTVICL DHQRLDWHQH VDIVLPAASF AEADGTVVSA
EGRAQRFFQA YDPNYYHPLY GIKEGWRWLH AVATSLNDEP FGWTQLDDVI DELIATHSHL
QGIKDAAPNA DFRISGLKVA REPRRYSGRT AMRASLSVHE PMQPKDLDTA LTFSMEGYVG
DKTPSGMIPF AWSAGWNSPQ AWNKYQNKVG GKLKAGDVGV CLFANKWHDN TADAHKTDKH
GQAFGQDDNF ANQSSVNTQQ HTNQNGLLLV PIYDLYASSP MAKRSAVVQS QLIAPSYRIN
TQLAKWLGIK ADDMLTIIND SQEFAYPIHI DDSMADGCIG FIANLMPIIN HRQAFTVKVQ
TVHAPQLIDN GEV
//
