ID A0A1T0CTS3_9GAMM Unreviewed; 1017 AA.
AC A0A1T0CTS3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=NADH-quinone oxidoreductase {ECO:0000256|RuleBase:RU003525};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU003525};
GN ORFNames=B0680_02715 {ECO:0000313|EMBL:OOS25746.1};
OS Moraxella pluranimalium.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=470453 {ECO:0000313|EMBL:OOS25746.1, ECO:0000313|Proteomes:UP000189800};
RN [1] {ECO:0000313|EMBL:OOS25746.1, ECO:0000313|Proteomes:UP000189800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 54913 {ECO:0000313|EMBL:OOS25746.1,
RC ECO:0000313|Proteomes:UP000189800};
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 pluranimalium CCUG 54913T type
RT 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:OOS25746.1}.
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DR EMBL; MUYU01000006; OOS25746.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T0CTS3; -.
DR STRING; 470453.B0680_02715; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000189800; 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; cd02788; MopB_CT_NDH-1_NuoG2-N7; 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; 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; 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; 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 Quinone {ECO:0000256|RuleBase:RU003525};
KW Reference proteome {ECO:0000313|Proteomes:UP000189800};
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 1017 AA; 111563 MW; E9E60F1BA6882207 CRC64;
MAVIHIDGKT VEVDSADNLL QACLSLGIDI PYFCYHPALG SVGSCRQCAV KQYNNAEDYE
AGRGRLVMSC MVAPTNDMYI SVDDEEAKGF RKRIVEYIMT NHPHDCPTCE EGGHCHLQDM
TYMSGHRQRR YRFTKRTHHN QDLGPFINHE MNRCIACYRC VRFYKDYAGG EDMGVYASNN
RVYFGREADG QFESEFSGNL TEVCPTGVFT DATHSDRYNR KWDMQYAPSV CHGCSSGCNI
SAGERYGEIR RIENRYNHDV NGYFLCDRGR FGYGYVNRAD RPVRPYANGA SGKQLMDANQ
ALDSAIELLK GKKTIGIGTD ATSLENNYAL KKLVGADNYS TGQSMATKAL VEKSVEILRN
DSVYNVSLAQ IEQADAVFVL GEDITQTAAR VALSVRQAAK NEAKKMATAL RTDHWLAEPV
KRIGQSAYSP IYVVDVVDTK LDDIAKVSAV ASIEEIARLG YLVGEVIESF DTHLENLSKP
ALNADADMLD LAYQIAVDLV TANQPLVVSG TSLASAQVIE AAGYIAQALS NKRRAIKSVN
DAELAAYQAL EDAAQTVPEH DPQLVAKPEH DGTGTDKDVQ AQLVRTPKPK ALDAKFVAMA
GIYLCLPSAN SAGLSLLGGQ SIEEVLAKDF DAVVVLENDL SQLSSINVLD KIDGKTVIVI
DHQYYAWHDK ANLVLSASSF AESDGTLVSA EGRAQRFFQA YDKKYYDPTS DIKDAWRWLY
ALAHDAGQVA SAAHLDEVIA DIAADYPQLA GIKDAAPEAD YRITGLKIAR EPRRYSGRTA
MRAPLSIHEP MQPKDVDTAL TFSMEGYVGN QTNPASIPFA WAAGWNSPQA WNKYQDKVGG
KLKGGDVGVR LFDSLPRLDV VYASNRSMVQ DPASTSVFNG VVRLVPVHNL FGSSPMASRS
PVVASQNQDI GWYMTQEDAD HWQVREGDLL SIQSVQGEIV LPVKFAEFIP DGCIGYAAGQ
VPLSPKVPTT IKRADTVDPV YRPAYAVSLD HLPSHHRNPL FKVSDTPIKV APSVEAV
//
