ID A0A0N9IEW6_9PSEU Unreviewed; 814 AA.
AC A0A0N9IEW6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=NADH-quinone oxidoreductase {ECO:0000256|RuleBase:RU003525};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU003525};
GN ORFNames=AOZ06_50245 {ECO:0000313|EMBL:ALG13973.1};
OS Kibdelosporangium phytohabitans.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Kibdelosporangium.
OX NCBI_TaxID=860235 {ECO:0000313|EMBL:ALG13973.1, ECO:0000313|Proteomes:UP000063699};
RN [1] {ECO:0000313|EMBL:ALG13973.1, ECO:0000313|Proteomes:UP000063699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KLBMP1111 {ECO:0000313|EMBL:ALG13973.1,
RC ECO:0000313|Proteomes:UP000063699};
RA Qin S., Xing K.;
RT "Genome sequencing of Kibdelosporangium phytohabitans.";
RL Submitted (JUL-2015) 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}.
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DR EMBL; CP012752; ALG13973.1; -; Genomic_DNA.
DR RefSeq; WP_054295846.1; NZ_JADBEI010000001.1.
DR AlphaFoldDB; A0A0N9IEW6; -.
DR STRING; 860235.AOZ06_50245; -.
DR KEGG; kphy:AOZ06_50245; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000063699; Chromosome.
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; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.740; -; 2.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
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; 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:SF12; NADH-QUINONE OXIDOREDUCTASE SUBUNIT G; 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|RuleBase:RU003525};
KW Quinone {ECO:0000256|RuleBase:RU003525};
KW Reference proteome {ECO:0000313|Proteomes:UP000063699};
KW Translocase {ECO:0000256|RuleBase:RU003525}.
FT DOMAIN 15..97
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 99..138
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 237..293
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 814 AA; 86356 MW; 99D24477ADB8115D CRC64;
MTVAPERNEL VVPEGHVKLV IDGIEVVAPK GELLIRTAER MGITIPRFCD HPLLDPAGAC
RQCLVEVEMG GRPMPKPQAS CTITVADGMV VKTQVTSPVA DKAQQGVMEL LLINHPLDCP
ICDKGGECPL QNQALAHGRT DSRFVDKKRT FPKPIPISTQ VLLDRERCVL CQRCTRFSAQ
IAGDPFIELL ERGAQQQIGI AEEKPFQSYF SGNTIQICPV GALTSAAYRF RSRPFDLVST
PSVCEHCSSG CAERTDWRRG KVMRKLAAND PEVNEEWICD KGRFAFRYAS AGDRVLRPQV
RDKETGQLRD ASWTEALQVA AEALTKARGA AGVLTGGRLT VEDAYAYSKF ARVALGTNDI
DFRARPHSVE EQEFLASTVV GTTPETGVTF QGIEAAPTVL CVAFEPEEEA PIVFLRLRKA
ARKGSTKVVH IGQWTTPSVE KTFGTLLATP PGGEADAVDA LSEHAADVVD GLAKPGSVIL
VGERAAQVPG LFSALLRLSA RTGAKIAWIP RRAGERGAVE VGALPTLLPG GRLVADAAAR
AEVEQAWGLE PGSLPGAPGR DTSAIVEAAA SGELKALVIG GVDPYDLPDP QLALEALAAA
DFVLSLELRH SAVSEYADVV LPIAPSVEKA GTFLNWEGRR REFGTTLDGT GALPDCRVLD
TLAVEMDADL FTQTPTAAAG DLARLGATGT AKAVAPEVES RQQGLPHNDG QALLATWRQL
LDNGSLQEGE PHLAGTARKV VARLSAHTAA VLGVDKAEAV TVSTDKGAVT VPVEYADLPD
GVVWLPGNSG DATVRRTLGA VHGTAVDVHP GGTS
//
