ID F8KV82_PARAV Unreviewed; 771 AA.
AC F8KV82;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=NADH-quinone oxidoreductase {ECO:0000256|RuleBase:RU003525};
DE EC=7.1.1.- {ECO:0000256|RuleBase:RU003525};
GN Name=nuoG {ECO:0000313|EMBL:CCB87604.1};
GN OrderedLocusNames=PUV_26540 {ECO:0000313|EMBL:CCB87604.1};
OS Parachlamydia acanthamoebae (strain UV7).
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Parachlamydiaceae;
OC Parachlamydia.
OX NCBI_TaxID=765952 {ECO:0000313|EMBL:CCB87604.1, ECO:0000313|Proteomes:UP000000495};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UV7;
RA Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E., Brunham R.C.,
RA Read T.D., Bavoil P.M., Sachse K., Kahane S., Friedman M.G., Rattei T.,
RA Myers G.S.A., Horn M.;
RT "Unity in variety -- the pan-genome of the Chlamydiae.";
RL Mol. Biol. Evol. 0:0-0(2011).
RN [2] {ECO:0000313|EMBL:CCB87604.1, ECO:0000313|Proteomes:UP000000495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UV7 {ECO:0000313|Proteomes:UP000000495};
RX PubMed=21690563; DOI=10.1093/molbev/msr161;
RA Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E., Brunham R.C.,
RA Read T.D., Bavoil P.M., Sachse K., Kahane S., Friedman M.G., Rattei T.,
RA Myers G.S., Horn M.;
RT "Unity in variety--the pan-genome of the Chlamydiae.";
RL Mol. Biol. Evol. 28:3253-3270(2011).
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; FR872580; CCB87604.1; -; Genomic_DNA.
DR RefSeq; WP_013925691.1; NC_015702.1.
DR AlphaFoldDB; F8KV82; -.
DR STRING; 765952.PUV_26540; -.
DR KEGG; puv:PUV_26540; -.
DR eggNOG; COG1034; Bacteria.
DR HOGENOM; CLU_000422_11_6_0; -.
DR OrthoDB; 9805142at2; -.
DR Proteomes; UP000000495; 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; cd02775; MopB_CT; 1.
DR CDD; cd02768; MopB_NADH-Q-OR-NuoG2; 1.
DR Gene3D; 2.40.40.20; -; 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 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:SF15; FORMATE DEHYDROGENASE H; 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}; NAD {ECO:0000256|RuleBase:RU003525};
KW Oxidoreductase {ECO:0000313|EMBL:CCB87604.1};
KW Quinone {ECO:0000256|RuleBase:RU003525};
KW Reference proteome {ECO:0000313|Proteomes:UP000000495};
KW Translocase {ECO:0000256|RuleBase:RU003525}.
FT DOMAIN 8..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 771 AA; 86003 MW; C2BD098F572123D9 CRC64;
MQKSVETTMI NLTIDGQAVT VPKGTTVYHA VKQLGIEIPI FCYQDRMPPF GACRVCLVEV
EKMAKLQTSC TLEATEGMVV RTQSDPAVDG RKAILEFLLI NHPLDCPICD RGGECPLQDQ
ALKFGPGESQ FFEDKRRFKK PLPLGHVLML DRERCITCAR CTRFGEIVAG DHALEFVNRG
YRTEVGTPDN GPAQSKFIGN TIQICPVGAL TSQVYRFRAR PWDNDPTNST CTLCPVGCST
TIDSRDGEIM RMRSHENPPV NDIWLCDKGW FGYEFTAHRN RLQTPMIRIN DKLEPATWDQ
AFSLIAEKIR EAKPQGRLAA WGGNPLTLEE NYLLQKLMRE GAAVNHLDHR IGMPIIDEKD
EGIAPGMEGT IGECEELAYA VIFGLDLTEE FPVIWLRLKQ ALNKGAIVHY FGHYAPEMSA
QLAHVVVHPP GQELEMIKQA NDFIDGMAEK GKGAIFVGKQ YLDMSNRAQL LSQLAQIRKQ
RQACALHVME GRGNSMGARL AGMRPDSGPF DEIIEKPGMN ANQVLEKAAQ SGWDFLYVVG
ADPVLKFPSK LWKACRNQLK FLVVQDLFLT ETALQADVVL PTLSFVEKEG SFVNIEGRVQ
KLHPGKQVPI DIYADGQIFN LIGQHLGLAL SLDVNIVEKI QSKMLSLPRN TNLHVNGVSL
LNPLPTDAFY ATFVYALFDR GNRMKHNPHV MHLAKEPFIR INPLEGQKRG FMDGDKVRVS
RQGNVIVGHI KLDRKVAEKT AVLPLGFPQV AVQELDLNLL NGLIVEINKE V
//
