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Database: UniProt
Entry: D2ZV23_NEIMU
LinkDB: D2ZV23_NEIMU
Original site: D2ZV23_NEIMU 
ID   D2ZV23_NEIMU            Unreviewed;       753 AA.
AC   D2ZV23;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 63.
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:EFC89179.1};
GN   ORFNames=NEIMUCOT_04464 {ECO:0000313|EMBL:EFC89179.1};
OS   Neisseria mucosa ATCC 25996.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=546266 {ECO:0000313|EMBL:EFC89179.1, ECO:0000313|Proteomes:UP000003344};
RN   [1] {ECO:0000313|EMBL:EFC89179.1, ECO:0000313|Proteomes:UP000003344}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25996 {ECO:0000313|EMBL:EFC89179.1,
RC   ECO:0000313|Proteomes:UP000003344};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (OCT-2009) 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}.
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:EFC89179.1}.
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DR   EMBL; ACDX02000004; EFC89179.1; -; Genomic_DNA.
DR   RefSeq; WP_003741950.1; NZ_ACDX02000004.1.
DR   AlphaFoldDB; D2ZV23; -.
DR   STRING; 546266.NEIMUCOT_04464; -.
DR   GeneID; 61323318; -.
DR   eggNOG; COG1034; Bacteria.
DR   Proteomes; UP000003344; 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; cd02772; MopB_NDH-1_NuoG2; 1.
DR   Gene3D; 3.10.20.740; -; 1.
DR   Gene3D; 3.30.200.210; -; 1.
DR   Gene3D; 3.30.70.20; -; 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; 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}; NAD {ECO:0000256|RuleBase:RU003525};
KW   Oxidoreductase {ECO:0000313|EMBL:EFC89179.1};
KW   Quinone {ECO:0000256|RuleBase:RU003525};
KW   Translocase {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   753 AA;  81498 MW;  B452DA3B6B27BA88 CRC64;
     MLQIEIDGKQ VSVEQGATVI EAAHKLGTYI PHFCYHKKLS IAANCRMCLV DVEKAPKPLP
     ACATPVTDGM IVRTHSAKAR EAQEGVMEFL LINHPLDCPT CDQGGECQLQ DLAVGYGKTT
     SRYTEEKRSV VGKDMGPLVS AEEMSRCIHC TRCVRFTEEI AGLQEIAMAN RGEHSEIMPF
     IGKAVETELS GNVIDLCPVG ALTSKPFRFN ARTWELNRRK SVSAHDALGS NLIVQTKDHT
     VRRVLPLENE AINECWLSDR DRFAYEGLYH ESRLKNPKIK QGGEWMDVDW KTALEYVRSA
     IECIAKDGNQ NQVGIWANPM NTVEELYLAK KFADGLGVKN FATRLRQQDK RLSDDLNGAQ
     WLGQSIESLA DNEAVLVVGA NLRKEQPLLT ARLRRAAKER MALSVLASSK EELLMPLLAQ
     EAVHPDEWAG RLKNLSADAE HAITASLKNA EKAAVILGAE VQNHPDYAAI YAAAQELADA
     TGAVLGILPQ AANSVGADVL GVNSGESVAE MANAPKQAVL LLNVEPEIDT ADGAKAVAAL
     KQAKSVMAFT PFVSETLLDV CDVLLPIAPF TETSGSFINM EGRLQSFHGV VQGFGDSRPL
     WKVLRVLGNL FDLQGFEYHD TAAILKDALD VESLPSKLNN RAASTQKDFQ TTSNRLVRVG
     GVGIYHTDAI VRRSAPLQAT SHAAVPAARV NPNTLARLGL QDGQTAIAKQ NGAGVSVVVK
     ADAGLPENVV HLPLHTENAA LGALMDTIEL AGA
//
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