Reviewed,
UniProtKB/Swiss-Prot Q7VRV7 (NUOG_BLOFL)
Last modified
June 16, 2009.
Version 41.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: NADH-quinone oxidoreductase subunit G EC=1.6.99.5 Alternative name(s): NADH dehydrogenase I subunit G NDH-1 subunit G NUO7 | ||||
| Gene names |
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| Organism | Blochmannia floridanus [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 203907 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › ant endosymbionts › Candidatus Blochmannia |
Protein attributes
| Sequence length | 941 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient By similarity. |
| Catalytic activity | NADH + quinone = NAD+ + quinol. |
| Cofactor | Binds 1 2Fe-2S cluster per subunit By similarity. Binds 3 4Fe-4S clusters per subunit By similarity. |
| Subunit structure | Composed of 13 different subunits. Subunits nuoCD, E, F, and G constitute the peripheral sector of the complex. |
| Sequence similarities | Belongs to the complex I 75 kDa subunit family. Contains 1 2Fe-2S ferredoxin-type domain. |
Ontologies
| Keywords | |
|---|---|
| Ligand | 2Fe-2S 4Fe-4S Iron Iron-sulfur Metal-binding NAD Ubiquinone |
| Molecular function | Oxidoreductase |
| PTM | Quinone |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | ATP synthesis coupled electron transport Inferred from electronic annotation. Source: InterPro |
| Cellular component | membrane Inferred from electronic annotation. Source: InterPro |
| Molecular function | 2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 4 iron, 4 sulfur cluster bindingInferred from electronic annotation. Source: UniProtKB-KW NADH dehydrogenase (ubiquinone) activityInferred from electronic annotation. Source: InterPro electron carrier activityInferred from electronic annotation. Source: InterPro iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW quinone bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 941 | 941 | NADH-quinone oxidoreductase subunit G | PRO_0000118545 | |||||
Regions | |||||||||
| Domain | 1 – 91 | 91 | 2Fe-2S ferredoxin-type | ||||||
Sites | |||||||||
| Metal binding | 35 | 1 | Iron-sulfur 1 (2Fe-2S) By similarity | ||||||
| Metal binding | 46 | 1 | Iron-sulfur 1 (2Fe-2S) By similarity | ||||||
| Metal binding | 49 | 1 | Iron-sulfur 1 (2Fe-2S) By similarity | ||||||
| Metal binding | 75 | 1 | Iron-sulfur 1 (2Fe-2S) By similarity | ||||||
| Metal binding | 107 | 1 | Iron-sulfur 2 (4Fe-4S); via pros nitrogen By similarity | ||||||
| Metal binding | 111 | 1 | Iron-sulfur 2 (4Fe-4S) By similarity | ||||||
| Metal binding | 114 | 1 | Iron-sulfur 2 (4Fe-4S) By similarity | ||||||
| Metal binding | 120 | 1 | Iron-sulfur 2 (4Fe-4S) By similarity | ||||||
| Metal binding | 159 | 1 | Iron-sulfur 3 (4Fe-4S) By similarity | ||||||
| Metal binding | 162 | 1 | Iron-sulfur 3 (4Fe-4S) By similarity | ||||||
| Metal binding | 165 | 1 | Iron-sulfur 3 (4Fe-4S) By similarity | ||||||
| Metal binding | 209 | 1 | Iron-sulfur 3 (4Fe-4S) By similarity | ||||||
| Metal binding | 236 | 1 | Iron-sulfur 4 (4Fe-4S) Potential | ||||||
| Metal binding | 239 | 1 | Iron-sulfur 4 (4Fe-4S) Potential | ||||||
| Metal binding | 243 | 1 | Iron-sulfur 4 (4Fe-4S) Potential | ||||||
| Metal binding | 271 | 1 | Iron-sulfur 4 (4Fe-4S) Potential | ||||||
Sequences
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References
| [1] | "The genome sequence of Blochmannia floridanus: comparative analysis of reduced genomes." Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F., Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B., van Ham R.C.H.J., Gross R., Moya A. Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003) [PubMed: 12886019] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| BX248583 Genomic DNA. Translation: CAD83177.1. | |
| RefSeq | NP_878771.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1499688. |
| GenomeReviews | Gene locus Bfl488 in contig BX248583_GR. |
| KEGG | bfl:Bfl488. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q7VRV7. |
| OMA | Q7VRV7. WVEVSWE. |
Enzyme and pathway databases | |
| BioCyc | CBLO203907:BFL488-MON. |
Family and domain databases | |
| InterPro | IPR006058. 2Fe2S_fd_BS. IPR001041. Ferredoxin. IPR006963. Mopterin_OxRdtase_Fe4S4. IPR000283. NADH_UbQ_OxRdtase_75KDa_su_CS. IPR010228. NADH_UbQ_OxRdtase_Gsu. IPR019574. NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd. [Graphical view] |
| Pfam | PF00111. Fer2. 1 hit. PF04879. Molybdop_Fe4S4. 1 hit. PF10588. NADH-G_4Fe-4S_3. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01973. NuoG. 1 hit. |
| PROSITE | PS00197. 2FE2S_FER_1. False negative. PS51085. 2FE2S_FER_2. 1 hit. PS00641. COMPLEX1_75K_1. 1 hit. PS00642. COMPLEX1_75K_2. 1 hit. PS00643. COMPLEX1_75K_3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NUOG_BLOFL | ||||||||
| Accession | Primary (citable) accession number: Q7VRV7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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