Reviewed,
UniProtKB/Swiss-Prot P59962 (NUOG_MYCBO)
Last modified
June 16, 2009.
Version 45.
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 | ||||
| Gene names |
| ||||
| Organism | Mycobacterium bovis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1765 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex |
Protein attributes
| Sequence length | 806 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 menaquinone. 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. |
| 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 |
| 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 molybdenum ion bindingInferred from electronic annotation. Source: InterPro 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 – 806 | 806 | NADH-quinone oxidoreductase subunit G | PRO_0000118558 | |||||
Regions | |||||||||
| Domain | 15 – 93 | 79 | 2Fe-2S ferredoxin-type | ||||||
Sites | |||||||||
| Metal binding | 49 | 1 | Iron-sulfur 1 (2Fe-2S) By similarity | ||||||
| Metal binding | 60 | 1 | Iron-sulfur 1 (2Fe-2S) By similarity | ||||||
| Metal binding | 63 | 1 | Iron-sulfur 1 (2Fe-2S) By similarity | ||||||
| Metal binding | 77 | 1 | Iron-sulfur 1 (2Fe-2S) By similarity | ||||||
| Metal binding | 111 | 1 | Iron-sulfur 2 (4Fe-4S); via pros nitrogen By similarity | ||||||
| Metal binding | 115 | 1 | Iron-sulfur 2 (4Fe-4S) By similarity | ||||||
| Metal binding | 118 | 1 | Iron-sulfur 2 (4Fe-4S) By similarity | ||||||
| Metal binding | 124 | 1 | Iron-sulfur 2 (4Fe-4S) By similarity | ||||||
| Metal binding | 164 | 1 | Iron-sulfur 3 (4Fe-4S) By similarity | ||||||
| Metal binding | 167 | 1 | Iron-sulfur 3 (4Fe-4S) By similarity | ||||||
| Metal binding | 170 | 1 | Iron-sulfur 3 (4Fe-4S) By similarity | ||||||
| Metal binding | 214 | 1 | Iron-sulfur 3 (4Fe-4S) By similarity | ||||||
| Metal binding | 240 | 1 | Iron-sulfur 4 (4Fe-4S) Potential | ||||||
| Metal binding | 243 | 1 | Iron-sulfur 4 (4Fe-4S) Potential | ||||||
| Metal binding | 247 | 1 | Iron-sulfur 4 (4Fe-4S) Potential | ||||||
| Metal binding | 275 | 1 | Iron-sulfur 4 (4Fe-4S) Potential | ||||||
Sequences
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References
| [1] | "The complete genome sequence of Mycobacterium bovis." Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J. Hewinson R.G.Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003) [PubMed: 12788972] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-935 / AF2122/97. |
Cross-references
Sequence databases | |
|---|---|
| BX248345 Genomic DNA. Translation: CAD95267.1. | |
| RefSeq | NP_856820.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1093502. |
| GenomeReviews | Gene locus Mb3175 in contig BX248333_GR. |
| KEGG | mbo:Mb3175. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P59962. |
| OMA | P59962. LKQGGQW. |
Enzyme and pathway databases | |
| BRENDA | 1.6.99.5. 3091. |
Family and domain databases | |
| InterPro | IPR006058. 2Fe2S_fd_BS. IPR009010. Asp_de-COase-like_fold. IPR001041. Ferredoxin. IPR006656. Mopterin_OxRdtase. IPR006963. Mopterin_OxRdtase_Fe4S4. IPR006657. MPT_dinuc_bd. IPR000283. NADH_UbQ_OxRdtase_75KDa_su_CS. IPR010228. NADH_UbQ_OxRdtase_Gsu. IPR019574. NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd. [Graphical view] |
| Gene3D | G3DSA:2.40.40.20. Asp_decarboxylase-like_fold. 1 hit. |
| Pfam | PF00111. Fer2. 1 hit. PF04879. Molybdop_Fe4S4. 1 hit. PF00384. Molybdopterin. 1 hit. PF01568. Molydop_binding. 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_MYCBO | ||||||||
| Accession | Primary (citable) accession number: P59962 | ||||||||
| 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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