Q9K1B0 (NUOL_NEIMB) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 68.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: NADH-quinone oxidoreductase subunit L EC=1.6.99.5 Alternative name(s): NADH dehydrogenase I subunit L NDH-1 subunit L | ||||
| Gene names |
| ||||
| Organism | Neisseria meningitidis serogroup B | ||||
| Taxonomic identifier | 491 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria |
Protein attributes
| Sequence length | 674 AA. |
| Sequence status | Complete. |
| 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. |
| Subcellular location | Cell membrane; Multi-pass membrane protein Potential. |
| Sequence similarities | Belongs to the complex I subunit 5 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell membrane Membrane |
| Domain | Transmembrane Transmembrane helix |
| Ligand | NAD Ubiquinone |
| Molecular function | Oxidoreductase |
| PTM | Quinone |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | ATP synthesis coupled electron transport Inferred from electronic annotation. Source: InterPro |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | NADH dehydrogenase (ubiquinone) activity Inferred 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 – 674 | 674 | NADH-quinone oxidoreductase subunit L | PRO_0000118220 | |||||
Regions | |||||||||
| Transmembrane | 4 – 24 | 21 | Helical; Potential | ||||||
| Transmembrane | 36 – 56 | 21 | Helical; Potential | ||||||
| Transmembrane | 67 – 87 | 21 | Helical; Potential | ||||||
| Transmembrane | 90 – 110 | 21 | Helical; Potential | ||||||
| Transmembrane | 115 – 135 | 21 | Helical; Potential | ||||||
| Transmembrane | 140 – 160 | 21 | Helical; Potential | ||||||
| Transmembrane | 180 – 200 | 21 | Helical; Potential | ||||||
| Transmembrane | 219 – 239 | 21 | Helical; Potential | ||||||
| Transmembrane | 259 – 279 | 21 | Helical; Potential | ||||||
| Transmembrane | 293 – 313 | 21 | Helical; Potential | ||||||
| Transmembrane | 348 – 368 | 21 | Helical; Potential | ||||||
| Transmembrane | 385 – 405 | 21 | Helical; Potential | ||||||
| Transmembrane | 425 – 445 | 21 | Helical; Potential | ||||||
| Transmembrane | 488 – 508 | 21 | Helical; Potential | ||||||
| Transmembrane | 549 – 569 | 21 | Helical; Potential | ||||||
| Transmembrane | 653 – 673 | 21 | Helical; Potential | ||||||
Sequences
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References
| [1] | "Complete genome sequence of Neisseria meningitidis serogroup B strain MC58." Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H., Salzberg S.L., White O. Venter J.C.Science 287:1809-1815(2000) [PubMed: 10710307] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MC58 / Serogroup B. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE002098 Genomic DNA. Translation: AAF40711.1. |
| PIR | D81220. |
| RefSeq | NP_273313.1. NC_003112.2. |
3D structure databases | |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBNEIT00000009598; EBNEIP00000009218; EBNEIG00000009598. |
| GeneID | 902368. |
| GenomeReviews | Gene locus NMB0257 in contig AE002098_GR. |
| KEGG | nme:NMB0257. |
| NMPDR | fig|122586.1.peg.247. |
| PATRIC | 20355592. VBINeiMen85645_0320. |
| TIGR | NMB0257. |
Phylogenomic databases | |
| GeneTree | EBGT00050000020201. |
| HOGENOM | HBG643593. |
| OMA | IGYMADD. |
| ProtClustDB | PRK06590. |
Enzyme and pathway databases | |
| BioCyc | NMEN122586:NMB_0257-MONOMER. |
Family and domain databases | |
| InterPro | IPR001750. NADH_UbQ/plastoQ_OxRdtase. IPR001516. NADH_UbQ_OxRdtase_chain5/L_N. IPR002128. NADH_UbQ_OxRdtase_chlpt_su5_C. IPR003945. NADHpl_OxRdtase_5. IPR018393. NADHpl_OxRdtase_5_subgr. [Graphical view] |
| KO | K00341. |
| Pfam | PF00361. Oxidored_q1. 1 hit. PF01010. Oxidored_q1_C. 1 hit. PF00662. Oxidored_q1_N. 1 hit. [Graphical view] |
| PRINTS | PR01435. NPOXDRDTASE5. |
| TIGRFAMs | TIGR01974. NDH_I_L. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | NUOL_NEIMB | ||||||||
| Accession | Primary (citable) accession number: Q9K1B0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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