Q8PU59 (FPOH_METMA) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 59.
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: F(420)H(2) oxidoreductase subunit H Alternative name(s): F(420)H(2) dehydrogenase subunit H FPO subunit H | ||||
| Gene names |
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| Organism | Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 192952 [NCBI] | ||||
| Taxonomic lineage | Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina |
Protein attributes
| Sequence length | 350 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | FPO shuttles electrons from F(420)H2, via FAD and iron-sulfur (Fe-S) centers, to quinones in the F(420)H2:heterodisulfide oxidoreduction chain. The immediate electron acceptor for the enzyme in this species is believed to be methanophenazine. Couples the redox reaction to proton translocation (for every two electrons transferred, 0.9 hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient By similarity. Ref.1 Ref.3 |
| Subunit structure | FPO is composed of at least 12 different subunits. Subunits fpoA, H, J, K, L, M, N constitute the membrane sector of the complex By similarity. |
| Subcellular location | Cell membrane; Multi-pass membrane protein Potential HAMAP MF_01350. |
| Sequence similarities | Belongs to the complex I subunit 1 family. |
| Sequence caution | The sequence AAF65735.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell membrane Membrane |
| Domain | Transmembrane Transmembrane helix |
| Ligand | FAD |
| Molecular function | Oxidoreductase |
| PTM | Quinone |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Cellular component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | oxidoreductase activity Inferred 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 – 350 | 350 | F(420)H(2) oxidoreductase subunit H HAMAP MF_01350 | PRO_0000240123 | |||||
Regions | |||||||||
| Transmembrane | 21 – 41 | 21 | Helical; Potential | ||||||
| Transmembrane | 94 – 114 | 21 | Helical; Potential | ||||||
| Transmembrane | 128 – 148 | 21 | Helical; Potential | ||||||
| Transmembrane | 173 – 193 | 21 | Helical; Potential | ||||||
| Transmembrane | 200 – 220 | 21 | Helical; Potential | ||||||
| Transmembrane | 261 – 281 | 21 | Helical; Potential | ||||||
| Transmembrane | 285 – 305 | 21 | Helical; Potential | ||||||
| Transmembrane | 330 – 350 | 21 | Helical; Potential | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The F(420)H(2) dehydrogenase from Methanosarcina mazei is a redox-driven proton pump closely related to NADH dehydrogenases." Baeumer S., Ide T., Jacobi C., Johann A., Gottschalk G., Deppenmeier U. J. Biol. Chem. 275:17968-17973(2000) [PubMed: 10751389] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, FPO COMPLEX. Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88. |
| [2] | "The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea." Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R. Gottschalk G.J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed: 12125824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88. |
| [3] | "Purification and properties of an F(420)H(2) dehydrogenase from Methanosarcina mazei Go1." Abken H.-J., Deppenmeier U. FEMS Microbiol. Lett. 154:231-237(1997) Cited for: FUNCTION, FPO COMPLEX, CATALYTIC ACTIVITY. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF228525 Genomic DNA. Translation: AAF65735.1. Different initiation. AE008384 Genomic DNA. Translation: AAM32183.1. |
| RefSeq | NP_634511.1. NC_003901.1. |
3D structure databases | |
| ModBase | Search... |
Protein family/group databases | |
| TCDB | 3.D.9.1.1. H+-translocating F420H2 dehydrogenase (F420H2DH) family. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1480829. |
| GenomeReviews | Gene locus MM_2487 in contig AE008384_GR. |
| KEGG | mma:MM_2487. |
| NMPDR | fig|192952.1.peg.2487. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG727670. |
| OMA | WNIFLQP. |
| PhylomeDB | Q8PU59. |
| ProtClustDB | CLSK568843. |
Enzyme and pathway databases | |
| BioCyc | MMAZ192952:MM2487-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01350. NDH1_NuoH. [Tree] |
| InterPro | IPR001694. NADH_UbQ_OxRdtase_su1/FPO. IPR018086. NADH_UbQ_OxRdtase_su1_CS. [Graphical view] |
| KO | K00337. |
| PANTHER | PTHR11432. Resp_NADH_DH_1. 1 hit. |
| Pfam | PF00146. NADHdh. 1 hit. [Graphical view] |
| PROSITE | PS00667. COMPLEX1_ND1_1. 1 hit. PS00668. COMPLEX1_ND1_2. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FPOH_METMA | ||||||||
| Accession | Primary (citable) accession number: Q8PU59 Secondary accession number(s): Q9P9F9 | ||||||||
| 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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