Q9HQ29 (FUMC_HALSA) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 74.
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: Fumarate hydratase class II Short name=Fumarase C EC=4.2.1.2 | ||||
| Gene names |
| ||||
| Organism | Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1) (Halobacterium halobium) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 64091 [NCBI] | ||||
| Taxonomic lineage | Archaea › Euryarchaeota › Halobacteria › Halobacteriales › Halobacteriaceae › Halobacterium › ![]() |
Protein attributes
| Sequence length | 470 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the reversible addition of water to fumarate to give L-malate By similarity. HAMAP-Rule MF_00743 |
| Catalytic activity | (S)-malate = fumarate + H2O. HAMAP-Rule MF_00743 |
| Pathway | Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1. HAMAP-Rule MF_00743 |
| Subunit structure | Homotetramer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Miscellaneous | There are 2 substrate binding sites: the catalytic A site, and the non-catalytic B site that may play a role in the transfer of substrate or product between the active site and the solvent. Alternatively, the B site may bind allosteric effectors By similarity. HAMAP-Rule MF_00743 |
| Sequence similarities | Belongs to the class-II fumarase/aspartase family. Fumarase subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Tricarboxylic acid cycle |
| Cellular component | Cytoplasm |
| Molecular function | Lyase |
| Technical term | Allosteric enzyme Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | fumarate metabolic process Inferred from electronic annotation. Source: InterPro tricarboxylic acid cycleInferred from electronic annotation. Source: HAMAP |
| Cellular_component | tricarboxylic acid cycle enzyme complex Inferred from electronic annotation. Source: InterPro |
| Molecular_function | fumarate hydratase activity Inferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 470 | 470 | Fumarate hydratase class II HAMAP-Rule MF_00743 | PRO_0000161332 | |||||
Regions | |||||||||
| Region | 99 – 101 | 3 | Substrate binding By similarity | ||||||
| Region | 129 – 132 | 4 | B site By similarity | ||||||
| Region | 139 – 141 | 3 | Substrate binding By similarity | ||||||
| Region | 187 – 188 | 2 | Substrate binding By similarity | ||||||
| Region | 324 – 326 | 3 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 188 | 1 | Proton donor/acceptor By similarity | ||||||
| Active site | 318 | 1 | By similarity | ||||||
| Binding site | 319 | 1 | Substrate By similarity | ||||||
| Site | 331 | 1 | Important for catalytic activity By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Genome sequence of Halobacterium species NRC-1." Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D., Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D., Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K. DasSarma S.Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700922 / JCM 11081 / NRC-1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE004437 Genomic DNA. Translation: AAG19688.1. |
| PIR | D84290. |
| RefSeq | NP_280208.1. NC_002607.1. |
3D structure databases | |
| ProteinModelPortal | Q9HQ29. |
| SMR | Q9HQ29. Positions 5-459. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 64091.VNG1356G. |
Proteomic databases | |
| PaxDb | Q9HQ29. |
| PRIDE | Q9HQ29. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAG19688; AAG19688; VNG_1356G. |
| GeneID | 1447987. |
| KEGG | hal:VNG1356G. |
Phylogenomic databases | |
| eggNOG | COG0114. |
| KO | K01679. |
| OMA | KDTMGEV. |
| ProtClustDB | PRK00485. |
Enzyme and pathway databases | |
| UniPathway | UPA00223; UER01007. |
Family and domain databases | |
| Gene3D | 1.10.275.10. 1 hit. |
| HAMAP | MF_00743. FumaraseC. |
| InterPro | IPR003031. D_crystallin. IPR005677. Fum_hydII. IPR024083. Fumarase/histidase_N. IPR018951. Fumarase_C_C. IPR000362. Fumarate_lyase. IPR020557. Fumarate_lyase_CS. IPR022761. Fumarate_lyase_N. IPR008948. L-Aspartase-like. [Graphical view] |
| Pfam | PF10415. FumaraseC_C. 1 hit. PF00206. Lyase_1. 1 hit. [Graphical view] |
| PRINTS | PR00145. ARGSUCLYASE. PR00149. FUMRATELYASE. |
| SUPFAM | SSF48557. L-Aspartase-like. 1 hit. |
| PROSITE | PS00163. FUMARATE_LYASES. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FUMC_HALSA | ||||||||
| Accession | Primary (citable) accession number: Q9HQ29 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
