Q9ZJQ9 (FUMC_HELPJ) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 92.
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 |
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| Organism | Helicobacter pylori (strain J99) (Campylobacter pylori J99) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 85963 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter › ![]() |
Protein attributes
| Sequence length | 463 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 |
| 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 – 463 | 463 | Fumarate hydratase class II HAMAP-Rule MF_00743 | PRO_0000161281 | |||||
Regions | |||||||||
| Region | 97 – 99 | 3 | Substrate binding By similarity | ||||||
| Region | 128 – 131 | 4 | B site By similarity | ||||||
| Region | 138 – 140 | 3 | Substrate binding By similarity | ||||||
| Region | 186 – 187 | 2 | Substrate binding By similarity | ||||||
| Region | 323 – 325 | 3 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 187 | 1 | Proton donor/acceptor By similarity | ||||||
| Active site | 317 | 1 | By similarity | ||||||
| Binding site | 318 | 1 | Substrate By similarity | ||||||
| Site | 330 | 1 | Important for catalytic activity By similarity | ||||||
Sequences
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References
| [1] | "Genomic sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori." Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D. Trust T.J.Nature 397:176-180(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: J99. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE001439 Genomic DNA. Translation: AAD06830.1. |
| PIR | H71830. |
| RefSeq | NP_223963.1. NC_000921.1. |
3D structure databases | |
| ProteinModelPortal | Q9ZJQ9. |
| SMR | Q9ZJQ9. Positions 4-459. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 85963.jhp1245. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAD06830; AAD06830; jhp_1245. |
| GeneID | 890413. |
| KEGG | hpj:jhp1245. |
| PATRIC | 20607334. VBIHelPyl98156_1348. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0114. |
| KO | K01679. |
| OMA | KDTMGEV. |
| ProtClustDB | PRK00485. |
Enzyme and pathway databases | |
| BioCyc | HPYL85963:GJB9-1281-MONOMER. |
| UniPathway | UPA00223; UER01007. |
Family and domain databases | |
| Gene3D | 1.10.275.10. 1 hit. |
| HAMAP | MF_00743. FumaraseC. |
| InterPro | 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 | PR00149. FUMRATELYASE. |
| SUPFAM | SSF48557. L-Aspartase-like. 1 hit. |
| TIGRFAMs | TIGR00979. fumC_II. 1 hit. |
| PROSITE | PS00163. FUMARATE_LYASES. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FUMC_HELPJ | ||||||||
| Accession | Primary (citable) accession number: Q9ZJQ9 | ||||||||
| Entry history |
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| 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
