P64172 (FUMC_STAAM) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 62.
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 | Staphylococcus aureus (strain Mu50 / ATCC 700699) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 158878 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus › ![]() |
Protein attributes
| Sequence length | 461 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
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 – 461 | 461 | Fumarate hydratase class II HAMAP-Rule MF_00743 | PRO_0000161312 | |||||
Regions | |||||||||
| Region | 97 – 99 | 3 | Substrate binding By similarity | ||||||
| Region | 127 – 130 | 4 | B site By similarity | ||||||
| Region | 137 – 139 | 3 | Substrate binding By similarity | ||||||
| Region | 185 – 186 | 2 | Substrate binding By similarity | ||||||
| Region | 322 – 324 | 3 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 186 | 1 | Proton donor/acceptor By similarity | ||||||
| Active site | 316 | 1 | By similarity | ||||||
| Binding site | 317 | 1 | Substrate By similarity | ||||||
| Site | 329 | 1 | Important for catalytic activity By similarity | ||||||
Sequences
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References
| [1] | "Whole genome sequencing of meticillin-resistant Staphylococcus aureus." Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. Hiramatsu K.Lancet 357:1225-1240(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Mu50 / ATCC 700699. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BA000017 Genomic DNA. Translation: BAB58013.1. |
| RefSeq | NP_372375.1. NC_002758.2. |
3D structure databases | |
| ProteinModelPortal | P64172. |
| SMR | P64172. Positions 3-457. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 158878.SAV1851. |
2D gel databases | |
| World-2DPAGE | 0002:P64172. |
Proteomic databases | |
| PRIDE | P64172. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | BAB58013; BAB58013; SAV1851. |
| GeneID | 1121833. |
| KEGG | sav:SAV1851. |
| PATRIC | 19564486. VBIStaAur52173_1913. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0114. |
| HOGENOM | HOG000061736. |
| KO | K01679. |
| OMA | KDTMGEV. |
| ProtClustDB | PRK00485. |
Enzyme and pathway databases | |
| BioCyc | SAUR158878:GJJ5-1875-MONOMER. |
| 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. |
| TIGRFAMs | TIGR00979. fumC_II. 1 hit. |
| PROSITE | PS00163. FUMARATE_LYASES. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | FUMC_STAAM | ||||||||
| Accession | Primary (citable) accession number: P64172 Secondary accession number(s): Q99T27 | ||||||||
| 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
