P07343 (FUMC_BACSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 111.
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 | Bacillus subtilis (strain 168) [Reference proteome] [HAMAP] | ||||||
| Taxonomic identifier | 224308 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › ![]() |
Protein attributes
| Sequence length | 462 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. |
| Subcellular location | |
| 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 – 462 | 462 | Fumarate hydratase class II HAMAP-Rule MF_00743 | PRO_0000161255 | |||||
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 | ||||||
Experimental info | |||||||||
| Sequence conflict | 66 | 1 | A → V in CAA25849. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Complete nucleotide sequence of the fumarase gene (citG) of Bacillus subtilis 168." Miles J.S., Guest J.R. Nucleic Acids Res. 13:131-140(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168. |
| [2] | "The yvsA-yvqA (293 degrees - 289 degrees) region of the Bacillus subtilis chromosome containing genes involved in metal ion uptake and a putative sigma factor." Wipat A., Brignell C.S., Guy J.B., Rose M., Emmerson P.T., Harwood C.R. Microbiology 144:1593-1600(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168. |
| [3] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. Danchin A.Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| [4] | "The nucleotide sequence of a spore germination gene (gerA) of Bacillus subtilis 168." Feavers I.M., Miles J.S., Moir A. Gene 38:95-102(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50. Strain: 168. |
| [5] | "Role of sigma H in expression of the fumarase gene (citG) in vegetative cells of Bacillus subtilis 168." Price V.A., Feavers I.M., Moir A. J. Bacteriol. 171:5933-5939(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-50. Strain: 168. |
| [6] | "Sequencing of regions downstream of addA (98 degrees) and citG (289 degrees) in Bacillus subtilis." Medina N., Vannier F., Roche B., Autret S., Levine A., Seror S.J. Microbiology 143:3305-3308(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 224-462. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X01701 Genomic DNA. Translation: CAA25849.1. AJ223978 Genomic DNA. Translation: CAA11749.1. AL009126 Genomic DNA. Translation: CAB15294.1. M11918 Genomic DNA. Translation: AAA22464.1. Z93941 Genomic DNA. Translation: CAB07973.1. |
| PIR | UFBSC8. A23033. |
| RefSeq | NP_391184.1. NC_000964.3. |
3D structure databases | |
| ProteinModelPortal | P07343. |
| SMR | P07343. Positions 4-457. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P07343. 1 interaction. |
| MINT | MINT-8365703. |
| STRING | 224308.BSU33040. |
Proteomic databases | |
| PaxDb | P07343. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAB15294; CAB15294; BSU33040. |
| GeneID | 938591. |
| KEGG | bsu:BSU33040. |
| PATRIC | 18978594. VBIBacSub10457_3460. |
Organism-specific databases | |
| GenoList | BSU33040. [Micado] |
Phylogenomic databases | |
| eggNOG | COG0114. |
| HOGENOM | HOG000061736. |
| KO | K01679. |
| OMA | KDTMGEV. |
| ProtClustDB | PRK00485. |
Enzyme and pathway databases | |
| BioCyc | BSUB:BSU33040-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_BACSU | ||||||||
| Accession | Primary (citable) accession number: P07343 Secondary accession number(s): O32194 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
