F4MBH3 (F4MBH3_ECOLX) Unreviewed, UniProtKB/TrEMBL
Last modified
April 3, 2013.
Version 10.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Phosphoenolpyruvate carboxylase HAMAP-Rule MF_00595 Short name=PEPC HAMAP-Rule MF_00595 Short name=PEPCase HAMAP-Rule MF_00595 EC=4.1.1.31 HAMAP-Rule MF_00595 | ||||
| Gene names |
| ||||
| Organism | Escherichia coli UMNK88 EMBL AEE59287.1 | ||||
| Taxonomic identifier | 696406 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › ![]() |
Protein attributes
| Sequence length | 883 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle By similarity. HAMAP-Rule MF_00595 SAAS SAAS022805 |
| Catalytic activity | Phosphate + oxaloacetate = H2O + phosphoenolpyruvate + HCO3-. HAMAP-Rule MF_00595 SAAS SAAS018129 |
| Cofactor | Magnesium By similarity. HAMAP-Rule MF_00595 SAAS SAAS018129 |
| Subunit structure | Homotetramer By similarity. HAMAP-Rule MF_00595 |
| Sequence similarities | Belongs to the PEPCase type 1 family. HAMAP-Rule MF_00595 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbon dioxide fixation HAMAP-Rule MF_00595 SAAS SAAS018129 |
| Ligand | Magnesium HAMAP-Rule MF_00595 SAAS SAAS018129 Pyruvate EMBL AEE59287.1 |
| Molecular function | Lyase HAMAP-Rule MF_00595 SAAS SAAS018129 |
| Gene Ontology (GO) | |
| Biological_process | carbon fixation Inferred from electronic annotation. Source: HAMAP oxaloacetate metabolic processInferred from electronic annotation. Source: HAMAP tricarboxylic acid cycleInferred from electronic annotation. Source: InterPro |
| Molecular_function | magnesium ion binding Inferred from electronic annotation. Source: HAMAP phosphoenolpyruvate carboxylase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Sites | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Active site | 138 | 1 | By similarity HAMAP-Rule MF_00595 | ||||||
| Active site | 546 | 1 | By similarity HAMAP-Rule MF_00595 | ||||||
Sequences
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References
| [1] | "Genome structure of porcine enterotoxigenic Escherichia coli." Johnson T.J., Shepard S.M., Isaacson R.E. Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: UMNK88 EMBL AEE59287.1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP002729 Genomic DNA. Translation: AEE59287.1. |
| RefSeq | YP_006136450.1. NC_017641.1. |
3D structure databases | |
| ProteinModelPortal | F4MBH3. |
| SMR | F4MBH3. Positions 4-883. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AEE59287; AEE59287; UMNK88_4794. |
| GeneID | 12688046. |
| KEGG | eun:UMNK88_4794. |
| PATRIC | 48577388. VBIEscCol159162_4692. |
Phylogenomic databases | |
| KO | K01595. |
| OMA | AIPWVFG. |
Family and domain databases | |
| HAMAP | MF_00595. PEPcase_type1. |
| InterPro | IPR021135. PEP_COase. IPR018129. PEP_COase_AS. IPR022805. PEP_COase_bac/pln-type. IPR015813. Pyrv/PenolPyrv_Kinase. [Graphical view] |
| Pfam | PF00311. PEPcase. 1 hit. [Graphical view] |
| PRINTS | PR00150. PEPCARBXLASE. |
| SUPFAM | SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit. |
| PROSITE | PS00781. PEPCASE_1. 1 hit. PS00393. PEPCASE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | F4MBH3_ECOLX | ||||||||
| Accession | Primary (citable) accession number: F4MBH3 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
