Reviewed,
UniProtKB/Swiss-Prot Q8XE72 (PANE_ECO57)
Last modified
February 9, 2010.
Version 58.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 2-dehydropantoate 2-reductase EC=1.1.1.169 Alternative name(s): Ketopantoate reductase Short name=KPA reductase Short name=KPR | ||||||
| Gene names |
| ||||||
| Organism | Escherichia coli O157:H7 [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 83334 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 303 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid. |
| Catalytic activity | (R)-pantoate + NADP+ = 2-dehydropantoate + NADPH. |
| Pathway | |
| Subunit structure | Monomer By similarity. |
| Subcellular location | Cytoplasm Potential. |
| Sequence similarities | Belongs to the ketopantoate reductase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pantothenate biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | NADP |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pantothenate biosynthetic processInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | 2-dehydropantoate 2-reductase activity Inferred from electronic annotation. Source: EC NADP or NADPH bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 303 | 303 | 2-dehydropantoate 2-reductase | PRO_0000157302 | |||||
Regions | |||||||||
| Nucleotide binding | 7 – 12 | 6 | NADP By similarity | ||||||
Sites | |||||||||
| Active site | 176 | 1 | Proton donor | ||||||
| Binding site | 31 | 1 | NADP; via amide nitrogen By similarity | ||||||
| Binding site | 98 | 1 | NADP; via amide nitrogen By similarity | ||||||
| Binding site | 98 | 1 | Substrate By similarity | ||||||
| Binding site | 122 | 1 | NADP; via amide nitrogen and carbonyl oxygen By similarity | ||||||
| Binding site | 180 | 1 | Substrate By similarity | ||||||
| Binding site | 184 | 1 | Substrate By similarity | ||||||
| Binding site | 194 | 1 | Substrate By similarity | ||||||
| Binding site | 241 | 1 | Substrate By similarity | ||||||
| Binding site | 244 | 1 | Substrate By similarity | ||||||
| Binding site | 256 | 1 | NADP By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. Blattner F.R.Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC. |
| [2] | "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. Shinagawa H.DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE005174 Genomic DNA. Translation: AAG54775.1. BA000007 Genomic DNA. Translation: BAB33902.1. |
| PIR | C85539. G90688. |
| RefSeq | NP_286167.1. NP_308506.1. |
3D structure databases | |
| SMR | Q8XE72. Positions 1-293. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 914581. 957394. |
| GenomeReviews | Gene locus Z0528 in contig AE005174_GR. Gene locus ECs0479 in contig BA000007_GR. |
| KEGG | ece:Z0528. ecs:ECs0479. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG668370. |
| OMA | QCHILLL. |
Enzyme and pathway databases | |
| BioCyc | ECOL83334:ECS0479-MONOMER. |
Family and domain databases | |
| InterPro | IPR008927. 6-PGluconate_DH_C-like. IPR003710. ApbA. IPR013752. ApbA_C. IPR013332. ApbA_N. IPR013328. DH_multihelical. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:1.10.1040.10. Opine_DH. 1 hit. |
| PANTHER | PTHR21708:SF21. ApbA. 1 hit. |
| Pfam | PF02558. ApbA. 1 hit. PF08546. ApbA_C. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00745. apbA_panE. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | PANE_ECO57 | ||||||||
| Accession | Primary (citable) accession number: Q8XE72 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


