Q9KPY2 (GMHA_VIBCH) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 59.
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: Phosphoheptose isomerase EC=5.3.1.28 Alternative name(s): Sedoheptulose 7-phosphate isomerase | ||||
| Gene names |
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| Organism | Vibrio cholerae | ||||
| Taxonomic identifier | 666 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Vibrio |
Protein attributes
| Sequence length | 191 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes the isomerization of sedoheptulose 7-phosphate in D-glycero-D-manno-heptose 7-phosphate By similarity. HAMAP MF_00067 |
| Catalytic activity | D-sedoheptulose 7-phosphate = D-glycero-D-manno-heptose 7-phosphate. HAMAP MF_00067 |
| Cofactor | Binds 1 zinc ion per subunit By similarity. HAMAP MF_00067 |
| Pathway | Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7-phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from sedoheptulose 7-phosphate: step 1/1. HAMAP MF_00067 Bacterial outer membrane biogenesis; LPS core biosynthesis. HAMAP MF_00067 |
| Subunit structure | Homotetramer By similarity. HAMAP MF_00067 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00067. |
| Miscellaneous | The reaction produces a racemic mixture of D-glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D-manno-heptose 7-phosphate By similarity. HAMAP MF_00067 |
| Sequence similarities | Belongs to the SIS family. GmhA subfamily. Contains 1 SIS domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Lipopolysaccharide biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | Metal-binding Zinc |
| Molecular function | Isomerase |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | lipopolysaccharide core region biosynthetic process Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | D-sedoheptulose 7-phosphate isomerase activity Inferred from electronic annotation. Source: InterPro metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW sugar 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 – 191 | 191 | Phosphoheptose isomerase HAMAP MF_00067 | PRO_0000136548 | |||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||
| Domain | 37 – 191 | 155 | SIS | ||||||||||||||||||||||||||||||||
| Region | 52 – 54 | 3 | Substrate binding By similarity | ||||||||||||||||||||||||||||||||
| Region | 93 – 94 | 2 | Substrate binding By similarity | ||||||||||||||||||||||||||||||||
| Region | 119 – 121 | 3 | Substrate binding By similarity | ||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||
| Metal binding | 61 | 1 | Zinc By similarity | ||||||||||||||||||||||||||||||||
| Metal binding | 65 | 1 | Zinc By similarity | ||||||||||||||||||||||||||||||||
| Metal binding | 172 | 1 | Zinc By similarity | ||||||||||||||||||||||||||||||||
| Metal binding | 180 | 1 | Zinc By similarity | ||||||||||||||||||||||||||||||||
| Binding site | 65 | 1 | Substrate By similarity | ||||||||||||||||||||||||||||||||
| Binding site | 124 | 1 | Substrate By similarity | ||||||||||||||||||||||||||||||||
| Binding site | 172 | 1 | Substrate By similarity | ||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||
| Helix | 3 – 21 | 19 | |||||||||||||||||||||||||||||||||
| Helix | 24 – 41 | 18 | |||||||||||||||||||||||||||||||||
| Turn | 42 – 44 | 3 | |||||||||||||||||||||||||||||||||
| Beta strand | 47 – 50 | 4 | |||||||||||||||||||||||||||||||||
| Beta strand | 52 – 54 | 3 | |||||||||||||||||||||||||||||||||
| Helix | 55 – 70 | 16 | |||||||||||||||||||||||||||||||||
| Beta strand | 78 – 81 | 4 | |||||||||||||||||||||||||||||||||
| Helix | 100 – 108 | 9 | |||||||||||||||||||||||||||||||||
| Beta strand | 114 – 122 | 9 | |||||||||||||||||||||||||||||||||
| Helix | 125 – 137 | 13 | |||||||||||||||||||||||||||||||||
| Beta strand | 140 – 146 | 7 | |||||||||||||||||||||||||||||||||
| Helix | 150 – 152 | 3 | |||||||||||||||||||||||||||||||||
| Turn | 153 – 155 | 3 | |||||||||||||||||||||||||||||||||
| Beta strand | 156 – 163 | 8 | |||||||||||||||||||||||||||||||||
| Helix | 168 – 189 | 22 | |||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "DNA sequence of both chromosomes of the cholera pathogen Vibrio cholerae." Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D., Vamathevan J.J., Bass S. Fraser C.M.Nature 406:477-483(2000) [PubMed: 10952301] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 39315 / El Tor Inaba N16961 / Serotype O1. |
| [2] | "Novel pathways for biosynthesis of nucleotide-activated glycero-manno-heptose precursors of bacterial glycoproteins and cell surface polysaccharides." Valvano M.A., Messner P., Kosma P. Microbiology 148:1979-1989(2002) [PubMed: 12101286] [Abstract] Cited for: BIOSYNTHESIS OF NUCLEOTIDE-ACTIVATED GLYCERO-MANNO-HEPTOSE. |
| [3] | "Crystal structures of two putative phosphoheptose isomerases." Seetharaman J., Rajashankar K.R., Solorzano V., Kniewel R., Lima C.D., Bonanno J.B., Burley S.K., Swaminathan S. Proteins 63:1092-1096(2006) [PubMed: 16477602] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AE003852 Genomic DNA. Translation: AAF95374.1. | ||||||||||||
| PIR | B82104. | ||||||||||||
| RefSeq | NP_231861.1. NC_002505.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | Q9KPY2. | ||||||||||||
| SMR | Q9KPY2. Positions 1-190. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 2613270. | ||||||||||||
| GenomeReviews | Gene locus VC_2230 in contig AE003852_GR. | ||||||||||||
| KEGG | vch:VC2230. | ||||||||||||
| PATRIC | 20083505. VBIVibCho83274_2127. | ||||||||||||
| TIGR | VC_2230. | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | HBG671955. | ||||||||||||
| OMA | ANDLGYD. | ||||||||||||
| PhylomeDB | Q9KPY2. | ||||||||||||
| ProtClustDB | PRK00414. | ||||||||||||
Family and domain databases | |||||||||||||
| HAMAP | MF_00067. GmhA. [Tree] | ||||||||||||
| InterPro | IPR004515. Phosphoheptose_Isoase_subgr. IPR020620. Phosphoheptose_isomerase. IPR001347. SIS. [Graphical view] | ||||||||||||
| KO | K03271. | ||||||||||||
| Pfam | PF01380. SIS. 1 hit. [Graphical view] | ||||||||||||
| TIGRFAMs | TIGR00441. GmhA. 1 hit. | ||||||||||||
| PROSITE | PS51464. SIS. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | GMHA_VIBCH | ||||||||
| Accession | Primary (citable) accession number: Q9KPY2 | ||||||||
| 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 |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

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