Reviewed,
UniProtKB/Swiss-Prot Q9PNE6 (GMHA1_CAMJE)
Last modified
June 16, 2009.
Version 54.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Phosphoheptose isomerase 1 EC=5.3.1.- Alternative name(s): Sedoheptulose 7-phosphate isomerase 1 | ||||||
| Gene names |
| ||||||
| Organism | Campylobacter jejuni [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 197 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter |
Protein attributes
| Sequence length | 186 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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. |
| Catalytic activity | D-sedoheptulose 7-phosphate = D-glycero-alpha-D-manno-heptose 7-phosphate + D-glycero-beta-D-manno-heptose 7-phosphate. HAMAP MF_00067 |
| Pathway | Carbohydrate biosynthesis; D-glycero-D-manno-heptose 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; LOS core biosynthesis. HAMAP MF_00067 |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the SIS family. GmhA subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism |
| Cellular component | Cytoplasm |
| Molecular function | Isomerase |
| Technical term | 3D-structure Complete 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: HAMAP protein bindingInferred from physical interaction. Source: IntAct sugar bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| fliH | Q0PBI9 | 1 | EBI-1193890,EBI-1191439 | |
| fliY | Q0PC74 | 1 | EBI-1193890,EBI-1191111 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 186 | 186 | Phosphoheptose isomerase 1 HAMAP MF_00067 | PRO_0000136522 | ||||||||||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 16 | 1 | V → A Ref.3 | |||||||||||||||||||||||||||||||||||||
| Sequence conflict | 18 | 1 | A → E Ref.1 | |||||||||||||||||||||||||||||||||||||
| Sequence conflict | 18 | 1 | A → E Ref.2 | |||||||||||||||||||||||||||||||||||||
| Sequence conflict | 18 | 1 | A → E Ref.3 | |||||||||||||||||||||||||||||||||||||
| Sequence conflict | 31 | 1 | E → D Ref.1 | |||||||||||||||||||||||||||||||||||||
| Sequence conflict | 31 | 1 | E → D Ref.2 | |||||||||||||||||||||||||||||||||||||
| Sequence conflict | 109 | 1 | K → N Ref.1 | |||||||||||||||||||||||||||||||||||||
| Sequence conflict | 109 | 1 | K → N Ref.2 | |||||||||||||||||||||||||||||||||||||
| Sequence conflict | 109 | 1 | K → N Ref.3 | |||||||||||||||||||||||||||||||||||||
| Sequence conflict | 128 | 1 | L → F Ref.1 | |||||||||||||||||||||||||||||||||||||
| Sequence conflict | 128 | 1 | L → F Ref.2 | |||||||||||||||||||||||||||||||||||||
| Sequence conflict | 128 | 1 | L → F Ref.3 | |||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||
| Helix | 2 – 18 | 17 | ||||||||||||||||||||||||||||||||||||||
| Helix | 19 – 22 | 4 | ||||||||||||||||||||||||||||||||||||||
| Helix | 23 – 38 | 16 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 43 – 48 | 6 | ||||||||||||||||||||||||||||||||||||||
| Helix | 50 – 63 | 14 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 66 – 68 | 3 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 75 – 79 | 5 | ||||||||||||||||||||||||||||||||||||||
| Helix | 82 – 91 | 10 | ||||||||||||||||||||||||||||||||||||||
| Helix | 94 – 96 | 3 | ||||||||||||||||||||||||||||||||||||||
| Helix | 97 – 105 | 9 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 111 – 115 | 5 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 117 – 119 | 3 | ||||||||||||||||||||||||||||||||||||||
| Helix | 122 – 133 | 12 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 137 – 143 | 7 | ||||||||||||||||||||||||||||||||||||||
| Helix | 144 – 148 | 5 | ||||||||||||||||||||||||||||||||||||||
| Helix | 149 – 152 | 4 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 154 – 160 | 7 | ||||||||||||||||||||||||||||||||||||||
| Helix | 164 – 185 | 22 | ||||||||||||||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Biosynthesis of ganglioside mimics in Campylobacter jejuni OH4384. Identification of the glycosyltransferase genes, enzymatic synthesis of model compounds, and characterization of nanomole amounts by 600-MHz (1)H and (13)C NMR analysis." Gilbert M., Brisson J.-R., Karwaski M.-F., Michniewicz J., Cunningham A.-M., Wu Y., Young N.M., Wakarchuk W.W. J. Biol. Chem. 275:3896-3906(2000) [PubMed: 10660542] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 43446 / MK104 / Serotype O:19. |
| [2] | Gilbert M. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION. |
| [3] | "Evidence for acquisition of the lipooligosaccharide biosynthesis locus in Campylobacter jejuni GB11, a strain isolated from a patient with Guillain-Barre syndrome, by horizontal exchange." Gilbert M., Godschalk P.C., Karwaski M.-F., Ang C.W., Van Belkum A., Li J., Wakarchuk W.W., Endtz H.P. Infect. Immun. 72:1162-1165(2004) [PubMed: 14742567] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: GB11. |
| [4] | "The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. Barrell B.G.Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2. |
| [5] | "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. |
| [6] | "Deciphering Campylobacter jejuni cell surface interactions from the genome sequence." Linton D., Karlyshev A.V., Wren B.W. Curr. Opin. Microbiol. 4:35-40(2001) [PubMed: 11173031] [Abstract] Cited for: CELL SURFACE. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| AF167344 Genomic DNA. Translation: AAR99164.1. AY422197 Genomic DNA. Translation: AAR82882.1. AL111168 Genomic DNA. Translation: CAL35264.1. | |||||||||||||
| PIR | G81319. | ||||||||||||
| RefSeq | YP_002344540.1. | ||||||||||||
3D structure databases | |||||||||||||
| |||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| IntAct | Q9PNE6. 105 interactions. | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 905439. | ||||||||||||
| GenomeReviews | Gene locus Cj1149c in contig AL111168_GR. | ||||||||||||
| KEGG | cje:Cj1149c. | ||||||||||||
Organism-specific databases | |||||||||||||
| CMR | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| OMA | Q9PNE6. ANDLGYD. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | CJEJ192222:CJ1149C-MON. | ||||||||||||
Family and domain databases | |||||||||||||
| HAMAP | MF_00067. [Tree] | ||||||||||||
| InterPro | IPR004515. GmhA. IPR001347. SIS. [Graphical view] | ||||||||||||
| Pfam | PF01380. SIS. 1 hit. [Graphical view] | ||||||||||||
| TIGRFAMs | TIGR00441. gmhA. 1 hit. | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | GMHA1_CAMJE | ||||||||
| Accession | Primary (citable) accession number: Q9PNE6 Secondary accession number(s): Q0P9A7, Q6TG10, Q7BPS4 | ||||||||
| Entry history |
| ||||||||
| 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 |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


