P46452 (GMHB_HAEIN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 87.
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: D,D-heptose 1,7-bisphosphate phosphatase EC=3.1.3.- Alternative name(s): D-glycero-D-manno-heptose 1,7-bisphosphate phosphatase HBP phosphatase | ||||
| Gene names |
| ||||
| Organism | Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 71421 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus › ![]() |
Protein attributes
| Sequence length | 184 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Converts the D-glycero-beta-D-manno-heptose 1,7-bisphosphate intermediate into D-glycero-beta-D-manno-heptose 1-phosphate by removing the phosphate group at the C-7 position By similarity. |
| Catalytic activity | D-glycero-D-manno-heptose 1,7-bisphosphate + H2O = D-glycero-beta-D-manno-heptose 1-phosphate + phosphate. |
| Cofactor | Magnesium By similarity. Zinc By similarity. |
| Pathway | |
| Subunit structure | Monomer By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Miscellaneous | This enzyme is insensitive to the anomeric configuration of the D-glycero-D-manno-heptose 1,7-bisphosphate By similarity. |
| Sequence similarities | Belongs to the GmhB family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism |
| Cellular component | Cytoplasm |
| Ligand | Magnesium Metal-binding Zinc |
| Molecular function | Hydrolase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | ADP-L-glycero-beta-D-manno-heptose biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway carbohydrate metabolic processInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | D,D-heptose 1,7-bisphosphate phosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB magnesium ion bindingInferred from sequence or structural similarity. Source: UniProtKB zinc ion bindingInferred from sequence or structural similarity. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 184 | 184 | D,D-heptose 1,7-bisphosphate phosphatase | PRO_0000209392 | |||||
Regions | |||||||||
| Region | 8 – 10 | 3 | Substrate binding By similarity | ||||||
| Region | 16 – 19 | 4 | Substrate binding By similarity | ||||||
| Region | 50 – 53 | 4 | Substrate binding By similarity | ||||||
| Region | 106 – 107 | 2 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 8 | 1 | Nucleophile By similarity | ||||||
| Active site | 10 | 1 | Proton donor By similarity | ||||||
| Metal binding | 8 | 1 | Magnesium By similarity | ||||||
| Metal binding | 10 | 1 | Magnesium; via carbonyl oxygen By similarity | ||||||
| Metal binding | 89 | 1 | Zinc By similarity | ||||||
| Metal binding | 91 | 1 | Zinc; via amide nitrogen By similarity | ||||||
| Metal binding | 103 | 1 | Zinc By similarity | ||||||
| Metal binding | 105 | 1 | Zinc By similarity | ||||||
| Metal binding | 132 | 1 | Magnesium By similarity | ||||||
| Metal binding | 133 | 1 | Magnesium By similarity | ||||||
| Binding site | 133 | 1 | Substrate By similarity | ||||||
| Site | 50 | 1 | Stabilize the phosphoryl group By similarity | ||||||
| Site | 106 | 1 | Contributes to substrate recognition By similarity | ||||||
| Site | 107 | 1 | Stabilize the phosphoryl group By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. Venter J.C.Science 269:496-512(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd. |
| [2] | Koonin E.V., Rudd K.E. Submitted (SEP-1995) to UniProtKB Cited for: IDENTIFICATION. |
| [3] | "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] [Europe PMC] [Abstract] Cited for: BIOSYNTHESIS OF NUCLEOTIDE-ACTIVATED GLYCERO-MANNO-HEPTOSE. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L42023 Genomic DNA. Translation: AAC22281.1. |
| RefSeq | NP_438781.1. NC_000907.1. |
3D structure databases | |
| ProteinModelPortal | P46452. |
| SMR | P46452. Positions 4-181. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 71421.HI0621.1. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAC22281; AAC22281; HI_0621.1. |
| GeneID | 949688. |
| KEGG | hin:HI0621.1. |
| PATRIC | 20189829. VBIHaeInf48452_0647. |
Phylogenomic databases | |
| eggNOG | COG0241. |
| KO | K03273. |
| OMA | INIDKGY. |
| ProtClustDB | PRK08942. |
Enzyme and pathway databases | |
| UniPathway | UPA00356; UER00438. UPA00976. |
Family and domain databases | |
| Gene3D | 3.40.50.1000. 1 hit. |
| InterPro | IPR023214. HAD-like_dom. IPR006549. HAD-SF_hydro_IIIA. IPR004446. Heptose_bisP_phosphatase. IPR006543. Histidinol-phos. [Graphical view] |
| PIRSF | PIRSF004682. GmhB. 1 hit. |
| SUPFAM | SSF56784. HAD-like_dom. 1 hit. |
| TIGRFAMs | TIGR00213. GmhB_yaeD. 1 hit. TIGR01662. HAD-SF-IIIA. 1 hit. TIGR01656. Histidinol-ppas. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | GMHB_HAEIN | ||||||||
| Accession | Primary (citable) accession number: P46452 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Haemophilus influenzae Haemophilus influenzae (strain Rd): entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
