Reviewed,
UniProtKB/Swiss-Prot P54746 (MNGB_ECOLI)
Last modified
June 16, 2009.
Version 64.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Alpha-mannosidase mngB EC=3.2.1.- | ||||||
| Gene names |
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| Organism | Escherichia coli (strain K12) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 83333 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 877 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | May hydrolyze mannosyl-D-glycerate to mannose-6-phosphate and glycerate. Ref.5 |
| Cofactor | Binds one divalent metal cation per subunit By similarity. |
| Induction | Repressed by mngR. Induced by mannosyl-D-glycerate. |
| Sequence similarities | Belongs to the glycosyl hydrolase 38 family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Metal-binding |
| Molecular function | Glycosidase Hydrolase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | mannose metabolic process Inferred from electronic annotation. Source: InterPro |
| Molecular function | alpha-mannosidase activity Inferred from electronic annotation. Source: InterPro metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 877 | 877 | Alpha-mannosidase mngB | PRO_0000168700 | |||||
Sites | |||||||||
| Active site | 126 | 1 | Nucleophile By similarity | ||||||
| Metal binding | 14 | 1 | Divalent metal cation By similarity | ||||||
| Metal binding | 16 | 1 | Divalent metal cation By similarity | ||||||
| Metal binding | 126 | 1 | Divalent metal cation By similarity | ||||||
| Metal binding | 338 | 1 | Divalent metal cation By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 87 – 100 | 14 | WYTQT…VSAES → GIPRPIPRLFCGNP Ref.4 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. Horiuchi T.DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [2] | "The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [3] | "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [4] | "Isolation and characterization of the heat-responsive genes in Escherichia coli." Utsumi R., Horie T., Katoh A., Kaino Y., Tanabe H., Noda M. Biosci. Biotechnol. Biochem. 60:309-315(1996) [PubMed: 9063979] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-100. |
| [5] | "Phosphotransferase-mediated transport of the osmolyte 2-O-alpha-mannosyl-D-glycerate in Escherichia coli occurs by the product of the mngA (hrsA) gene and is regulated by the mngR (farR) gene product acting as repressor." Sampaio M.-M., Chevance F., Dippel R., Eppler T., Schlegel A., Boos W., Lu Y.-J., Rock C.O. J. Biol. Chem. 279:5537-5548(2004) [PubMed: 14645248] [Abstract] Cited for: FUNCTION AS A MANNOSIDASE. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574. |
Cross-references
Sequence databases | |
|---|---|
| U00096 Genomic DNA. Translation: AAC73826.1. AP009048 Genomic DNA. Translation: BAA35398.1. D64014 Genomic DNA. No translation available. | |
| PIR | C64809. |
| RefSeq | AP_001369.1. NP_415260.1. |
3D structure databases | |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | GH38. Glycoside Hydrolase Family 38. |
Genome annotation databases | |
| GeneID | 945359. |
| GenomeReviews | Gene locus JW0721 in contig AP009048_GR. Gene locus b0732 in contig U00096_GR. |
| KEGG | ecj:JW0721. eco:b0732. |
Organism-specific databases | |
| EchoBASE | EB3025. |
| EcoGene | EG13236. mngB. |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P54746. |
| OMA | P54746. DMADNLL. |
Enzyme and pathway databases | |
| BioCyc | EcoCyc:EG13236-MON. MetaCyc:EG13236-MON. |
Family and domain databases | |
| InterPro | IPR011682. Glyco_hydro_38_C. IPR000602. Glyco_hydro_38_core. [Graphical view] |
| Gene3D | G3DSA:3.20.110.10. Glyco_hydro_38_core. 1 hit. |
| Pfam | PF01074. Glyco_hydro_38. 1 hit. PF07748. Glyco_hydro_38C. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | MNGB_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P54746 Secondary accession number(s): P75753 | ||||||||
| 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
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


