Q9K1P9 (GLMS_NEIMB) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 68.
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: Glucosamine--fructose-6-phosphate aminotransferase [isomerizing] EC=2.6.1.16 Alternative name(s): D-fructose-6-phosphate amidotransferase GFAT Glucosamine-6-phosphate synthase Hexosephosphate aminotransferase L-glutamine-D-fructose-6-phosphate amidotransferase | ||||
| Gene names |
| ||||
| Organism | Neisseria meningitidis serogroup B | ||||
| Taxonomic identifier | 491 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria |
Protein attributes
| Sequence length | 612 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source By similarity. HAMAP MF_00164 |
| Catalytic activity | L-glutamine + D-fructose 6-phosphate = L-glutamate + D-glucosamine 6-phosphate. HAMAP MF_00164 |
| Subunit structure | Homodimer By similarity. HAMAP MF_00164 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00164. |
| Sequence similarities | Contains 1 glutamine amidotransferase type-2 domain. Contains 2 SIS domains. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Domain | Glutamine amidotransferase Repeat |
| Molecular function | Aminotransferase Transferase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | carbohydrate biosynthetic process Inferred from electronic annotation. Source: InterPro glutamine metabolic processInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | glutamine-fructose-6-phosphate transaminase (isomerizing) activity Inferred from electronic annotation. Source: EC 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 612 | 611 | Glucosamine--fructose-6-phosphate aminotransferase [isomerizing] HAMAP MF_00164 | PRO_0000135361 | |||||
Regions | |||||||||
| Domain | 2 – 220 | 219 | Glutamine amidotransferase type-2 | ||||||
| Domain | 288 – 428 | 141 | SIS 1 | ||||||
| Domain | 461 – 602 | 142 | SIS 2 | ||||||
Sites | |||||||||
| Active site | 2 | 1 | Nucleophile; for GATase activity By similarity | ||||||
| Active site | 607 | 1 | For Fru-6P isomerization activity By similarity | ||||||
Sequences
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References
| [1] | "Complete genome sequence of Neisseria meningitidis serogroup B strain MC58." Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H., Salzberg S.L., White O. Venter J.C.Science 287:1809-1815(2000) [PubMed: 10710307] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: MC58 / Serogroup B. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE002098 Genomic DNA. Translation: AAF40502.1. |
| PIR | B81246. |
| RefSeq | NP_273097.1. NC_003112.2. |
3D structure databases | |
| ProteinModelPortal | Q9K1P9. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | C44.971. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBNEIT00000009583; EBNEIP00000009203; EBNEIG00000009583. |
| GeneID | 902134. |
| GenomeReviews | Gene locus NMB0031 in contig AE002098_GR. |
| KEGG | nme:NMB0031. |
| NMPDR | fig|122586.1.peg.31. |
| PATRIC | 20355011. VBINeiMen85645_0042. |
| TIGR | NMB0031. |
Phylogenomic databases | |
| GeneTree | EBGT00050000020652. |
| HOGENOM | HBG645312. |
| OMA | QFAKKTS. |
| ProtClustDB | PRK00331. |
Enzyme and pathway databases | |
| BioCyc | NMEN122586:NMB_0031-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00164. GlmS. [Tree] |
| InterPro | IPR000583. GATase_2. IPR017932. GATase_II. IPR005855. GlmS_trans. IPR001347. SIS. [Graphical view] |
| KO | K00820. |
| Pfam | PF00310. GATase_2. 2 hits. PF01380. SIS. 2 hits. [Graphical view] |
| TIGRFAMs | TIGR01135. GlmS. 1 hit. |
| PROSITE | PS51278. GATASE_TYPE_2. 1 hit. PS51464. SIS. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GLMS_NEIMB | ||||||||
| Accession | Primary (citable) accession number: Q9K1P9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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