Q9KG45 (GLMS_BACHD) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 73.
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 |
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| Organism | Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 272558 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 600 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 |
| 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 – 600 | 599 | Glucosamine--fructose-6-phosphate aminotransferase [isomerizing] HAMAP MF_00164 | PRO_0000135296 | |||||
Regions | |||||||||
| Domain | 2 – 217 | 216 | Glutamine amidotransferase type-2 | ||||||
| Domain | 283 – 422 | 140 | SIS 1 | ||||||
| Domain | 452 – 590 | 139 | SIS 2 | ||||||
Sites | |||||||||
| Active site | 2 | 1 | Nucleophile; for GATase activity By similarity | ||||||
| Active site | 595 | 1 | For Fru-6P isomerization activity By similarity | ||||||
Sequences
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References
| [1] | "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis." Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K. Nucleic Acids Res. 28:4317-4331(2000) [PubMed: 11058132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BA000004 Genomic DNA. Translation: BAB03987.1. |
| PIR | D83683. |
| RefSeq | NP_241134.1. NC_002570.2. |
3D structure databases | |
| ProteinModelPortal | Q9KG45. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000050711; EBBACP00000049350; EBBACG00000050702. |
| GeneID | 892397. |
| GenomeReviews | Gene locus BH0268 in contig BA000004_GR. |
| KEGG | bha:BH0268. |
| NMPDR | fig|272558.1.peg.268. |
| PATRIC | 18937448. VBIBacHal18977_0283. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000000004. |
| HOGENOM | HBG645312. |
| OMA | LCASQES. |
| ProtClustDB | PRK00331. |
Enzyme and pathway databases | |
| BioCyc | BHAL272558:BH0268-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_BACHD | ||||||||
| Accession | Primary (citable) accession number: Q9KG45 | ||||||||
| 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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