Reviewed,
UniProtKB/Swiss-Prot Q9HJM3 (GUAAA_THEAC)
Last modified
February 9, 2010.
Version 59.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: GMP synthase [glutamine-hydrolyzing] subunit A EC=6.3.5.2 Alternative name(s): Glutamine amidotransferase | ||||
| Gene names |
| ||||
| Organism | Thermoplasma acidophilum [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 2303 [NCBI] | ||||
| Taxonomic lineage | Archaea › Euryarchaeota › Thermoplasmata › Thermoplasmatales › Thermoplasmataceae › Thermoplasma |
Protein attributes
| Sequence length | 200 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Catalyzes the synthesis of GMP from XMP By similarity. HAMAP MF_01510 |
| Catalytic activity | ATP + xanthosine 5'-phosphate + L-glutamine + H2O = AMP + diphosphate + GMP + L-glutamate. HAMAP MF_01510 |
| Pathway | Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. HAMAP MF_01510 |
| Subunit structure | Heterodimer composed of a glutamine amidotransferase subunit (A) and a GMP-binding subunit (B) Potential. HAMAP MF_01510 |
| Sequence similarities | Contains 1 glutamine amidotransferase type-1 domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | GMP biosynthesis Purine biosynthesis |
| Domain | Glutamine amidotransferase |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Ligase |
| Technical term | 3D-structure Complete proteome |
| Gene Ontology (GO) | |
| Biological process | GMP biosynthetic process Inferred from electronic annotation. Source: HAMAP glutamine metabolic processInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW GMP synthase (glutamine-hydrolyzing) activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 200 | 200 | GMP synthase [glutamine-hydrolyzing] subunit A HAMAP MF_01510 | PRO_0000140235 | ||||||||||||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||||||||||||
| Domain | 3 – 193 | 191 | Glutamine amidotransferase type-1 | |||||||||||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||||||||||
| Active site | 80 | 1 | Nucleophile By similarity | |||||||||||||||||||||||||||||||||||||
| Active site | 167 | 1 | By similarity | |||||||||||||||||||||||||||||||||||||
| Active site | 169 | 1 | By similarity | |||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||
| Beta strand | 3 – 10 | 8 | ||||||||||||||||||||||||||||||||||||||
| Helix | 16 – 23 | 8 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 30 – 32 | 3 | ||||||||||||||||||||||||||||||||||||||
| Helix | 37 – 40 | 4 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 44 – 48 | 5 | ||||||||||||||||||||||||||||||||||||||
| Helix | 55 – 57 | 3 | ||||||||||||||||||||||||||||||||||||||
| Helix | 59 – 61 | 3 | ||||||||||||||||||||||||||||||||||||||
| Helix | 62 – 71 | 10 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 76 – 79 | 4 | ||||||||||||||||||||||||||||||||||||||
| Helix | 81 – 89 | 9 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 93 – 110 | 18 | ||||||||||||||||||||||||||||||||||||||
| Helix | 114 – 116 | 3 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 121 – 135 | 15 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 140 – 145 | 6 | ||||||||||||||||||||||||||||||||||||||
| Beta strand | 152 – 166 | 15 | ||||||||||||||||||||||||||||||||||||||
| Helix | 176 – 195 | 20 | ||||||||||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum." Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W. Nature 407:508-513(2000) [PubMed: 11029001] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 25905 / AMRC-C165 / DSM 1728 / IFO 15155 / JCM 9062. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AL445066 Genomic DNA. Translation: CAC12073.1. Different initiation. | ||||||||||||
| RefSeq | NP_394403.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ModBase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 1457057. | ||||||||||||
| NMPDR | fig|273075.1.peg.925. | ||||||||||||
Organism-specific databases | |||||||||||||
| CMR | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | HBG292341. | ||||||||||||
| OMA | GQYVHRI. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | TACI273075:TA0944-MONOMER. | ||||||||||||
| BRENDA | 6.3.5.2. 435. | ||||||||||||
Family and domain databases | |||||||||||||
| HAMAP | MF_01510. GMP_synthase_A. [Tree] | ||||||||||||
| InterPro | IPR006220. Anth_synthII. IPR017926. GATASE_1. IPR000991. GATase_class1_C. IPR004739. GMP_synth_N. [Graphical view] | ||||||||||||
| Pfam | PF00117. GATase. 1 hit. [Graphical view] | ||||||||||||
| PRINTS | PR00097. ANTSNTHASEII. | ||||||||||||
| TIGRFAMs | TIGR00888. guaA_Nterm. 1 hit. | ||||||||||||
| PROSITE | PS51273. GATASE_TYPE_1. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | GUAAA_THEAC | ||||||||
| Accession | Primary (citable) accession number: Q9HJM3 | ||||||||
| 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
| 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


