Q9Y2T3 · GUAD_HUMAN
- ProteinGuanine deaminase
- GeneGDA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids454 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia.
Catalytic activity
- guanine + H+ + H2O = NH4+ + xanthineThis reaction proceeds in the forward direction.
Cofactor
Note: Binds 1 zinc ion per subunit.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
9.5 μM | guanine |
kcat is 17.4 sec-1 with guanine as substrate.
Pathway
Purine metabolism; guanine degradation; xanthine from guanine: step 1/1.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 82 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 84 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 84-87 | substrate | ||||
Sequence: HASQ | ||||||
Binding site | 213-214 | substrate | ||||
Sequence: RF | ||||||
Binding site | 240 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 240-243 | substrate | ||||
Sequence: HISE | ||||||
Binding site | 330 | substrate | ||||
Sequence: D | ||||||
Binding site | 330 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | guanine deaminase activity | |
Molecular Function | zinc ion binding | |
Biological Process | allantoin metabolic process | |
Biological Process | amide catabolic process | |
Biological Process | deoxyguanosine catabolic process | |
Biological Process | dGMP catabolic process | |
Biological Process | GMP catabolic process | |
Biological Process | guanine catabolic process | |
Biological Process | guanine metabolic process | |
Biological Process | nervous system development | |
Biological Process | nucleobase-containing compound metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameGuanine deaminase
- EC number
- Short namesGuanase; Guanine aminase
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9Y2T3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 527 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000122298 | 1-454 | Guanine deaminase | |||
Sequence: MCAAQMPPLAHIFRGTFVHSTWTCPMEVLRDHLLGVSDSGKIVFLEEASQQEKLAKEWCFKPCEIRELSHHEFFMPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQNIDFAEEVYTRVVRRTLKNGTTTACYFATIHTDSSLLLADITDKFGQRAFVGKVCMDLNDTFPEYKETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILLINKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKASDSPIDLFYGDFFGDISEAVIQKFLYLGDDRNIEEVYVGGKQVVPFSSSV | ||||||
Modified residue | 453 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Structure
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q9Y2T3-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length454
- Mass (Da)51,003
- Last updated1999-11-01 v1
- ChecksumA45C868E6EEA7380
Q9Y2T3-2
- Name2
- Synonymsc
- Differences from canonical
- 1-74: Missing
Q9Y2T3-3
- Name3
- Synonymsa
- Differences from canonical
- 454-454: V → VKETIHLPASSPHPPPFP
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, sequence conflict.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF095286 EMBL· GenBank· DDBJ | AAD25978.1 EMBL· GenBank· DDBJ | mRNA | ||
AF019638 EMBL· GenBank· DDBJ | AAF13301.1 EMBL· GenBank· DDBJ | mRNA | ||
AF144745 EMBL· GenBank· DDBJ | AAG40469.1 EMBL· GenBank· DDBJ | mRNA | ||
AB033084 EMBL· GenBank· DDBJ | BAA86572.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK300418 EMBL· GenBank· DDBJ | BAG62147.1 EMBL· GenBank· DDBJ | mRNA | ||
AK315988 EMBL· GenBank· DDBJ | BAH14359.1 EMBL· GenBank· DDBJ | mRNA | ||
AL583829 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL590311 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL135924 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471089 EMBL· GenBank· DDBJ | EAW62529.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC053584 EMBL· GenBank· DDBJ | AAH53584.1 EMBL· GenBank· DDBJ | mRNA |