A0A3S0HB28 · A0A3S0HB28_STEMA
- ProteinAdenylosuccinate lyase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids455 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
Catalyzes two reactions in de novo purine nucleotide biosynthesis. Catalyzes the breakdown of 5-aminoimidazole- (N-succinylocarboxamide) ribotide (SAICAR or 2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate) to 5-aminoimidazole-4-carboxamide ribotide (AICAR or 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide) and fumarate, and of adenylosuccinate (ADS or N6-(1,2-dicarboxyethyl)-AMP) to adenosine monophosphate (AMP) and fumarate.
Catalytic activity
- (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + fumarateThis reaction proceeds in the forward direction.
Pathway
Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 2/2.
Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity | |
Molecular Function | N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity | |
Biological Process | 'de novo' AMP biosynthetic process | |
Biological Process | 'de novo' IMP biosynthetic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAdenylosuccinate lyase
- EC number
- Short namesASL
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Lysobacterales > Lysobacteraceae > Stenotrophomonas > Stenotrophomonas maltophilia group
Accessions
- Primary accessionA0A3S0HB28
Proteomes
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 14-312 | Fumarate lyase N-terminal | ||||
Sequence: GRYAGKVDALRPIFSEYGLIKARITVEVEWLLALAAEPGIVELAPFSDAAVARLRALAASFSPAQAARVKEIERTTNHDVKAVEYFIKEQLKDDAELAPALEFVHFACTSEDINNLSYGLMLEQARREVLLPTLDGIASSLRTLAHAQAGQPMLSRTHGQTASPTTLGKELANVVARLERQRKQIAAVELTGKINGAVGNYNAHIASYPDVDWPAFAERFVTGLGLVFNPYTTQIEPHDNIAEIGDAARRANIILIDLARDIWGYVSLGYFKQRLKEGEVGSSTMPHKVNPIDFENAEG | ||||||
Domain | 331-445 | Adenylosuccinate lyase PurB C-terminal | ||||
Sequence: SRWQRDLTDSTVLRALGTAFGHSQVALDSLAKGLGKLEVNPQRLDADLDAAWEVLAEAVQTVMRRHGLPNPYEQLKALTRGQGITAESMRAFVQGLELPADAKQRLLEMTPGSYT |
Sequence similarities
Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length455
- Mass (Da)49,632
- Last updated2019-04-10 v1
- ChecksumC6457C89A97FEC2F