A0A397GPE7 · A0A397GPE7_9EURO
- ProteinUncharacterized protein
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids3158 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
Catalytic activity
- 2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H+ + L-glutamate + phosphate
Pathway
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 345 | Nucleophile | ||||
Sequence: C | ||||||
Active site | 429 | |||||
Sequence: H | ||||||
Active site | 431 | |||||
Sequence: E |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Molecular Function | 3-phytase activity | |
Molecular Function | amino acid binding | |
Molecular Function | aspartate carbamoyltransferase activity | |
Molecular Function | ATP binding | |
Molecular Function | carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity | |
Molecular Function | metal ion binding | |
Molecular Function | transmembrane transporter activity | |
Biological Process | 'de novo' pyrimidine nucleobase biosynthetic process | |
Biological Process | 'de novo' UMP biosynthetic process | |
Biological Process | glutamine metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Submitted names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Fumigati
Accessions
- Primary accessionA0A397GPE7
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 2327-2345 | Helical | ||||
Sequence: MYLTGLTLYFIGYVAFEVP | ||||||
Transmembrane | 2357-2376 | Helical | ||||
Sequence: IWLPTLTLLWGIIATLLGVV | ||||||
Transmembrane | 2388-2405 | Helical | ||||
Sequence: ALGIAESGLFPGVVFYLS | ||||||
Transmembrane | 2417-2438 | Helical | ||||
Sequence: VALFFSAASLAGAFGGILAWGI | ||||||
Transmembrane | 2450-2472 | Helical | ||||
Sequence: WRWIFILEGLATVVMSIVAYFWV | ||||||
Transmembrane | 2520-2540 | Helical | ||||
Sequence: VWLYGLCFHTMSLPLYTLSLF | ||||||
Transmembrane | 2560-2577 | Helical | ||||
Sequence: VPPYALGFIMTITVAILS | ||||||
Transmembrane | 2584-2603 | Helical | ||||
Sequence: APFIIGSTAFACIGYILLLT | ||||||
Transmembrane | 2609-2631 | Helical | ||||
Sequence: ISYAGVFFAAGGIYPSVAIVLSW | ||||||
Transmembrane | 2676-2697 | Helical | ||||
Sequence: HGFALGYLLANIVVVSVLWAVL |
Keywords
- Cellular component
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 607-799 | ATP-grasp | ||||
Sequence: ARSMESINEKCAKSASASNLEEALRVVEDIGFPVIVRAAYALGGLGSGFADDMGQLKELCAKAFAVSPQVLIEKSMKGWKEIEYEVVRDCQDNCITVCNMENFDPLGIHTGDSIVVAPSQTLSDEDYNMLRTTAVNVIRHLGVVGECNIQYALNPFSKEYCIIEVNARLSRSSALASKATGYPLAFIAAKLGL | ||||||
Domain | 1142-1333 | ATP-grasp | ||||
Sequence: SRMLDRIGVDQPAWKELTSIEEAKGFCDKVGYPVLVRPSYVLSGAAMNTVYSEHDLATYLNQAADVSREHPVVITKYIENAKEIEMDAVARNGVMVGHFISEHVENAGVHSGDATLILPPQDLDPETVRRIEEATAKIGNALNVTGPFNIQFIAKDNDIKVIECNVRASRSFPFVSKVMGVDLIEMATKAMI | ||||||
Domain | 1399-1578 | MGS-like | ||||
Sequence: FRLPKKNILFSIGSYKEKREMLPSIKKLHQLGFNLFATSGTADFLKENGVPVKYLEVLPGQEEELKSEYSLTQHLANNLIDLYINLPSNNRFRRPANYMSKGYRTRRMAVDYQTPLVTNVKNAKILIEAIARHYALNVQTIDYQTSHRTIILPGLINITAFVPGLVTPGSKDFELVTKAS | ||||||
Region | 1890-1938 | Disordered | ||||
Sequence: AMSPMVQARPESSLDRRLSISGTPGRIFKPRPAESAANELGPPLYTPAQ | ||||||
Domain | 2291-2703 | Major facilitator superfamily (MFS) profile | ||||
Sequence: LLPPLTILYLLSFLDRSNVGNARLDGMATDIGMTGNMYLTGLTLYFIGYVAFEVPSNIVLKRTTPRIWLPTLTLLWGIIATLLGVVQNYAGYLTSRTALGIAESGLFPGVVFYLSMWYKRSEQHYRVALFFSAASLAGAFGGILAWGIGHMRGVGGYNGWRWIFILEGLATVVMSIVAYFWVYNYPATAEFLSDKERAFIQFRLKNDSDATRDEKFSWTAVFDAFKDVKVWLYGLCFHTMSLPLYTLSLFMPTIINELGYSAAQAQLLTVPPYALGFIMTITVAILSERTSRRAPFIIGSTAFACIGYILLLTSKRASISYAGVFFAAGGIYPSVAIVLSWPANNVSGQTKRAIANAMQISIGNLGAVMGTQLYRTESSPHYYLGHGFALGYLLANIVVVSVLWAVLNRENLD |
Sequence similarities
Belongs to the histidine acid phosphatase family.
In the 2nd section; belongs to the CarB family.
In the 3rd section; belongs to the metallo-dependent hydrolases superfamily. DHOase family. CAD subfamily.
In the C-terminal section; belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family.
In the N-terminal section; belongs to the CarA family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length3,158
- Mass (Da)347,866
- Last updated2018-12-05 v1
- ChecksumDB751AB46BC42FE5
Keywords
- Technical term