A0A1A8W5B0 · A0A1A8W5B0_9APIC
- Proteinglutamate synthase (NADH)
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids2936 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
Catalytic activity
- 2 L-glutamate + NAD+ = 2-oxoglutarate + H+ + L-glutamine + NADH
Cofactor
Protein has several cofactor binding sites:
Pathway
Amino-acid biosynthesis; L-glutamate biosynthesis via GLT pathway; L-glutamate from 2-oxoglutarate and L-glutamine (NAD+ route): step 1/1.
Energy metabolism; nitrogen metabolism.
Nitrogen metabolism.
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 3 iron, 4 sulfur cluster binding | |
Molecular Function | glutamate synthase activity | |
Molecular Function | metal ion binding | |
Molecular Function | oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor | |
Biological Process | glutamine metabolic process | |
Biological Process | L-glutamate biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameglutamate synthase (NADH)
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Sar > Alveolata > Apicomplexa > Aconoidasida > Haemosporida > Plasmodiidae > Plasmodium > Plasmodium (Plasmodium)
Accessions
- Primary accessionA0A1A8W5B0
Proteomes
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 20-567 | Glutamine amidotransferase type-2 | ||||
Sequence: CGVGVVADINGKSSRNVIQKAMQILLRLSHRGGVQSNNGDGAGILVGIPHDYFQMLSDTCQLPFLLPERGDYAVAQIYLPQNEERRLFLYHEIEREVYNHGLVVLGWRSPIPVRSDVISATVKKSEPFIAQMFVCKRSVFKNYDDFNIYPFSDINFTDDRNLKLNDLPDDIELLSFFIRKKLVRHNDMYFCSFSSRTIVYKGLLTPSQIYLYFEDLLSEQFTTYLAMVHVRFSTNTSPTWYAAHPFRRICHNGEINTISVNTLLFKERMHLAKSPSFFKSVSIKDLKPINEENYIIYDNDDEIIQKRDTFEDIMLTKNRLKKKSRRNLLLKLKRDYTYNSSALHYKIKREYINSDINNSNSEILSNLNEISKSSSDDIMDVSEENEMYTYRDKSNQRDVGKNEIKTHLIYGESKKTKGAISFPSDSSIFDNAIDFLTMTGREIEHAVMMLMPRAYQKDPNISPLEKAFYEYHTCLMEPWDGPALIIFTDGNKVGASLDRNGLRPARYSITNYGLFVLSSETGVVDLPYDKITHQGCVYPGKVVLVDFK | ||||||
Region | 1157-1182 | Disordered | ||||
Sequence: MGLKSNTGEGGEAEERIKPPSNEANT | ||||||
Region | 1555-1640 | Disordered | ||||
Sequence: CHEESVTYEGEDADDADEEGEDEEEEEDEEEEEDEEEEEEEDEEEEEEVEDEEEEEEEETELGEGRSEGEENREMLEKGTFLANGE | ||||||
Compositional bias | 1562-1619 | Acidic residues | ||||
Sequence: YEGEDADDADEEGEDEEEEEDEEEEEDEEEEEEEDEEEEEEVEDEEEEEEEETELGEG | ||||||
Compositional bias | 2728-2757 | Polar residues | ||||
Sequence: PVVTPGGTATSDGNAATGSSSTANPNHGCS | ||||||
Region | 2728-2771 | Disordered | ||||
Sequence: PVVTPGGTATSDGNAATGSSSTANPNHGCSKVRTKSKKPHGKTN |
Sequence similarities
Belongs to the glutamate synthase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,936
- Mass (Da)331,606
- Last updated2016-10-05 v1
- Checksum4547F0246271E1B6
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1562-1619 | Acidic residues | ||||
Sequence: YEGEDADDADEEGEDEEEEEDEEEEEDEEEEEEEDEEEEEEVEDEEEEEEEETELGEG | ||||||
Compositional bias | 2728-2757 | Polar residues | ||||
Sequence: PVVTPGGTATSDGNAATGSSSTANPNHGCS |
Keywords
- Technical term