Q0JKD0 · GLT1_ORYSJ
- ProteinGlutamate synthase 1 [NADH], chloroplastic
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids2167 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score5/5
Function
function
Involved in glutamate biosynthesis and plays a major role in the primary ammonium ions assimilation in seedling roots. May be involved in the reutilization of glutamine in developing organs. Plays a role in the development of tillers.
Catalytic activity
- 2 L-glutamate + NAD+ = 2-oxoglutarate + H+ + L-glutamine + NADH
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 [3Fe-4S] cluster.
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.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 100 | Nucleophile | ||||
Sequence: C | ||||||
Binding site | 1192-1249 | FMN (UniProtKB | ChEBI) | ||||
Sequence: LAETHQTLVANGLRGRAILQTDGQLKTGKDVAVACLLGAEEFGFSTAPLITLGCIMMR | ||||||
Binding site | 1245 | [3Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1251 | [3Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1256 | [3Fe-4S] cluster (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 1956-1970 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GGGDTGTDCIGTSIR |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chloroplast | |
Cellular Component | plastid | |
Molecular Function | 3 iron, 4 sulfur cluster binding | |
Molecular Function | flavin adenine dinucleotide binding | |
Molecular Function | FMN binding | |
Molecular Function | glutamate synthase (NADH) activity | |
Molecular Function | iron ion binding | |
Biological Process | ammonia assimilation cycle | |
Biological Process | developmental growth | |
Biological Process | glutamate biosynthetic process | |
Biological Process | L-glutamate biosynthetic process | |
Biological Process | response to ammonium ion |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGlutamate synthase 1 [NADH], chloroplastic
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > BOP clade > Oryzoideae > Oryzeae > Oryzinae > Oryza > Oryza sativa
Accessions
- Primary accessionQ0JKD0
- Secondary accessions
Proteomes
Genome annotation databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Inhibition of the main root elongation when grown in presence of ammonium chloride. Reduced plant height, biomass and panicle number.
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Transit peptide | 1-36 | UniProt | Chloroplast | ||||
Sequence: MSAAQGMAYKLRTDAAPTGAGRRARRSHSSVAAPYR | |||||||
Chain | PRO_0000395201 | 37-2167 | UniProt | Glutamate synthase 1 [NADH], chloroplastic | |||
Sequence: AARLVQGGVSIEGGLVGGCQLTEERVAARPPRAAARDAEPVRPLSTLPESSIGLYDPSRERDSCGVGFVAELSGDYKRATVNDALEMLERMAHRGACGCEKNTGDGAGILVALPHNFFREVTKDAGFELPQPGEYAVGMVFLPIDEKRRERSKAEFQKVAESLGHVILGWRRVPTDNSDLGESALQTEPVIEQVFLTKSSSSEADFEQQLYILRRLSILSIRAALNLRRGGKRDFYMCSLSSRTIVYKGQLKPCQLKGYYYADLGHENFTSYMALVHSRFSTNTFPSWDRAQPMRVLGHNGEINTLKGNKNWMKAREGLLECEKLGLTKDQFSKILPIVDATSSDSGAFDGVLELLIRGGRSLPEAVMMMIPEAWQNDVNMEPEKKALYEFLSALMEPWDGPALISFTDGRYLGATLDRNGLRPGRFYVTHSGRVVMGSEVGVVDVPSKDVLRKGRLNPGMMLLVDFENHTVVDDEALKAQYSKAHPYGEWLKRQKIYLKDIVESVPETERVAPGISGSLTQKNEKKEHAGVNGIVTPLKAFGYTVEALEMLLLPMAKDGVEALGSMGNDTPLAVMSNREKLTFEYFKQMFAQVTNPPIDPIREKIVTSMECMIGPEGDLLETTEKQCNRLALEGPLVSIDEMEAIKKMNYRGWRSKVLDITYPKKSGRKGLEETLDRICTEARGAIKKGYTVLVLSDRGFSSDRVAVSSLLAVGAVHQHLVANLERTRVGLLVESAEPREVHHFCTLVGFGADAVCPYLAIEAIWCLQNDGKIPPNGDGKPYSKEELVKKYFYASNYGMMKVLAKMGISTLASYKGAQIFEALGLSSEVIRKCFDGTPSRIEGATFEMLARDALRLHELAFPSRAPPPGSADAKALPNPGDYHWRKNGEVHLNDPLAMAKLQEAARVNSRAAYKEYSRRIQELNKTCNLRGMLKFKDTADMISVDEVEPASEIVKRFVTGAMSYGSISLEAHTALAMAMNKLGGKSNTGEGGEQPSRMEPLANGSMNPKRSAIKQVASGRFGVSSYYLTNADELQIKMAQGAKPGEGGELPGHKVIGDIAVTRHSTAGVGLISPPPHHDIYSIEDLAQLIHDLKNSNPRARISVKLVSEAGVGVVASGVVKGHADHVLISGHDGGTGASRWTGIKNAGLPWELGLAETHQTLVANGLRGRAILQTDGQLKTGKDVAVACLLGAEEFGFSTAPLITLGCIMMRKCHTNTCPVGIATQDPVLREKFAGEPEHVINFFFMLAEELREIMSQLGFRTITEMVGRSDMLEVDPEVVKSNEKLENIDLSLILKPAAEIRPGAAQYCVEKQDHGLDMALDNKLIALSKAALEKEVRVFIETPIQNTNRAVGTMLSHEVTKRYHMKGLPAGTIHVKLTGSAGQSLGAFLCPGITLELEGDSNDYVGKGLSGGKIVVYPPRDSTFIPEDNIVIGNVALYGATIGEAYFNGMAAERFCVRNSGAQAVVEGIGDHGCEYMTGGTVVILGKTGRNFAAGMSGGIAYVYDIDGKFSVRCNHELVDLYHVEEEEDITTLKMMIEQHRLNTGSVVARDILSNFDTLLPKFVKVFPRDYKRVLDNMKAEKAAAKLAKEPKISNGVSVTTKKVQPEQSTNRPTRVSNAKKYRGFISYERESISYRDPNERVKDWKEVAIESVPGPLLNTQSARCMDCGTPFCHQESSGAGCPLGNKIPEFNELVHQNRWREALDRLLETNNFPEFTGRVCPAPCEGSCVLGIIENPVSIKSIECAIIDKGFEEGWMVPRPPLQRTGKKVAIIGSGPAGLAAADQLNKMGHFVTVFERADRIGGLMMYGVPNMKTDKIEIVQRRVNLMAEEGITFVVNANVGSDPLYSIERLRSENDAVILACGATKPRDLGIPGRELSGVHFAMEFLHANTKSLLDSNLEDGRYISAKGKKVVVIGGGDTGTDCIGTSIRHGCTSIVNLELLTKPPSKRAADNPWPQWPRIFRVDYGHQEASSKFGNDPRTYEVLTKRFIGDENGNVKALEVVRVKWEKVDGRFQFKEIEGSNETIEADLVLLAMGFLGPEATIAEKLGLEKDNRSNFKAQFGNFATSVDGIFAAGDCRRGQSLVVWAITEGRQAAAAVDKYLSRNEQDAAEDITPSGAGFVQPVAA | |||||||
Modified residue (large scale data) | 214 | PTMeXchange | Phosphoserine | ||||
Sequence: S |
Proteomic databases
Expression
Tissue specificity
Highly expressed in roots.
Induction
By ammonium supply in roots.
Interaction
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-31 | Disordered | ||||
Sequence: MSAAQGMAYKLRTDAAPTGAGRRARRSHSSV | ||||||
Domain | 100-504 | Glutamine amidotransferase type-2 | ||||
Sequence: CGVGFVAELSGDYKRATVNDALEMLERMAHRGACGCEKNTGDGAGILVALPHNFFREVTKDAGFELPQPGEYAVGMVFLPIDEKRRERSKAEFQKVAESLGHVILGWRRVPTDNSDLGESALQTEPVIEQVFLTKSSSSEADFEQQLYILRRLSILSIRAALNLRRGGKRDFYMCSLSSRTIVYKGQLKPCQLKGYYYADLGHENFTSYMALVHSRFSTNTFPSWDRAQPMRVLGHNGEINTLKGNKNWMKAREGLLECEKLGLTKDQFSKILPIVDATSSDSGAFDGVLELLIRGGRSLPEAVMMMIPEAWQNDVNMEPEKKALYEFLSALMEPWDGPALISFTDGRYLGATLDRNGLRPGRFYVTHSGRVVMGSEVGVVDVPSKDVLRKGRLNPGMMLLVDFE | ||||||
Region | 1022-1042 | Disordered | ||||
Sequence: KSNTGEGGEQPSRMEPLANGS |
Sequence similarities
Belongs to the glutamate synthase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length2,167
- Mass (Da)236,895
- Last updated2006-10-03 v1
- Checksum1CDED150F52B00EB
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 769 | in Ref. 1; BAA35120 | ||||
Sequence: Missing | ||||||
Sequence conflict | 2056 | in Ref. 1; BAA35120 | ||||
Sequence: F → L |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB008845 EMBL· GenBank· DDBJ | BAA35120.1 EMBL· GenBank· DDBJ | mRNA | ||
AP008207 EMBL· GenBank· DDBJ | BAF05798.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP014957 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |