Reviewed,
UniProtKB/Swiss-Prot P09831 (GLTB_ECOLI)
Last modified
June 16, 2009.
Version 94.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Glutamate synthase [NADPH] large chain EC=1.4.1.13 Alternative name(s): Glutamate synthase subunit alpha Short name=GLTS alpha chain NADPH-GOGAT | ||||||
| Gene names |
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| Organism | Escherichia coli (strain K12) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 83333 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 1517 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | 2 L-glutamate + NADP+ = L-glutamine + 2-oxoglutarate + NADPH. |
| Cofactor | Binds 1 3Fe-4S cluster. FAD. FMN. |
| Pathway | |
| Subunit structure | Aggregate of 4 catalytic active heterodimers, consisting of a large and a small subunit. |
| Miscellaneous | Glutamine binds to the large subunit and transfers the amido group to 2-oxo-glutamate that apparently binds to the small subunit. |
| Sequence similarities | Belongs to the glutamate synthase family. Contains 1 glutamine amidotransferase type-2 domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Glutamate biosynthesis |
| Domain | Glutamine amidotransferase |
| Ligand | 3Fe-4S FAD FMN Flavoprotein Iron Iron-sulfur Metal-binding NADP |
| Molecular function | Oxidoreductase |
| PTM | Zymogen |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | glutamate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW glutamine metabolic processInferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 3 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW glutamate synthase (NADPH) activityInferred from electronic annotation. Source: EC iron ion bindingInferred from electronic annotation. Source: UniProtKB-KW protein bindingInferred from physical interaction. Source: IntAct |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Propeptide | 1 – 42 | 42 | PRO_0000011620 | ||||||
| Chain | 43 – 1517 | 1475 | Glutamate synthase [NADPH] large chain | PRO_0000011621 | |||||
Regions | |||||||||
| Domain | 43 – 433 | 391 | Glutamine amidotransferase type-2 | ||||||
| Nucleotide binding | 1080 – 1132 | 53 | FMN By similarity | ||||||
Sites | |||||||||
| Active site | 43 | 1 | For GATase activity By similarity | ||||||
| Metal binding | 1133 | 1 | Iron-sulfur (3Fe-4S) By similarity | ||||||
| Metal binding | 1139 | 1 | Iron-sulfur (3Fe-4S) By similarity | ||||||
| Metal binding | 1144 | 1 | Iron-sulfur (3Fe-4S) By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 105 – 109 | 5 | GWRLA → LAFR in AAA23904. Ref.1 | ||||||
| Sequence conflict | 140 | 1 | E → N in AAA23904. Ref.1 | ||||||
| Sequence conflict | 220 – 240 | 21 | LCMPT…LRLES → CVCRRICRVLSGSCGPASGM in AAA23904. Ref.1 | ||||||
| Sequence conflict | 259 – 282 | 24 | LAQPF…NRQWA → WRNRSAIWRITVKSTPSPVT ANG Ref.1 | ||||||
| Sequence conflict | 259 – 282 | 24 | LAQPF…NRQWA → WRNRSAIWRITVKSTPSPVT ANG Ref.4 | ||||||
| Sequence conflict | 460 | 1 | N → K in AAA23904. Ref.1 | ||||||
| Sequence conflict | 574 | 1 | A → T in AAA23904. Ref.1 | ||||||
| Sequence conflict | 863 | 1 | D → H in AAA23904. Ref.1 | ||||||
| Sequence conflict | 1286 – 1290 | 5 | THGDQ → DARRS in AAA23904. Ref.1 | ||||||
| Sequence conflict | 1373 | 1 | G → A in AAA23904. Ref.1 | ||||||
| Sequence conflict | 1376 | 1 | G → R in AAA23904. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Determination of the nucleotide sequence for the glutamate synthase structural genes of Escherichia coli K-12." Oliver G., Gosset G., Sanchez-Pescador R., Lozoya E., Ku L.M., Flores N., Becerril B., Valle F., Bolivar F. Gene 60:1-11(1987) [PubMed: 3326786] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: K12. |
| [2] | "The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [3] | "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [4] | "Mutations affecting the Shine-Dalgarno sequences of the untranslated region of the Escherichia coli gltBDF operon." Velazquez L., Camarena L., Reyes J.L., Bastarrachea F. J. Bacteriol. 173:3261-3264(1991) [PubMed: 1673677] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-304. |
| [5] | "Amino acid sequence analysis of the glutamate synthase enzyme from Escherichia coli K-12." Gosset G., Merino E., Recillas F., Oliver G., Becerril B., Bolivar F. Protein Seq. Data Anal. 2:9-16(1989) [PubMed: 2643092] [Abstract] Cited for: DISCUSSION OF SEQUENCE. |
Cross-references
Sequence databases | |
|---|---|
| M18747 Genomic DNA. Translation: AAA23904.1. U18997 Genomic DNA. Translation: AAA58014.1. U00096 Genomic DNA. Translation: AAC76244.1. AP009048 Genomic DNA. Translation: BAE77256.1. M68876 Genomic DNA. Translation: AAA23906.1. | |
| PIR | F65112. |
| RefSeq | AP_003755.1. NP_417679.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1LM1 based on UniProtKB P55038. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP:9802N. |
| IntAct | P09831. 8 interactions. |
Genome annotation databases | |
| GeneID | 947724. |
| GenomeReviews | Gene locus JW3179 in contig AP009048_GR. Gene locus b3212 in contig U00096_GR. |
| KEGG | ecj:JW3179. eco:b3212. |
Organism-specific databases | |
| EchoBASE | EB0398. |
| EcoGene | EG10403. gltB. |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P09831. |
| OMA | P09831. DSAAMSI. |
Enzyme and pathway databases | |
| BioCyc | EcoCyc:GLUSYNLARGE-MON. MetaCyc:GLUSYNLARGE-MON. |
| BRENDA | 1.4.1.13. 246. |
Family and domain databases | |
| InterPro | IPR013785. Aldolase_TIM. IPR000583. GATase_2. IPR017932. GATase_II. IPR002932. Glu_synth_centr_C. IPR006982. Glu_synth_centr_N. IPR002489. Glu_synthase_C. [Graphical view] |
| Gene3D | G3DSA:3.20.20.70. Aldolase_TIM. 2 hits. G3DSA:2.160.20.60. Glu_synthase_C. 1 hit. |
| Pfam | PF00310. GATase_2. 1 hit. PF04898. Glu_syn_central. 1 hit. PF01645. Glu_synthase. 1 hit. PF01493. GXGXG. 1 hit. [Graphical view] |
| PROSITE | PS51278. GATASE_TYPE_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GLTB_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P09831 Secondary accession number(s): Q2M900 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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