Q55665 (GSA_SYNY3) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 99.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Glutamate-1-semialdehyde 2,1-aminomutase Short name=GSA EC=5.4.3.8 Alternative name(s): Glutamate-1-semialdehyde aminotransferase Short name=GSA-AT | ||||||
| Gene names |
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| Organism | Synechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1111708 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechocystis › ![]() |
Protein attributes
| Sequence length | 433 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | (S)-4-amino-5-oxopentanoate = 5-aminolevulinate. HAMAP-Rule MF_00375 |
| Cofactor | Pyridoxal phosphate By similarity. |
| Pathway | Porphyrin metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 2/2. HAMAP-Rule MF_00375 Porphyrin biosynthesis; chlorophyll biosynthesis. HAMAP-Rule MF_00375 |
| Subunit structure | Homodimer. |
| Subcellular location | Cytoplasm Potential HAMAP-Rule MF_00375. |
| Sequence similarities | Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily. |
| Sequence caution | The sequence BAA10185.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Chlorophyll biosynthesis Porphyrin biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | Pyridoxal phosphate |
| Molecular function | Isomerase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | chlorophyll biosynthetic process Inferred from electronic annotation. Source: HAMAP protoporphyrinogen IX biosynthetic processInferred from electronic annotation. Source: UniProtKB-UniPathway |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | glutamate-1-semialdehyde 2,1-aminomutase activity Inferred from electronic annotation. Source: HAMAP pyridoxal phosphate bindingInferred from electronic annotation. Source: InterPro transaminase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 433 | 433 | Glutamate-1-semialdehyde 2,1-aminomutase HAMAP-Rule MF_00375 | PRO_0000120462 | |||||
Amino acid modifications | |||||||||
| Modified residue | 273 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome." Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., Sugiura M., Tabata S. DNA Res. 2:153-166(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 27184 / PCC 6803 / N-1. |
| [2] | "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. Tabata S.DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PCC 6803 / Kazusa. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BA000022 Genomic DNA. Translation: BAA10185.1. Different initiation. |
| PIR | S76333. |
| RefSeq | YP_007451992.1. NC_020286.1. |
3D structure databases | |
| ProteinModelPortal | Q55665. |
| SMR | Q55665. Positions 7-433. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q55665. 1 interaction. |
| STRING | 1148.sll0017. |
Proteomic databases | |
| PaxDb | Q55665. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | BAA10185; BAA10185; BAA10185. |
| GeneID | 14617666. |
| PATRIC | 23841832. VBISynSp132158_2460. |
Phylogenomic databases | |
| eggNOG | COG0001. |
| HOGENOM | HOG000020210. |
| OMA | FNGNPIS. |
| ProtClustDB | PRK00062. |
Enzyme and pathway databases | |
| UniPathway | UPA00251; UER00317. UPA00668. |
Family and domain databases | |
| Gene3D | 3.40.640.10. 1 hit. 3.90.1150.10. 2 hits. |
| HAMAP | MF_00375. HemL_aminotrans_3. |
| InterPro | IPR004639. 4pyrrol_synth_GluAld_NH2Trfase. IPR005814. Aminotrans_3. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view] |
| PANTHER | PTHR11986. PTHR11986. 1 hit. PTHR11986:SF5. PTHR11986:SF5. 1 hit. |
| Pfam | PF00202. Aminotran_3. 1 hit. [Graphical view] |
| SUPFAM | SSF53383. PyrdxlP-dep_Trfase_major. 1 hit. |
| TIGRFAMs | TIGR00713. hemL. 1 hit. |
| PROSITE | PS00600. AA_TRANSFER_CLASS_3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GSA_SYNY3 | ||||||||
| Accession | Primary (citable) accession number: Q55665 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Synechocystis PCC 6803 Synechocystis (strain PCC 6803): entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
