P71084 (GSAB_BACSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 106.
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 2 Short name=GSA 2 EC=5.4.3.8 Alternative name(s): Glutamate-1-semialdehyde aminotransferase 2 Short name=GSA-AT 2 | ||||
| Gene names |
| ||||
| Organism | Bacillus subtilis (strain 168) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 224308 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › ![]() |
Protein attributes
| Sequence length | 429 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 |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | Cytoplasm Potential HAMAP-Rule MF_00375. |
| Sequence similarities | Belongs to the class-III pyridoxal-phosphate-dependent aminotransferase family. HemL subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | 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 – 429 | 429 | Glutamate-1-semialdehyde 2,1-aminomutase 2 HAMAP-Rule MF_00375 | PRO_0000120395 | |||||
Amino acid modifications | |||||||||
| Modified residue | 267 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 338 | 1 | L → M in CAB04811. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The Bacillus subtilis 168 chromosome from sspE to katA." Cummings N.J., Connerton I.F. Microbiology 143:1855-1859(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168. |
| [2] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. Danchin A.Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| [3] | "From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later." Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A. Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract] Cited for: SEQUENCE REVISION TO 338. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Z82044 Genomic DNA. Translation: CAB04811.1. AL009126 Genomic DNA. Translation: CAB12699.3. |
| PIR | G69637. |
| RefSeq | NP_388751.3. NC_000964.3. |
3D structure databases | |
| ProteinModelPortal | P71084. |
| SMR | P71084. Positions 3-429. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 224308.BSU08710. |
Proteomic databases | |
| PaxDb | P71084. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAB12699; CAB12699; BSU08710. |
| GeneID | 936194. |
| KEGG | bsu:BSU08710. |
| PATRIC | 18973394. VBIBacSub10457_0911. |
Organism-specific databases | |
| GenoList | BSU08710. [Micado] |
Phylogenomic databases | |
| eggNOG | COG0001. |
| HOGENOM | HOG000020210. |
| KO | K01845. |
| ProtClustDB | PRK12389. |
Enzyme and pathway databases | |
| BioCyc | BSUB:BSU08710-MONOMER. |
| UniPathway | UPA00251; UER00317. |
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 | GSAB_BACSU | ||||||||
| Accession | Primary (citable) accession number: P71084 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
