P07345 (TRPB_PSEAE) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 91.
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: Tryptophan synthase beta chain EC=4.2.1.20 | ||||
| Gene names |
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| Organism | Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) | ||||
| Taxonomic identifier | 208964 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas |
Protein attributes
| Sequence length | 402 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. HAMAP MF_00133 |
| Catalytic activity | L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + glyceraldehyde 3-phosphate + H2O. HAMAP MF_00133 |
| Cofactor | Pyridoxal phosphate By similarity. HAMAP MF_00133 |
| Pathway | Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. HAMAP MF_00133 |
| Subunit structure | Tetramer of two alpha and two beta chains By similarity. |
| Sequence similarities | Belongs to the TrpB family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Aromatic amino acid biosynthesis Tryptophan biosynthesis |
| Ligand | Pyridoxal phosphate |
| Molecular function | Lyase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Molecular function | pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro tryptophan synthase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 402 | 402 | Tryptophan synthase beta chain HAMAP MF_00133 | PRO_0000098981 | |||||
Amino acid modifications | |||||||||
| Modified residue | 93 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 16 | 1 | R → G in AAA88462. Ref.1 | ||||||
| Sequence conflict | 123 | 1 | V → L in AAA88462. Ref.1 | ||||||
| Sequence conflict | 325 | 1 | T → I in AAA88462. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Nucleotide sequence of the genes for tryptophan synthase in Pseudomonas aeruginosa." Hadero A., Crawford I.P. Mol. Biol. Evol. 3:191-204(1986) [PubMed: 3127651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228. |
| [2] | Crawford I.P. Submitted (MAY-1987) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION. |
| [3] | "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen." Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. Olson M.V.Nature 406:959-964(2000) [PubMed: 10984043] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M15826 Genomic DNA. Translation: AAA88462.1. AE004091 Genomic DNA. Translation: AAG03426.1. |
| PIR | TSPSBA. A25355. H83640. |
| RefSeq | NP_248726.1. NC_002516.2. |
3D structure databases | |
| ProteinModelPortal | P07345. |
| SMR | P07345. Positions 14-393. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 879212. |
| GenomeReviews | Gene locus PA0036 in contig AE004091_GR. |
| KEGG | pae:PA0036. |
| PATRIC | 19834268. VBIPseAer58763_0036. |
Organism-specific databases | |
| PseudoCAP | PA0036. |
Phylogenomic databases | |
| HOGENOM | HBG303148. |
| OMA | LKREDLC. |
| ProtClustDB | PRK04346. |
Enzyme and pathway databases | |
| BioCyc | PAER208964:PA0036-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00133. Trp_synth_beta. [Tree] |
| InterPro | IPR001926. PyrdxlP-dep_enz_bsu. IPR006653. Trp_synth_b_CS. IPR006654. Trp_synth_beta. IPR023026. Trp_synth_beta/beta-like. [Graphical view] |
| KO | K01696. |
| PANTHER | PTHR10314:SF3. PTHR10314:SF3. 1 hit. |
| Pfam | PF00291. PALP. 1 hit. [Graphical view] |
| PIRSF | PIRSF001413. Trp_syn_beta. 1 hit. |
| SUPFAM | SSF53686. PyrdxlP-dep_enz_bsu. 1 hit. |
| TIGRFAMs | TIGR00263. TrpB. 1 hit. |
| PROSITE | PS00168. TRP_SYNTHASE_BETA. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | TRPB_PSEAE | ||||||||
| Accession | Primary (citable) accession number: P07345 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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