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C3LLL5 (TRPA_VIBCM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tryptophan synthase alpha chain

EC=4.2.1.20
Gene names
Name:trpA
Ordered Locus Names:VCM66_1124
OrganismVibrio cholerae serotype O1 (strain M66-2) [Complete proteome] [HAMAP]
Taxonomic identifier579112 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length268 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate By similarity. HAMAP-Rule MF_00131

Catalytic activity

L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H2O. HAMAP-Rule MF_00131

Pathway

Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5. HAMAP-Rule MF_00131

Subunit structure

Tetramer of two alpha and two beta chains By similarity.

Sequence similarities

Belongs to the TrpA family.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Aromatic amino acid biosynthesis
Tryptophan biosynthesis
   Molecular functionLyase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Molecular_functiontryptophan synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 268268Tryptophan synthase alpha chain HAMAP-Rule MF_00131
PRO_1000198733

Sites

Active site491Proton acceptor By similarity
Active site601Proton acceptor By similarity

Secondary structure

............................................. 268
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
C3LLL5 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: A04BEA6FAEECB028

FASTA26828,494
        10         20         30         40         50         60 
MNRYQALFQR LSAAQQGAFV PFVTIGDPNP EQSLAIMQTL IDAGADALEL GMPFSDPLAD 

        70         80         90        100        110        120 
GPTIQGANLR ALAAKTTPDI CFELIAQIRA RNPETPIGLL MYANLVYARG IDDFYQRCQK 

       130        140        150        160        170        180 
AGVDSVLIAD VPTNESQPFV AAAEKFGIQP IFIAPPTASD ETLRAVAQLG KGYTYLLSRA 

       190        200        210        220        230        240 
GVTGAETKAN MPVHALLERL QQFDAPPALL GFGISEPAQV KQAIEAGAAG AISGSAVVKI 

       250        260 
IETHLDNPAK QLTELANFTQ AMKKATKI 

« Hide

References

[1]"A recalibrated molecular clock and independent origins for the cholera pandemic clones."
Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J., Wang W., Wang J., Qian W., Li D., Wang L.
PLoS ONE 3:E4053-E4053(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: M66-2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001233 Genomic DNA. Translation: ACP05441.1.
RefSeqYP_002809892.1. NC_012578.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3NAVX-ray2.10A/B1-268[»]
ProteinModelPortalC3LLL5.
SMRC3LLL5. Positions 1-267.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING579112.VCM66_1124.

Proteomic databases

PRIDEC3LLL5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACP05441; ACP05441; VCM66_1124.
GeneID7772402.
KEGGvcm:VCM66_1124.
PATRIC20066039. VBIVibCho108967_1074.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0159.
HOGENOMHOG000223814.
KOK01695.
OMAATTEHVT.
OrthoDBEOG6RVG0K.
ProtClustDBPRK13111.

Enzyme and pathway databases

BioCycVCHO579112:GJAW-1186-MONOMER.
UniPathwayUPA00035; UER00044.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00131. Trp_synth_alpha.
InterProIPR013785. Aldolase_TIM.
IPR011060. RibuloseP-bd_barrel.
IPR018204. Trp_synthase_alpha_AS.
IPR002028. Trp_synthase_suA.
[Graphical view]
PfamPF00290. Trp_syntA. 1 hit.
[Graphical view]
SUPFAMSSF51366. SSF51366. 1 hit.
TIGRFAMsTIGR00262. trpA. 1 hit.
PROSITEPS00167. TRP_SYNTHASE_ALPHA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceC3LLL5.

Entry information

Entry nameTRPA_VIBCM
AccessionPrimary (citable) accession number: C3LLL5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: June 16, 2009
Last modified: February 19, 2014
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways