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Q81TL7 (TRPA_BACAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:BA_1254, GBAA_1254, BAS1162
OrganismBacillus anthracis [Reference proteome] [HAMAP]
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length258 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 + 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 258258Tryptophan synthase alpha chain HAMAP-Rule MF_00131
PRO_0000098732

Sites

Active site471Proton acceptor By similarity
Active site581Proton acceptor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q81TL7 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 78A7946B146004EF

FASTA25828,355
        10         20         30         40         50         60 
MGVERIKAAF ENGKKAFIPY VMGGDGGLEI LKERIRFLDE AGASIVEIGI PFSDPVADGP 

        70         80         90        100        110        120 
TIQRAGKRAL DSGVTVKGIF QALIEVRKEV QIPFVLMTYL NPVLAFGKER FIENCMEAGV 

       130        140        150        160        170        180 
DGIIVPDLPY EEQDIIAPLL REANIALIPL VTVTSPIERI KKITSESEGF VYAVTVAGVT 

       190        200        210        220        230        240 
GVRQNFKDEI HSYLEKVKSH THLPVVAGFG ISTKEHVEEM VTICDGVVVG SKVIELLENE 

       250 
KREEICEFIQ ATKQKEEA 

« Hide

References

[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"The complete genome sequence of Bacillus anthracis Ames 'Ancestor'."
Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D., Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.
J. Bacteriol. 191:445-446(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.
[3]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016879 Genomic DNA. Translation: AAP25212.1.
AE017334 Genomic DNA. Translation: AAT30344.1.
AE017225 Genomic DNA. Translation: AAT53484.1.
RefSeqNP_843726.1. NC_003997.3.
YP_017869.1. NC_007530.2.
YP_027433.1. NC_005945.1.

3D structure databases

ProteinModelPortalQ81TL7.
ModBaseSearch...

Protein-protein interaction databases

IntActQ81TL7. 1 interaction.
STRING198094.BA_1254.

Protocols and materials databases

DNASU1085329.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP25212; AAP25212; BA_1254.
AAT30344; AAT30344; GBAA_1254.
AAT53484; AAT53484; BAS1162.
GeneID1085329.
2814761.
2852220.
KEGGban:BA_1254.
bar:GBAA_1254.
bat:BAS1162.

Phylogenomic databases

eggNOGCOG0159.
HOGENOMHOG000223816.
KOK01695.
OMAVFICPPN.
ProtClustDBPRK13111.

Enzyme and pathway databases

BioCycBANT260799:GJAJ-1237-MONOMER.
BANT261594:GJ7F-1291-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. RibP_bind_barrel. 1 hit.
TIGRFAMsTIGR00262. trpA. 1 hit.
PROSITEPS00167. TRP_SYNTHASE_ALPHA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTRPA_BACAN
AccessionPrimary (citable) accession number: Q81TL7
Secondary accession number(s): Q6I1U7, Q6KVN9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: June 1, 2003
Last modified: May 1, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families