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P42390 (TRPA_MAIZE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. 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:
Indole-3-glycerol phosphate lyase, chloroplastic

EC=4.1.2.8
Alternative name(s):
Benzoxazineless 1
Indole synthase
Tryptophan synthase alpha chain
EC=4.2.1.20
Gene names
Name:BX1
OrganismZea mays (Maize)
Taxonomic identifier4577 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaePACMAD cladePanicoideaeAndropogoneaeZea

Protein attributes

Sequence length347 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. In bacteria, tryptophan synthase alpha (TSA) activity is almost completely dependent on formation of an active alpha2beta2 complex with tryptophan synthase beta (TSB), and indole is usually not released during tryptophan synthesis. In maize, the TSA homolog BX1 catalyzes the formation of free indole from indole-3-glycerol phosphate, independently of TSB. Ref.3

Catalytic activity

(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate = indole + D-glyceraldehyde 3-phosphate. HAMAP-Rule MF_00131

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

Pathway

Secondary metabolite biosynthesis; 2,4-dihydroxy-1,4-benzoxazin-3-one biosynthesis; 2,4-dihydroxy-1,4-benzoxazin-3-one from indoleglycerol phosphate: step 1/5. HAMAP-Rule MF_00131

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 for the tryptophan synthase activity. Homodimer of alpha chains for the indole-3-glycerol phosphate lyase activity. Ref.4

Subcellular location

Plastidchloroplast Probable HAMAP-Rule MF_00131.

Miscellaneous

Mutant rescue experiments indicate the existence of a second tryptophan synthase alpha gene whose product might be involved in tryptophan biosynthesis while BX1 might be restricted to free indol production.

Sequence similarities

Belongs to the TrpA family.

Biophysicochemical properties

Kinetic parameters:

KM=0.013 mM for indole-3-glycerol phosphate Ref.3

Sequence caution

The sequence CAA54131.1 differs from that shown. Reason: Frameshift at positions 69 and 84.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Aromatic amino acid biosynthesis
Tryptophan biosynthesis
   Cellular componentChloroplast
Plastid
   DomainTransit peptide
   Molecular functionLyase
   Technical term3D-structure
Gene Ontology (GO)
   Cellular_componentchloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionindole-3-glycerol-phosphate lyase activity

Inferred from electronic annotation. Source: UniProtKB-EC

tryptophan synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5353Chloroplast Potential
Chain54 – 347294Indole-3-glycerol phosphate lyase, chloroplastic HAMAP-Rule MF_00131
PRO_0000035782

Regions

Compositional bias47 – 515Poly-Thr HAMAP-Rule MF_00131
Compositional bias52 – 12271Ala-rich HAMAP-Rule MF_00131

Secondary structure

............................................ 347
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P42390 [UniParc].

Last modified August 30, 2005. Version 2.
Checksum: 110D4215101F2012

FASTA34736,521
        10         20         30         40         50         60 
MAFAPKTSSS SSLSSALQAA QSPPLLLRRM SSTATPRRRY DAAVVVTTTT TARAAAAAVT 

        70         80         90        100        110        120 
VPAAPPQAPA PAPVPPKQAA APAERRSRPV SDTMAALMAK GKTAFIPYIT AGDPDLATTA 

       130        140        150        160        170        180 
EALRLLDGCG ADVIELGVPC SDPYIDGPII QASVARALAS GTTMDAVLEM LREVTPELSC 

       190        200        210        220        230        240 
PVVLLSYYKP IMSRSLAEMK EAGVHGLIVP DLPYVAAHSL WSEAKNNNLE LVLLTTPAIP 

       250        260        270        280        290        300 
EDRMKEITKA SEGFVYLVSV NGVTGPRANV NPRVESLIQE VKKVTNKPVA VGFGISKPEH 

       310        320        330        340 
VKQIAQWGAD GVIIGSAMVR QLGEAASPKQ GLRRLEEYAR GMKNALP 

« Hide

References

[1]"Structure of a maize tryptophan synthase alpha subunit gene with pith enhanced expression."
Kramer V.C., Koziel M.G.
Plant Mol. Biol. 27:1183-1188(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: cv. CG000237.
[2]"Transformation of Nicotiana tabacum cv. Samsun with melanin and indigo genes."
Jordaan A., Botha A.-M.
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Analysis of a chemical plant defense mechanism in grasses."
Frey M., Chomet P., Glawischnig E., Stettner C., Grun S., Winklmair A., Eisenreich W., Bacher A., Meeley R.B., Briggs S.P., Simcox K., Gierl A.
Science 277:696-699(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[4]"Crystal structure of tryptophan synthase alpha chain."
Kulik V., Weyand M., Frey M., Dunn M., Schlichting I.
Submitted (DEC-2004) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 86-347, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X76713 Genomic DNA. Translation: CAA54131.1. Frameshift.
AY254103 mRNA. Translation: AAP33667.1.
AY254104 mRNA. Translation: AAP33668.1.
PIRS56665.
RefSeqNP_001105219.1. NM_001111749.1.
UniGeneZm.283.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RD5X-ray2.02A/B87-347[»]
1TJRX-ray2.30A/B87-347[»]
ProteinModelPortalP42390.
SMRP42390. Positions 87-347.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID542117.
KEGGzma:542117.

Organism-specific databases

GrameneP42390.
MaizeGDB102199.

Phylogenomic databases

HOGENOMHOG000223816.
KOK13222.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-10162.
UniPathwayUPA00035; UER00044.
UPA00872; UER00847.

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

EvolutionaryTraceP42390.

Entry information

Entry nameTRPA_MAIZE
AccessionPrimary (citable) accession number: P42390
Secondary accession number(s): Q84K75
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: August 30, 2005
Last modified: July 9, 2014
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant 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