P42390 (TRPA_MAIZE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Zea mays (Maize)

Taxonomic identifier

4577 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › PACMAD clade › Panicoideae › Andropogoneae › Zea

Protein attributes

Sequence length	347 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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. L-serine + 1-C-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + glyceraldehyde 3-phosphate + H2O.
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. Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
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	Plastid › chloroplast Probable.
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 process	Amino-acid biosynthesis Aromatic amino acid biosynthesis Tryptophan biosynthesis
Cellular component	Chloroplast Plastid
Domain	Transit peptide
Molecular function	Lyase
Technical term	3D-structure
Gene Ontology (GO)
Cellular component	chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	indole-3-glycerol-phosphate lyase activity Inferred from electronic annotation. Source: EC tryptophan synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 53

53

Chloroplast Potential

Chain

54 – 347

294

Indole-3-glycerol phosphate lyase, chloroplastic

PRO_0000035782

Regions

Compositional bias

47 – 51

5

Poly-Thr

Compositional bias

52 – 122

71

Ala-rich

Secondary structure

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347

Helix Strand Turn

Details...

Helix

90 – 99

10

Beta strand

104 – 110

7

Helix

116 – 128

13

Beta strand

132 – 137

6

Helix

148 – 158

11

Turn

159 – 161

3

Helix

164 – 174

11

Helix

175 – 177

3

Beta strand

182 – 185

4

Helix

189 – 192

4

Helix

197 – 201

5

Beta strand

206 – 208

3

Turn

214 – 216

3

Helix

217 – 226

10

Beta strand

233 – 235

3

Helix

241 – 250

10

Beta strand

255 – 258

4

Helix

273 – 284

12

Beta strand

289 – 293

5

Helix

298 – 306

9

Beta strand

310 – 314

5

Helix

316 – 323

8

Beta strand

324 – 327

4

Helix

328 – 346

19

Sequences

	Sequence		Length	Mass (Da)
	P42390 [UniParc]. Last modified August 30, 2005. Version 2. Checksum: 110D4215101F2012	FASTA	347	36,521
	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

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: 7766899] [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: 9235894] [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.

PIR

S56665.

RefSeq

NP_001105219.1. NM_001111749.1.

UniGene

Zm.283.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RD5	X-ray	2.02	A/B	87-346	[»]
1TJR	X-ray	2.30	A/B	87-346	[»]

ProteinModelPortal

P42390.

SMR

P42390. Positions 87-347.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblPlants

GRMZM2G085381_T01; GRMZM2G085381_P01; GRMZM2G085381.

GeneID

542117.

KEGG

zma:542117.

Organism-specific databases

Gramene

P42390.

MaizeGDB

102199.

Phylogenomic databases

GeneTree

EPGT00050000007771.

Enzyme and pathway databases

BioCyc

MetaCyc:MONOMER-10162.

Family and domain databases

InterPro

IPR013785. Aldolase_TIM.
IPR011060. RibuloseP-bd_barrel.
IPR018204. Trp_synthase_alpha_AS.
IPR002028. Trp_synthase_suA.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.

KO

K13222.

Pfam

PF00290. Trp_syntA. 1 hit.
[Graphical view]

SUPFAM

SSF51366. RibP_bind_barrel. 1 hit.

TIGRFAMs

TIGR00262. TrpA. 1 hit.

PROSITE

PS00167. TRP_SYNTHASE_ALPHA. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

TRPA_MAIZE

Accession

Primary (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:	November 16, 2011
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program