ID   TRPA_MAIZE              Reviewed;         347 AA.
AC   P42390; Q84K75;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 2.
DT   27-MAR-2024, entry version 156.
DE   RecName: Full=Indole-3-glycerol phosphate lyase, chloroplastic;
DE            EC=4.1.2.8 {ECO:0000305|PubMed:9235894};
DE   AltName: Full=Benzoxazineless 1;
DE   AltName: Full=Indole synthase;
DE   AltName: Full=Tryptophan synthase alpha chain;
DE            EC=4.2.1.20;
DE   Flags: Precursor;
GN   Name=BX1;
OS   Zea mays (Maize).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC   Panicoideae; Andropogonodae; Andropogoneae; Tripsacinae; Zea.
OX   NCBI_TaxID=4577;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. CG000237;
RX   PubMed=7766899; DOI=10.1007/bf00020891;
RA   Kramer V.C., Koziel M.G.;
RT   "Structure of a maize tryptophan synthase alpha subunit gene with pith
RT   enhanced expression.";
RL   Plant Mol. Biol. 27:1183-1188(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Jordaan A., Botha A.-M.;
RT   "Transformation of Nicotiana tabacum cv. Samsun with melanin and indigo
RT   genes.";
RL   Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=9235894; DOI=10.1126/science.277.5326.696;
RA   Frey M., Chomet P., Glawischnig E., Stettner C., Grun S., Winklmair A.,
RA   Eisenreich W., Bacher A., Meeley R.B., Briggs S.P., Simcox K., Gierl A.;
RT   "Analysis of a chemical plant defense mechanism in grasses.";
RL   Science 277:696-699(1997).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 86-347, AND SUBUNIT.
RA   Kulik V., Weyand M., Frey M., Dunn M., Schlichting I.;
RT   "Crystal structure of tryptophan synthase alpha chain.";
RL   Submitted (DEC-2004) to the PDB data bank.
CC   -!- FUNCTION: The alpha subunit is responsible for the aldol cleavage of
CC       indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. In
CC       bacteria, tryptophan synthase alpha (TSA) activity is almost completely
CC       dependent on formation of an active alpha2beta2 complex with tryptophan
CC       synthase beta (TSB), and indole is usually not released during
CC       tryptophan synthesis. In maize, the TSA homolog BX1 catalyzes the
CC       formation of free indole from indole-3-glycerol phosphate,
CC       independently of TSB. {ECO:0000269|PubMed:9235894}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate = D-
CC         glyceraldehyde 3-phosphate + indole; Xref=Rhea:RHEA:14081,
CC         ChEBI:CHEBI:16881, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.1.2.8;
CC         Evidence={ECO:0000305|PubMed:9235894};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14082;
CC         Evidence={ECO:0000305|PubMed:9235894};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-
CC         glyceraldehyde 3-phosphate + H2O + L-tryptophan;
CC         Xref=Rhea:RHEA:10532, ChEBI:CHEBI:15377, ChEBI:CHEBI:33384,
CC         ChEBI:CHEBI:57912, ChEBI:CHEBI:58866, ChEBI:CHEBI:59776; EC=4.2.1.20;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.013 mM for indole-3-glycerol phosphate
CC         {ECO:0000269|PubMed:9235894};
CC         Note=kcat is 0.02 sec(-1) with indole-3-glycerol phosphate as
CC         substrate. {ECO:0000269|PubMed:9235894};
CC   -!- PATHWAY: Secondary metabolite biosynthesis; 2,4-dihydroxy-1,4-
CC       benzoxazin-3-one biosynthesis; 2,4-dihydroxy-1,4-benzoxazin-3-one from
CC       indoleglycerol phosphate: step 1/5.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 5/5.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains for the tryptophan
CC       synthase activity. Homodimer of alpha chains for the indole-3-glycerol
CC       phosphate lyase activity. {ECO:0000269|Ref.4}.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- MISCELLANEOUS: Mutant rescue experiments indicate the existence of a
CC       second tryptophan synthase alpha gene whose product might be involved
CC       in tryptophan biosynthesis while BX1 might be restricted to free indol
CC       production.
CC   -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA54131.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X76713; CAA54131.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AY254103; AAP33667.1; -; mRNA.
DR   EMBL; AY254104; AAP33668.1; -; mRNA.
DR   PIR; S56665; S56665.
DR   RefSeq; NP_001105219.1; NM_001111749.1.
DR   PDB; 1RD5; X-ray; 2.02 A; A/B=87-347.
DR   PDB; 1TJR; X-ray; 2.30 A; A/B=87-347.
DR   PDBsum; 1RD5; -.
DR   PDBsum; 1TJR; -.
DR   AlphaFoldDB; P42390; -.
DR   SMR; P42390; -.
DR   STRING; 4577.P42390; -.
DR   PaxDb; 4577-GRMZM2G085381_P03; -.
DR   EnsemblPlants; Zm00001eb165610_T001; Zm00001eb165610_P001; Zm00001eb165610.
DR   GeneID; 542117; -.
DR   Gramene; Zm00001eb165610_T001; Zm00001eb165610_P001; Zm00001eb165610.
DR   KEGG; zma:542117; -.
DR   MaizeGDB; 102199; -.
DR   eggNOG; KOG4175; Eukaryota.
DR   HOGENOM; CLU_016734_0_2_1; -.
DR   InParanoid; P42390; -.
DR   OMA; NINAHGQ; -.
DR   OrthoDB; 447892at2759; -.
DR   BioCyc; MetaCyc:MONOMER-10162; -.
DR   BRENDA; 4.1.2.8; 6752.
DR   SABIO-RK; P42390; -.
DR   UniPathway; UPA00035; UER00044.
DR   UniPathway; UPA00872; UER00847.
DR   EvolutionaryTrace; P42390; -.
DR   Proteomes; UP000007305; Chromosome 4.
DR   ExpressionAtlas; P42390; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0033984; F:indole-3-glycerol-phosphate lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004834; F:tryptophan synthase activity; IBA:GO_Central.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
DR   CDD; cd04724; Tryptophan_synthase_alpha; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_00131; Trp_synth_alpha; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   InterPro; IPR018204; Trp_synthase_alpha_AS.
DR   InterPro; IPR002028; Trp_synthase_suA.
DR   NCBIfam; TIGR00262; trpA; 1.
DR   PANTHER; PTHR43406:SF3; INDOLE-3-GLYCEROL PHOSPHATE LYASE, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43406; TRYPTOPHAN SYNTHASE, ALPHA CHAIN; 1.
DR   Pfam; PF00290; Trp_syntA; 1.
DR   SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR   PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1.
DR   Genevisible; P42390; ZM.
PE   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Chloroplast; Lyase; Plastid; Reference proteome; Transit peptide;
KW   Tryptophan biosynthesis.
FT   TRANSIT         1..53
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           54..347
FT                   /note="Indole-3-glycerol phosphate lyase, chloroplastic"
FT                   /id="PRO_0000035782"
FT   REGION          1..38
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          64..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..78
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           90..99
FT                   /evidence="ECO:0007829|PDB:1RD5"
FT   STRAND          104..110
FT                   /evidence="ECO:0007829|PDB:1RD5"
FT   HELIX           116..128
FT                   /evidence="ECO:0007829|PDB:1RD5"
FT   STRAND          132..137
FT                   /evidence="ECO:0007829|PDB:1RD5"
FT   HELIX           148..158
FT                   /evidence="ECO:0007829|PDB:1RD5"
FT   TURN            159..161
FT                   /evidence="ECO:0007829|PDB:1RD5"
FT   HELIX           164..174
FT                   /evidence="ECO:0007829|PDB:1RD5"
FT   HELIX           175..177
FT                   /evidence="ECO:0007829|PDB:1RD5"
FT   STRAND          182..185
FT                   /evidence="ECO:0007829|PDB:1RD5"
FT   HELIX           189..192
FT                   /evidence="ECO:0007829|PDB:1RD5"
FT   HELIX           197..201
FT                   /evidence="ECO:0007829|PDB:1RD5"
FT   STRAND          206..208
FT                   /evidence="ECO:0007829|PDB:1RD5"
FT   TURN            214..216
FT                   /evidence="ECO:0007829|PDB:1RD5"
FT   HELIX           217..226
FT                   /evidence="ECO:0007829|PDB:1RD5"
FT   STRAND          233..235
FT                   /evidence="ECO:0007829|PDB:1RD5"
FT   HELIX           241..250
FT                   /evidence="ECO:0007829|PDB:1RD5"
FT   STRAND          255..258
FT                   /evidence="ECO:0007829|PDB:1RD5"
FT   HELIX           273..284
FT                   /evidence="ECO:0007829|PDB:1RD5"
FT   STRAND          289..293
FT                   /evidence="ECO:0007829|PDB:1RD5"
FT   HELIX           298..306
FT                   /evidence="ECO:0007829|PDB:1RD5"
FT   STRAND          310..314
FT                   /evidence="ECO:0007829|PDB:1RD5"
FT   HELIX           316..323
FT                   /evidence="ECO:0007829|PDB:1RD5"
FT   STRAND          324..327
FT                   /evidence="ECO:0007829|PDB:1RD5"
FT   HELIX           328..346
FT                   /evidence="ECO:0007829|PDB:1RD5"
SQ   SEQUENCE   347 AA;  36521 MW;  110D4215101F2012 CRC64;
     MAFAPKTSSS SSLSSALQAA QSPPLLLRRM SSTATPRRRY DAAVVVTTTT TARAAAAAVT
     VPAAPPQAPA PAPVPPKQAA APAERRSRPV SDTMAALMAK GKTAFIPYIT AGDPDLATTA
     EALRLLDGCG ADVIELGVPC SDPYIDGPII QASVARALAS GTTMDAVLEM LREVTPELSC
     PVVLLSYYKP IMSRSLAEMK EAGVHGLIVP DLPYVAAHSL WSEAKNNNLE LVLLTTPAIP
     EDRMKEITKA SEGFVYLVSV NGVTGPRANV NPRVESLIQE VKKVTNKPVA VGFGISKPEH
     VKQIAQWGAD GVIIGSAMVR QLGEAASPKQ GLRRLEEYAR GMKNALP
//