TRPA_MAIZE
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 03-AUG-2022, entry version 147.
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.GRMZM2G085381_P03; -.
DR PaxDb; P42390; -.
DR PRIDE; P42390; -.
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 OMA; NINAHGQ; -.
DR OrthoDB; 1143233at2759; -.
DR BioCyc; MetaCyc:MON-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 Genevisible; P42390; ZM.
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; -; 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 PANTHER; PTHR43406; PTHR43406; 1.
DR Pfam; PF00290; Trp_syntA; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR00262; trpA; 1.
DR PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1.
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
