ID   TRPB1_MAIZE             Reviewed;         389 AA.
AC   P43283;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 121.
DE   RecName: Full=Tryptophan synthase beta chain 1;
DE            EC=4.2.1.20;
DE   AltName: Full=Orange pericarp 1;
DE   Flags: Fragment;
GN   Name=TSB1; Synonyms=ORP1;
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 [MRNA].
RX   PubMed=1356534; DOI=10.2307/3869529;
RA   Wright A.D., Moehlenkamp C.A., Perrot G.H., Neuffer M.G., Cone K.C.;
RT   "The maize auxotrophic mutant orange pericarp is defective in duplicate
RT   genes for tryptophan synthase beta.";
RL   Plant Cell 4:711-719(1992).
CC   -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC       tryptophan from indole and L-serine.
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
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.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000305}.
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DR   EMBL; M76684; AAA33490.1; -; mRNA.
DR   PIR; PQ0449; PQ0449.
DR   AlphaFoldDB; P43283; -.
DR   SMR; P43283; -.
DR   MaizeGDB; 15412; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P43283; baseline and differential.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
DR   CDD; cd06446; Trp-synth_B; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   HAMAP; MF_00133; Trp_synth_beta; 1.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR006653; Trp_synth_b_CS.
DR   InterPro; IPR006654; Trp_synth_beta.
DR   InterPro; IPR023026; Trp_synth_beta/beta-like.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   PIRSF; PIRSF001413; Trp_syn_beta; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR00263; trpB; 1.
DR   PROSITE; PS00168; TRP_SYNTHASE_BETA; 1.
PE   2: Evidence at transcript level;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Chloroplast;
KW   Lyase; Plastid; Pyridoxal phosphate; Reference proteome;
KW   Tryptophan biosynthesis.
FT   CHAIN           <1..389
FT                   /note="Tryptophan synthase beta chain 1"
FT                   /id="PRO_0000099061"
FT   MOD_RES         84
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   389 AA;  42519 MW;  64DB87D3CAC918EB CRC64;
     GRFGGKYVPE TLMHALTELE NAFHALATDD EFQKELDGIL KDYVGRESPL YFAERLTEHY
     KRADGTGPLI YLKREDLNHR GAHKINNAVA QALLAKRLGK QRIIAETGAG QHGVATATVC
     ARFGLQCIIY MGAQDMERQA LNVFRMKLLG AEVRAVHSGT ATLKDATSEA IRDWVTNVET
     THYILGSVAG PHPYPMMVRE FHKVIGKETR RQAMHKWGGK PDVLVACVGG GSNAMGLFHE
     FVEDQDVRLI GVEAAGHGVD TDKHAATLTK GQVGVLHGSM SYLLQDDDGQ VIEPHSISAG
     LDYPGVGPEH SFLKDIGRAE YDSVTDQEAL DAFKRVSRLE GIIPALETSH ALAYLEKLCP
     TLPDGVRVVL NCSGRGDKDV HTASKYLDV