ID   TRPB2_MAIZE             Reviewed;         443 AA.
AC   P43284;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Tryptophan synthase beta chain 2, chloroplastic;
DE            EC=4.2.1.20;
DE   AltName: Full=Orange pericarp 2;
DE   Flags: Precursor; Fragment;
GN   Name=TSB2; Synonyms=ORP2;
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; M76685; AAA33491.1; -; mRNA.
DR   PIR; PQ0450; PQ0450.
DR   AlphaFoldDB; P43284; -.
DR   SMR; P43284; -.
DR   STRING; 4577.GRMZM2G005024_P01; -.
DR   PaxDb; P43284; -.
DR   PRIDE; P43284; -.
DR   MaizeGDB; 15412; -.
DR   eggNOG; KOG1395; Eukaryota.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000007305; Unplaced.
DR   ExpressionAtlas; P43284; 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; Transit peptide;
KW   Tryptophan biosynthesis.
FT   TRANSIT         <1..45
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           46..443
FT                   /note="Tryptophan synthase beta chain 2, chloroplastic"
FT                   /id="PRO_0000035786"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         138
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   443 AA;  47844 MW;  FC11A64D0761C9EC CRC64;
     PGPPPPAPEG RRRRGRGRNA AGQAVAAEAS PAAVEMGNGA AAPGLQRPDA MGRFGRFGGK
     YVPETLMHAL TELESAFHAL ATDDEFQKEL DGILKDYVGR ESPLYFAERL TEHYKRADGT
     GPLIYLKRED LNHTGAHKIN NAVAQALLAK RLGKQRIIAE TGAGQHGVAT ATVCRRFGLQ
     CIIYMGAQDM ERQALNVFRM RLLGAEVRAV HSGTATLKDA TSEAIRDWVT NVETTHYILG
     SVAGPHPYPM MVREFHKVIG KETRRQAMDK WGGKPDVLVA CVGGGSNAMG LFHEFVEDQD
     VRLVGLEAAG HGVDTDKHAA TLTKGQVGVL HGSMSYLLQD DDGQVIEPHS ISAGLDYPGV
     GPEHSFLKDI GRAEYDSVTD QEALDAFKRV SRLEGIIPAL ETSHALAYLE KLCPTLADGV
     RVVVNCSGRG DKDVHTASKY LDV