ID A0A0E0LDQ0_ORYPU Unreviewed; 518 AA.
AC A0A0E0LDQ0;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=tryptophan synthase {ECO:0000256|ARBA:ARBA00012043};
DE EC=4.2.1.20 {ECO:0000256|ARBA:ARBA00012043};
OS Oryza punctata (Red rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4537 {ECO:0000313|EnsemblPlants:OPUNC06G19640.1};
RN [1] {ECO:0000313|EnsemblPlants:OPUNC06G19640.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OPUNC06G19640.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC tryptophan from indole and L-serine. {ECO:0000256|ARBA:ARBA00002786}.
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 Evidence={ECO:0000256|ARBA:ARBA00000003};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 5/5. {ECO:0000256|ARBA:ARBA00004733}.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC {ECO:0000256|ARBA:ARBA00011270}.
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DR AlphaFoldDB; A0A0E0LDQ0; -.
DR STRING; 4537.A0A0E0LDQ0; -.
DR EnsemblPlants; OPUNC06G19640.1; OPUNC06G19640.1; OPUNC06G19640.
DR Gramene; OPUNC06G19640.1; OPUNC06G19640.1; OPUNC06G19640.
DR eggNOG; KOG1395; Eukaryota.
DR HOGENOM; CLU_042858_1_0_1; -.
DR OMA; MYTIGAD; -.
DR Proteomes; UP000026962; Chromosome 6.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004834; F:tryptophan synthase activity; IEA:InterPro.
DR CDD; cd06446; Trp-synth_B; 1.
DR Gene3D; 3.40.50.1100; -; 3.
DR InterPro; IPR006316; Trp_synth_b-like.
DR InterPro; IPR006654; Trp_synth_beta.
DR InterPro; IPR023026; Trp_synth_beta/beta-like.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR PANTHER; PTHR48077:SF6; TRYPTOPHAN SYNTHASE BETA CHAIN; 1.
DR PANTHER; PTHR48077; TRYPTOPHAN SYNTHASE-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR PIRSF; PIRSF001413; Trp_syn_beta; 2.
DR PIRSF; PIRSF500824; TrpB_prok; 2.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000026962};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822}.
FT DOMAIN 111..339
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 518 AA; 56191 MW; ADE77FE994009F6C CRC64;
MATSASVRPP LLQQAAGSEK ASLCKPKQSV SVSKRSFITR ASSNPVSIPK QWYNLVADLP
VKPPPPLHPQ THQPLNPSDL SPLFPDELIR QEVTEERFID IPEEVAEVYK LWRPTPLIRA
RRLEKLLGTP AKIYYKYEGT SPAGSHKPNT AVPQAWYNAV AGVKNVVTET GAGQWGSALS
FASSLFGLNC EVWQVRASYD QKPYRRLMME TWGARVHPSP STVTESGKKI LERDPASPGS
LGIAISEAVE VAATNADTKY CLGSVLNHVL LHQTVIGEEC LEQLAAVGDV PDVVIGCTGG
GSNFGGLVFP FMREKLAGRM SPAFKAVEPA ACPTLTKGVY AYDFGDTAGL TPLMKMHTLG
HGFVPDPIHA GLEFLISTMH TSSCPNLKFL VAIKPKPLFA IAGGLRYHGM APLISHVYEL
GFMEAIAIQQ TECFDAALKF ARTEGIIPAP EPTHAIAAAI REAMECKRTG EKKVILMAMC
GHGHFDLASY EKYLRGDMVD LSHSDEKLQE ALAAVPKI
//
