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Database: UniProt
Entry: Q0WS13_ARATH
LinkDB: Q0WS13_ARATH
Original site: Q0WS13_ARATH 
ID   Q0WS13_ARATH            Unreviewed;       475 AA.
AC   Q0WS13;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=Tryptophan synthase {ECO:0000256|ARBA:ARBA00012043, ECO:0000256|RuleBase:RU003663};
DE            EC=4.2.1.20 {ECO:0000256|ARBA:ARBA00012043, ECO:0000256|RuleBase:RU003663};
GN   OrderedLocusNames=At4g27070 {ECO:0000313|EMBL:BAF00086.1};
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702 {ECO:0000313|EMBL:BAF00086.1};
RN   [1] {ECO:0000313|EMBL:BAF00086.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Morosawa T.,
RA   Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K.,
RA   Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K.,
RA   Akiyama K., Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
RA   Hayashizaki Y., Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
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         ECO:0000256|RuleBase:RU003663};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU003663};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 5/5. {ECO:0000256|ARBA:ARBA00004733,
CC       ECO:0000256|RuleBase:RU003663}.
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DR   EMBL; AK228129; BAF00086.1; -; mRNA.
DR   RefSeq; NP_194437.1; NM_118841.5.
DR   AlphaFoldDB; Q0WS13; -.
DR   SMR; Q0WS13; -.
DR   EnsemblPlants; AT4G27070.1; AT4G27070.1; AT4G27070.
DR   GeneID; 828815; -.
DR   Gramene; AT4G27070.1; AT4G27070.1; AT4G27070.
DR   KEGG; ath:AT4G27070; -.
DR   TAIR; AT4G27070; -.
DR   HOGENOM; CLU_016734_3_1_1; -.
DR   OMA; GPEHAMF; -.
DR   OrthoDB; 9569at2759; -.
DR   PhylomeDB; Q0WS13; -.
DR   UniPathway; UPA00035; UER00044.
DR   ExpressionAtlas; Q0WS13; baseline and differential.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-EC.
DR   CDD; cd06446; Trp-synth_B; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   HAMAP; MF_00133; Trp_synth_beta; 1.
DR   InterPro; IPR006653; Trp_synth_b_CS.
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   NCBIfam; TIGR00263; trpB; 1.
DR   PANTHER; PTHR48077:SF12; TRYPTOPHAN SYNTHASE BETA CHAIN 1, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR48077; TRYPTOPHAN SYNTHASE-RELATED; 1.
DR   Pfam; PF00291; PALP; 1.
DR   PIRSF; PIRSF001413; Trp_syn_beta; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
DR   PROSITE; PS00168; TRP_SYNTHASE_BETA; 1.
PE   2: Evidence at transcript level;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|RuleBase:RU003663};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW   ECO:0000256|RuleBase:RU003663};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU003663};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003663};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW   ECO:0000256|RuleBase:RU003663}.
FT   DOMAIN          132..460
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..25
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   475 AA;  51601 MW;  1222EDA3B4CDBEEB CRC64;
     MATASTAATF RPSSVSASSE LTHLRSPSKL PKFTPLPSAR SRSSSSFSVS CTIAKDPAVV
     MADSEKIKAA GSDPTMWQRP DSFGRFGKFG GKYVPETLMH ALSELETAFY SLATDEDFQR
     ELAEILKDYV GRESPLYFAE RLTEHYRREN GEGPLIYLKR EDLNHTGAHK INNAVAQALL
     AKRLGKKRII AETGAGQHGV ATATVCARFG LQCIIYMGAQ DMERQALNVF RMRLLGAEVR
     GVHSGTATLK DATSEAIRDW VTNVETTHYI LGSVAGPHPY PMMVRDFHAV IGKETRKQAM
     EKWGGKPDVL VACVGGGSNA MGLFHEFVDD TEVRMIGVEA AGFGLDSGKH AATLTKGDVG
     VLHGAMSYLL QDDDGQIIEP HSISAGLDYP GVGPEHSFLK DVGRAEYFSV TDEEALEAFK
     RVSRLEGIIP ALETSHALAH LEKLCPTLPD GARVVLNFSG RGDKDVQTAI KYLEV
//
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