ID A4RVE9_OSTLU Unreviewed; 302 AA.
AC A4RVE9;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 24-JAN-2024, entry version 87.
DE RecName: Full=tryptophan synthase {ECO:0000256|ARBA:ARBA00012043};
DE EC=4.2.1.20 {ECO:0000256|ARBA:ARBA00012043};
GN ORFNames=OSTLU_49484 {ECO:0000313|EMBL:ABO95416.1};
OS Ostreococcus lucimarinus (strain CCE9901).
OC Eukaryota; Viridiplantae; Chlorophyta; Mamiellophyceae; Mamiellales;
OC Bathycoccaceae; Ostreococcus.
OX NCBI_TaxID=436017 {ECO:0000313|EMBL:ABO95416.1, ECO:0000313|Proteomes:UP000001568};
RN [1] {ECO:0000313|EMBL:ABO95416.1, ECO:0000313|Proteomes:UP000001568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCE9901 {ECO:0000313|EMBL:ABO95416.1,
RC ECO:0000313|Proteomes:UP000001568};
RX PubMed=17460045; DOI=10.1073/pnas.0611046104;
RA Palenik B., Grimwood J., Aerts A., Rouze P., Salamov A., Putnam N.,
RA Dupont C., Jorgensen R., Derelle E., Rombauts S., Zhou K., Otillar R.,
RA Merchant S.S., Podell S., Gaasterland T., Napoli C., Gendler K.,
RA Manuell A., Tai V., Vallon O., Piganeau G., Jancek S., Heijde M.,
RA Jabbari K., Bowler C., Lohr M., Robbens S., Werner G., Dubchak I.,
RA Pazour G.J., Ren Q., Paulsen I., Delwiche C., Schmutz J., Rokhsar D.,
RA Van de Peer Y., Moreau H., Grigoriev I.V.;
RT "The tiny eukaryote Ostreococcus provides genomic insights into the paradox
RT of plankton speciation.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7705-7710(2007).
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 -!- 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}.
CC -!- SIMILARITY: Belongs to the TrpA family.
CC {ECO:0000256|RuleBase:RU003662}.
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DR EMBL; CP000584; ABO95416.1; -; Genomic_DNA.
DR RefSeq; XP_001417123.1; XM_001417086.1.
DR AlphaFoldDB; A4RVE9; -.
DR STRING; 436017.A4RVE9; -.
DR EnsemblPlants; ABO95416; ABO95416; OSTLU_49484.
DR GeneID; 5001442; -.
DR Gramene; ABO95416; ABO95416; OSTLU_49484.
DR KEGG; olu:OSTLU_49484; -.
DR eggNOG; KOG4175; Eukaryota.
DR HOGENOM; CLU_016734_0_2_1; -.
DR OMA; LVMTYWN; -.
DR OrthoDB; 447892at2759; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000001568; Chromosome 4.
DR GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-EC.
DR CDD; cd04724; Tryptophan_synthase_alpha; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 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 NCBIfam; TIGR00262; trpA; 1.
DR PANTHER; PTHR43406:SF1; TRYPTOPHAN SYNTHASE ALPHA CHAIN, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43406; TRYPTOPHAN SYNTHASE, ALPHA CHAIN; 1.
DR Pfam; PF00290; Trp_syntA; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000001568};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822}.
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 302 AA; 31753 MW; EDF5A816E0EEDEE7 CRC64;
MAASASRALR AAPRAPRASR ARRNPERGAA SRAVATRASV SEAFKAVLDD GKRAFIPFIC
AGDPDLESTK KALKILDDAG ADVIELGVPY SDPLADGPVI QAAATRALEN GATLNKVIDL
VREMTPQIKA PIVMFTYYNP IYQRGVDKFC ADIAAAGAKG LLVPDIPLEE TYDVSEIASK
HGIELVLLST PTTPVERAKK IAQATKGFVY LVSVTGVTGV QSNVATRVEQ LVEELRSVTD
KPIAVGFGVS EAKHAKQIVD WGADGVIVGS ALVRALGEAK TPEEGLAALK AKAEEIRGGA
TL
//
