ID TRPA_PYRFU Reviewed; 248 AA. AC Q8U094; DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 27-MAR-2024, entry version 125. DE RecName: Full=Tryptophan synthase alpha chain {ECO:0000255|HAMAP-Rule:MF_00131}; DE EC=4.2.1.20 {ECO:0000255|HAMAP-Rule:MF_00131}; GN Name=trpA {ECO:0000255|HAMAP-Rule:MF_00131}; OrderedLocusNames=PF1705; OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=186497; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10. RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1; RX PubMed=12435500; DOI=10.1111/j.1574-6968.2002.tb11433.x; RA Ishida M., Oshima T., Yutani K.; RT "Overexpression in Escherichia coli of the AT-rich trpA and trpB genes from RT the hyperthermophilic archaeon Pyrococcus furiosus."; RL FEMS Microbiol. Lett. 216:179-183(2002). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1; RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299; RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., RA DiRuggiero J., Robb F.T.; RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. RT horikoshii inferred from complete genomic sequences."; RL Genetics 152:1299-1305(1999). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). RG RIKEN structural genomics initiative (RSGI); RT "Structures of mutant tryptophan synthase alpha-subunits from a RT hyperthermophile, Pyrococcus furiosus."; RL Submitted (OCT-2007) to the PDB data bank. CC -!- FUNCTION: The alpha subunit is responsible for the aldol cleavage of CC indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate. 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:0000255|HAMAP-Rule:MF_00131}; CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 5/5. {ECO:0000255|HAMAP- CC Rule:MF_00131}. CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000255|HAMAP- CC Rule:MF_00131}. CC -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000255|HAMAP- CC Rule:MF_00131}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB080770; BAC11856.1; -; Genomic_DNA. DR EMBL; AE009950; AAL81829.1; -; Genomic_DNA. DR RefSeq; WP_011012851.1; NZ_CP023154.1. DR PDB; 1GEQ; X-ray; 2.00 A; A/B=1-248. DR PDB; 1WDW; X-ray; 3.00 A; A/C/E/G/I/K=1-248. DR PDB; 2DZP; X-ray; 2.40 A; A/B=1-248. DR PDB; 2DZS; X-ray; 2.40 A; A/B=1-248. DR PDB; 2DZT; X-ray; 2.40 A; A/B=1-248. DR PDB; 2DZU; X-ray; 2.46 A; A/B=1-248. DR PDB; 2DZV; X-ray; 2.40 A; A/B=1-248. DR PDB; 2DZW; X-ray; 2.40 A; A/B=1-248. DR PDB; 2DZX; X-ray; 2.40 A; A/B=1-248. DR PDB; 2E09; X-ray; 2.40 A; A/B=1-248. DR PDB; 5E0K; X-ray; 2.76 A; A/C/E/G/I/K=1-248. DR PDBsum; 1GEQ; -. DR PDBsum; 1WDW; -. DR PDBsum; 2DZP; -. DR PDBsum; 2DZS; -. DR PDBsum; 2DZT; -. DR PDBsum; 2DZU; -. DR PDBsum; 2DZV; -. DR PDBsum; 2DZW; -. DR PDBsum; 2DZX; -. DR PDBsum; 2E09; -. DR PDBsum; 5E0K; -. DR AlphaFoldDB; Q8U094; -. DR SMR; Q8U094; -. DR STRING; 186497.PF1705; -. DR PaxDb; 186497-PF1705; -. DR GeneID; 41713536; -. DR KEGG; pfu:PF1705; -. DR PATRIC; fig|186497.12.peg.1773; -. DR eggNOG; arCOG01086; Archaea. DR HOGENOM; CLU_016734_0_2_2; -. DR OrthoDB; 25658at2157; -. DR PhylomeDB; Q8U094; -. DR BRENDA; 4.2.1.20; 5243. DR UniPathway; UPA00035; UER00044. DR EvolutionaryTrace; Q8U094; -. DR Proteomes; UP000001013; Chromosome. DR GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule. 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 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Direct protein sequencing; Lyase; Reference proteome; KW Tryptophan biosynthesis. FT CHAIN 1..248 FT /note="Tryptophan synthase alpha chain" FT /id="PRO_0000098897" FT ACT_SITE 36 FT /note="Proton acceptor" FT ACT_SITE 47 FT /note="Proton acceptor" FT STRAND 6..12 FT /evidence="ECO:0007829|PDB:1GEQ" FT HELIX 18..28 FT /evidence="ECO:0007829|PDB:1GEQ" FT HELIX 29..31 FT /evidence="ECO:0007829|PDB:1GEQ" FT STRAND 35..38 FT /evidence="ECO:0007829|PDB:1GEQ" FT HELIX 49..60 FT /evidence="ECO:0007829|PDB:1GEQ" FT HELIX 65..76 FT /evidence="ECO:0007829|PDB:1GEQ" FT STRAND 83..87 FT /evidence="ECO:0007829|PDB:1GEQ" FT HELIX 89..95 FT /evidence="ECO:0007829|PDB:1GEQ" FT HELIX 97..107 FT /evidence="ECO:0007829|PDB:1GEQ" FT STRAND 111..114 FT /evidence="ECO:0007829|PDB:1GEQ" FT HELIX 119..121 FT /evidence="ECO:0007829|PDB:1GEQ" FT HELIX 122..132 FT /evidence="ECO:0007829|PDB:1GEQ" FT STRAND 135..140 FT /evidence="ECO:0007829|PDB:1GEQ" FT HELIX 146..155 FT /evidence="ECO:0007829|PDB:1GEQ" FT STRAND 157..163 FT /evidence="ECO:0007829|PDB:1GEQ" FT HELIX 177..189 FT /evidence="ECO:0007829|PDB:1GEQ" FT STRAND 194..198 FT /evidence="ECO:0007829|PDB:1GEQ" FT HELIX 203..211 FT /evidence="ECO:0007829|PDB:1GEQ" FT STRAND 215..219 FT /evidence="ECO:0007829|PDB:1GEQ" FT HELIX 221..230 FT /evidence="ECO:0007829|PDB:1GEQ" FT HELIX 231..233 FT /evidence="ECO:0007829|PDB:1GEQ" FT HELIX 235..246 FT /evidence="ECO:0007829|PDB:1GEQ" SQ SEQUENCE 248 AA; 27497 MW; 45D6C877FB8393EE CRC64; MFKDGSLIPY LTAGDPDKQS TLNFLLALDE YAGAIELGIP FSDPIADGKT IQESHYRALK NGFKLREAFW IVKEFRRHSS TPIVLMTYYN PIYRAGVRNF LAEAKASGVD GILVVDLPVF HAKEFTEIAR EEGIKTVFLA APNTPDERLK VIDDMTTGFV YLVSLYGTTG AREEIPKTAY DLLRRAKRIC RNKVAVGFGV SKREHVVSLL KEGANGVVVG SALVKIIGEK GREATEFLKK KVEELLGI //