ID TRPA_RUTMC Reviewed; 265 AA.
AC A1AXS3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 85.
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=Rmag_1025;
OS Ruthia magnifica subsp. Calyptogena magnifica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC Candidatus Ruthturnera.
OX NCBI_TaxID=413404;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17303757; DOI=10.1126/science.1138438;
RA Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J.,
RA Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M.,
RA Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.;
RT "The Calyptogena magnifica chemoautotrophic symbiont genome.";
RL Science 315:998-1000(2007).
CC -!- FUNCTION: The alpha subunit is responsible for the aldol cleavage of
CC indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
CC {ECO:0000255|HAMAP-Rule:MF_00131}.
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}.
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DR EMBL; CP000488; ABL02730.1; -; Genomic_DNA.
DR RefSeq; WP_011738355.1; NC_008610.1.
DR AlphaFoldDB; A1AXS3; -.
DR SMR; A1AXS3; -.
DR STRING; 413404.Rmag_1025; -.
DR KEGG; rma:Rmag_1025; -.
DR eggNOG; COG0159; Bacteria.
DR HOGENOM; CLU_016734_0_0_6; -.
DR OrthoDB; 9804578at2; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000002587; 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 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW Tryptophan biosynthesis.
FT CHAIN 1..265
FT /note="Tryptophan synthase alpha chain"
FT /id="PRO_1000018275"
FT ACT_SITE 48
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT ACT_SITE 59
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
SQ SEQUENCE 265 AA; 28552 MW; 380C7E602A2184F4 CRC64;
MSRLSTIFTQ LPVGKKVFIP FITAGDSGLD NTFELMQVLV KNGADVIELG VPFSDPIADG
PIIAKSHERA VADGVGLCDV LSLVKKFRQS NDTTAIVLMG YLNPIEAFGY QAFANAASES
AVDGVLVVDM PPEEAHDLKR SLDDVNIDLI FLVALTTTDE RLAFLATIAS GFIYFISLKG
VTGAEHLDVD LVKMYLLRVR KMINLPIGVG FGIKNAKSAK AVSKYADAVI VGSLLVAFVE
QYANDRNKML ANVGYFADEI STAIK
//
