TRPA_THENN
ID TRPA_THENN Reviewed; 240 AA.
AC B9K6Z6;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 25-MAY-2022, entry version 64.
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=CTN_0553;
OS Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=309803;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E;
RA Lim S.K., Kim J.S., Cha S.H., Park B.C., Lee D.S., Tae H.S., Kim S.-J.,
RA Kim J.J., Park K.J., Lee S.Y.;
RT "The genome sequence of the hyperthermophilic bacterium Thermotoga
RT neapolitana.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000916; ACM22729.1; -; Genomic_DNA.
DR RefSeq; WP_015919048.1; NC_011978.1.
DR AlphaFoldDB; B9K6Z6; -.
DR SMR; B9K6Z6; -.
DR STRING; 309803.CTN_0553; -.
DR EnsemblBacteria; ACM22729; ACM22729; CTN_0553.
DR KEGG; tna:CTN_0553; -.
DR eggNOG; COG0159; Bacteria.
DR HOGENOM; CLU_016734_0_0_0; -.
DR OMA; LVMTYWN; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000000445; 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; -; 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 PANTHER; PTHR43406; PTHR43406; 1.
DR Pfam; PF00290; Trp_syntA; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
DR TIGRFAMs; TIGR00262; trpA; 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..240
FT /note="Tryptophan synthase alpha chain"
FT /id="PRO_1000198731"
FT ACT_SITE 34
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT ACT_SITE 45
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
SQ SEQUENCE 240 AA; 27102 MW; 9FECD9E3CB73F64C CRC64;
MKGFIAYIPA GFPDLETTRK VLLALNDLRI TGVEVGVPFS DPVADGPVIQ LAHSVALRNG
VTMKKILEML REISVDYELY LMSYLNPIVN YPEGKDRLLD ELRRLGVKGL IIPDLPLREV
KNIEISFPIV PFVAPNTRDE DLEAINTIRA PFVYYISRYG VTGEREDLPF AEHIKKVKKK
IALPLFVGFG ISRHEQVRKV WEIADGVIVG SALVRIMEES KRQEIPQKVV ARVKELIGEK
