TRPA_THEMA
ID TRPA_THEMA Reviewed; 239 AA.
AC P50908;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 139.
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=TM_0137;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7556082; DOI=10.1002/j.1460-2075.1995.tb00118.x;
RA Sterner R., Dahm A., Darimont B., Ivens A., Liebl W., Kirschner K.;
RT "(Beta alpha)8-barrel proteins of tryptophan biosynthesis in the
RT hyperthermophile Thermotoga maritima.";
RL EMBO J. 14:4395-4402(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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; X92729; CAA63392.1; -; Genomic_DNA.
DR EMBL; AE000512; AAD35230.1; -; Genomic_DNA.
DR PIR; S59050; S59050.
DR RefSeq; NP_227952.1; NC_000853.1.
DR RefSeq; WP_004082732.1; NZ_CP011107.1.
DR AlphaFoldDB; P50908; -.
DR SMR; P50908; -.
DR STRING; 243274.THEMA_04120; -.
DR DNASU; 896967; -.
DR EnsemblBacteria; AAD35230; AAD35230; TM_0137.
DR KEGG; tma:TM0137; -.
DR eggNOG; COG0159; Bacteria.
DR InParanoid; P50908; -.
DR OMA; LVMTYWN; -.
DR OrthoDB; 912786at2; -.
DR BioCyc; MetaCyc:MON-344; -.
DR SABIO-RK; P50908; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004834; F:tryptophan synthase activity; IBA:GO_Central.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
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 Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..239
FT /note="Tryptophan synthase alpha chain"
FT /id="PRO_0000098864"
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"
FT CONFLICT 189
FT /note="F -> L (in Ref. 1; CAA63392)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 239 AA; 26759 MW; F6B06FBCA83294FA CRC64;
MKGFIAYIPA GFPDLETTRK ILIALNELGI TGVEIGVPFS DPVADGPVIQ LAHSVALRNG
VTIKKILEML SEISVDYDLY LMSYLNPIVN YPEGKEKLLD ELKKLGVKGL IIPDLPLREV
KNVDIAYPIV PFVAPNTKDE EIDLINSVQA PFVYYISRYG VTGEREDLPF ADHIKRVKER
IKLPLFVGFG ISRHEQVKKV WEIADGVIVG SALVRIMEEN PKDEIPRKVV EKVKELLGK
