ID TRPA_LISMF Reviewed; 257 AA.
AC Q71Z41;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 94.
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};
GN OrderedLocusNames=LMOf2365_1649;
OS Listeria monocytogenes serotype 4b (strain F2365).
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=265669;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F2365;
RX PubMed=15115801; DOI=10.1093/nar/gkh562;
RA Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T., Kolonay J.F.,
RA Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T., Peterson J.D.,
RA White O., Nelson W.C., Nierman W.C., Beanan M.J., Brinkac L.M.,
RA Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Haft D.H.,
RA Selengut J., Van Aken S.E., Khouri H.M., Fedorova N., Forberger H.A.,
RA Tran B., Kathariou S., Wonderling L.D., Uhlich G.A., Bayles D.O.,
RA Luchansky J.B., Fraser C.M.;
RT "Whole genome comparisons of serotype 4b and 1/2a strains of the food-borne
RT pathogen Listeria monocytogenes reveal new insights into the core genome
RT components of this species.";
RL Nucleic Acids Res. 32:2386-2395(2004).
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; AE017262; AAT04423.1; -; Genomic_DNA.
DR RefSeq; WP_003726797.1; NC_002973.6.
DR AlphaFoldDB; Q71Z41; -.
DR SMR; Q71Z41; -.
DR KEGG; lmf:LMOf2365_1649; -.
DR HOGENOM; CLU_016734_0_0_9; -.
DR UniPathway; UPA00035; UER00044.
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..257
FT /note="Tryptophan synthase alpha chain"
FT /id="PRO_0000098804"
FT ACT_SITE 47
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT ACT_SITE 58
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
SQ SEQUENCE 257 AA; 27902 MW; 0715A9569318B12A CRC64;
MTKTLTNKLA KKDHAAVVTY IMGGDGGLDN LEEQLLFLEK SGVSAIEIGI PFSDPVADGP
IIQLAGLRAL KEQVSLEAIL NKLARSKVQI PLIIMSYINP IFHLGIPKFV ELVQKTPVKG
LIIPDLPYEH QTLITPELQG TDIALIPLVS LTSPKERLEE IAKQAEGFIY AVTVNGTTGV
RSEFDAHIDN HLAYLKSISP VPVLAGFGVS SIEHVEKFAH VCDGVIIGSK VVQMLHEEKT
AELGAFLQKA AEVRIEN
//
