ID Q6JZ36_ECOLX Unreviewed; 242 AA.
AC Q6JZ36;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 24-JAN-2024, entry version 89.
DE RecName: Full=tryptophan synthase {ECO:0000256|ARBA:ARBA00012043};
DE EC=4.2.1.20 {ECO:0000256|ARBA:ARBA00012043};
DE Flags: Fragment;
GN Name=trpA {ECO:0000313|EMBL:AAP50156.1};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:AAP50156.1};
RN [1] {ECO:0000313|EMBL:AAP50156.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DEC4a {ECO:0000313|EMBL:AAP50156.1};
RX PubMed=15014151; DOI=10.1093/molbev/msh118;
RA Escobar-Paramo P., Clermont O., Blanc-Potard A.B., Bui H., Le Bouguenec C.,
RA Denamur E.;
RT "A specific genetic background is required for acquisition and expression
RT of virulence factors in Escherichia coli.";
RL Mol. Biol. Evol. 21:1085-1094(2004).
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:0000256|ARBA:ARBA00000003};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 5/5. {ECO:0000256|ARBA:ARBA00004733}.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC {ECO:0000256|ARBA:ARBA00011270}.
CC -!- SIMILARITY: Belongs to the TrpA family.
CC {ECO:0000256|RuleBase:RU003662}.
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DR EMBL; AY246159; AAP50156.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6JZ36; -.
DR UniPathway; UPA00035; UER00044.
DR GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-EC.
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 {ECO:0000256|ARBA:ARBA00022605};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAP50156.1"
FT NON_TER 242
FT /evidence="ECO:0000313|EMBL:AAP50156.1"
SQ SEQUENCE 242 AA; 25810 MW; CAD82AC5FB26F9A3 CRC64;
LKERKEGAFV PFVTLGDPGI EQSLKIIDTL IEAGADTLEL GIPFSDPLAD GPTIQNATLR
AFAAGVTPAQ CFEMLALIRQ KHPTIPIGLL MYANLVFNKG IDEFYAQCEK VGVDSVLVAD
VPVEESAPFR QAALRHNVAP IFICPPNADD DLLRQIASYG RGYTYLLSRA GVTGAENRAG
LPLNYLVAKL KEYNAAPPLQ GFGISAPDQV KAAIDAGAAG AISGSAIVKI IEQHINEPKK
ML
//
