TRPA_CAMJE
ID TRPA_CAMJE Reviewed; 249 AA.
AC Q9PIF1; Q0PBG0;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=Cj0349;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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; AL111168; CAL34500.1; -; Genomic_DNA.
DR PIR; D81377; D81377.
DR RefSeq; WP_002854645.1; NC_002163.1.
DR RefSeq; YP_002343787.1; NC_002163.1.
DR PDB; 3THA; X-ray; 2.37 A; A/B=1-249.
DR PDBsum; 3THA; -.
DR AlphaFoldDB; Q9PIF1; -.
DR SMR; Q9PIF1; -.
DR IntAct; Q9PIF1; 2.
DR STRING; 192222.Cj0349; -.
DR PaxDb; Q9PIF1; -.
DR EnsemblBacteria; CAL34500; CAL34500; Cj0349.
DR GeneID; 904673; -.
DR KEGG; cje:Cj0349; -.
DR PATRIC; fig|192222.6.peg.341; -.
DR eggNOG; COG0159; Bacteria.
DR HOGENOM; CLU_016734_0_0_7; -.
DR OMA; LVMTYWN; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000000799; 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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Lyase; Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..249
FT /note="Tryptophan synthase alpha chain"
FT /id="PRO_0000098762"
FT ACT_SITE 43
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT ACT_SITE 54
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:3THA"
FT STRAND 9..18
FT /evidence="ECO:0007829|PDB:3THA"
FT HELIX 24..32
FT /evidence="ECO:0007829|PDB:3THA"
FT HELIX 33..36
FT /evidence="ECO:0007829|PDB:3THA"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:3THA"
FT HELIX 57..67
FT /evidence="ECO:0007829|PDB:3THA"
FT HELIX 72..81
FT /evidence="ECO:0007829|PDB:3THA"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:3THA"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:3THA"
FT HELIX 102..111
FT /evidence="ECO:0007829|PDB:3THA"
FT STRAND 114..118
FT /evidence="ECO:0007829|PDB:3THA"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:3THA"
FT HELIX 128..136
FT /evidence="ECO:0007829|PDB:3THA"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:3THA"
FT HELIX 151..158
FT /evidence="ECO:0007829|PDB:3THA"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:3THA"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:3THA"
FT HELIX 178..192
FT /evidence="ECO:0007829|PDB:3THA"
FT STRAND 199..204
FT /evidence="ECO:0007829|PDB:3THA"
FT HELIX 208..214
FT /evidence="ECO:0007829|PDB:3THA"
FT TURN 215..217
FT /evidence="ECO:0007829|PDB:3THA"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:3THA"
FT HELIX 225..230
FT /evidence="ECO:0007829|PDB:3THA"
FT HELIX 236..246
FT /evidence="ECO:0007829|PDB:3THA"
SQ SEQUENCE 249 AA; 27967 MW; 79FF358CD7CAC987 CRC64;
MVDFRKFYKE NANVAYTVLG YPNLQTSEAF LQRLDQSPID ILELGVAYSD PIADGEIIAD
AAKIALDQGV DIHSVFELLA RIKTKKALVF MVYYNLIFSY GLEKFVKKAK SLGICALIVP
ELSFEESDDL IKECERYNIA LITLVSVTTP KERVKKLVKH AKGFIYLLAS IGITGTKSVE
EAILQDKVKE IRSFTNLPIF VGFGIQNNQD VKRMRKVADG VIVGTSIVKC FKQGNLDIIM
KDIEEIFKK
