TRPA_FRATT
ID TRPA_FRATT Reviewed; 269 AA.
AC Q5NE80;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=FTT_1772c;
OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=177416;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCHU S4 / Schu 4;
RX PubMed=15640799; DOI=10.1038/ng1499;
RA Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT "The complete genome sequence of Francisella tularensis, the causative
RT agent of tularemia.";
RL Nat. Genet. 37:153-159(2005).
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; AJ749949; CAG46405.1; -; Genomic_DNA.
DR RefSeq; WP_003022758.1; NZ_CP010290.1.
DR RefSeq; YP_170662.1; NC_006570.2.
DR PDB; 5KZM; X-ray; 2.80 A; A=1-269.
DR PDBsum; 5KZM; -.
DR AlphaFoldDB; Q5NE80; -.
DR SMR; Q5NE80; -.
DR STRING; 177416.FTT_1772c; -.
DR DNASU; 3190980; -.
DR EnsemblBacteria; CAG46405; CAG46405; FTT_1772c.
DR GeneID; 39482346; -.
DR KEGG; ftu:FTT_1772c; -.
DR eggNOG; COG0159; Bacteria.
DR OMA; LVMTYWN; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000001174; 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..269
FT /note="Tryptophan synthase alpha chain"
FT /id="PRO_0000098782"
FT ACT_SITE 50
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT ACT_SITE 61
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT HELIX 4..14
FT /evidence="ECO:0007829|PDB:5KZM"
FT STRAND 19..25
FT /evidence="ECO:0007829|PDB:5KZM"
FT HELIX 31..43
FT /evidence="ECO:0007829|PDB:5KZM"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:5KZM"
FT HELIX 63..74
FT /evidence="ECO:0007829|PDB:5KZM"
FT HELIX 79..92
FT /evidence="ECO:0007829|PDB:5KZM"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:5KZM"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:5KZM"
FT HELIX 112..121
FT /evidence="ECO:0007829|PDB:5KZM"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:5KZM"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:5KZM"
FT HELIX 138..147
FT /evidence="ECO:0007829|PDB:5KZM"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:5KZM"
FT HELIX 161..170
FT /evidence="ECO:0007829|PDB:5KZM"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:5KZM"
FT HELIX 194..203
FT /evidence="ECO:0007829|PDB:5KZM"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:5KZM"
FT HELIX 218..225
FT /evidence="ECO:0007829|PDB:5KZM"
FT TURN 226..228
FT /evidence="ECO:0007829|PDB:5KZM"
FT STRAND 230..235
FT /evidence="ECO:0007829|PDB:5KZM"
FT HELIX 236..243
FT /evidence="ECO:0007829|PDB:5KZM"
FT TURN 244..247
FT /evidence="ECO:0007829|PDB:5KZM"
FT HELIX 249..265
FT /evidence="ECO:0007829|PDB:5KZM"
SQ SEQUENCE 269 AA; 29068 MW; BA29866C4CB3171F CRC64;
MTNRYTTLFA NLEKRNEGAF IPFVTIGDPN KALSFEIIDT LVSSGADALE LGIPFSDPLA
DGPTIQEANI RALESGITPK DCFDILTKIR AKYPHIPIGL LLYANLVYAN GIENFYQKCL
DAGVDSILIA DVPAHESKEF RDIAKKVGIA QIFIAPPDAS ESTLKQISEL GSGYTYLLSR
VGVTGTETAA NMPVEDVLTK LREYNAPKPV LGFGISKPEQ VQQAIKAGAA GAISGSATVK
IIQNNISNKQ KMLNELTYFV KEMKAATLN
