TRPA_THET2
ID TRPA_THET2 Reviewed; 271 AA.
AC P16608;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2004, sequence version 2.
DT 25-MAY-2022, entry version 144.
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=TT_C0729;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2188962; DOI=10.1128/jb.172.6.3490-3495.1990;
RA Koyama Y., Furukawa K.;
RT "Cloning and sequence analysis of tryptophan synthetase genes of an extreme
RT thermophile, Thermus thermophilus HB27: plasmid transfer from replica-
RT plated Escherichia coli recombinant colonies to competent T. thermophilus
RT cells.";
RL J. Bacteriol. 172:3490-3495(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(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; M32108; AAA27509.1; -; Genomic_DNA.
DR EMBL; AE017221; AAS81077.1; -; Genomic_DNA.
DR PIR; B35407; B35407.
DR RefSeq; WP_011173168.1; NC_005835.1.
DR PDB; 1UJP; X-ray; 1.34 A; A=1-270.
DR PDB; 1WXJ; X-ray; 1.70 A; A=1-270.
DR PDBsum; 1UJP; -.
DR PDBsum; 1WXJ; -.
DR AlphaFoldDB; P16608; -.
DR SMR; P16608; -.
DR STRING; 262724.TT_C0729; -.
DR DrugBank; DB03171; Indole-3-Propanol Phosphate.
DR EnsemblBacteria; AAS81077; AAS81077; TT_C0729.
DR KEGG; tth:TT_C0729; -.
DR eggNOG; COG0159; Bacteria.
DR HOGENOM; CLU_016734_0_0_0; -.
DR OMA; LVMTYWN; -.
DR OrthoDB; 912786at2; -.
DR UniPathway; UPA00035; UER00044.
DR EvolutionaryTrace; P16608; -.
DR Proteomes; UP000000592; 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; Tryptophan biosynthesis.
FT CHAIN 1..271
FT /note="Tryptophan synthase alpha chain"
FT /id="PRO_0000098865"
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"
FT CONFLICT 171
FT /note="V -> S (in Ref. 1; AAA27509)"
FT /evidence="ECO:0000305"
FT HELIX 3..12
FT /evidence="ECO:0007829|PDB:1UJP"
FT STRAND 17..23
FT /evidence="ECO:0007829|PDB:1UJP"
FT HELIX 29..39
FT /evidence="ECO:0007829|PDB:1UJP"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:1UJP"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:1UJP"
FT HELIX 60..71
FT /evidence="ECO:0007829|PDB:1UJP"
FT HELIX 76..89
FT /evidence="ECO:0007829|PDB:1UJP"
FT STRAND 94..97
FT /evidence="ECO:0007829|PDB:1UJP"
FT HELIX 100..106
FT /evidence="ECO:0007829|PDB:1UJP"
FT HELIX 108..118
FT /evidence="ECO:0007829|PDB:1UJP"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:1UJP"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:1UJP"
FT HELIX 134..143
FT /evidence="ECO:0007829|PDB:1UJP"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:1UJP"
FT HELIX 157..164
FT /evidence="ECO:0007829|PDB:1UJP"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:1UJP"
FT HELIX 191..198
FT /evidence="ECO:0007829|PDB:1UJP"
FT STRAND 205..209
FT /evidence="ECO:0007829|PDB:1UJP"
FT HELIX 214..220
FT /evidence="ECO:0007829|PDB:1UJP"
FT STRAND 223..228
FT /evidence="ECO:0007829|PDB:1UJP"
FT HELIX 230..237
FT /evidence="ECO:0007829|PDB:1UJP"
FT HELIX 242..253
FT /evidence="ECO:0007829|PDB:1UJP"
SQ SEQUENCE 271 AA; 28937 MW; 88A7B82187223AA5 CRC64;
MTTLEAFAKA RSEGRAALIP YLTAGFPSRE GFLQAVEEVL PYADLLEIGL PYSDPLGDGP
VIQRASELAL RKGMSVQGAL ELVREVRALT EKPLFLMTYL NPVLAWGPER FFGLFKQAGA
TGVILPDLPP DEDPGLVRLA QEIGLETVFL LAPTSTDARI ATVVRHATGF VYAVSVTGVT
GMRERLPEEV KDLVRRIKAR TALPVAVGFG VSGKATAAQA AVADGVVVGS ALVRALEEGR
SLAPLLQEIR QGLQRLEANP GLKESSKKPL S
