TRPA_LEGPH
ID TRPA_LEGPH Reviewed; 272 AA.
AC Q5ZVY3;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=lpg1305;
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(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; AE017354; AAU27388.1; -; Genomic_DNA.
DR RefSeq; WP_010947036.1; NC_002942.5.
DR RefSeq; YP_095335.1; NC_002942.5.
DR PDB; 5K9X; X-ray; 2.02 A; A=1-272.
DR PDBsum; 5K9X; -.
DR AlphaFoldDB; Q5ZVY3; -.
DR SMR; Q5ZVY3; -.
DR STRING; 272624.lpg1305; -.
DR PaxDb; Q5ZVY3; -.
DR PRIDE; Q5ZVY3; -.
DR EnsemblBacteria; AAU27388; AAU27388; lpg1305.
DR GeneID; 66490440; -.
DR KEGG; lpn:lpg1305; -.
DR PATRIC; fig|272624.6.peg.1375; -.
DR eggNOG; COG0159; Bacteria.
DR HOGENOM; CLU_016734_0_0_6; -.
DR OMA; LVMTYWN; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000000609; 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..272
FT /note="Tryptophan synthase alpha chain"
FT /id="PRO_0000098797"
FT ACT_SITE 49
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT ACT_SITE 60
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT HELIX 3..13
FT /evidence="ECO:0007829|PDB:5K9X"
FT STRAND 18..24
FT /evidence="ECO:0007829|PDB:5K9X"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:5K9X"
FT HELIX 33..42
FT /evidence="ECO:0007829|PDB:5K9X"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:5K9X"
FT HELIX 62..72
FT /evidence="ECO:0007829|PDB:5K9X"
FT TURN 73..75
FT /evidence="ECO:0007829|PDB:5K9X"
FT HELIX 78..89
FT /evidence="ECO:0007829|PDB:5K9X"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:5K9X"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:5K9X"
FT HELIX 103..109
FT /evidence="ECO:0007829|PDB:5K9X"
FT HELIX 111..121
FT /evidence="ECO:0007829|PDB:5K9X"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:5K9X"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:5K9X"
FT HELIX 137..145
FT /evidence="ECO:0007829|PDB:5K9X"
FT HELIX 160..169
FT /evidence="ECO:0007829|PDB:5K9X"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:5K9X"
FT HELIX 190..201
FT /evidence="ECO:0007829|PDB:5K9X"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:5K9X"
FT HELIX 217..224
FT /evidence="ECO:0007829|PDB:5K9X"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:5K9X"
FT HELIX 235..245
FT /evidence="ECO:0007829|PDB:5K9X"
FT HELIX 250..266
FT /evidence="ECO:0007829|PDB:5K9X"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:5K9X"
SQ SEQUENCE 272 AA; 29937 MW; E35CE6977F5DF49E CRC64;
MNRIDKTLEK LKANRKKMLS PYITAGDPYP ELTVSLMHQL VKSGADVLEL GIPFSDPMAE
GPVIQRAMER ALAHSIHCDD VLNMVRQFRK TDTETPVILM GYLNPIEQYG YDLFAQQAVE
AGVDGTILVD LPPEEADGVS RVWQKHGLYS IYLCSPTTSA ERMNYINQHA NGYLYYVSLK
GVTGSDALKL PELKAQYLQR KAQSKLPLMV GFGIKTPEMA AQVAEFADGV IVGAALINEI
IEAYEAKKDP LQASGALLSS MRQAIDNIGS MV
