TRPA_PSEAE
ID TRPA_PSEAE Reviewed; 268 AA.
AC P07344;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 3.
DT 03-AUG-2022, entry version 150.
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=PA0035;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=3127651; DOI=10.1093/oxfordjournals.molbev.a040388;
RA Hadero A., Crawford I.P.;
RT "Nucleotide sequence of the genes for tryptophan synthase in Pseudomonas
RT aeruginosa.";
RL Mol. Biol. Evol. 3:191-204(1986).
RN [2]
RP SEQUENCE REVISION.
RA Crawford I.P., Eberly L.;
RL Submitted (MAR-1989) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(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; M15826; AAA88463.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG03425.1; -; Genomic_DNA.
DR PIR; B25355; TSPSAA.
DR PIR; G83640; G83640.
DR RefSeq; NP_248725.1; NC_002516.2.
DR RefSeq; WP_003115801.1; NZ_QZGE01000012.1.
DR AlphaFoldDB; P07344; -.
DR SMR; P07344; -.
DR STRING; 287.DR97_2989; -.
DR PaxDb; P07344; -.
DR PRIDE; P07344; -.
DR DNASU; 879479; -.
DR EnsemblBacteria; AAG03425; AAG03425; PA0035.
DR GeneID; 879479; -.
DR KEGG; pae:PA0035; -.
DR PATRIC; fig|208964.12.peg.35; -.
DR PseudoCAP; PA0035; -.
DR HOGENOM; CLU_016734_0_4_6; -.
DR InParanoid; P07344; -.
DR OMA; LVMTYWN; -.
DR PhylomeDB; P07344; -.
DR BioCyc; PAER208964:G1FZ6-36-MON; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004834; F:tryptophan synthase activity; IBA:GO_Central.
DR GO; GO:0000162; P:tryptophan biosynthetic process; IDA:PseudoCAP.
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 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..268
FT /note="Tryptophan synthase alpha chain"
FT /id="PRO_0000098825"
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 CONFLICT 42
FT /note="A -> G (in Ref. 1; AAA88463)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="D -> E (in Ref. 1; AAA88463)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="I -> L (in Ref. 1; AAA88463)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 268 AA; 28488 MW; 6EB7052524A9BEAD CRC64;
MSRLQTRFAQ LKQENRAALV TFVTAGDPDY ASSLEILKGL PAAGADVIEL GMPFTDPMAD
GPAIQLANIR ALDGGQTLAR TLQMVREFRS GDSETPLVLM GYFNPIHHYG VERFIAEAKE
VGVDGLIVVD LPPEHNEDLC HPAQAAGIDF IRLTTPTTGD QRLPTVLEGS SGFVYYVSVA
GVTGANAATL EHVEEAVARL RRHTDLPIGI GFGIRSAEHA AAVARLADGV VVGSALIDRI
AKARDNAQAV KDVLALCGEL AEGVRNAR
