TRPA_DESPS
ID TRPA_DESPS Reviewed; 254 AA.
AC Q6AMR6;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 25-MAY-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=DP1630;
OS Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC Desulfocapsaceae; Desulfotalea.
OX NCBI_TaxID=177439;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12343 / LSv54;
RX PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT permanently cold Arctic sediments.";
RL Environ. Microbiol. 6:887-902(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; CR522870; CAG36359.1; -; Genomic_DNA.
DR RefSeq; WP_011188871.1; NC_006138.1.
DR AlphaFoldDB; Q6AMR6; -.
DR SMR; Q6AMR6; -.
DR STRING; 177439.DP1630; -.
DR EnsemblBacteria; CAG36359; CAG36359; DP1630.
DR KEGG; dps:DP1630; -.
DR eggNOG; COG0159; Bacteria.
DR HOGENOM; CLU_016734_0_4_7; -.
DR OMA; LVMTYWN; -.
DR OrthoDB; 912786at2; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000000602; 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 3: Inferred from homology;
KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..254
FT /note="Tryptophan synthase alpha chain"
FT /id="PRO_0000098776"
FT ACT_SITE 48
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT ACT_SITE 59
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
SQ SEQUENCE 254 AA; 28182 MW; 96AD8C8163649DEC CRC64;
MTLEKILREK KKDKDILLMT HIVLGYPSFA ANREVIEQMV KNGVDCIEMQ IPFSEPMADG
PVILKANQES LARGTRVAQC FDFAREMTRK HQIPFLFMTY YNIVFKYGEE RFFQDAKEAG
IKGLIVPDLP PEMGEDYFAY AEQYQLAPII IYAPTSTPER MKTLAGSATG FIYCAARRGV
TGNNSALDEN FDNYLSNCRA ATTLPLAVGF GIKSKADVQA LIGKADMAVI GSQTIRLVDE
NGPKAVGPFV ASLR
