TRPA_FLAPJ
ID TRPA_FLAPJ Reviewed; 253 AA.
AC A6GWZ0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 76.
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=FP0507;
OS Flavobacterium psychrophilum (strain ATCC 49511 / DSM 21280 / CIP 103535 /
OS JIP02/86).
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=402612;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49511 / DSM 21280 / CIP 103535 / JIP02/86;
RX PubMed=17592475; DOI=10.1038/nbt1313;
RA Duchaud E., Boussaha M., Loux V., Bernardet J.-F., Michel C., Kerouault B.,
RA Mondot S., Nicolas P., Bossy R., Caron C., Bessieres P., Gibrat J.-F.,
RA Claverol S., Dumetz F., Le Henaff M., Benmansour A.;
RT "Complete genome sequence of the fish pathogen Flavobacterium
RT psychrophilum.";
RL Nat. Biotechnol. 25:763-769(2007).
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; AM398681; CAL42613.1; -; Genomic_DNA.
DR RefSeq; WP_011962671.1; NC_009613.3.
DR RefSeq; YP_001295431.1; NC_009613.3.
DR AlphaFoldDB; A6GWZ0; -.
DR SMR; A6GWZ0; -.
DR STRING; 402612.FP0507; -.
DR PRIDE; A6GWZ0; -.
DR EnsemblBacteria; CAL42613; CAL42613; FP0507.
DR KEGG; fps:FP0507; -.
DR PATRIC; fig|402612.5.peg.519; -.
DR eggNOG; COG0159; Bacteria.
DR HOGENOM; CLU_016734_0_0_10; -.
DR OMA; LVMTYWN; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000006394; 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..253
FT /note="Tryptophan synthase alpha chain"
FT /id="PRO_1000018201"
FT ACT_SITE 45
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT ACT_SITE 56
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
SQ SEQUENCE 253 AA; 28330 MW; 5665B4A493901F96 CRC64;
MNRINQKLQE DKKILSIYFS AGYPNLNDTV QIIQDLEKSG VDMIEIGLPF SDPLADGPTI
QESSTQALEN GMTTKLLFEQ LKNIRQTVQI PLIIMGYFNP ILQYGVENFC KKCQETGIDG
LIIPDLPVDI YAENYKETFE KHGLTNVFLI TPQTSNERIR HIDSVSNGFI YLVSSASVTG
SSSGFDNIQT NYFKRISEMN LKNPQIIGFG INNKETFNQA TQYQKGAIIG SAFIKNLTEN
GVSSISKFVS EIF
