TRPA_GLOVI
ID TRPA_GLOVI Reviewed; 276 AA.
AC Q7NHC5;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=gll2612;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
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; BA000045; BAC90553.1; -; Genomic_DNA.
DR RefSeq; NP_925558.1; NC_005125.1.
DR RefSeq; WP_011142606.1; NC_005125.1.
DR AlphaFoldDB; Q7NHC5; -.
DR SMR; Q7NHC5; -.
DR STRING; 251221.35213181; -.
DR PRIDE; Q7NHC5; -.
DR EnsemblBacteria; BAC90553; BAC90553; BAC90553.
DR KEGG; gvi:gll2612; -.
DR PATRIC; fig|251221.4.peg.2652; -.
DR eggNOG; COG0159; Bacteria.
DR HOGENOM; CLU_016734_0_2_3; -.
DR InParanoid; Q7NHC5; -.
DR OMA; LVMTYWN; -.
DR OrthoDB; 912786at2; -.
DR PhylomeDB; Q7NHC5; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000000557; 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; IBA:GO_Central.
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..276
FT /note="Tryptophan synthase alpha chain"
FT /id="PRO_0000098785"
FT ACT_SITE 55
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT ACT_SITE 66
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
SQ SEQUENCE 276 AA; 28840 MW; 6BB6F1BAEF00A610 CRC64;
MSSLASPGRI ARVFAALHAR REVAFIPFIT AGDPDLETTA EALLTLDRNG ADLLELGLPY
SDPLADGPTI QAAATRALAR GTTPGAVLDL VARLTPELRA PLIVFTYFNL ILAVGIEAFV
ERLAASGASG LLVPDLPVEE GDALQTAANV QGLDVIWLVA PTSPPERLRR IAERTTGFVY
LVSTTGVTGA RTQVASSVRT SLAQLRALTT RPVAVGFGIS TPEQAHEVAS LGADGVIVGS
ACVQLLATAA PEERLGQLAE FCRQLKKASQ TLPVKS