ID   TRPA_PSYCK              Reviewed;         272 AA.
AC   Q1QDK2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=Pcryo_0468;
OS   Psychrobacter cryohalolentis (strain ATCC BAA-1226 / DSM 17306 / VKM B-2378
OS   / K5).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Psychrobacter.
OX   NCBI_TaxID=335284;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1226 / DSM 17306 / VKM B-2378 / K5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Sims D.R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Richardson P.;
RT   "Complete sequence of chromosome of Psychrobacter cryohalolentis K5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000323; ABE74251.1; -; Genomic_DNA.
DR   RefSeq; WP_011512836.1; NC_007969.1.
DR   AlphaFoldDB; Q1QDK2; -.
DR   SMR; Q1QDK2; -.
DR   STRING; 335284.Pcryo_0468; -.
DR   KEGG; pcr:Pcryo_0468; -.
DR   eggNOG; COG0159; Bacteria.
DR   HOGENOM; CLU_016734_0_0_6; -.
DR   OMA; LVMTYWN; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000002425; 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   Tryptophan biosynthesis.
FT   CHAIN           1..272
FT                   /note="Tryptophan synthase alpha chain"
FT                   /id="PRO_1000018262"
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"
SQ   SEQUENCE   272 AA;  29051 MW;  1B0201610D14E47A CRC64;
     MTRIESTFET LKAQNKKALI PYVMAGDPNP SNFVGLLHDL VKHGADMIEV GLPFSDPMAD
     GPTVALAGER ALAAGTSTRD ALKMVKEFRQ QDTQTPIILM GYLNPVEIIG YDNFVSLCEQ
     SGVDGILMVD LPPAEAGSFT QHLTEHAMNE IFLLSPTTLA ERRQQVLTHC GGYIYYVSLK
     GVTGSATLDT DDVAKQVQAI KAETDLPVCV GFGIRDATSA KAIGAHADGI IVGSALVQNF
     ADIDANDITA VANAQQKIMA KMDELRGALD SL