ID   TRPA_HALVD              Reviewed;         277 AA.
AC   P18284; D4GU19;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 2.
DT   25-MAY-2022, entry version 117.
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=HVO_0789;
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS   NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DS2 / DSM 5716 / WFD11;
RX   PubMed=2118654; DOI=10.1073/pnas.87.17.6614;
RA   Lam W.L., Cohen A., Tsouluhas D., Doolittle W.F.;
RT   "Genes for tryptophan biosynthesis in the archaebacterium Haloferax
RT   volcanii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:6614-6618(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2;
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA   Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA   Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(2010).
RN   [3]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=DS2 / DS70;
RX   PubMed=14766575; DOI=10.1128/aem.70.2.943-953.2004;
RA   Allers T., Ngo H.-P., Mevarech M., Lloyd R.G.;
RT   "Development of additional selectable markers for the halophilic archaeon
RT   Haloferax volcanii based on the leuB and trpA genes.";
RL   Appl. Environ. Microbiol. 70:943-953(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, ECO:0000269|PubMed:14766575}.
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   -!- DISRUPTION PHENOTYPE: Auxotrophic for tryptophan.
CC       {ECO:0000269|PubMed:14766575}.
CC   -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00131}.
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DR   EMBL; M36177; AAA72864.1; -; Genomic_DNA.
DR   EMBL; CP001956; ADE05134.1; -; Genomic_DNA.
DR   PIR; A36044; A36044.
DR   RefSeq; WP_004044148.1; NZ_AOHU01000097.1.
DR   AlphaFoldDB; P18284; -.
DR   SMR; P18284; -.
DR   STRING; 309800.C498_14788; -.
DR   EnsemblBacteria; ADE05134; ADE05134; HVO_0789.
DR   GeneID; 8924299; -.
DR   KEGG; hvo:HVO_0789; -.
DR   eggNOG; arCOG01086; Archaea.
DR   HOGENOM; CLU_016734_0_0_2; -.
DR   OMA; LVMTYWN; -.
DR   OrthoDB; 65368at2157; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000008243; 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..277
FT                   /note="Tryptophan synthase alpha chain"
FT                   /id="PRO_0000098887"
FT   ACT_SITE        43
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00131"
FT   ACT_SITE        54
FT                   /note="Proton acceptor"
FT   CONFLICT        92
FT                   /note="T -> R (in Ref. 1; AAA72864)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   277 AA;  29665 MW;  27552AE527C8A861 CRC64;
     MSLEDAFSDG PAFVPYLAAG DPDYESSLEY VEALERGGAD VIELGLPFSE PIAEGPTIQN
     AVVRSLEGGM TPTRFFEFVE DLDVSVPLVC MTYYNLIYRY GDEPGPRPFV EKAAEVGIEG
     FVVPDLPAEE AGPLREACDE FGLDLVFIVA PTTRGERLDR IMEQVSGYVY VQARLGTTGA
     QSSVSDQTDS SLERLTDYDV PKAVGFGISD GDHAERIVAS GADGIIVGSA LVDIVAEGHE
     NGDDAETVAD RLETLARELE DGAVAGASQR PPHPERT