ID   TRPB1_AQUAE             Reviewed;         397 AA.
AC   O66923;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 136.
DE   RecName: Full=Tryptophan synthase beta chain 1;
DE            EC=4.2.1.20;
GN   Name=trpB1; OrderedLocusNames=aq_706;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC       tryptophan from indole and L-serine. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 5/5.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000305}.
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DR   EMBL; AE000657; AAC06880.1; -; Genomic_DNA.
DR   PIR; G70361; G70361.
DR   RefSeq; NP_213483.1; NC_000918.1.
DR   RefSeq; WP_010880421.1; NC_000918.1.
DR   AlphaFoldDB; O66923; -.
DR   SMR; O66923; -.
DR   STRING; 224324.aq_706; -.
DR   EnsemblBacteria; AAC06880; AAC06880; aq_706.
DR   KEGG; aae:aq_706; -.
DR   PATRIC; fig|224324.8.peg.565; -.
DR   eggNOG; COG0133; Bacteria.
DR   HOGENOM; CLU_016734_3_1_0; -.
DR   InParanoid; O66923; -.
DR   OMA; HGMKSYF; -.
DR   OrthoDB; 912282at2; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
DR   CDD; cd06446; Trp-synth_B; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   HAMAP; MF_00133; Trp_synth_beta; 1.
DR   InterPro; IPR001926; PLP-dep.
DR   InterPro; IPR006653; Trp_synth_b_CS.
DR   InterPro; IPR006654; Trp_synth_beta.
DR   InterPro; IPR023026; Trp_synth_beta/beta-like.
DR   InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR   Pfam; PF00291; PALP; 1.
DR   PIRSF; PIRSF001413; Trp_syn_beta; 1.
DR   SUPFAM; SSF53686; SSF53686; 1.
DR   TIGRFAMs; TIGR00263; trpB; 1.
DR   PROSITE; PS00168; TRP_SYNTHASE_BETA; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW   Pyridoxal phosphate; Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..397
FT                   /note="Tryptophan synthase beta chain 1"
FT                   /id="PRO_0000098912"
FT   MOD_RES         90
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   397 AA;  43543 MW;  3302F177E0E1B0E4 CRC64;
     MYNYPDERGY FGPFGGKFVP ETLMYALEEL EEKYRELKSD PEFQKELDYY LREYAGRPTP
     LYFAEKLTKY VGGAKIYLKR EDLLHTGAHK INNTIGQCLL TKRMGKKRVI AETGAGQHGV
     ATATASALFG LECVVYMGEE DAERQALNVF RMKLLGAKVE IVKSGSRTLK DAINEALRDW
     VTNVESTHYV IGSVVGPHPF PMIVRDFQSV IGRETKEQIL QKEGRLPDAI VACVGGGSNA
     MGIFYPFVED KGVQLIGVEA GGYGLETGQH AASICGGSVG ILHGMKSYFL QDEEGQIQPT
     HSISAGLDYP GVGPEHALFH EIKRAKYTTA TDEEALEGFK LLARTEGIIP ALESAHAVIK
     AVEVARELGK DGIVVINLSG RGDKDMAHVM KHLSLEG