ID   TRPB1_NOSS1             Reviewed;         409 AA.
AC   Q8YZP7;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=Tryptophan synthase beta chain 1;
DE            EC=4.2.1.20;
GN   Name=trpB1; OrderedLocusNames=all0410;
OS   Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=103690;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX   PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA   Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA   Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT   "Complete genomic sequence of the filamentous nitrogen-fixing
RT   cyanobacterium Anabaena sp. strain PCC 7120.";
RL   DNA Res. 8:205-213(2001).
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; BA000019; BAB72368.1; -; Genomic_DNA.
DR   PIR; AI1857; AI1857.
DR   RefSeq; WP_010994586.1; NZ_RSCN01000017.1.
DR   AlphaFoldDB; Q8YZP7; -.
DR   SMR; Q8YZP7; -.
DR   STRING; 103690.17129755; -.
DR   EnsemblBacteria; BAB72368; BAB72368; BAB72368.
DR   KEGG; ana:all0410; -.
DR   eggNOG; COG0133; Bacteria.
DR   OMA; GPEHAMF; -.
DR   OrthoDB; 912282at2; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000002483; Chromosome.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
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..409
FT                   /note="Tryptophan synthase beta chain 1"
FT                   /id="PRO_0000098910"
FT   MOD_RES         104
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   409 AA;  44756 MW;  4B048D5029EF8607 CRC64;
     MVSTPEIKNQ LARPDALGRF GKFGGKYVPE TLMPALGELE TAYQKYRDDA SYQTELQNLL
     RDYVGRPSPL YFAERLTEYY ARPDGTGAQI YLKREDLNHT GAHKINNALA QVLLAKRIGK
     QRVIAETGAG QHGVATATVC ARFGLDCVIY MGIHDMERQA LNVFRMKLMG AEVRPVEAGT
     GTLKDATSEA IRDWVTNVET THYILGSVAG PHPYPMIVRD FHAIIGKETR VQCQEKWGGL
     PDILLACVGG GSNAIGLFHE FIDEPSIRLI GVEAAGEGVD TDKHAATLTL GRVGVLHGAM
     SYLLQDEDGQ VIEAHSISAG LDYPGVGPEH SYLKDIRRAE YYSVTDKQAL DGFQQLSRLE
     GIIPALETSH AIAYLETLCP QLNGSPRIVI NCSGRGDKDV QTVAKVLNY