ID   TRPB_SYNY3              Reviewed;         412 AA.
AC   Q59992;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 142.
DE   RecName: Full=Tryptophan synthase beta chain;
DE            EC=4.2.1.20;
GN   Name=trpB; OrderedLocusNames=slr0543;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8159786; DOI=10.1104/pp.104.2.461;
RA   Zhao G.P., Somerville R.L., Chitnis P.R.;
RT   "Synechocystis PCC 6803 contains a single gene for the beta subunit of
RT   tryptophan synthase with strong homology to the trpB genes of Arabidopsis
RT   and maize (Zea mays L.).";
RL   Plant Physiol. 104:461-466(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27184 / PCC 6803 / N-1;
RX   PubMed=8590279; DOI=10.1093/dnares/2.4.153;
RA   Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N.,
RA   Sugiura M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region
RT   from map positions 64% to 92% of the genome.";
RL   DNA Res. 2:153-166(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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; L14596; AAA27302.1; -; Genomic_DNA.
DR   EMBL; BA000022; BAA10837.1; -; Genomic_DNA.
DR   PIR; S75990; S75990.
DR   AlphaFoldDB; Q59992; -.
DR   SMR; Q59992; -.
DR   IntAct; Q59992; 4.
DR   STRING; 1148.1001350; -.
DR   PaxDb; Q59992; -.
DR   EnsemblBacteria; BAA10837; BAA10837; BAA10837.
DR   KEGG; syn:slr0543; -.
DR   eggNOG; COG0133; Bacteria.
DR   InParanoid; Q59992; -.
DR   OMA; HGMKSYF; -.
DR   PhylomeDB; Q59992; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000001425; 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..412
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_0000099012"
FT   MOD_RES         105
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   412 AA;  45070 MW;  C009A39658D09AE3 CRC64;
     MNITSPLSAP SHQYPDALGR FGNYGGKYVP ETLMPALTEL EEAYYRYRAE SSFQEELAGL
     LKDYVGRSSP LYFAERLSAH YARPDGTYPL IYLKREDLNH TGAHKINNAL GQVLLAKRMG
     KKRIIAETGA GQHGVATATV CARFGLECII YMGVQDMERQ KLNVFRMNLL GARVQPVTAG
     TGTLKDATSE AIRDWVTNVE TTHYILGSVA GPHPYPMMVR DFHRVIGQET RQQALKKWGG
     LPDILLACVG GGSNAMGLFY DFIDEPAVRL IGIEAAGESI VSGKHAATLT MGKPGVLHGA
     MSYLLQDKEG QVTEAHSISA GLDYPGVGPE HSYLKDAGRA EYYSVTDQEA ITALQRLSQL
     EGIIPALETA HAFAYLETLC PQLKNGERIV INCSGRGDKD VQTVAKYLQM EI