ID   TRPB_CERS4              Reviewed;         409 AA.
AC   Q9X4E5; Q3IW96;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 125.
DE   RecName: Full=Tryptophan synthase beta chain;
DE            EC=4.2.1.20;
GN   Name=trpB; OrderedLocusNames=RHOS4_36200; ORFNames=RSP_3585;
OS   Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS   31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10511537; DOI=10.1093/genetics/153.2.525;
RA   Mackenzie C., Simmons A.E., Kaplan S.;
RT   "Multiple chromosomes in bacteria. The yin and yang of trp gene
RT   localization in Rhodobacter sphaeroides 2.4.1.";
RL   Genetics 153:525-538(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203
RC   / NCIMB 8253 / ATH 2.4.1.;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 2 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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; AF107093; AAD29261.1; -; Genomic_DNA.
DR   EMBL; CP000144; ABA81188.1; -; Genomic_DNA.
DR   RefSeq; WP_002724529.1; NZ_CP030272.1.
DR   RefSeq; YP_355089.1; NC_007494.2.
DR   AlphaFoldDB; Q9X4E5; -.
DR   SMR; Q9X4E5; -.
DR   STRING; 272943.RSP_3585; -.
DR   PRIDE; Q9X4E5; -.
DR   EnsemblBacteria; ABA81188; ABA81188; RSP_3585.
DR   GeneID; 57471920; -.
DR   KEGG; rsp:RSP_3585; -.
DR   PATRIC; fig|272943.9.peg.4021; -.
DR   eggNOG; COG0133; Bacteria.
DR   OMA; HGMKSYF; -.
DR   PhylomeDB; Q9X4E5; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000002703; Chromosome 2.
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"
FT                   /id="PRO_0000098992"
FT   MOD_RES         98
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   409 AA;  44714 MW;  E37F52359D93BE67 CRC64;
     MAEDGINSYM TGPDEQGRFG IFGGRFVSET LMPLILDLEA RYEHAKTDPD FWAEMDDLWK
     NYVGRPSPLY FAPRLTEHLG GAKIYLKRDE LNHTGAHKIN NVLGQIILAR RMGKTRIIAE
     TGAGQHGVAT ATVCAKFGLK CVVYMGAHDV ERQAPNVFRM RLLGAEVVPV TSGRGTLKDA
     MNDALRDWVT NVRDTFYCIG TVAGPHPYPA MVRDFQSIIG REVRWQLAEQ EEGRLPDTLV
     AAIGGGSNAM GLFHPFLDDP SVRIVGVEAG GKGVDDRMEH CASLTGGRPG VLHGNRTYLL
     QDADGQILEG FSISAGLDYP GIGPEHAWLH DTGRAEYVSI TDAEALEAFQ LCCALEGIIP
     ALEPSHALAH VIKIAPTLPR DHIIVMNMCG RGDKDIFTVA KHLGFDMKI