ID   TRPB_RHIEC              Reviewed;         406 AA.
AC   Q2KE82; P56929;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Tryptophan synthase beta chain {ECO:0000255|HAMAP-Rule:MF_00133};
DE            EC=4.2.1.20 {ECO:0000255|HAMAP-Rule:MF_00133};
GN   Name=trpB {ECO:0000255|HAMAP-Rule:MF_00133}; OrderedLocusNames=RHE_CH00021;
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN SYMBIOSIS.
RC   STRAIN=CE3;
RX   PubMed=10517032; DOI=10.1094/mpmi.1999.12.10.926;
RA   Tate R., Riccio A., Caputo E., Cermola M., Favre R., Patriarca E.J.;
RT   "The Rhizobium etli trpB gene is essential for an effective symbiotic
RT   interaction with Phaseolus vulgaris.";
RL   Mol. Plant Microbe Interact. 12:926-933(1999).
RN   [2]
RP   SEQUENCE REVISION TO 92; 143; 171; 219; 262 AND 337.
RA   Patriarca E.J.;
RL   Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251;
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT   seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
CC   -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC       tryptophan from indole and L-serine. Essential for production of nod
CC       factors and establishment of symbiosis. {ECO:0000255|HAMAP-
CC       Rule:MF_00133, ECO:0000269|PubMed:10517032}.
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_00133};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00133};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC       tryptophan from chorismate: step 5/5. {ECO:0000255|HAMAP-
CC       Rule:MF_00133}.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000255|HAMAP-
CC       Rule:MF_00133}.
CC   -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00133}.
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DR   EMBL; AJ245564; CAB55324.2; -; Genomic_DNA.
DR   EMBL; CP000133; ABC88854.1; -; Genomic_DNA.
DR   RefSeq; WP_011423426.1; NC_007761.1.
DR   AlphaFoldDB; Q2KE82; -.
DR   SMR; Q2KE82; -.
DR   STRING; 347834.RHE_CH00021; -.
DR   EnsemblBacteria; ABC88854; ABC88854; RHE_CH00021.
DR   GeneID; 61478483; -.
DR   KEGG; ret:RHE_CH00021; -.
DR   eggNOG; COG0133; Bacteria.
DR   HOGENOM; CLU_016734_3_1_5; -.
DR   OMA; HGMKSYF; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000001936; 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   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Lyase;
KW   Pyridoxal phosphate; Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..406
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_1000018380"
FT   MOD_RES         99
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
FT   CONFLICT        57..58
FT                   /note="KH -> ND (in Ref. 1; CAB55324)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        61..62
FT                   /note="AH -> RD (in Ref. 1; CAB55324)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        91..92
FT                   /note="EL -> DV (in Ref. 1; CAB55324)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        133
FT                   /note="T -> A (in Ref. 1; CAB55324)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   406 AA;  43538 MW;  218B41FE6DA26D9E CRC64;
     MNETPKPNSF RSGPDEDGRF GIYGGRFVAE TLMPLILDLQ DEWNKAKSDP AFQAELKHLG
     AHYIGRPSPL YFAERLTAEL GGAKIYFKRE ELNHTGSHKI NNCIGQILLA KRMGKTRIIA
     ETGAGQHGVA SATVAARFGL PCVVYMGATD VERQAPNVFR MKLLGAEVKP VTAGSGTLKD
     AMNEALRDWV TNVEDTYYLI GTAAGPHPYP EMVRDFQSVI GAEAKEQMLA AEGRLPDLVV
     AAVGGGSNAI GIFHPFLDDS SVKIVGVEAG GKGLQGDEHC ASITAGSPGV LHGNRTYLLQ
     DGDGQIKEGH SISAGLDYPG IGPEHSWLSD IGRVDYVPIM DHEALEAFQT LTRLEGIIPA
     LEAAHAIAEV IKRAPKMGKD EIILMNLSGR GDKDIFTVGK ILGMGL