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TRPB_RHOPA
ID   TRPB_RHOPA              Reviewed;         404 AA.
AC   Q6NDN6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=RPA0069;
OS   Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=258594;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-98 / CGA009;
RX   PubMed=14704707; DOI=10.1038/nbt923;
RA   Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L.,
RA   Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R.,
RA   Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C.,
RA   Harrison F.H., Gibson J., Harwood C.S.;
RT   "Complete genome sequence of the metabolically versatile photosynthetic
RT   bacterium Rhodopseudomonas palustris.";
RL   Nat. Biotechnol. 22:55-61(2004).
CC   -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC       tryptophan from indole and L-serine. {ECO:0000255|HAMAP-Rule:MF_00133}.
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; BX572593; CAE25513.1; -; Genomic_DNA.
DR   RefSeq; WP_011155640.1; NC_005296.1.
DR   AlphaFoldDB; Q6NDN6; -.
DR   SMR; Q6NDN6; -.
DR   STRING; 258594.RPA0069; -.
DR   PRIDE; Q6NDN6; -.
DR   EnsemblBacteria; CAE25513; CAE25513; RPA0069.
DR   GeneID; 66891070; -.
DR   KEGG; rpa:RPA0069; -.
DR   eggNOG; COG0133; Bacteria.
DR   HOGENOM; CLU_016734_3_1_5; -.
DR   OMA; HGMKSYF; -.
DR   PhylomeDB; Q6NDN6; -.
DR   BioCyc; RPAL258594:TX73_RS00360-MON; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000001426; 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..404
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_1000095811"
FT   MOD_RES         98
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ   SEQUENCE   404 AA;  43570 MW;  861ADB30E2A49457 CRC64;
     MNQALPNSFR SGPDERGHFG IYGGRFVAET LMPLILDLEK AYAEAKADPA FRAEMDNHLK
     HYVGRPSALY FAERLTEHFG GAKIYFKRED LNHTGAHKVN NVLGQIMLAK RMGKPRVIAE
     TGAGMHGVAT ATMCAKFGLE CVVFMGAVDV ERQQPNVLRM KALGAEVRPV TSGANTLKDA
     MNEALRDWVT NVHDTFYCIG TVAGPHPYPM MVRDFQAVIG QEVREQIMQA EGRLPDSLVA
     CIGGGSNAMG LFHPFLDDPG VAIYGVEAAG HGLDKLHAAS IAGGKPGVLH GNRTYLLMDA
     DGQIEEAHSI SAGLDYPGVG PEHSWLHDVG RVNFLSATDT EALDAFKLCC RLEGIIPALE
     PSHALAKVAD LAPKLPKDHL MVVNMSGRGD KDLASVAEHL GGKF
 
 
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