TRPB_BACFR
ID TRPB_BACFR Reviewed; 390 AA.
AC Q64SX9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 99.
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=BF2650;
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=295405;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCH46;
RX PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT regulating cell surface adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(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; AP006841; BAD49400.1; -; Genomic_DNA.
DR RefSeq; WP_005788278.1; NZ_UYXF01000003.1.
DR RefSeq; YP_099934.1; NC_006347.1.
DR AlphaFoldDB; Q64SX9; -.
DR SMR; Q64SX9; -.
DR STRING; 295405.BF2650; -.
DR EnsemblBacteria; BAD49400; BAD49400; BF2650.
DR GeneID; 66328292; -.
DR KEGG; bfr:BF2650; -.
DR PATRIC; fig|295405.11.peg.2561; -.
DR HOGENOM; CLU_016734_3_1_10; -.
DR OMA; HGMKSYF; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000002197; 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; Tryptophan biosynthesis.
FT CHAIN 1..390
FT /note="Tryptophan synthase beta chain"
FT /id="PRO_1000095776"
FT MOD_RES 90
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ SEQUENCE 390 AA; 43027 MW; F8ECD1F3F7F8422C CRC64;
MKSFLVDQDG YYGEFGGAYV PEILHKCVEE LQNTYLDVIE SEDFKKEFDQ LLRDYVGRPS
PLYPARRLSE KYGCKMYLKR EDLNHTGAHK INNTIGQILL ARRMGKKRII AETGAGQHGV
ATATVCALMN MECIVYMGKT DVERQHINVE KMKMLGATVV PVTSGNMTLK DATNEAIRDW
CCHPSDTYYI IGSTVGPHPY PDMVARLQSV ISEEIKKQLQ EKEGRDYPDY LIACVGGGSN
AAGTIYHYID DERVRIVLAE AGGKGIETGM TAATIQLGKM GIIHGARTFV IQNEDGQIEE
PYSISAGLDY PGIGPMHANL ADKKRAMVLA VNDDEAIRAA YELTRLEGII PALESAHALG
ALEKITFKPE DVVVLTVSGR GDKDIETYLG