TRPB_THIDA
ID TRPB_THIDA Reviewed; 399 AA.
AC Q3SHL9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 104.
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=Tbd_1914;
OS Thiobacillus denitrificans (strain ATCC 25259).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=292415;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25259;
RX PubMed=16452431; DOI=10.1128/jb.188.4.1473-1488.2006;
RA Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT anaerobic bacterium Thiobacillus denitrificans.";
RL J. Bacteriol. 188:1473-1488(2006).
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; CP000116; AAZ97867.1; -; Genomic_DNA.
DR RefSeq; WP_011312426.1; NC_007404.1.
DR AlphaFoldDB; Q3SHL9; -.
DR SMR; Q3SHL9; -.
DR STRING; 292415.Tbd_1914; -.
DR EnsemblBacteria; AAZ97867; AAZ97867; Tbd_1914.
DR KEGG; tbd:Tbd_1914; -.
DR eggNOG; COG0133; Bacteria.
DR HOGENOM; CLU_016734_3_1_4; -.
DR OMA; HGMKSYF; -.
DR OrthoDB; 912282at2; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000008291; 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..399
FT /note="Tryptophan synthase beta chain"
FT /id="PRO_1000095834"
FT MOD_RES 92
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ SEQUENCE 399 AA; 42799 MW; 0FD96B5BCE356395 CRC64;
MKLTDLPDSR GHFGPYGGIF VSETLMAALD ALRVEYDAAC RDPGFMAEFE YELKHYVGRP
SPVYHARRLS EEYGGAQIYL KREDLNHTGA HKINNTIGQA LLARRMGKKR VIAETGAGQH
GVASATVAAR YGMECVVYMG AEDVARQAPN VFRMKLLGAT VVPVSSGSKT LKDALNEAMR
DWVTNVESTF YILGTAAGPH PYPMLVRDFQ CVIGRECIAQ MPELVGRQPD AVVACVGGGS
NAIGIFHPYI PHENVRLIGV EAGGSGVASG KHAAPLTAGT PGVLHGFRSY LMQDENGQII
ETHSVSAGLD YPGVGPEHSY LKDAGRAEYV PINDDEALAA FHDLCRFEGI IPALESSHAV
AQAKKLAPTM KKDQVILVNL SGRGDKDINT VAKAAGITL