TRPB_THET8
ID TRPB_THET8 Reviewed; 418 AA.
AC Q5SJB9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 103.
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=TTHA1095;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) 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: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; AP008226; BAD70918.1; -; Genomic_DNA.
DR RefSeq; WP_011173169.1; NC_006461.1.
DR RefSeq; YP_144361.1; NC_006461.1.
DR AlphaFoldDB; Q5SJB9; -.
DR SMR; Q5SJB9; -.
DR STRING; 300852.55772477; -.
DR EnsemblBacteria; BAD70918; BAD70918; BAD70918.
DR GeneID; 3168938; -.
DR KEGG; ttj:TTHA1095; -.
DR PATRIC; fig|300852.9.peg.1075; -.
DR eggNOG; COG0133; Bacteria.
DR HOGENOM; CLU_016734_3_1_0; -.
DR OMA; HGMKSYF; -.
DR PhylomeDB; Q5SJB9; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000000532; 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..418
FT /note="Tryptophan synthase beta chain"
FT /id="PRO_1000018417"
FT MOD_RES 109
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ SEQUENCE 418 AA; 45340 MW; 173833F8B58099FB CRC64;
MGVVLARGAF RERSMLTLPD FPLPDARGRF GPYGGRYVPE TLIPALEELE AAYREAKKDP
AFLEELDHYL RQFAGRPTPL YHAKRLSEYW GGAQVFLKRE DLLHTGAHKI NNTLGQALLA
RRMGKRRVIA ETGAGQHGVS VATVAALFGL ECVVYMGEED VRRQALNVFR MKLLGAEVRP
VAAGSRTLKD ATNEAIRDWI TNVRTTFYIL GSVVGPHPYP MMVRDFQSVI GEEVKRQSLE
LFGRLPDALI AAVGGGSNAI GLFAPFAYLP EGRPKLIGVE AAGEGLSTGR HAASIGAGKR
GVLHGSYMYL LYDHDGQITP AHSVSAGLDY PGVGPEHSYY ADAGVAEYAS VTDEEALEGF
KLLARLEGII PALESAHAIA YAAKVVPEMD KDQVVVINLS GRGDKDVTEV MRLLGGEL
