TRPB_THET2
ID TRPB_THET2 Reviewed; 404 AA.
AC P16609;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 25-MAY-2022, entry version 141.
DE RecName: Full=Tryptophan synthase beta chain;
DE EC=4.2.1.20;
GN Name=trpB; OrderedLocusNames=TT_C0730;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2188962; DOI=10.1128/jb.172.6.3490-3495.1990;
RA Koyama Y., Furukawa K.;
RT "Cloning and sequence analysis of tryptophan synthetase genes of an extreme
RT thermophile, Thermus thermophilus HB27: plasmid transfer from replica-
RT plated Escherichia coli recombinant colonies to competent T. thermophilus
RT cells.";
RL J. Bacteriol. 172:3490-3495(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
RX PubMed=2283046; DOI=10.1016/0378-1097(90)90352-q;
RA Koyama Y., Arikawa Y., Furukawa K.;
RT "A plasmid vector for an extreme thermophile, Thermus thermophilus.";
RL FEMS Microbiol. Lett. 60:97-101(1990).
CC -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC tryptophan from indole and L-serine. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 5/5.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAS81078.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M32108; AAA27508.1; -; Genomic_DNA.
DR EMBL; AE017221; AAS81078.1; ALT_INIT; Genomic_DNA.
DR EMBL; X58673; CAA41527.1; -; Genomic_DNA.
DR RefSeq; WP_024119035.1; NC_005835.1.
DR PDB; 1X1Q; X-ray; 2.50 A; A/B=1-404.
DR PDBsum; 1X1Q; -.
DR AlphaFoldDB; P16609; -.
DR SMR; P16609; -.
DR STRING; 262724.TT_C0730; -.
DR EnsemblBacteria; AAS81078; AAS81078; TT_C0730.
DR GeneID; 3168938; -.
DR KEGG; tth:TT_C0730; -.
DR eggNOG; COG0133; Bacteria.
DR HOGENOM; CLU_016734_3_1_0; -.
DR OMA; HGMKSYF; -.
DR UniPathway; UPA00035; UER00044.
DR EvolutionaryTrace; P16609; -.
DR Proteomes; UP000000592; 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 3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW Lyase; Pyridoxal phosphate; Tryptophan biosynthesis.
FT CHAIN 1..404
FT /note="Tryptophan synthase beta chain"
FT /id="PRO_0000099015"
FT MOD_RES 95
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:1X1Q"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:1X1Q"
FT HELIX 29..44
FT /evidence="ECO:0007829|PDB:1X1Q"
FT HELIX 46..58
FT /evidence="ECO:0007829|PDB:1X1Q"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:1X1Q"
FT HELIX 70..76
FT /evidence="ECO:0007829|PDB:1X1Q"
FT STRAND 78..85
FT /evidence="ECO:0007829|PDB:1X1Q"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:1X1Q"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:1X1Q"
FT HELIX 96..109
FT /evidence="ECO:0007829|PDB:1X1Q"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:1X1Q"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:1X1Q"
FT HELIX 122..134
FT /evidence="ECO:0007829|PDB:1X1Q"
FT STRAND 137..143
FT /evidence="ECO:0007829|PDB:1X1Q"
FT HELIX 144..148
FT /evidence="ECO:0007829|PDB:1X1Q"
FT HELIX 151..159
FT /evidence="ECO:0007829|PDB:1X1Q"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:1X1Q"
FT HELIX 174..187
FT /evidence="ECO:0007829|PDB:1X1Q"
FT TURN 188..191
FT /evidence="ECO:0007829|PDB:1X1Q"
FT STRAND 192..194
FT /evidence="ECO:0007829|PDB:1X1Q"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:1X1Q"
FT HELIX 205..213
FT /evidence="ECO:0007829|PDB:1X1Q"
FT HELIX 215..228
FT /evidence="ECO:0007829|PDB:1X1Q"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:1X1Q"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:1X1Q"
FT HELIX 244..253
FT /evidence="ECO:0007829|PDB:1X1Q"
FT STRAND 261..267
FT /evidence="ECO:0007829|PDB:1X1Q"
FT STRAND 272..274
FT /evidence="ECO:0007829|PDB:1X1Q"
FT HELIX 276..283
FT /evidence="ECO:0007829|PDB:1X1Q"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:1X1Q"
FT STRAND 292..296
FT /evidence="ECO:0007829|PDB:1X1Q"
FT HELIX 321..328
FT /evidence="ECO:0007829|PDB:1X1Q"
FT STRAND 331..337
FT /evidence="ECO:0007829|PDB:1X1Q"
FT HELIX 339..353
FT /evidence="ECO:0007829|PDB:1X1Q"
FT HELIX 359..371
FT /evidence="ECO:0007829|PDB:1X1Q"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:1X1Q"
FT STRAND 380..385
FT /evidence="ECO:0007829|PDB:1X1Q"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:1X1Q"
FT HELIX 393..398
FT /evidence="ECO:0007829|PDB:1X1Q"
SQ SEQUENCE 404 AA; 43809 MW; 74D09A1EEC2A04E6 CRC64;
MLTLPDFPLP DARGRFGPYG GRYVPETLIP ALEELEAAYR EAKKDPAFLE ELDHYLRQFA
GRPTPLYHAK RLSEYWGGAQ VFLKREDLLH TGAHKINNTL GQALLARRMG KRRVIAETGA
GQHGVSVATV AALFGLECVV YMGEEDVRRQ ALNVFRMKLL GAEVRPVAAG SRTLKDATNE
AIRDWITNVR TTFYILGSVV GPHPYPMMVR DFQSVIGEEV KRQSLELFGR LPDALIAAVG
GGSNAIGLFA PFAYLPEGRP KLIGVEAAGE GLSTGRHAAS IGAGKRGVLH GSYMYLLYDH
DGQITPAHSV SAGLDYPGVG PEHSYYADAG VAEYASVTDE EALEGFKLLA RLEGIIPALE
SAHAIAYAAK VVPEMDKDQV VVINLSGRGD KDVTEVMRLL GGEL
