TRPB1_PYRFU
ID TRPB1_PYRFU Reviewed; 388 AA.
AC Q8U093;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Tryptophan synthase beta chain 1;
DE EC=4.2.1.20;
GN Name=trpB1; OrderedLocusNames=PF1706;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=12435500; DOI=10.1111/j.1574-6968.2002.tb11433.x;
RA Ishida M., Oshima T., Yutani K.;
RT "Overexpression in Escherichia coli of the AT-rich trpA and trpB genes from
RT the hyperthermophilic archaeon Pyrococcus furiosus.";
RL FEMS Microbiol. Lett. 216:179-183(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
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}.
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DR EMBL; AB080770; BAC11855.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL81830.1; -; Genomic_DNA.
DR RefSeq; WP_011012852.1; NC_018092.1.
DR PDB; 1V8Z; X-ray; 2.21 A; A/B/C/D=1-388.
DR PDB; 1WDW; X-ray; 3.00 A; B/D/F/H/J/L=1-385.
DR PDB; 5DVZ; X-ray; 1.69 A; A/B/C/D=1-388.
DR PDB; 5DW0; X-ray; 2.01 A; A/B/C/D=1-388.
DR PDB; 5DW3; X-ray; 1.74 A; A/B/C/D=1-388.
DR PDB; 5E0K; X-ray; 2.76 A; B/D/F/H/J/L=1-388.
DR PDB; 5IXJ; X-ray; 1.54 A; A/B/C/D=1-388.
DR PDB; 5T6M; X-ray; 1.80 A; A/B/C/D=1-388.
DR PDB; 5VM5; X-ray; 1.67 A; A/B/C/D=1-388.
DR PDB; 6AM7; X-ray; 1.47 A; A/B/C/D=1-388.
DR PDB; 6AM8; X-ray; 1.83 A; A/B/C/D=1-388.
DR PDB; 6AM9; X-ray; 2.09 A; A/B/C/D=1-388.
DR PDB; 6AMC; X-ray; 1.93 A; A/B/C/D=1-388.
DR PDB; 6AMH; X-ray; 1.63 A; A/B/C/D=1-388.
DR PDB; 6AMI; X-ray; 1.97 A; A/B/C/D=1-388.
DR PDB; 6CUT; X-ray; 1.77 A; A/B/C/D=1-388.
DR PDB; 6CUV; X-ray; 2.26 A; A/B/C/D=1-388.
DR PDB; 6CUZ; X-ray; 1.75 A; A/B/C/D=1-388.
DR PDBsum; 1V8Z; -.
DR PDBsum; 1WDW; -.
DR PDBsum; 5DVZ; -.
DR PDBsum; 5DW0; -.
DR PDBsum; 5DW3; -.
DR PDBsum; 5E0K; -.
DR PDBsum; 5IXJ; -.
DR PDBsum; 5T6M; -.
DR PDBsum; 5VM5; -.
DR PDBsum; 6AM7; -.
DR PDBsum; 6AM8; -.
DR PDBsum; 6AM9; -.
DR PDBsum; 6AMC; -.
DR PDBsum; 6AMH; -.
DR PDBsum; 6AMI; -.
DR PDBsum; 6CUT; -.
DR PDBsum; 6CUV; -.
DR PDBsum; 6CUZ; -.
DR AlphaFoldDB; Q8U093; -.
DR SMR; Q8U093; -.
DR STRING; 186497.PF1706; -.
DR PRIDE; Q8U093; -.
DR EnsemblBacteria; AAL81830; AAL81830; PF1706.
DR GeneID; 41713537; -.
DR KEGG; pfu:PF1706; -.
DR PATRIC; fig|186497.12.peg.1774; -.
DR eggNOG; arCOG01433; Archaea.
DR HOGENOM; CLU_016734_3_1_2; -.
DR OMA; HGMKSYF; -.
DR OrthoDB; 24741at2157; -.
DR PhylomeDB; Q8U093; -.
DR BRENDA; 4.2.1.20; 5243.
DR UniPathway; UPA00035; UER00044.
DR EvolutionaryTrace; Q8U093; -.
DR Proteomes; UP000001013; 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 Direct protein sequencing; Lyase; Pyridoxal phosphate; Reference proteome;
KW Tryptophan biosynthesis.
FT CHAIN 1..388
FT /note="Tryptophan synthase beta chain 1"
FT /id="PRO_0000099050"
FT MOD_RES 82
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:6AMH"
FT HELIX 13..29
FT /evidence="ECO:0007829|PDB:6AM7"
FT HELIX 33..45
FT /evidence="ECO:0007829|PDB:6AM7"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:6AM7"
FT HELIX 57..63
FT /evidence="ECO:0007829|PDB:6AM7"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:6AM7"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:6AM7"
FT HELIX 84..95
FT /evidence="ECO:0007829|PDB:6AM7"
FT STRAND 100..108
FT /evidence="ECO:0007829|PDB:6AM7"
FT HELIX 109..120
FT /evidence="ECO:0007829|PDB:6AM7"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:6AM7"
FT HELIX 131..136
FT /evidence="ECO:0007829|PDB:6AM7"
FT HELIX 138..146
FT /evidence="ECO:0007829|PDB:6AM7"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:6AM7"
FT HELIX 161..175
FT /evidence="ECO:0007829|PDB:6AM7"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:6AM7"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:6AM7"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:5DW3"
FT HELIX 192..200
FT /evidence="ECO:0007829|PDB:6AM7"
FT HELIX 202..215
FT /evidence="ECO:0007829|PDB:6AM7"
FT STRAND 220..225
FT /evidence="ECO:0007829|PDB:6AM7"
FT STRAND 227..229
FT /evidence="ECO:0007829|PDB:6AM7"
FT HELIX 230..236
FT /evidence="ECO:0007829|PDB:6AM7"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:6AM7"
FT STRAND 245..254
FT /evidence="ECO:0007829|PDB:6AM7"
FT TURN 257..260
FT /evidence="ECO:0007829|PDB:6AM7"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:6AM7"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:6AM7"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:6AM7"
FT STRAND 285..289
FT /evidence="ECO:0007829|PDB:6CUZ"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:6AM7"
FT HELIX 306..313
FT /evidence="ECO:0007829|PDB:6AM7"
FT STRAND 316..323
FT /evidence="ECO:0007829|PDB:6AM7"
FT HELIX 324..338
FT /evidence="ECO:0007829|PDB:6AM7"
FT HELIX 344..358
FT /evidence="ECO:0007829|PDB:6AM7"
FT STRAND 365..369
FT /evidence="ECO:0007829|PDB:6AM7"
FT STRAND 372..374
FT /evidence="ECO:0007829|PDB:6AM7"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:6AM7"
FT HELIX 378..383
FT /evidence="ECO:0007829|PDB:6AM7"
SQ SEQUENCE 388 AA; 42529 MW; 62C811579520E04B CRC64;
MWFGEFGGQY VPETLIEPLK ELEKAYKRFK DDEEFNRQLN YYLKTWAGRP TPLYYAKRLT
EKIGGAKIYL KREDLVHGGA HKTNNAIGQA LLAKFMGKTR LIAETGAGQH GVATAMAGAL
LGMKVDIYMG AEDVERQKMN VFRMKLLGAN VIPVNSGSRT LKDAINEALR DWVATFEYTH
YLIGSVVGPH PYPTIVRDFQ SVIGREAKAQ ILEAEGQLPD VIVACVGGGS NAMGIFYPFV
NDKKVKLVGV EAGGKGLESG KHSASLNAGQ VGVFHGMLSY FLQDEEGQIK PTHSIAPGLD
YPGVGPEHAY LKKIQRAEYV TVTDEEALKA FHELSRTEGI IPALESAHAV AYAMKLAKEM
SRDEIIIVNL SGRGDKDLDI VLKVSGNV
