TRPB1_PYRAB
ID TRPB1_PYRAB Reviewed; 388 AA.
AC Q9V1G8; G8ZGG3;
DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Tryptophan synthase beta chain 1;
DE EC=4.2.1.20;
GN Name=trpB1; Synonyms=trpB-1; OrderedLocusNames=PYRAB04590;
GN ORFNames=PAB2048;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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; AJ248284; CAB49381.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE69842.1; -; Genomic_DNA.
DR PIR; F75162; F75162.
DR RefSeq; WP_010867583.1; NC_000868.1.
DR AlphaFoldDB; Q9V1G8; -.
DR SMR; Q9V1G8; -.
DR STRING; 272844.PAB2048; -.
DR EnsemblBacteria; CAB49381; CAB49381; PAB2048.
DR GeneID; 1495355; -.
DR KEGG; pab:PAB2048; -.
DR PATRIC; fig|272844.11.peg.486; -.
DR eggNOG; arCOG01433; Archaea.
DR HOGENOM; CLU_016734_3_1_2; -.
DR OMA; GPEHAMF; -.
DR OrthoDB; 24741at2157; -.
DR PhylomeDB; Q9V1G8; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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..388
FT /note="Tryptophan synthase beta chain 1"
FT /id="PRO_0000099047"
FT MOD_RES 82
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 388 AA; 42624 MW; DED4A785E5816E72 CRC64;
MWFGKFGGQY VPETLMEPLR ELEKAYKRLK NDEEFNRQLD YYLRTWAGRP TPLYYAERLT
KKVGGAKIYL KREDLLHGGA HKTNNAIGQA LLAKFMGKTR LIAETGAGQH GVATAMAGAL
LGMKVDIYMG AEDVERQKMN VFRMKLLGAN VIPVHTGSKT LKDAINEALR DWVATFEYSH
YLIGSVVGPH PYPIIVRDFQ SVIGREAREQ ILEAEGDLPD VIVACVGGGS NAMGIFYPFV
KDKSVRLIGV EAGGKGIESG KHSASLNAGE IGVFHGMLSY FLQDEEGQIR TTHSIAPGLD
YPGVGPEHAY LKESGRAEYV TVTDEEALRA FHELSRTEGI IPALESAHAV AYAIKLAREM
SRDDVIIVNL SGRGDKDLDI VLKVSGNV