TRPB_HALS3
ID TRPB_HALS3 Reviewed; 430 AA.
AC B0R332;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 81.
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=OE_1470F;
OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=478009;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(2008).
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; AM774415; CAP13142.1; -; Genomic_DNA.
DR RefSeq; WP_010902181.1; NC_010364.1.
DR AlphaFoldDB; B0R332; -.
DR SMR; B0R332; -.
DR EnsemblBacteria; CAP13142; CAP13142; OE_1470F.
DR GeneID; 5954430; -.
DR GeneID; 62885999; -.
DR KEGG; hsl:OE_1470F; -.
DR HOGENOM; CLU_016734_3_1_2; -.
DR OMA; HGMKSYF; -.
DR PhylomeDB; B0R332; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000001321; 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..430
FT /note="Tryptophan synthase beta chain"
FT /id="PRO_1000095792"
FT MOD_RES 95
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ SEQUENCE 430 AA; 45451 MW; B1B56DAC9AD0BCDC CRC64;
MSTNTDDTTR TDGTFGDYGG QYVPEVLMPA VEELTDAYER YVLDNEDGFV DDFRQRIRSF
GGRPTPLTHA PTLSQRHGVD VYLKREDLLH GGAHKLNNAL GQVLLAKYMG KDRIVAETGA
GQHGTATAMA CAALEMPCEI YMGRTDVNRQ RPNVFRMRLH DADVNPVTVG SGTLKEAINE
TMRDWATNVA DTHYVIGSVV GPHPFPSMVR DFQAIISEEL RAQSREQLGE LPAAVIACAG
GGSNTMGAFG AFVGSASLPG APAGTHEPAP DVDLLAVEAG GSRLGVDDDA GYAPNSASLS
TGTEGVLHGA RTKLLQTETG QIVESHSVSA GLDYAGVGPE LAHLVDTGRI TPTNVDDDAA
LAAFHRLSRD EGVIPALETS HAVAALDQYD GDGPVVVNVS GRGDKDLDTV IEASAANDID
AAPDMEVFEQ