TRPB_THEAC
ID TRPB_THEAC Reviewed; 424 AA.
AC Q9HKD2;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Tryptophan synthase beta chain;
DE EC=4.2.1.20;
GN Name=trpB; OrderedLocusNames=Ta0669;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
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; AL445065; CAC11807.1; -; Genomic_DNA.
DR RefSeq; WP_010901091.1; NC_002578.1.
DR AlphaFoldDB; Q9HKD2; -.
DR SMR; Q9HKD2; -.
DR STRING; 273075.Ta0669; -.
DR EnsemblBacteria; CAC11807; CAC11807; CAC11807.
DR GeneID; 1456241; -.
DR KEGG; tac:Ta0669; -.
DR eggNOG; arCOG01432; Archaea.
DR HOGENOM; CLU_042858_1_0_2; -.
DR OMA; RYHAVAP; -.
DR OrthoDB; 24741at2157; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000001024; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.1100; -; 2.
DR HAMAP; MF_00133; Trp_synth_beta; 1.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR006316; Trp_synth_b-like.
DR InterPro; IPR006653; Trp_synth_b_CS.
DR InterPro; IPR023026; Trp_synth_beta/beta-like.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR PANTHER; PTHR48077:SF6; PTHR48077:SF6; 1.
DR Pfam; PF00291; PALP; 1.
DR PIRSF; PIRSF001413; Trp_syn_beta; 1.
DR PIRSF; PIRSF500824; TrpB_prok; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR01415; trpB_rel; 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..424
FT /note="Tryptophan synthase beta chain"
FT /id="PRO_0000099059"
FT MOD_RES 108
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 424 AA; 47384 MW; F4CA59E1041CB928 CRC64;
MIRIDLKQDE MPDHWYNILP DLPEELPTPR DETGEAFDTL KKAVPAKVLE YEFSGERYPK
IPDEILERYM QVGRPTPIIR AKKLEELLGG NLKIFLKMES YTYSGSHKIN SALAHVFFAR
EEGAKFVSTE TGAGQWGSAV ALASALFHME SHIFMVRTSF YAKPYRKYMM YMYGAHPHPS
PSEFTEYGRE VLKRMPDTPG SLGLAISEAI HYALDNGGKY IAGSVINSDI LFKTIAGMEA
KKQMEMAGED PDYIVGVVGG GSNYAALAFP FLADELSSGK IRRTYIASGS KEVPKMTEGE
YRYDYPDTGK VLPLLKMYTI GYDFIPPAVY AGGLRYHAVA PTLSLLMNKG IVSARDYDQE
EAFKWARIFS ETEGYIPAPE TSHALPILKE IADKNRGEKK TVLVSFSGHG LLDLGNYAEA
LHFE
