TRPB_THEVO
ID TRPB_THEVO Reviewed; 426 AA.
AC Q97A51;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=Tryptophan synthase beta chain;
DE EC=4.2.1.20;
GN Name=trpB; OrderedLocusNames=TV0959; ORFNames=TVG0983765;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(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; BA000011; BAB60101.1; -; Genomic_DNA.
DR RefSeq; WP_010917189.1; NC_002689.2.
DR AlphaFoldDB; Q97A51; -.
DR SMR; Q97A51; -.
DR STRING; 273116.14325176; -.
DR EnsemblBacteria; BAB60101; BAB60101; BAB60101.
DR GeneID; 1442037; -.
DR KEGG; tvo:TVG0983765; -.
DR eggNOG; arCOG01432; Archaea.
DR HOGENOM; CLU_042858_1_0_2; -.
DR OMA; RYHAVAP; -.
DR OrthoDB; 24741at2157; -.
DR PhylomeDB; Q97A51; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000001017; 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; Tryptophan biosynthesis.
FT CHAIN 1..426
FT /note="Tryptophan synthase beta chain"
FT /id="PRO_0000099060"
FT MOD_RES 108
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 426 AA; 47544 MW; ABD99604E9BE6D26 CRC64;
MIRIDLKQDD MPDHWYNILP DLPEELPTPR DETGEAFETL KKAVPTKVLE YEFSGERYPK
IPGEIYEKYM QVGRPTPIIR AKNLEEFLGG NIKIYLKMES YTYSGSHKIN SALAHVFFAK
QDNAKFVSTE TGAGQWGSAV ALASALFGVD SHIFMVRTSF YAKPYRKYMM YMYGAHPHPS
PSEFTEYGKE VLKKNPDTPG SLGLAISEAI HYALDNGGKY IAGSVINSDI LFKTIAGMEA
KKQMEMAGED PDYVVGVVGG GSNYAALAFP FLADELQSGK VKRTYIASGS KEVPKMTEGE
YRYDYPDTGK VLPLLKMYTI GYDFIPPAVY AGGLRYHAVA PTLSLLMNKG IVQARDYDQE
EAFKWARIFS EKEGYIPAPE TSHALPILKE IADSNRGERE KKTVLVSFSG HGLLDLGNYA
EAMHFE