TRPB_PYRHO
ID TRPB_PYRHO Reviewed; 459 AA.
AC O59265;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Tryptophan synthase beta chain;
DE EC=4.2.1.20;
GN Name=trpB; OrderedLocusNames=PH1583;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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; BA000001; BAA30695.1; -; Genomic_DNA.
DR PIR; G71036; G71036.
DR AlphaFoldDB; O59265; -.
DR SMR; O59265; -.
DR STRING; 70601.3258012; -.
DR EnsemblBacteria; BAA30695; BAA30695; BAA30695.
DR KEGG; pho:PH1583; -.
DR eggNOG; arCOG01432; Archaea.
DR OMA; MLHQTII; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
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; IPR006316; Trp_synth_b-like.
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 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..459
FT /note="Tryptophan synthase beta chain"
FT /id="PRO_0000099052"
FT MOD_RES 121
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 459 AA; 50980 MW; 106B23BBD765E9F1 CRC64;
MIVFGSKAEI HAKSILKDGE IPKRWYNILP DLPEPLSPPL DPETNETINP EKLTRIFAKE
LIKQEFSEKR YIKIPKEVRE LYAKIGRPTP LFRATNLEKI LKTPARIYFK YEGATVTGSH
KINTALAQAY YAKKEGIKRL VTETGAGQWG TALSLAGALI GLKVRVYMTR ASYYQKPYRK
ILMEIYGAEV FPSPSENTEV GKRFLREDPN HPGSLGIAIS EAIEDVLSDE KARYSLGSVL
NHVLMHQTVI GLEAKKQVKE FEEPDVIIGC VGGGSNFAGL SYPFIKDVLD GKAEYEFIAV
EPRAVPTMTK GVYTYDYGDS AGLTPKIKMY TLGHTYYVPP IHAGGLRYHG LAPTLSVLMN
HGIVKPMAYH QTEVFEAAVL FAKAEGIVPA PESAHAVRAV IDKALEAKRK GEETVILFNL
SGHGLLDLKG YEDYLEGKLE DYEPQILNLS MAPRPPNAL