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TRPB_DESA1
ID   TRPB_DESA1              Reviewed;         428 AA.
AC   B8D4P0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=DKAM_0745;
OS   Desulfurococcus amylolyticus (strain DSM 18924 / JCM 16383 / VKM B-2413 /
OS   1221n) (Desulfurococcus kamchatkensis).
OC   Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC   Desulfurococcaceae; Desulfurococcus.
OX   NCBI_TaxID=490899;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18924 / JCM 16383 / VKM B-2413 / 1221n;
RX   PubMed=19114480; DOI=10.1128/jb.01525-08;
RA   Ravin N.V., Mardanov A.V., Beletsky A.V., Kublanov I.V., Kolganova T.V.,
RA   Lebedinsky A.V., Chernyh N.A., Bonch-Osmolovskaya E.A., Skryabin K.G.;
RT   "Complete genome sequence of the anaerobic, protein-degrading
RT   hyperthermophilic crenarchaeon Desulfurococcus kamchatkensis.";
RL   J. Bacteriol. 191:2371-2379(2009).
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; CP001140; ACL11071.1; -; Genomic_DNA.
DR   RefSeq; WP_012608412.1; NC_011766.1.
DR   AlphaFoldDB; B8D4P0; -.
DR   SMR; B8D4P0; -.
DR   STRING; 490899.DKAM_0745; -.
DR   EnsemblBacteria; ACL11071; ACL11071; DKAM_0745.
DR   GeneID; 7170912; -.
DR   KEGG; dka:DKAM_0745; -.
DR   eggNOG; arCOG01432; Archaea.
DR   HOGENOM; CLU_042858_1_0_2; -.
DR   OMA; MLHQTII; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000006903; 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; Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..428
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_1000198761"
FT   MOD_RES         111
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ   SEQUENCE   428 AA;  46870 MW;  06F9330300743BAB CRC64;
     MELRSTQTPD ILPSYWYNIV PDLPEPLPPM IHPSGEPVKR SELEVLFPRS LVDQEISTQS
     RIPIPEAVRE TLLMLGRPTP LIRARRLEEA LKTNARIFFK YEGVLPTGSH KINTAVAQAY
     YNAVESVERV STETGAGQWG SALSLAGNIY GLKVRVFMVR ASYLQKPYRR ILMEAYGAEV
     YPSPSTKTNT GRKLLAENPD HPGSLGIAIS EAIEDVVLSG GRAKYSLGSV LNHVLLHQSV
     IGLEAIKQLE LLGVERVDYV IGCVGGGSNF AGLSYPFIGY NYNNGEPPVF IAVEPETVPS
     MTRGEYRYDY GDTAGLTPLL KMYTLGHDYI PPPIYAGGLR YHGVAPSLSI LVKNNIVKPV
     AYPQDEVLEA GLVFARTQGI LPAPESSHAV KAVIDVALKY RGASEKPTIL FNLSGHGLLD
     LSAYTRNH
 
 
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