ID   TRPB1_ARCFU             Reviewed;         397 AA.
AC   O28672;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 131.
DE   RecName: Full=Tryptophan synthase beta chain 1;
DE            EC=4.2.1.20;
GN   Name=trpB1; Synonyms=trpB; OrderedLocusNames=AF_1600;
OS   Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS   100126 / VC-16).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=224325;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX   PubMed=9389475; DOI=10.1038/37052;
RA   Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA   Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA   Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA   Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA   Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA   Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA   Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA   Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA   Smith H.O., Woese C.R., Venter J.C.;
RT   "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT   archaeon Archaeoglobus fulgidus.";
RL   Nature 390:364-370(1997).
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; AE000782; AAB89649.1; -; Genomic_DNA.
DR   PIR; G69449; G69449.
DR   AlphaFoldDB; O28672; -.
DR   SMR; O28672; -.
DR   STRING; 224325.AF_1600; -.
DR   EnsemblBacteria; AAB89649; AAB89649; AF_1600.
DR   KEGG; afu:AF_1600; -.
DR   eggNOG; arCOG01433; Archaea.
DR   HOGENOM; CLU_016734_3_1_2; -.
DR   OMA; HGMKSYF; -.
DR   PhylomeDB; O28672; -.
DR   BRENDA; 4.2.1.20; 414.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000002199; 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; Reference proteome; Tryptophan biosynthesis.
FT   CHAIN           1..397
FT                   /note="Tryptophan synthase beta chain 1"
FT                   /id="PRO_0000099032"
FT   MOD_RES         94
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   397 AA;  43745 MW;  9FBE4544A3272924 CRC64;
     MRCWLENLSG GRKMKFGEFG GRFVPEVLIP PLEELEKAYD RFKDDEEFKA RLEYYLKSYA
     GRPTPLYFAE NLSRELGVKI YLKREDLLHG GAHKINNTIG QALLAKFMGK KRVIAETGAG
     QHGVATAMAA ALLGLEAEIY MGAEDYERQK MNVFRMELLG AKVTAVESGS RTLKDAINEA
     LRDWVESFEH THYLIGSVVG PHPFPTIVRD FQAVIGKEAR RQIIEAEGGM PDAIIACVGG
     GSNAMGIFHP FLNDDVRLIG VEAGGEGIES GRHSASLTAG SKGVLHGMLS YFLQDEEGMM
     LDTHSVSAGL DYPGVGPEHA YLKETGRCEY VTVNDEEALR AFKTLSKLEG IIPALESAHA
     IAYAMKMAEE MQRDDVLVVN LSGRGDKDMD IVRRRLA