ID   TRPB_HALSA              Reviewed;         430 AA.
AC   Q9HSC0;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=Tryptophan synthase beta chain;
DE            EC=4.2.1.20;
GN   Name=trpB; OrderedLocusNames=VNG_0307G;
OS   Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS   (Halobacterium halobium).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halobacteriaceae; Halobacterium.
OX   NCBI_TaxID=64091;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700922 / JCM 11081 / NRC-1;
RX   PubMed=11016950; DOI=10.1073/pnas.190337797;
RA   Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA   Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA   Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA   Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA   Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA   Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA   Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA   DasSarma S.;
RT   "Genome sequence of Halobacterium species NRC-1.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE004437; AAG18887.1; -; Genomic_DNA.
DR   PIR; C84190; C84190.
DR   RefSeq; WP_010902181.1; NC_002607.1.
DR   AlphaFoldDB; Q9HSC0; -.
DR   SMR; Q9HSC0; -.
DR   STRING; 64091.VNG_0307G; -.
DR   PaxDb; Q9HSC0; -.
DR   EnsemblBacteria; AAG18887; AAG18887; VNG_0307G.
DR   GeneID; 5954430; -.
DR   GeneID; 62885999; -.
DR   KEGG; hal:VNG_0307G; -.
DR   PATRIC; fig|64091.14.peg.226; -.
DR   HOGENOM; CLU_016734_3_1_2; -.
DR   InParanoid; Q9HSC0; -.
DR   OMA; HGMKSYF; -.
DR   OrthoDB; 24741at2157; -.
DR   PhylomeDB; Q9HSC0; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000000554; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central.
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..430
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_0000099034"
FT   MOD_RES         95
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   430 AA;  45451 MW;  B1B56DAC9AD0BCDC CRC64;
     MSTNTDDTTR TDGTFGDYGG QYVPEVLMPA VEELTDAYER YVLDNEDGFV DDFRQRIRSF
     GGRPTPLTHA PTLSQRHGVD VYLKREDLLH GGAHKLNNAL GQVLLAKYMG KDRIVAETGA
     GQHGTATAMA CAALEMPCEI YMGRTDVNRQ RPNVFRMRLH DADVNPVTVG SGTLKEAINE
     TMRDWATNVA DTHYVIGSVV GPHPFPSMVR DFQAIISEEL RAQSREQLGE LPAAVIACAG
     GGSNTMGAFG AFVGSASLPG APAGTHEPAP DVDLLAVEAG GSRLGVDDDA GYAPNSASLS
     TGTEGVLHGA RTKLLQTETG QIVESHSVSA GLDYAGVGPE LAHLVDTGRI TPTNVDDDAA
     LAAFHRLSRD EGVIPALETS HAVAALDQYD GDGPVVVNVS GRGDKDLDTV IEASAANDID
     AAPDMEVFEQ