ID   TRPB_HALVD              Reviewed;         422 AA.
AC   P18285; D4GU17;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 2.
DT   25-MAY-2022, entry version 119.
DE   RecName: Full=Tryptophan synthase beta chain;
DE            EC=4.2.1.20;
GN   Name=trpB; OrderedLocusNames=HVO_0788;
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS   NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DS2 / DSM 5716 / WFD11;
RX   PubMed=2118654; DOI=10.1073/pnas.87.17.6614;
RA   Lam W.L., Cohen A., Tsouluhas D., Doolittle W.F.;
RT   "Genes for tryptophan biosynthesis in the archaebacterium Haloferax
RT   volcanii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:6614-6618(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC   B-1768 / DS2;
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA   Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA   Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(2010).
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; M36177; AAA72863.1; -; Genomic_DNA.
DR   EMBL; CP001956; ADE02680.1; -; Genomic_DNA.
DR   PIR; B36044; B36044.
DR   RefSeq; WP_004044149.1; NZ_AOHU01000097.1.
DR   AlphaFoldDB; P18285; -.
DR   SMR; P18285; -.
DR   STRING; 309800.C498_14793; -.
DR   EnsemblBacteria; ADE02680; ADE02680; HVO_0788.
DR   GeneID; 8924730; -.
DR   KEGG; hvo:HVO_0788; -.
DR   eggNOG; arCOG01433; Archaea.
DR   HOGENOM; CLU_016734_3_1_2; -.
DR   OMA; HGMKSYF; -.
DR   OrthoDB; 24741at2157; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000008243; 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..422
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_0000099035"
FT   MOD_RES         87
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        178
FT                   /note="A -> E (in Ref. 1; AAA72863)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        366..368
FT                   /note="SVV -> VWSS (in Ref. 1; AAA72863)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   422 AA;  45711 MW;  E1853028FFB6AC5D CRC64;
     MSADGKFGDY GGQYVPEALM PAIEELTDAY ERYVLDNEDG FMDDFRARLR DFGGRPTPLQ
     RADRLSERYD REVYLKREDL LHGGAHKLNN ALGQVLLAKY MGKERIIAET GAGQHGTATA
     MACAHLDMPC EIYMGERDIN RQRPNVFRMK LNGSEVNPVT VGRGTLKEAI SETMRDWATN
     VEDTHYVIGS VVGPHPFPSM VRDFQSVISE EARTQAREKL GRLPDAVVAC AGGGSNTMGA
     FAEFVDDEET ALYAVEAGGS TLEVDEEAGV APNSASLTTG SEGILHGART RLLQDRDGQI
     MESHSVSSGL DYAGVGPELA HLVDTGRVTA VNVDDDAALT AFHRLSQMEG IIPALESAHA
     FGYLESVVGP DAPDAENADD LGEYVVVNVS GRGDKDLESA IEETYERDID IAPNMDEFTG
     GL