ID   TRPB_ACICA              Reviewed;         403 AA.
AC   P16706;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 2.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Tryptophan synthase beta chain;
DE            EC=4.2.1.20;
GN   Name=trpB;
OS   Acinetobacter calcoaceticus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=471;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2211532; DOI=10.1128/jb.172.10.6151-6155.1990;
RA   Kishan V., Hillen W.;
RT   "Molecular cloning, nucleotide sequence, and promoter structure of the
RT   Acinetobacter calcoaceticus trpFB operon.";
RL   J. Bacteriol. 172:6151-6155(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-106.
RX   PubMed=2299982; DOI=10.1093/oxfordjournals.molbev.a040587;
RA   Ross C.M., Kaplan J.B., Winkler M.E., Nichols B.P.;
RT   "An evolutionary comparison of Acinetobacter calcoaceticus trpF with trpF
RT   genes of several organisms.";
RL   Mol. Biol. Evol. 7:74-81(1990).
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; M58444; AAA21902.1; -; Genomic_DNA.
DR   EMBL; M34485; AAA21898.1; -; Genomic_DNA.
DR   PIR; B36151; B36151.
DR   AlphaFoldDB; P16706; -.
DR   SMR; P16706; -.
DR   STRING; 471.BUM88_16525; -.
DR   UniPathway; UPA00035; UER00044.
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; Tryptophan biosynthesis.
FT   CHAIN           1..403
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_0000098908"
FT   MOD_RES         93
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   403 AA;  44322 MW;  2B4AA1F3EE46E357 CRC64;
     MIDYTQYPDA RGHFGIHGGR FVSETLMAAL EDLENLYNRM KNDEQFLAEF DRDLAYYVGR
     PSPLYYAERW SKKLGGAQIY LKREDLNHTG SHKVNNTIGQ ALLAKLSGKK RIIAETGAGQ
     HGVATATIAA RLGLECVVFM GAEDVKRQAM NVYRMRLLGA TVIPVQSGSK TLKDAMNEAM
     RDWVTNVDST YYVIGTVAGP HPYPQLVRDF QSIIGREARR QIQEQAGRLP DALVACVGGG
     SNAIGLFYPF LNDQDVKMYG VEAAGHGIET GKHSAPLNAG HVGVLHGNRT YLMSDPQGQI
     IETHSISAGL DYPGVGPEHS FLKDMHRVEY VPIDDNEALQ GFRDLTRIEG IIPAIESAHA
     MAYVTKLAPT MDKDQIIIAN VSGRGDKDLM TVARIDGIEM VEM