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TRPB_STRPN
ID   TRPB_STRPN              Reviewed;         407 AA.
AC   Q97P32;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 120.
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=SP_1812;
OS   Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=170187;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-334 / TIGR4;
RX   PubMed=11463916; DOI=10.1126/science.1061217;
RA   Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA   Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA   Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA   Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA   Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA   McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA   Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA   Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT   "Complete genome sequence of a virulent isolate of Streptococcus
RT   pneumoniae.";
RL   Science 293:498-506(2001).
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; AE005672; AAK75885.1; -; Genomic_DNA.
DR   PIR; D95211; D95211.
DR   RefSeq; WP_000331293.1; NZ_AKVY01000001.1.
DR   PDB; 5KIN; X-ray; 2.45 A; B/D=4-402.
DR   PDBsum; 5KIN; -.
DR   AlphaFoldDB; Q97P32; -.
DR   SMR; Q97P32; -.
DR   STRING; 170187.SP_1812; -.
DR   EnsemblBacteria; AAK75885; AAK75885; SP_1812.
DR   KEGG; spn:SP_1812; -.
DR   eggNOG; COG0133; Bacteria.
DR   OMA; HGMKSYF; -.
DR   PhylomeDB; Q97P32; -.
DR   BioCyc; SPNE170187:G1FZB-1844-MON; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000000585; 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   1: Evidence at protein level;
KW   3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis;
KW   Lyase; Pyridoxal phosphate; Tryptophan biosynthesis.
FT   CHAIN           1..407
FT                   /note="Tryptophan synthase beta chain"
FT                   /id="PRO_0000099008"
FT   MOD_RES         91
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
FT   STRAND          10..12
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   HELIX           22..40
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   HELIX           42..54
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   STRAND          62..64
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   HELIX           66..72
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   STRAND          74..81
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   HELIX           82..84
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   HELIX           93..104
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   STRAND          109..113
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   STRAND          115..117
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   HELIX           118..129
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   STRAND          133..139
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   HELIX           140..143
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   HELIX           147..155
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   STRAND          159..163
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   HELIX           170..183
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   TURN            184..187
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   STRAND          188..190
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   HELIX           201..209
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   HELIX           211..224
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   STRAND          230..235
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   STRAND          237..239
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   HELIX           240..246
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   HELIX           247..249
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   STRAND          256..262
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   STRAND          269..271
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   HELIX           275..278
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   STRAND          280..284
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   STRAND          287..291
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   HELIX           307..309
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   HELIX           316..323
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   STRAND          326..332
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   HELIX           334..347
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   HELIX           354..370
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   STRAND          375..380
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   STRAND          382..384
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   HELIX           385..387
FT                   /evidence="ECO:0007829|PDB:5KIN"
FT   HELIX           388..401
FT                   /evidence="ECO:0007829|PDB:5KIN"
SQ   SEQUENCE   407 AA;  44275 MW;  73BA3B7C7A78CE02 CRC64;
     MAYQEPNKDG FYGKFGGRFV PETLMTAVLE LEKAYRESQA DPSFQEELNQ LLRQYVGRET
     PLYYAKNLTQ HIGGAKIYLK REDLNHTGAH KINNALGQVW LAKRMGKKKI IAETGAGQHG
     VATATAAALF NMECTIYMGE EDVKRQALNV FRMELLGAKV EAVTDGSRVL KDAVNAALRS
     WVANIDDTHY ILGSALGPHP FPEIVRDFQS VIGREAKQQY RDLTGRDLPD ALVACVGGGS
     NAIGLFHPFV EDESVAMYGT EAAGLGVDTE HHAATLTKGR PGVLHGSLMD VLQDAHGQIL
     EAFSISAGLD YPGIGPEHSH YHDIKRASYV PVTDEEALEG FQLLSRVEGI IPALESSHAI
     AFAVKLAKEL GPEKSMIVCL SGRGDKDVVQ VKDRLEADAA KKGEAHA
 
 
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