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 27-MAR-2024, entry version 128.
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; Bacillota; 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_CP089948.1.
DR PDB; 5KIN; X-ray; 2.45 A; B/D=4-402.
DR PDBsum; 5KIN; -.
DR AlphaFoldDB; Q97P32; -.
DR SMR; Q97P32; -.
DR PaxDb; 170187-SP_1812; -.
DR EnsemblBacteria; AAK75885; AAK75885; SP_1812.
DR KEGG; spn:SP_1812; -.
DR eggNOG; COG0133; Bacteria.
DR PhylomeDB; Q97P32; -.
DR BioCyc; SPNE170187:G1FZB-1844-MONOMER; -.
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; IPR006653; Trp_synth_b_CS.
DR InterPro; IPR006654; Trp_synth_beta.
DR InterPro; IPR023026; Trp_synth_beta/beta-like.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR00263; trpB; 1.
DR PANTHER; PTHR48077:SF3; TRYPTOPHAN SYNTHASE; 1.
DR PANTHER; PTHR48077; TRYPTOPHAN SYNTHASE-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR PIRSF; PIRSF001413; Trp_syn_beta; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 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; Reference proteome; 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
//
