TRPB_FRATT
ID TRPB_FRATT Reviewed; 396 AA.
AC Q5NE79;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=FTT_1773c;
OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=177416;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCHU S4 / Schu 4;
RX PubMed=15640799; DOI=10.1038/ng1499;
RA Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT "The complete genome sequence of Francisella tularensis, the causative
RT agent of tularemia.";
RL Nat. Genet. 37:153-159(2005).
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; AJ749949; CAG46406.1; -; Genomic_DNA.
DR RefSeq; WP_003022755.1; NZ_CP010290.1.
DR RefSeq; YP_170663.1; NC_006570.2.
DR PDB; 5KZM; X-ray; 2.80 A; B=1-396.
DR PDBsum; 5KZM; -.
DR AlphaFoldDB; Q5NE79; -.
DR SMR; Q5NE79; -.
DR IntAct; Q5NE79; 4.
DR STRING; 177416.FTT_1773c; -.
DR DNASU; 3190984; -.
DR EnsemblBacteria; CAG46406; CAG46406; FTT_1773c.
DR GeneID; 39482396; -.
DR KEGG; ftu:FTT_1773c; -.
DR eggNOG; COG0133; Bacteria.
DR OMA; HGMKSYF; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000001174; 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; Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..396
FT /note="Tryptophan synthase beta chain"
FT /id="PRO_1000018345"
FT MOD_RES 86
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
FT STRAND 7..10
FT /evidence="ECO:0007829|PDB:5KZM"
FT HELIX 18..20
FT /evidence="ECO:0007829|PDB:5KZM"
FT HELIX 21..36
FT /evidence="ECO:0007829|PDB:5KZM"
FT HELIX 38..50
FT /evidence="ECO:0007829|PDB:5KZM"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:5KZM"
FT TURN 64..67
FT /evidence="ECO:0007829|PDB:5KZM"
FT STRAND 68..76
FT /evidence="ECO:0007829|PDB:5KZM"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:5KZM"
FT HELIX 88..98
FT /evidence="ECO:0007829|PDB:5KZM"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:5KZM"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:5KZM"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:5KZM"
FT HELIX 113..124
FT /evidence="ECO:0007829|PDB:5KZM"
FT STRAND 128..134
FT /evidence="ECO:0007829|PDB:5KZM"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:5KZM"
FT HELIX 142..150
FT /evidence="ECO:0007829|PDB:5KZM"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:5KZM"
FT HELIX 165..179
FT /evidence="ECO:0007829|PDB:5KZM"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:5KZM"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:5KZM"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:5KZM"
FT HELIX 196..204
FT /evidence="ECO:0007829|PDB:5KZM"
FT HELIX 206..218
FT /evidence="ECO:0007829|PDB:5KZM"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:5KZM"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:5KZM"
FT HELIX 234..240
FT /evidence="ECO:0007829|PDB:5KZM"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:5KZM"
FT STRAND 249..258
FT /evidence="ECO:0007829|PDB:5KZM"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:5KZM"
FT TURN 270..272
FT /evidence="ECO:0007829|PDB:5KZM"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:5KZM"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:5KZM"
FT HELIX 301..303
FT /evidence="ECO:0007829|PDB:5KZM"
FT HELIX 310..317
FT /evidence="ECO:0007829|PDB:5KZM"
FT STRAND 320..327
FT /evidence="ECO:0007829|PDB:5KZM"
FT HELIX 328..340
FT /evidence="ECO:0007829|PDB:5KZM"
FT HELIX 348..363
FT /evidence="ECO:0007829|PDB:5KZM"
FT STRAND 369..375
FT /evidence="ECO:0007829|PDB:5KZM"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:5KZM"
FT HELIX 380..382
FT /evidence="ECO:0007829|PDB:5KZM"
FT HELIX 383..393
FT /evidence="ECO:0007829|PDB:5KZM"
SQ SEQUENCE 396 AA; 43079 MW; E2A4B441C8930606 CRC64;
MSKLNAYFGE YGGQFVPQIL VPALDQLEQE FIKAQADESF KQEFKELLQE YAGRPTALTK
TRNIVKNTRT KLYLKREDLL HGGAHKTNQV LGQALLAKRM GKKEIIAETG AGQHGVATAL
ACALLDLKCR VYMGAKDVER QSPNVFRMKL MGAEVIPVHS GSATLKDACN EALRDWSANY
SKAHYLLGTA AGPHPFPTIV REFQRMIGEE TKQQMLAKEG RLPDAVIACV GGGSNAIGMF
ADFIDEKNVK LIGVEPAGKG IETGEHGAPL KHGKTGIFFG MKAPLMQNSD GQIEESYSIS
AGLDFPSVGP QHAHLLAIGR AKYASATDDE ALDAFKLLCK KEGIIPALES SHALAHALKL
AYEDPNKEQL LVVNLSGRGD KDIFTVHDIL KEKGEI
