TRPB_BRUMB
ID TRPB_BRUMB Reviewed; 406 AA.
AC C0RFZ4;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 68.
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=BMEA_A2170;
OS Brucella melitensis biotype 2 (strain ATCC 23457).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=546272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23457;
RA Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W., Lu J.,
RA Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M., Snyder E.E.,
RA Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., Munk C., Tapia R.,
RA Han C., Detter J.C., Bruce D., Brettin T.S.;
RT "Brucella melitensis ATCC 23457 whole genome shotgun sequencing project.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001488; ACO01816.1; -; Genomic_DNA.
DR RefSeq; WP_004686731.1; NC_012441.1.
DR AlphaFoldDB; C0RFZ4; -.
DR SMR; C0RFZ4; -.
DR EnsemblBacteria; ACO01816; ACO01816; BMEA_A2170.
DR GeneID; 29594913; -.
DR KEGG; bmi:BMEA_A2170; -.
DR HOGENOM; CLU_016734_3_1_5; -.
DR OMA; HGMKSYF; -.
DR UniPathway; UPA00035; UER00044.
DR PRO; PR:C0RFZ4; -.
DR Proteomes; UP000001748; Chromosome I.
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..406
FT /note="Tryptophan synthase beta chain"
FT /id="PRO_1000198741"
FT MOD_RES 99
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ SEQUENCE 406 AA; 43525 MW; 517F7BD6C69E24A1 CRC64;
MNKPVAPNSY KTGPDEEGMF GIFGGRFVAE TLMPLILELQ QAYETAKNDP EFKAELNALS
TFYAGRPSKL YYAEGLSKHL GGAKIYFKRE DLNHTGSHKI NNCLGQILLA KRMGKTRIIA
ETGAGQHGVA SATVAARFGL PCIVYVGASD VERQKPNVFR MKLLGAEVKP VSAGNGTLKD
AMNEALRDWV TNVEDTYYLI GTAAGPHPYP ELVRDFQSVI GTEARQQILE QEGRLPDVIV
AAVGGGSNAI GLFHPFLDDA SVKIVGVEAG GRGLEGEEHC ASMSAGRPGV LHGNRTYLLQ
NADGQILEGH SVSAGLDYPG VGPEHSWLKD SGRVDYVPIL DNEALDAFQL CTRTEGIIPA
LESAHAIAQA VKMAPTMGKD KVMIVNLSGR GDKDVHTVGK LLGMDI