TRPB_SINMW
ID TRPB_SINMW Reviewed; 406 AA.
AC A6UEI1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 80.
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=Smed_3237;
OS Sinorhizobium medicae (strain WSM419) (Ensifer medicae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=366394;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WSM419;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Reeve W.G.,
RA Richardson P.;
RT "Complete sequence of Sinorhizobium medicae WSM419 chromosome.";
RL Submitted (JUN-2007) 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; CP000738; ABR62061.1; -; Genomic_DNA.
DR RefSeq; WP_012067442.1; NC_009636.1.
DR RefSeq; YP_001328896.1; NC_009636.1.
DR AlphaFoldDB; A6UEI1; -.
DR SMR; A6UEI1; -.
DR STRING; 366394.Smed_3237; -.
DR EnsemblBacteria; ABR62061; ABR62061; Smed_3237.
DR KEGG; smd:Smed_3237; -.
DR PATRIC; fig|366394.8.peg.6475; -.
DR eggNOG; COG0133; Bacteria.
DR HOGENOM; CLU_016734_3_1_5; -.
DR OMA; HGMKSYF; -.
DR OrthoDB; 912282at2; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000001108; 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 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_1000018402"
FT MOD_RES 99
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ SEQUENCE 406 AA; 43762 MW; 48F37ED3D09CE6DD CRC64;
MNQPPKPNSF RSGPDEEGRF GIFGGRFVAE TLMPLILDLQ DEWARAKNDP AFKAELENLG
RHYIGRPSPL YFAERLTAEL GGAKIYFKRE ELNHTGSHKI NNCIGQILLA KRMGKTRIIA
ETGAGQHGVA SATVAARFGL PCVVYMGATD VERQAPNVFR MKLLGAEVKP VTAGHGTLKD
AMNEALRDWV TNVDSTYYLI GTAAGPHPYP EMVRDFQAVI GEEAKQQMLE AEGRLPDLVV
AAVGGGSNAI GIFHPFLDDG GVRIVGVEAG GKGLDGDEHC ASLTAGSPGV LHGNRTYLLQ
DGDGQIKEGH SISAGLDYPG IGPEHAWLND IGRVEYVPIM DHEALEAFQI LTRLEGIIPA
LEPSHALAEV IKRAPKMGKD EIILMNLSGR GDKDIFTVGK ILGMGQ