TRPB_METS4
ID TRPB_METS4 Reviewed; 406 AA.
AC B0UIA8;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 25-MAY-2022, entry version 79.
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=M446_2507;
OS Methylobacterium sp. (strain 4-46).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=426117;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4-46;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Marx C.J., Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium sp. 4-46.";
RL Submitted (FEB-2008) 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; CP000943; ACA16959.1; -; Genomic_DNA.
DR RefSeq; WP_012332366.1; NC_010511.1.
DR AlphaFoldDB; B0UIA8; -.
DR SMR; B0UIA8; -.
DR STRING; 426117.M446_2507; -.
DR EnsemblBacteria; ACA16959; ACA16959; M446_2507.
DR KEGG; met:M446_2507; -.
DR eggNOG; COG0133; Bacteria.
DR HOGENOM; CLU_016734_3_1_5; -.
DR OMA; HGMKSYF; -.
DR OrthoDB; 912282at2; -.
DR UniPathway; UPA00035; UER00044.
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_1000198751"
FT MOD_RES 99
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ SEQUENCE 406 AA; 43944 MW; ACF505D42C2D5435 CRC64;
MNAPQTPNSF RTGPDERGRF GIFGGRFVAE TLMPNILELE RAYAEAKADP AFQGEMNAYL
THYVGRPSPL YFAERLSAHF GGAKIYFKRE ELNHTGSHKV NNVLGQILLA RRMGKPRIIA
ETGAGQHGVA TATLCARFGL KCVVYMGAVD VERQKPNVFR MKMLGAEVVP VQSGTRTLKD
AMNEALRDWV TNVADTFYCI GTVAGPHPYP AMVRDFQSVI GRETREQMLA QEGRLPDSLV
ACIGGGSNAM GLFHPFLDDR EIEIYGVEAA GHGVSSGLHA ASLTGGKPGV LHGNRTYLLM
NEDGQIADAH SISAGLDYPG IGPEHAWLHE VGRVTYLSAT DSETLEAFRL CSLMEGIIPA
LEPAHALAKV AELAPTKPRD HLMVVNLSGR GDKDIPQVAE ILGDAL