TRPB2_COREF
ID TRPB2_COREF Reviewed; 439 AA.
AC Q8FT12;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 2.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Tryptophan synthase beta chain 2;
DE EC=4.2.1.20;
GN Name=trpB2; OrderedLocusNames=CE2880;
OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS / NBRC 100395).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX PubMed=12840036; DOI=10.1101/gr.1285603;
RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT "Comparative complete genome sequence analysis of the amino acid
RT replacements responsible for the thermostability of Corynebacterium
RT efficiens.";
RL Genome Res. 13:1572-1579(2003).
CC -!- FUNCTION: The beta subunit is responsible for the synthesis of L-
CC tryptophan from indole and L-serine. {ECO:0000250}.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 5/5.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC19690.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000035; BAC19690.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_006768763.1; NZ_GG700684.1.
DR AlphaFoldDB; Q8FT12; -.
DR SMR; Q8FT12; -.
DR STRING; 196164.23494725; -.
DR EnsemblBacteria; BAC19690; BAC19690; BAC19690.
DR KEGG; cef:CE2880; -.
DR eggNOG; COG0133; Bacteria.
DR HOGENOM; CLU_016734_3_1_11; -.
DR OrthoDB; 912282at2; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000001409; 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; Reference proteome; Tryptophan biosynthesis.
FT CHAIN 1..439
FT /note="Tryptophan synthase beta chain 2"
FT /id="PRO_0000098945"
FT MOD_RES 99
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 439 AA; 46998 MW; F3E6D7627B974584 CRC64;
MTTPATPTRQ TLLDAYFGEY GGQFVPEVLL PALDELERAY VEALEDPTFQ QELDDLYTNY
LGRPTPITEC ANLPLEGQGR GTARIFLKRE DLVHGGAHKG NQTIGQALLA KRLGKTRLIA
ETGAGQHGTA TAMVAALFGM KCTVYMGAKD VARQQPNVYR MRLMGAEVVA VDEQSGNGLS
SAIDVAINDW VNNLEDTHYL LGTAAGPHPF PTLVKKFHSV ISRESREQML ERTGALPDAV
VACVGGGSNA IGAFAQYLED QPGNEKVRLI GVEPAGYGLD TDLNGAPIHE GRTMHLHGSN
SYALLDEDGN LRNSHSVSAG LDYPGVGPEH AHLKDTGRAE YVGATDAEAL QAFRMLSRYE
GIIPALESSH ALAHALKMAA EATEPINILV NLSGRGDKDV AYVRQLLGDH AALDPATDVL
TEVDVLGVLE ELTPQADTA
