TRPB1_WOLSU
ID TRPB1_WOLSU Reviewed; 403 AA.
AC Q7M9S1;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Tryptophan synthase beta chain 1;
DE EC=4.2.1.20;
GN Name=trpB1; OrderedLocusNames=WS0719;
OS Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC
OS 11488 / FDC 602W) (Vibrio succinogenes).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Wolinella.
OX NCBI_TaxID=273121;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC
RC 11488 / FDC 602W;
RX PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O.,
RA Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA Meyer F., Lederer H., Schuster S.C.;
RT "Complete genome sequence and analysis of Wolinella succinogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(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}.
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DR EMBL; BX571658; CAE09842.1; -; Genomic_DNA.
DR AlphaFoldDB; Q7M9S1; -.
DR SMR; Q7M9S1; -.
DR STRING; 273121.WS0719; -.
DR EnsemblBacteria; CAE09842; CAE09842; WS0719.
DR KEGG; wsu:WS0719; -.
DR eggNOG; COG0133; Bacteria.
DR HOGENOM; CLU_016734_3_1_7; -.
DR OMA; QWGMAVS; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000000422; 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..403
FT /note="Tryptophan synthase beta chain 1"
FT /id="PRO_0000099023"
FT MOD_RES 96
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 403 AA; 43806 MW; 3BB3A369658D08AA CRC64;
MMHKPYLKSF PNKEGYFGKY GGAYLPPLLI EHFKEIGEAY LKISQSFDFI QELKSIRKHY
QGRPTPLYYA RRLSQKAGGA AIYLKREDLN HTGAHKLNHC MAEALLAKHL GKKKLIAETG
AGQHGVALAT AAAYFGMECE IHMGEVDIAK EHPNVIRMKM LGAKVVPVSF GERTLKEAVD
SAFEAYLKDP ANAIYAIGSV VGPHPFPKMV RDFQSVVGAE AKEQFLEMTG ELPDHIVACV
GGGSNAMGIF SAFIDDPVEL WGVEPLGKGK SLGEHAASLS YGKEGVMHGF NSIMLQNEDG
SPASVHSVAS GLDYPSVGPE HAYLHEIGRT HSVGVSDEEA IKNFFALSRL EGIIPAIESA
HAIAYGMKLA KERLGEKILI NLSGRGDKDI DYVSETFGFG GEE
