TRPB_OCEIH
ID TRPB_OCEIH Reviewed; 399 AA.
AC Q8ESU4;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 25-MAY-2022, entry version 117.
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=OB0522;
OS Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS 3954 / HTE831).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=221109;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX PubMed=12235376; DOI=10.1093/nar/gkf526;
RA Takami H., Takaki Y., Uchiyama I.;
RT "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT and its unexpected adaptive capabilities to extreme environments.";
RL Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC12478.1; -; Genomic_DNA.
DR RefSeq; WP_011064925.1; NC_004193.1.
DR AlphaFoldDB; Q8ESU4; -.
DR SMR; Q8ESU4; -.
DR STRING; 221109.22776201; -.
DR EnsemblBacteria; BAC12478; BAC12478; BAC12478.
DR KEGG; oih:OB0522; -.
DR eggNOG; COG0133; Bacteria.
DR HOGENOM; CLU_016734_3_1_9; -.
DR OMA; HGMKSYF; -.
DR OrthoDB; 912282at2; -.
DR PhylomeDB; Q8ESU4; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000000822; 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..399
FT /note="Tryptophan synthase beta chain"
FT /id="PRO_0000098975"
FT MOD_RES 92
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ SEQUENCE 399 AA; 43449 MW; 0009E5661C11BBA5 CRC64;
MTTYSFPNTK GKYGEFGGRF VPELLMPAVL ELEKAYEDAL KDESFNEELQ TYLTEYIGRE
TPLYHAKKLT EHAGGAQIYL KREDLNHTGA HKINNTIGQA LLTLRMGKKK VVAETGAGQH
GVATATVCSL LGLECIVFMG EEDIKRQKLN VFRMELLGAE VVSVSQGSGT LKDAVNEALR
YWVNNVNDTH YIIGSVVGPH PFPKIVRDFQ SVIGKETKEQ SMKKIGSLPD AVVACVGGGS
NAMGMFYPFI DDKEVTLFGV EAAGAGLDTK QHAATLTGGS PGMLHGTFTY LLQDDCGQIE
EAFSISAGLD YPGIGPEHSH LHQTKRVTYS SITDEEALEA FQLLSKTEGI IPALESAHAV
SYATKLAKEM NPEQSIVICL SGRGDKDVEQ VKERLEGEQ
