TRPB2_NOSS1
ID TRPB2_NOSS1 Reviewed; 413 AA.
AC Q8YQM6;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Tryptophan synthase beta chain 2;
DE EC=4.2.1.20;
GN Name=trpB2; OrderedLocusNames=all3794;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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; BA000019; BAB75493.1; -; Genomic_DNA.
DR PIR; AC2280; AC2280.
DR RefSeq; WP_010997935.1; NZ_RSCN01000011.1.
DR AlphaFoldDB; Q8YQM6; -.
DR SMR; Q8YQM6; -.
DR STRING; 103690.17132928; -.
DR EnsemblBacteria; BAB75493; BAB75493; BAB75493.
DR KEGG; ana:all3794; -.
DR eggNOG; COG0133; Bacteria.
DR OMA; HGMKSYF; -.
DR OrthoDB; 912282at2; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000002483; 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..413
FT /note="Tryptophan synthase beta chain 2"
FT /id="PRO_0000098911"
FT MOD_RES 107
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 413 AA; 44812 MW; E4C865B5F3A03BEE CRC64;
MTTTPLSPST PSNVQVPDIQ GRFGRFGGKY VPETLMPALA ELETAYQQYR NDPGFQAELQ
QLLRDYVGRA TPLYFAERLT AHYARPDGTG AQIYLKREDL NHTGAHKINN ALGQVLLAKR
MGKQRIIAET GAGQHGVATA TVCARFGLEC VIYMGVHDME RQALNVFRMR LMGAEVRPVA
AGTGTLKDAT SEAIRDWVTN VETTHYILGS VAGPHPYPMM VRDFHAVIGQ ETRAQALEKW
GGLPDILLAC VGGGSNAMGL FYEFVNESSI KLIGVEAAGE GVNTEKHAAT LTKGRVGVLH
GAMSYLLQDE DGQVIEAHSI SAGLDYPGVG PEHSYLKDVG RAEYYSVTDE EALAAFQRLS
RLEGIIPALE TAHAIAYLET LCPQLDGSPR IVINCSGRGD KDVQTVAKFL IPQ