TRPB_TRIV2
ID TRPB_TRIV2 Reviewed; 413 AA.
AC Q3MBV3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 99.
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=Ava_1911;
OS Trichormus variabilis (strain ATCC 29413 / PCC 7937) (Anabaena variabilis).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Trichormus.
OX NCBI_TaxID=240292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29413 / PCC 7937;
RX PubMed=25197444; DOI=10.4056/sigs.3899418;
RA Thiel T., Pratte B.S., Zhong J., Goodwin L., Copeland A., Lucas S., Han C.,
RA Pitluck S., Land M.L., Kyrpides N.C., Woyke T.;
RT "Complete genome sequence of Anabaena variabilis ATCC 29413.";
RL Stand. Genomic Sci. 9:562-573(2014).
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; CP000117; ABA21533.1; -; Genomic_DNA.
DR AlphaFoldDB; Q3MBV3; -.
DR SMR; Q3MBV3; -.
DR STRING; 240292.Ava_1911; -.
DR EnsemblBacteria; ABA21533; ABA21533; Ava_1911.
DR KEGG; ava:Ava_1911; -.
DR eggNOG; COG0133; Bacteria.
DR HOGENOM; CLU_016734_3_1_3; -.
DR OMA; HGMKSYF; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000002533; 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; Tryptophan biosynthesis.
FT CHAIN 1..413
FT /note="Tryptophan synthase beta chain"
FT /id="PRO_1000018319"
FT MOD_RES 107
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00133"
SQ SEQUENCE 413 AA; 44906 MW; 21D3E6435F44FB05 CRC64;
MTTTPLSPST PSNAQVPDIQ GRFGRFGGKY VPETLMPALA ELETAYQKYR HDPGFQAELQ
QLLRDYVGRA TPLYFAERLT AHYARPDGTG AQIYLKREDL NHTGAHKINN ALGQVLLAKR
MGKQRIIAET GAGQHGVATA TVCARFGLEC VIYMGVHDME RQALNVFRMR LMGAEVRPVE
AGTGTLKDAT SEAIRDWVTN VETTHYILGS VAGPHPYPMM VRDFHAVIGQ ETRAQALEKW
GGLPDILLAC VGGGSNAMGL FYEFVNESSI RLIGVEAAGE GVNTEKHAAT LTKGRVGVLH
GAMSYLLQDE DGQVIEAHSI SAGLDYPGVG PEHSYLKDVG RAEYYSVTDE QALAAFQRLS
RLEGIIPALE TAHAIAYLET LCPQLDGSPR IIINCSGRGD KDVQTVAKFL IPQ
