ID O05628_STRGR Unreviewed; 109 AA.
AC O05628;
DT 01-JUL-1997, integrated into UniProtKB/TrEMBL.
DT 01-JUL-1997, sequence version 1.
DT 28-JUN-2023, entry version 67.
DE RecName: Full=tryptophan synthase {ECO:0000256|ARBA:ARBA00012043};
DE EC=4.2.1.20 {ECO:0000256|ARBA:ARBA00012043};
DE Flags: Fragment;
GN Name=trpB {ECO:0000313|EMBL:AAB52400.1};
OS Streptomyces griseus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1911 {ECO:0000313|EMBL:AAB52400.1};
RN [1] {ECO:0000313|EMBL:AAB52400.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=N2-3-11 {ECO:0000313|EMBL:AAB52400.1};
RX PubMed=9097426;
RA Huddleston A.S., Cresswell N., Neves M.C., Beringer J.E., Baumberg S.,
RA Thomas D.I., Wellington E.M.;
RT "Molecular detection of streptomycin-producing streptomycetes in Brazilian
RT soils.";
RL Appl. Environ. Microbiol. 63:1288-1297(1997).
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:0000256|ARBA:ARBA00000003};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 5/5. {ECO:0000256|ARBA:ARBA00004733}.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains.
CC {ECO:0000256|ARBA:ARBA00011270}.
CC -!- SIMILARITY: Belongs to the TrpB family.
CC {ECO:0000256|ARBA:ARBA00009982}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U72183; AAB52400.1; -; Genomic_DNA.
DR AlphaFoldDB; O05628; -.
DR GO; GO:0004834; F:tryptophan synthase activity; IEA:InterPro.
DR Gene3D; 3.40.50.1100; -; 1.
DR InterPro; IPR023026; Trp_synth_beta/beta-like.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR PANTHER; PTHR48077:SF3; TRYPTOPHAN SYNTHASE; 1.
DR PANTHER; PTHR48077; TRYPTOPHAN SYNTHASE-RELATED; 1.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822}.
FT DOMAIN 14..71
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAB52400.1"
SQ SEQUENCE 109 AA; 11460 MW; B07FAB85BFF14C1D CRC64;
PGIGPEHSYL KDVGRGEYRA VTDDAAMQAL RLLSRTEGII PAIESAHALA GALDLGKELG
KDGLILVNLS GRGDKDMDTA ARYFGLYDAD AAVEADADSD RAEIEGDAK
//
