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Database: UniProt
Entry: G1AQS6_KITGR
LinkDB: G1AQS6_KITGR
Original site: G1AQS6_KITGR 
ID   G1AQS6_KITGR            Unreviewed;       247 AA.
AC   G1AQS6;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 40.
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:AEM36940.1};
OS   Kitasatospora griseola (Streptomyces griseolosporeus).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Kitasatospora.
OX   NCBI_TaxID=2064 {ECO:0000313|EMBL:AEM36940.1};
RN   [1] {ECO:0000313|EMBL:AEM36940.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KCTC 9745 {ECO:0000313|EMBL:AEM36940.1};
RA   Han J.-H., Cho M., Kim S.B.;
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEM36940.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KCTC 9745 {ECO:0000313|EMBL:AEM36940.1};
RX   PubMed=22154623; DOI=10.1016/j.syapm.2011.08.007;
RA   Han J.H., Cho M.H., Kim S.B.;
RT   "Ribosomal and protein coding gene based multigene phylogeny on the family
RT   Streptomycetaceae.";
RL   Syst. Appl. Microbiol. 35:1-6(2012).
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}.
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DR   EMBL; JF423982; AEM36940.1; -; Genomic_DNA.
DR   AlphaFoldDB; G1AQS6; -.
DR   GO; GO:0004834; F:tryptophan synthase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.1100; -; 2.
DR   InterPro; IPR006654; Trp_synth_beta.
DR   InterPro; IPR023026; Trp_synth_beta/beta-like.
DR   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR00263; trpB; 1.
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          7..246
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AEM36940.1"
FT   NON_TER         247
FT                   /evidence="ECO:0000313|EMBL:AEM36940.1"
SQ   SEQUENCE   247 AA;  26455 MW;  E0DA417A44C6A500 CRC64;
     LGQALLTRRM GKTRIIAETG AGQHGVATAT ACALFGFDCT IYMGEVDTQR QALNVARMRM
     LGAEVIPVKS GSRTLKDAIN EAFRDWVANV DSTHYLFGTV AGPHPFPMMV RDFHRVIGIE
     ARQQVLDRTG RLPDAVVACV GGGSNAMGIF HEFIPDAGVR LIGCEAAGDG ADTPKHAATL
     TKGDPGVLHG SRTYVLQDED GQTIESHSIS AGLDYPGVGP EHAWLEDTGR AEYRPVTDRA
     AMEALRL
//
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