ID A0A0C3IQ62_PISTI Unreviewed; 467 AA.
AC A0A0C3IQ62;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=tryptophan synthase {ECO:0000256|ARBA:ARBA00012043};
DE EC=4.2.1.20 {ECO:0000256|ARBA:ARBA00012043};
GN ORFNames=M404DRAFT_30710 {ECO:0000313|EMBL:KIN99092.1};
OS Pisolithus tinctorius Marx 270.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Sclerodermatineae; Pisolithaceae; Pisolithus.
OX NCBI_TaxID=870435 {ECO:0000313|EMBL:KIN99092.1, ECO:0000313|Proteomes:UP000054217};
RN [1] {ECO:0000313|EMBL:KIN99092.1, ECO:0000313|Proteomes:UP000054217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marx 270 {ECO:0000313|EMBL:KIN99092.1,
RC ECO:0000313|Proteomes:UP000054217};
RG DOE Joint Genome Institute;
RA Kuo A., Kohler A., Costa M.D., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000054217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marx 270 {ECO:0000313|Proteomes:UP000054217};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
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; KN832008; KIN99092.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3IQ62; -.
DR STRING; 870435.A0A0C3IQ62; -.
DR HOGENOM; CLU_016734_3_0_1; -.
DR InParanoid; A0A0C3IQ62; -.
DR OrthoDB; 9569at2759; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000054217; Unassembled WGS sequence.
DR GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.1100; -; 2.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR InterPro; IPR023026; Trp_synth_beta/beta-like.
DR InterPro; IPR002028; Trp_synthase_suA.
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 Pfam; PF00290; Trp_syntA; 1.
DR SUPFAM; SSF51366; Ribulose-phoshate binding barrel; 1.
DR SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000054217};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822}.
FT DOMAIN 183..460
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
SQ SEQUENCE 467 AA; 51095 MW; F0B138C3F40425F9 CRC64;
MPHLPDGNHR LFHQNGFMNS ELPDIIARIR KHASVPLAVD FGVATCIHFD IAVEAEADGV
VVGSRIVSLI KEAPAGQVPQ LVENFCRGFK GSSPSNSSTA GVQSSRYHYP VVAVITRPTG
MSLLPPRFCR YVLEAHYDCL LELEEASNAT RNNPMFWDEF ESHYGYMNCP SKLYDLAETR
RSQPYGSHKI NNAVGQILLA IRLGKTRVIA ETGARQHGVA TATVCACVGM ECVIYMSADD
VRRQALNVFC MRMLGAKVVA VESGSKTLKD AVNEAMGDWV TNLATTHFLI GSCYGHQPSL
TIVRDYRKLI GREIKAEMKE ATGKLPDVVV ACVGGGSNAV GSFYEFIPDT SVHLVGVAAG
GEGMYGYRRS ATLARGKPGR RTISARFDYP GVGPEHPWWK DSKRAEYVVV THEEALRGFC
LCTQLKGIVP ALEPLHALWE VIPRAKTLPK KTNSVICLSG RGDKDVE
//
