ID A0A165H8Y3_9BASI Unreviewed; 716 AA.
AC A0A165H8Y3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 13-SEP-2023, entry version 21.
DE RecName: Full=Tryptophan synthase {ECO:0000256|ARBA:ARBA00018724, ECO:0000256|RuleBase:RU003663};
DE EC=4.2.1.20 {ECO:0000256|ARBA:ARBA00012043, ECO:0000256|RuleBase:RU003663};
GN ORFNames=CALCODRAFT_431776 {ECO:0000313|EMBL:KZT58997.1};
OS Calocera cornea HHB12733.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Dacrymycetes;
OC Dacrymycetales; Dacrymycetaceae; Calocera.
OX NCBI_TaxID=1353952 {ECO:0000313|EMBL:KZT58997.1, ECO:0000313|Proteomes:UP000076842};
RN [1] {ECO:0000313|EMBL:KZT58997.1, ECO:0000313|Proteomes:UP000076842}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB12733 {ECO:0000313|EMBL:KZT58997.1,
RC ECO:0000313|Proteomes:UP000076842};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
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 ECO:0000256|RuleBase:RU003663};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|RuleBase:RU003663};
CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-
CC tryptophan from chorismate: step 5/5. {ECO:0000256|ARBA:ARBA00004733,
CC ECO:0000256|RuleBase:RU003663}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the TrpB family.
CC {ECO:0000256|ARBA:ARBA00005761}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the TrpA family.
CC {ECO:0000256|ARBA:ARBA00006095}.
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DR EMBL; KV423945; KZT58997.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165H8Y3; -.
DR STRING; 1353952.A0A165H8Y3; -.
DR InParanoid; A0A165H8Y3; -.
DR OrthoDB; 9569at2759; -.
DR UniPathway; UPA00035; UER00044.
DR Proteomes; UP000076842; Unassembled WGS sequence.
DR GO; GO:0004834; F:tryptophan synthase activity; IEA:UniProtKB-EC.
DR CDD; cd06446; Trp-synth_B; 1.
DR CDD; cd04724; Tryptophan_synthase_alpha; 1.
DR Gene3D; 3.40.50.1100; -; 2.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_00131; Trp_synth_alpha; 1.
DR HAMAP; MF_00133; Trp_synth_beta; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR InterPro; IPR006653; Trp_synth_b_CS.
DR InterPro; IPR006654; Trp_synth_beta.
DR InterPro; IPR023026; Trp_synth_beta/beta-like.
DR InterPro; IPR018204; Trp_synthase_alpha_AS.
DR InterPro; IPR002028; Trp_synthase_suA.
DR InterPro; IPR001926; TrpB-like_PALP.
DR InterPro; IPR036052; TrpB-like_PALP_sf.
DR NCBIfam; TIGR00262; trpA; 1.
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 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.
DR PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1.
DR PROSITE; PS00168; TRP_SYNTHASE_BETA; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW ECO:0000256|RuleBase:RU003663};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW ECO:0000256|RuleBase:RU003663};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU003663};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003663};
KW Reference proteome {ECO:0000313|Proteomes:UP000076842};
KW Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW ECO:0000256|RuleBase:RU003663}.
FT DOMAIN 363..689
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
SQ SEQUENCE 716 AA; 75927 MW; 216BC33D6DBDF945 CRC64;
MTESLKRVFA AKKAHGVPAF VTFVTAGYPS PADTVPLMFA MADGGADVIE LGVPFSDPIA
DGPAIQDSNN VALAFEVSYA HVLGMLRDAR NKGLTTPVLL MGYYNPLLSY GEEKAVQDAA
AAGANGFIMV DLPPEEAIRF RSICTREGIS YVPLVAPSTS LARIKFLASI ADSFIYVVSK
MGTTGSSAEV AMNVELPQLL ARIRAYTPVP LAVGFGVATR AHFQSVAAAG SDGVVVGSRI
VSLIKASPPG EMLGNVRKFC AELTNHASTM PTPAHIANGA GAQAVPAAPS PALPVPAAPA
AIPAELKVTE PTVLPSRFGA FGGQYVPEAL VDALAELEEA HKAALADPAF WAEFESFYGY
INRPSRLYHA ERLSAYAGGA NIWFKREDLN HTGSHKINNA IGQILLARRI GKKRIIAETG
AGQHGVATAT ACARFGLECV VYMGAEDVRR QALNVFRMKM LGAKVGAVIP VHSGSKTLKD
AINEAMRDWV TNLSTTHYLV GSAIGPHPFP TIVRDFQRII GREIKAQMAE IKGKLPDVVV
ACVGGGSNAI GTFYDFIKED GVRIVGVEAG GDGVDTARHS ATLALGTPGV LHGVRTYLLQ
SPTGQIIETH SISAGLDYPG VGPEHAWLKD SGRAQYIVAN DEEALRGFRM CTQLEGIIPA
LESAHAVWGA VQIAKTLPKD QDVVLCLSGR GDKDVEQISE ILPGQWADKL DWHIEM
//
