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Database: UniProt
Entry: A0A066X5Y0_COLSU
LinkDB: A0A066X5Y0_COLSU
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ID   A0A066X5Y0_COLSU        Unreviewed;       683 AA.
AC   A0A066X5Y0;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 33.
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};
DE   Flags: Fragment;
GN   ORFNames=CSUB01_06233 {ECO:0000313|EMBL:KDN64352.1};
OS   Colletotrichum sublineola (Sorghum anthracnose fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN64352.1, ECO:0000313|Proteomes:UP000027238};
RN   [1] {ECO:0000313|Proteomes:UP000027238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX   PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA   Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT   "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT   of cultivated sorghum.";
RL   Genome Announc. 2:E0054014-E0054014(2014).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KDN64352.1}.
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DR   EMBL; JMSE01001140; KDN64352.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A066X5Y0; -.
DR   STRING; 1173701.A0A066X5Y0; -.
DR   eggNOG; KOG1395; Eukaryota.
DR   eggNOG; KOG4175; Eukaryota.
DR   HOGENOM; CLU_016734_1_0_1; -.
DR   OMA; VDTARHS; -.
DR   OrthoDB; 9569at2759; -.
DR   UniPathway; UPA00035; UER00044.
DR   Proteomes; UP000027238; 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:UP000027238};
KW   Tryptophan biosynthesis {ECO:0000256|ARBA:ARBA00022822,
KW   ECO:0000256|RuleBase:RU003663}.
FT   DOMAIN          367..682
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   NON_TER         683
FT                   /evidence="ECO:0000313|EMBL:KDN64352.1"
SQ   SEQUENCE   683 AA;  73280 MW;  8DDBC955167928B0 CRC64;
     MEGIRQTFQR CKAQNRPALV TYVTAGYPTP QDTPNVLLAM EKGGADVIEL GAPFTDPIAD
     GPTIQTSNTV ALQHGVTIES TLKMVKDARD QGLKAPVMLM GYYNPLLSYG EERLLTDCKT
     SGVNGFIVVD LPPEEAISFR KLCTKGGLSY VPLIAPATSD ARMKILCKLA DSFIYVVSRQ
     GVTGASGSLN ANLPALVERV KKYSGNKPAA VGFGVSTREH FLSVSQLADG VVVGSQIITT
     LQKAAPGELC NDVEKYCAYL CGRDNANDET TREVGMVEAM AAAKEPTDPT VDETITADQD
     SSLVAELAAM HGKIPDRFGD FGGQYVPESL MDCLSELEEG FNKIKDDPSF WEEYRSYYDY
     MGRPGHLHLA ERLTEYAGGA NIWLKREDLN HTGSHKINNA LGQLLLAKRL GKTKIIAETG
     AGQHGVATAT VCAKFGMECT VYMGAEDVRR QALNVFRMKL LGAKVVAVEA GSKTLRDAVN
     EALRAWVVEL DTTHYIIGSA IGPHPFPTIV RTFQSVIGNE TKAQMLEKRG KLPDAVVACV
     GGGSNAVGMF YPFANDPSVR LLGVEAGGDG VDTPRHSATL SGGTKGVLHG VKTYILQDEH
     GQVAETHSVS AGLDYPGVGP ELSCWKDSER AKYVAATDAE AFIGFRLMSQ LEGIIPALET
     AHGIYGAIEL AKTMNKGEDV VIC
//
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