GenomeNet

Database: UniProt
Entry: A0A061H612_9BASI
LinkDB: A0A061H612_9BASI
Original site: A0A061H612_9BASI 
ID   A0A061H612_9BASI        Unreviewed;       465 AA.
AC   A0A061H612;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   08-NOV-2023, entry version 45.
DE   RecName: Full=Chorismate synthase {ECO:0000256|ARBA:ARBA00013036, ECO:0000256|RuleBase:RU000605};
DE            EC=4.2.3.5 {ECO:0000256|ARBA:ARBA00013036, ECO:0000256|RuleBase:RU000605};
GN   ORFNames=PFL1_04199 {ECO:0000313|EMBL:EPQ28372.1};
OS   Pseudozyma flocculosa PF-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX   NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ28372.1, ECO:0000313|Proteomes:UP000053664};
RN   [1] {ECO:0000313|EMBL:EPQ28372.1, ECO:0000313|Proteomes:UP000053664}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PF-1 {ECO:0000313|EMBL:EPQ28372.1,
RC   ECO:0000313|Proteomes:UP000053664};
RX   PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA   Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA   Bakkeren G., Belanger R.R.;
RT   "The transition from a phytopathogenic smut ancestor to an anamorphic
RT   biocontrol agent deciphered by comparative whole-genome analysis.";
RL   Plant Cell 25:1946-1959(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-O-(1-carboxyvinyl)-3-phosphoshikimate = chorismate +
CC         phosphate; Xref=Rhea:RHEA:21020, ChEBI:CHEBI:29748,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57701; EC=4.2.3.5;
CC         Evidence={ECO:0000256|RuleBase:RU000605};
CC   -!- COFACTOR:
CC       Name=FMNH2; Xref=ChEBI:CHEBI:57618;
CC         Evidence={ECO:0000256|RuleBase:RU000605};
CC       Note=Reduced FMN (FMNH(2)). {ECO:0000256|RuleBase:RU000605};
CC   -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis;
CC       chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step
CC       7/7. {ECO:0000256|ARBA:ARBA00005044, ECO:0000256|RuleBase:RU000605}.
CC   -!- SIMILARITY: Belongs to the chorismate synthase family.
CC       {ECO:0000256|ARBA:ARBA00008014, ECO:0000256|RuleBase:RU000605}.
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; KE361635; EPQ28372.1; -; Genomic_DNA.
DR   RefSeq; XP_007879913.1; XM_007881722.1.
DR   AlphaFoldDB; A0A061H612; -.
DR   GeneID; 19318305; -.
DR   KEGG; pfp:PFL1_04199; -.
DR   eggNOG; KOG4492; Eukaryota.
DR   HOGENOM; CLU_034547_0_1_1; -.
DR   OrthoDB; 275401at2759; -.
DR   UniPathway; UPA00053; UER00090.
DR   Proteomes; UP000053664; Unassembled WGS sequence.
DR   GO; GO:0004107; F:chorismate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd07304; Chorismate_synthase; 1.
DR   Gene3D; 3.60.150.10; Chorismate synthase AroC; 2.
DR   HAMAP; MF_00300; Chorismate_synth; 1.
DR   InterPro; IPR000453; Chorismate_synth.
DR   InterPro; IPR035904; Chorismate_synth_AroC_sf.
DR   InterPro; IPR020541; Chorismate_synthase_CS.
DR   NCBIfam; TIGR00033; aroC; 2.
DR   PANTHER; PTHR21085; CHORISMATE SYNTHASE; 1.
DR   PANTHER; PTHR21085:SF0; CHORISMATE SYNTHASE; 1.
DR   Pfam; PF01264; Chorismate_synt; 1.
DR   SUPFAM; SSF103263; Chorismate synthase, AroC; 1.
DR   PROSITE; PS00787; CHORISMATE_SYNTHASE_1; 1.
DR   PROSITE; PS00788; CHORISMATE_SYNTHASE_2; 1.
DR   PROSITE; PS00789; CHORISMATE_SYNTHASE_3; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605,
KW   ECO:0000256|RuleBase:RU000605};
KW   Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141,
KW   ECO:0000256|RuleBase:RU000605};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000605};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053664}.
FT   REGION          171..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          434..465
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..465
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   465 AA;  50355 MW;  80C9114BA5EC9CE0 CRC64;
     MSTFGSHFRV TTWGESHCAS VGCIVDGVPP GMALTAADVQ TQLSRRRPGQ SNLTTPRDEK
     DRVEIQSGVE KDVTLGTPLA MLVRNQDQRP HDYTDETLDL FPRPSHADFT YLEKYGVKAS
     SGGGRSSARE TIGRVAAGAV AEKYLREAYG IEIVAFVSSV GKVHVPRYPG EQLAPSQPNT
     AAPVAANGDE GKSFYGEAAN AGPPQGKVDN IYNTDSLTEE EAEEPLSKEF RQLLATITRE
     QVDQNQIRCP HEEAAERMRQ RILLAKANND SIGGTVTCII RRVPSGLGEP CFDKLEAKLA
     HAMLSIPATK GFEIGSGFRG TEVAGSRHND KFILKDDGRL GTVTNWSGGI QGGISNGEDI
     YFRVGFKSPA TISQNQATSR YDGTDGTLNT RGRHDPCVVP RAVPIVEAMS ALVVMDALLA
     QDSRSLAATR LSREPVAALP QSMRMPEGKK RKQMETEEVE KSQQA
//
DBGET integrated database retrieval system