ID A0A2G7FRS3_9EURO Unreviewed; 1174 AA.
AC A0A2G7FRS3;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=3-deoxy-7-phosphoheptulonate synthase {ECO:0000256|ARBA:ARBA00012694};
DE EC=2.5.1.54 {ECO:0000256|ARBA:ARBA00012694};
GN ORFNames=AARAC_001079 {ECO:0000313|EMBL:PIG83327.1};
OS Aspergillus arachidicola.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=656916 {ECO:0000313|EMBL:PIG83327.1, ECO:0000313|Proteomes:UP000231358};
RN [1] {ECO:0000313|EMBL:PIG83327.1, ECO:0000313|Proteomes:UP000231358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 117610 {ECO:0000313|EMBL:PIG83327.1,
RC ECO:0000313|Proteomes:UP000231358};
RA Moore G., Beltz S.B., Mack B.M.;
RT "Genome sequence for an aflatoxigenic pathogen of Argentinian peanut,
RT Aspergillus arachidicola.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-erythrose 4-phosphate + H2O + phosphoenolpyruvate = 7-
CC phospho-2-dehydro-3-deoxy-D-arabino-heptonate + phosphate;
CC Xref=Rhea:RHEA:14717, ChEBI:CHEBI:15377, ChEBI:CHEBI:16897,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58394, ChEBI:CHEBI:58702; EC=2.5.1.54;
CC Evidence={ECO:0000256|ARBA:ARBA00001370};
CC -!- SIMILARITY: Belongs to the class-I DAHP synthase family.
CC {ECO:0000256|ARBA:ARBA00007985}.
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:PIG83327.1}.
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DR EMBL; NEXV01000455; PIG83327.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G7FRS3; -.
DR STRING; 656916.A0A2G7FRS3; -.
DR OrthoDB; 2309095at2759; -.
DR Proteomes; UP000231358; Unassembled WGS sequence.
DR GO; GO:0003849; F:3-deoxy-7-phosphoheptulonate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006218; DAHP1/KDSA.
DR InterPro; IPR006219; DAHP_synth_1.
DR NCBIfam; TIGR00034; aroFGH; 1.
DR PANTHER; PTHR21225; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE DAHP SYNTHETASE; 1.
DR PANTHER; PTHR21225:SF18; PHOSPHO-2-DEHYDRO-3-DEOXYHEPTONATE ALDOLASE, PHENYLALANINE-INHIBITED; 1.
DR Pfam; PF00793; DAHP_synth_1; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW Aromatic amino acid biosynthesis {ECO:0000256|ARBA:ARBA00023141};
KW Reference proteome {ECO:0000313|Proteomes:UP000231358}.
FT DOMAIN 857..1156
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
FT REGION 101..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..292
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 425..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 495..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..397
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..541
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1174 AA; 128253 MW; 85A2377B7E01159C CRC64;
METCFGAGYD DQNPVYMAEL NLVTRLRSAA TESEGDMGIH FSGDMVEHLL RDDTPLETNN
VNEIELSVST IKSKTQRSSS AVVSLDTAEV VVRKSKRISE ARARSNESAV TASQNRQLMS
RNKPSALSFN NKNNPQLSNT QESLIFHSRR AYRRVYAAHR KAAVDWDEDL RPSGESELSK
GDELTPVSSP TSGKRSAFYK KPVMAQKGTR EASSSAGNRR RPLAQSTGSA IKERGCISKA
VSYDVSVNKA IEVPGYKRGL RNFENIGIRN EDHSSSSDSE HPVSGKCATD DGNLIEISSK
GETSWLKIEE HRQHAPVPNL AVHSGDDHGD DAHAHVTDAN AFGLSQTSPK PRLLGEKHIG
RGQSIGGKLA AAFQLEEASS QCKRYHNHGH DAPPDHKSQS NPETATSSAP SIEVLPREKL
LEPILSENDE DQGDHYMVPR SSDTDRLNLF IGQKRPDEVR ETKQNNSQGV LGETEMISAS
IETVALGGGR WETKAGADGF MSPTNSRQSR RHAQPRYGNT PIIRSDHSSS ISSSEAAKSK
SCSGSDEPAP GPESSGIMRA AISDHSVPVF TKSLLPHDSQ QAQEHTAEHQ RTTPRKSIVD
PNGSPRLLSH MENKLIISDG TVHCEGQSGQ LTQDVKQSPA RSIVDESGYD GSIEESFVEV
SDARNTLATT TCGESYGVRI GDPFAQGPIL PKSCEGQTRS VRRNLFRAAS EPHRQHSRVD
IASQCPYQSL LQGELASIDP PWDTAVTSST HGKNLKETNG DTSLQALQRY TQSLLLDSSN
RLKRGLETEK QTVHSVLETY RRQCHRVLDQ LFEAQEERIN LFRGYNPLTP PNLLQHEIAM
TETSRQTVLQ ARQEASAVVH GTDTDKRRLL VVVGPCSIHD PEMALEYCDR LLKLKEKYKD
ELLIVMRAYL EKPRTTVGWK GLINDPDIDN SFKINKGLRT SRQLFVDLTN KGMPIASEML
DTISPQFLAD CLSVGAVGAR TTESQVHREL ASGLSFPVGF KNGTDGSLDV AVDAIGSVKH
PHHFLSVTKP GVVSIVGTVG NPDCFVILRG GKKGPNYDAQ SIAEAKAKLS AQGMEPRLMV
DCSHGNSQKN HKNQPKVAAV LAEQIAAGET AIMGVMIESN INEGNQKVPP EGKAGLKYGV
SITDACIHWE DTEAVLENLA QAVRTRKEKL AVNN
//
