ID A0A1V6Q3A5_9EURO Unreviewed; 1168 AA.
AC A0A1V6Q3A5;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, 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=PENANT_c015G01520 {ECO:0000313|EMBL:OQD83733.1};
OS Penicillium antarcticum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD83733.1, ECO:0000313|Proteomes:UP000191672};
RN [1] {ECO:0000313|Proteomes:UP000191672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQD83733.1}.
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DR EMBL; MDYN01000015; OQD83733.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6Q3A5; -.
DR STRING; 416450.A0A1V6Q3A5; -.
DR OrthoDB; 2332549at2759; -.
DR Proteomes; UP000191672; 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:UP000191672}.
FT DOMAIN 854..1152
FT /note="DAHP synthetase I/KDSA"
FT /evidence="ECO:0000259|Pfam:PF00793"
FT REGION 1..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 479..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 539..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..606
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..86
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..592
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..702
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1168 AA; 128063 MW; F3BDDF26DD854A64 CRC64;
MSAIKDHVPV DSGFIDSGPK DSVATRSRSP APAVYNRRIS GRQKPKATSP QRGPVVPRLK
LTKPRKPKSN SLEVDWEEDL RPTPNESKDN QEAVASASGG PGTTDKKSTG KREIQFKDPA
VLAKRRKTNP KESATAMKNN IKVPQLPLIT LDTVVAPTAQ DKAFVGLGIS NGGSAIKNIG
DMPEASHRKL PQNNGPFGNA NKGKQPVVIE IPSCTSVSSG TPFYPDYEDQ GPFRETTSKV
SIMEYRAQSQ IQGNRENPVC KRPTTASSSD IDYLGSSRPS ASKVTILQAR IQPKRQTRKA
NVAHDKKGSG RHGRAESVGS KLMLALQGAM VSSQSQASAE KEAIIVRRSN TPTNPVQTEE
PFDKQSLEHL PAEEPTKILE VDRAQDDTKL NEKNGQQADP DPGNEDSMDR TNQPSIEEHQ
QTDLTQLWES LSSTHGDSSD LEVGRGLVGD HPSVLDYHME MEHLPGFAAL EPIRSLPNTS
SQATNLYQSQ DDTSSETSSA EMATEIQEIT AASAQGREYT LTPESQKPLL ANEVLMELDS
SPKPPKSVPK ASIVDSNGSP RLMLRHTKNA DVPELALEDD PNHKEEIRAT DSRPSQYSRS
SCDLATDDTH DSLVWTKFQR DMFLEYGIQT EKLKQTRLDP RPLSVYHPPS LPQEGTAEAM
DADRTSNSSQ RTLDEKKLKT SASENRGPID RTWCHKAPES HRANPESQPS TLAHDPMEWI
TALGVAQKNA HDLLHETNSH LSTQLAAEKA TITQVLEIYR KGCGQILDDL FQAQEVRMQM
YQQQMQYVKG QHALICEDMF FIDNPNVGNH SHLEDSRILG YNPLTPPNLL QHEIALTDKS
RETVLKGRDE AVAVVHGTDT ERQRLMVVIG PCSIHDPEMA LEYCDRLMKM KEKYADDLLI
VMRSYLEKPR TTVGWKGLIN DPDIDNSFKI NKGLRISRQL FVDLTNKGMP IASEMLDTIS
PQFLADCLSV GAVGARTTES QVHRELSSGL SFPVGFKNGT DGSLDVAVDA IGSVKHPHHF
LSVTKPGVVS IVGTVGNPDC FVILRGGKKG PNYDAASIAD AKAKLNAKGM RPRLMVDCSH
GNSEKNHKNQ PKVAAVLAEQ LAAGEDAIMG VMIESNINEG NQKVPAEGKS GLKYGVSITD
ACINWEDTED VLEVLAQGVR ARRAKTTK
//
