ID A0A0A2KEG4_PENEN Unreviewed; 1967 AA.
AC A0A0A2KEG4;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Dihydroxy-acid/6-phosphogluconate dehydratase {ECO:0000313|EMBL:KGO60384.1};
GN ORFNames=PEX2_033730 {ECO:0000313|EMBL:KGO60384.1};
OS Penicillium expansum (Blue mold rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=27334 {ECO:0000313|EMBL:KGO60384.1, ECO:0000313|Proteomes:UP000030143};
RN [1] {ECO:0000313|EMBL:KGO60384.1, ECO:0000313|Proteomes:UP000030143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MD-8 {ECO:0000313|EMBL:KGO60384.1,
RC ECO:0000313|Proteomes:UP000030143};
RX PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT "Genome, transcriptome, and functional analyses of Penicillium expansum
RT provide new insights into secondary metabolism and pathogenicity.";
RL Mol. Plant Microbe Interact. 28:232-248(2015).
CC -!- SIMILARITY: Belongs to the IlvD/Edd family.
CC {ECO:0000256|ARBA:ARBA00006486}.
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:KGO60384.1}.
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DR EMBL; JQFZ01000074; KGO60384.1; -; Genomic_DNA.
DR RefSeq; XP_016601450.1; XM_016740648.1.
DR STRING; 27334.A0A0A2KEG4; -.
DR GeneID; 27676067; -.
DR HOGENOM; CLU_001870_0_0_1; -.
DR OrthoDB; 3686044at2759; -.
DR PhylomeDB; A0A0A2KEG4; -.
DR Proteomes; UP000030143; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004497; F:monooxygenase activity; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR GO; GO:0043386; P:mycotoxin biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044238; P:primary metabolic process; IEA:UniProt.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR Gene3D; 3.50.30.80; IlvD/EDD C-terminal domain-like; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
DR InterPro; IPR048591; Ctf4-like_C.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR036396; Cyt_P450_sf.
DR InterPro; IPR042096; Dihydro-acid_dehy_C.
DR InterPro; IPR000581; DiOHA_6PGluconate_deHydtase.
DR InterPro; IPR020558; DiOHA_6PGluconate_deHydtase_CS.
DR InterPro; IPR037237; IlvD/EDD_N.
DR InterPro; IPR022100; Mcl1_mid.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001680; WD40_rpt.
DR PANTHER; PTHR43183:SF1; HYPOTHETICAL DIHYDROXY-ACID DEHYDRATASE (EUROFUNG)-RELATED; 1.
DR PANTHER; PTHR43183; HYPOTHETICAL DIHYDROXYACID DEHYDRATASE (EUROFUNG)-RELATED; 1.
DR Pfam; PF20946; Ctf4_C; 1.
DR Pfam; PF00920; ILVD_EDD; 1.
DR Pfam; PF12341; Mcl1_mid; 1.
DR Pfam; PF00067; p450; 1.
DR Pfam; PF00400; WD40; 1.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR SUPFAM; SSF143975; IlvD/EDD N-terminal domain-like; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS00886; ILVD_EDD_1; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000256|ARBA:ARBA00023239}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000030143};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW WD repeat {ECO:0000256|ARBA:ARBA00022574, ECO:0000256|PROSITE-
KW ProRule:PRU00221}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REPEAT 1139..1180
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT REPEAT 1357..1398
FT /note="WD"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00221"
FT DOMAIN 1547..1834
FT /note="Minichromosome loss protein Mcl1 middle region"
FT /evidence="ECO:0000259|Pfam:PF12341"
FT DOMAIN 1854..1958
FT /note="DNA polymerase alpha-binding protein Ctf4-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF20946"
SQ SEQUENCE 1967 AA; 217016 MW; 9B05DE80CE204594 CRC64;
MERYETLSLV QAIREKYFGV NWSTVFAIVV FVCITTRIIS GLQSRRERDP SKPQTVRLAP
YWFPWIGHGP AFLWNHVTFF TRTRKSMNEP VFGIYIRGVK HNVVASPSMM KTALSVKSAT
THSQVLDQAL HNVFGDRGLI RHLDMDRHQG VSDKAPTILN EEAFVAEASS AITRLVQREM
PNLVSFCRSI VDQYPWERGI SGVELPDEGD QTVCEANLFA LVSNFIGHVT STFLMGEAFV
ENFPNLSEDL GRLDDCFVTL FLGTPRWAPH PAASAGHAAS DRLCHIFSVF HRAFTAWDDG
IDPGIELRDL DDVSELFKDR MRTFRKLELS PGASAAGHLS LYYDLIEHTT KITFWTITHL
YAEPSLLDQV RKEIAPYVVA SRPTREETGF PFDEPPRLSL DIEKVLTSCP LFKACYYETV
RLHSAGISFN NLASDVTLSE SAEEAAYGLT EPRTYKIAKG EDIIVPHGAY YHDARYFSNP
EQYDPLRFLV TDPATGKQRA DSNILAPFAD GLYGSTNNGF TERAILTFTA GIVVLWDIEP
TNSKFLSVPG HKTSWGAFRP TKELRVKMKL RNPNRDYDLT TPIISTTGLR QGLTSYGDAH
FSLFLRKVFI KALGYSEDAL SRPIVGIINT FSGFNPCHAN VPQLIEAAKR GVQLNGGLAI
EFPTISVAES FSHPTSMFLR NLMSMDTEEM IRAQPLDACI MIGGCDKTVP AQLMGGISAN
KPILPLITGP MMPGSHRGQR IGACTDCRNN WAAFRAGEID VEEISAINEE LAPTMGTCGV
MGTASTMACV TAALGMMPLR GATAPAVSSA RLRIAEETGA NAVLIAKSKR KPQEILTKES
FWNAITVLQA IGGSTNAVVH LLAIANRHPE LQGVITLDTI EEIGRKTPLL IDLKPSGDNY
MNDFHNAGGM MALLHVLRPL LHLSALTITG QTLGEVLDAS QSKRLSFAQQ IIRPMSDPLF
PASSLAVLRG NLAPDGAVLK ASASKYRHLL SHTGPAVVFE NSADLAQRID DPNLVVTKDS
VLVLKNIGPV GNPGMPEAGL IPIPKKLAEA GVKDMLRLSD GRMSGTAGGT IILHISPEAA
LPESPFGVVE TGDLIICDIE TRKLHLEVSE AVLQTRIEKR RQSLVSFAMS FDPLRPRGRP
AHTPGTTILA YTPDGRRIIT GGSNSAIRIY TVGEDGEPKT IDEGVDAHFG IGATNRSFIM
GAEDGTVWKY DIISGKMQNL LVRCALPVRD IAVTRDGEWV AVASDELTVK IVKVDDMTQV
KYLREQSKGT KHVTFDPSGR YATVSGTDGI LYIYSMHEEE PELVRKLDGV IRRLEPDAEA
TSRAVWHPDG TAFASAEATR DISIYSTSEW KKEKTFTGGH TGDITALSWA PNGSLLASAA
ADGYIVLWEA KTQKILQRYD FGNVMNLSWH PTKNSLSFTT SDGELFIYDN FVPKDHESLL
QKPLQAAPIL PGPLGEISNN VGRTTLAERS KEAIQRAARR GTPDSLDDIL GGDDQMMDFV
EDDDGAGYAD EELNLYGKRP NDHLDDLGGT SNKRLYSGFE KPKAHPPLQP GSTPWAGSRR
YLCLNLTGAV WTVDQETHHT VTVEFYDREA HRDFHFTDPY MYDKACLNDN GTLFANNPSD
GSPATIFYRP HETWTARADW RTELPEGEQI RALALSDSYI VVVTSKDYVR VYTLFGTPFK
VYRQKSQAVT CAAWRNYIMS IGNGPIGIDG HATLRYTVEN VKRDEICQNE DTVALPEGAS
LQSVFFSDNG DPCIYDSTGV LLVLQHWRTP GQARWVPLLD TKQMARLAGG RKEETYWPVA
VAQDKFHCII LKGGDKNPYF PRPLLSEFDF QIPVASAPPK DSSESEDTTA EGARFEESFV
RGNVLLSLFR DLLSSTNATA SQRSDLARRE LDLDKNLLQM LAIECREGEE RGMKALELVA
LMTDRNGKML EAAAKVAQRY GRGVLEDKIR DLAERRVMGM GDDDELA
//
