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Database: UniProt
Entry: A0A0A2KFX5_PENIT
LinkDB: A0A0A2KFX5_PENIT
Original site: A0A0A2KFX5_PENIT 
ID   A0A0A2KFX5_PENIT        Unreviewed;       356 AA.
AC   A0A0A2KFX5;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Polyketide synthase, enoylreductase {ECO:0000313|EMBL:KGO66717.1};
GN   ORFNames=PITC_056100 {ECO:0000313|EMBL:KGO66717.1};
OS   Penicillium italicum (Blue mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO66717.1, ECO:0000313|Proteomes:UP000030104};
RN   [1] {ECO:0000313|EMBL:KGO66717.1, ECO:0000313|Proteomes:UP000030104}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHI-1 {ECO:0000313|EMBL:KGO66717.1,
RC   ECO:0000313|Proteomes:UP000030104};
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 zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000256|ARBA:ARBA00008072}.
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:KGO66717.1}.
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DR   EMBL; JQGA01001363; KGO66717.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2KFX5; -.
DR   STRING; 40296.A0A0A2KFX5; -.
DR   HOGENOM; CLU_026673_16_1_1; -.
DR   OMA; RICGVTH; -.
DR   OrthoDB; 2267374at2759; -.
DR   PhylomeDB; A0A0A2KFX5; -.
DR   Proteomes; UP000030104; Unassembled WGS sequence.
DR   GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro.
DR   CDD; cd08249; enoyl_reductase_like; 1.
DR   Gene3D; 3.90.180.10; Medium-chain alcohol dehydrogenases, catalytic domain; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH-like_N.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   InterPro; IPR047122; Trans-enoyl_RdTase-like.
DR   PANTHER; PTHR45348; HYPOTHETICAL OXIDOREDUCTASE (EUROFUNG); 1.
DR   PANTHER; PTHR45348:SF2; ZINC-TYPE ALCOHOL DEHYDROGENASE-LIKE PROTEIN C2E1P3.01; 1.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; GroES-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030104}.
FT   DOMAIN          13..343
FT                   /note="Enoyl reductase (ER)"
FT                   /evidence="ECO:0000259|SMART:SM00829"
SQ   SEQUENCE   356 AA;  38341 MW;  F5DB12C5A5926AE8 CRC64;
     MATHRAITVQ SQGKAVIQDR LMPQLTDDCI LVKTTAVSLN PTDWKHLDFE ACTGTVIGCD
     YAGVVEAVGP AVQKVWKRGD RVAGFIHGCD AVNPANGAFS EYALAKGDLQ IKIPDYMSFE
     AACTIGLGIL TVGFGLYHLL GEEMLDDLEN INDKKPAQDQ SASILIYGGA TATGSLAIQV
     CKLLGLQVIT TCSEVNRAFM YELGADAVFD YHDAQVGDTI RQGTGDSLEI VFDTISTPQT
     AAICAAAISS TGGAYNALLD VRCPRLDVDT NVTMTYDIIG DDYQLGGRNI PGDKINLEFG
     VRWVRAAEIL VQSRRIFPHR YAVKPSGLAG ILDGLQLLRQ GKVRACKLVY KLEDTS
//
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