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Database: UniProt
Entry: B0Y0K7_ASPFC
LinkDB: B0Y0K7_ASPFC
Original site: B0Y0K7_ASPFC 
ID   B0Y0K7_ASPFC            Unreviewed;       256 AA.
AC   B0Y0K7;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   SubName: Full=3-hydroxyacyl-CoA dehydrogenase, putative {ECO:0000313|EMBL:EDP51748.1};
GN   ORFNames=AFUB_057660 {ECO:0000313|EMBL:EDP51748.1};
OS   Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya
OS   fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=451804 {ECO:0000313|EMBL:EDP51748.1, ECO:0000313|Proteomes:UP000001699};
RN   [1] {ECO:0000313|EMBL:EDP51748.1, ECO:0000313|Proteomes:UP000001699}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CEA10 / CBS 144.89 / FGSC A1163
RC   {ECO:0000313|Proteomes:UP000001699};
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
CC   -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009463}.
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DR   EMBL; DS499597; EDP51748.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0Y0K7; -.
DR   EnsemblFungi; EDP51748; EDP51748; AFUB_057660.
DR   VEuPathDB; FungiDB:AFUB_057660; -.
DR   HOGENOM; CLU_009834_2_0_1; -.
DR   PhylomeDB; B0Y0K7; -.
DR   Proteomes; UP000001699; Unassembled WGS sequence.
DR   GO; GO:0070403; F:NAD+ binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR022694; 3-OHacyl-CoA_DH.
DR   InterPro; IPR006176; 3-OHacyl-CoA_DH_NAD-bd.
DR   InterPro; IPR006108; 3HC_DH_C.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR48075; 3-HYDROXYACYL-COA DEHYDROGENASE FAMILY PROTEIN; 1.
DR   PANTHER; PTHR48075:SF10; DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G10070)-RELATED; 1.
DR   Pfam; PF00725; 3HCDH; 1.
DR   Pfam; PF02737; 3HCDH_N; 1.
DR   PIRSF; PIRSF000105; HCDH; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          16..186
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          192..226
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   SITE            146
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-1"
SQ   SEQUENCE   256 AA;  28382 MW;  269C4C107CAA00A7 CRC64;
     MHSTWQPPTN YRQRPVAILG AGVLGRRLAC VWASAGYNVH VRDPSPQQRE DCLAYVRDNV
     AAYAESTGQK PGTVGTTESL EEAVDNAWLV IEAVPEKIQL KIDAFAELDA RAPSDCILAS
     NSSSYKSSEM LEKVSEATKS RILNMHYYMP PQCMIVELMT DGHTAAEIFP FMVERSKEAA
     TVPYVARKES TGFIFNRLWA AVKREVLTML AEGVSVPEEI DSMWKEMFVK GGVLPCRTMD
     GTYALFLFLA AVSKSD
//
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