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Database: UniProt
Entry: A0A2G7FRE1_9EURO
LinkDB: A0A2G7FRE1_9EURO
Original site: A0A2G7FRE1_9EURO 
ID   A0A2G7FRE1_9EURO        Unreviewed;       295 AA.
AC   A0A2G7FRE1;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AARAC_001238 {ECO:0000313|EMBL:PIG83126.1}, BDV24DRAFT_145349
GN   {ECO:0000313|EMBL:KAE8334721.1};
OS   Aspergillus arachidicola.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=656916 {ECO:0000313|EMBL:PIG83126.1, ECO:0000313|Proteomes:UP000231358};
RN   [1] {ECO:0000313|EMBL:PIG83126.1, ECO:0000313|Proteomes:UP000231358}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 117610 {ECO:0000313|EMBL:PIG83126.1,
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.
RN   [2] {ECO:0000313|EMBL:KAE8334721.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CBS 117612 {ECO:0000313|EMBL:KAE8334721.1};
RG   DOE Joint Genome Institute;
RA   Kjaerbolling I., Vesth T., Frisvad J.C., Nybo J.L., Theobald S.,
RA   Kildgaard S., Isbrandt T., Kuo A., Sato A., Lyhne E.K., Kogle M.E.,
RA   Wiebenga A., Kun R.S., Lubbers R.J., Makela M.R., Barry K., Chovatia M.,
RA   Clum A., Daum C., Haridas S., He G., LaButti K., Lipzen A., Mondo S.,
RA   Riley R., Salamov A., Simmons B.A., Magnuson J.K., Henrissat B.,
RA   Mortensen U.H., Larsen T.O., Devries R.P., Grigoriev I.V., Machida M.,
RA   Baker S.E., Andersen M.R.;
RT   "Friends and foes A comparative genomics study of 23 Aspergillus species
RT   from section Flavi.";
RL   Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00009463}.
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DR   EMBL; ML737250; KAE8334721.1; -; Genomic_DNA.
DR   EMBL; NEXV01000466; PIG83126.1; -; Genomic_DNA.
DR   STRING; 656916.A0A2G7FRE1; -.
DR   OrthoDB; 4517707at2759; -.
DR   Proteomes; UP000231358; Unassembled WGS sequence.
DR   Proteomes; UP000325558; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000231358}.
FT   DOMAIN          15..185
FT                   /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF02737"
FT   DOMAIN          191..285
FT                   /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00725"
FT   SITE            145
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000105-1"
SQ   SEQUENCE   295 AA;  32703 MW;  EFBBCD2E81642D4F CRC64;
     MAPWKHPEDY QNRPVAVLGA GVLGRRIGCI WASGGYDVII RDPSAEQRTD GIAYIEKNVA
     LYAQKTGKKP GKAEAVEELA DAVKHAWLVI EAVPEKLHLK IDTFAELETL APADCILASN
     SSSYKTSEML AKVETDTKTR ILNMHYYMPP DCMIVEIMTD GYTDDAVFPF IVERSKEVAT
     LPYVARKEST GFIFNRLWAA VKREALTILA EGVSVPEELD SMWLEMFVKG GAAPCRTMDA
     VGLDTVAFIE RHYVDERGLS PEKTVDFLQQ KYLDHGKLGS KCPQGGLYPP AEDKA
//
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