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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//