ID A0A317XXQ4_9BASI Unreviewed; 254 AA.
AC A0A317XXQ4;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=3-hydroxyacyl-CoA dehydrogenase {ECO:0000256|ARBA:ARBA00013000};
DE EC=1.1.1.35 {ECO:0000256|ARBA:ARBA00013000};
GN ORFNames=BCV70DRAFT_197328 {ECO:0000313|EMBL:PWZ03096.1};
OS Testicularia cyperi.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Anthracoideaceae; Testicularia.
OX NCBI_TaxID=1882483 {ECO:0000313|EMBL:PWZ03096.1, ECO:0000313|Proteomes:UP000246740};
RN [1] {ECO:0000313|EMBL:PWZ03096.1, ECO:0000313|Proteomes:UP000246740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 3645 {ECO:0000313|EMBL:PWZ03096.1,
RC ECO:0000313|Proteomes:UP000246740};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) +
CC NADH; Xref=Rhea:RHEA:22432, ChEBI:CHEBI:15378, ChEBI:CHEBI:57318,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:90726; EC=1.1.1.35;
CC Evidence={ECO:0000256|ARBA:ARBA00023693};
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005005}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC {ECO:0000256|ARBA:ARBA00004305}.
CC -!- SIMILARITY: Belongs to the 3-hydroxyacyl-CoA dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00009463}.
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DR EMBL; KZ819188; PWZ03096.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317XXQ4; -.
DR STRING; 1882483.A0A317XXQ4; -.
DR InParanoid; A0A317XXQ4; -.
DR Proteomes; UP000246740; Unassembled WGS sequence.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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; IPR006180; 3-OHacyl-CoA_DH_CS.
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; PTHR43561; -; 1.
DR PANTHER; PTHR43561:SF3; HYDROXYACYL-COENZYME A DEHYDROGENASE, MITOCHONDRIAL; 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.
DR PROSITE; PS00067; 3HCDH; 1.
PE 3: Inferred from homology;
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000246740}.
FT DOMAIN 8..191
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 194..234
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT BINDING 48
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-3"
FT BINDING 55
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-3"
FT BINDING 125
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-3"
FT SITE 148
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR000105-1"
SQ SEQUENCE 254 AA; 27218 MW; BEBED5B521F91BC7 CRC64;
MCLTDSFGAG LMGAGIAQVL AHKGKFNVTL SDVTDKALAN GQSIISKSLT RIAKKAMAES
SADEQSKFVK GIVDSIKVTT DPEAAVKDTD LVIEAIIENV GIKKDLFGFL DGKAPKDAIF
ASNTSSLSIT DVAEAVSSER QQRFGGFHAF NPVPQMKLVE VIRTTKTDND TFDSLLEVAK
RMGKTPVSCI DSPGFIVNRL LVPYMLEAVR LVERGEATAK DVDTAMKLGA GCKYSHESYS
RTPLSSIQST CRAC
//
