ID A0A395SEM9_9HYPO Unreviewed; 334 AA.
AC A0A395SEM9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Hydroxylacyl-dehydrogenase {ECO:0000313|EMBL:RGP70833.1};
GN ORFNames=FLONG3_7289 {ECO:0000313|EMBL:RGP70833.1};
OS Fusarium longipes.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=694270 {ECO:0000313|EMBL:RGP70833.1, ECO:0000313|Proteomes:UP000266234};
RN [1] {ECO:0000313|EMBL:RGP70833.1, ECO:0000313|Proteomes:UP000266234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 20695 {ECO:0000313|EMBL:RGP70833.1,
RC ECO:0000313|Proteomes:UP000266234};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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:RGP70833.1}.
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DR EMBL; PXOG01000167; RGP70833.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395SEM9; -.
DR STRING; 694270.A0A395SEM9; -.
DR Proteomes; UP000266234; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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:SF1; LAMBDA-CRYSTALLIN HOMOLOG; 1.
DR Pfam; PF00725; 3HCDH; 1.
DR Pfam; PF02737; 3HCDH_N; 1.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000266234};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..193
FT /note="3-hydroxyacyl-CoA dehydrogenase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF02737"
FT DOMAIN 197..255
FT /note="3-hydroxyacyl-CoA dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF00725"
FT REGION 283..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 334 AA; 36736 MW; 0F594B9A1AEB697B CRC64;
MPGEKKQETI ALIGLGTIGI SFAALHLRYS YANIRLYDVR SDLQEHIESL LPVYLDSTKK
ESNSEDISVQ KLISDGRVVI CSSLSEACSN ATIVQEQGPD SVEFKKSTWA QVIEYAPSSA
HLWSSTSGLQ ASKQVEDLQD KSRVLVVHPF NPPHIMPLIE VVPSPHTSPE RTQFAIDYFK
NLGSGHRPVR INKETQGFVG NRLAFALFRE ACHLVSNDVV SVEDLDTIVE ASIAPRWAVA
GPFQTYNSAG GTAGIAAFLH NLADTMEACW DDGGKLSLKG TSATRSLQDR DEDEDWTDKI
SKETEKAYGR PTAESLARRD HNLQKIIAAQ PNEA
//
