ID A0A0B1P3A4_UNCNE Unreviewed; 911 AA.
AC A0A0B1P3A4;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Putative peroxisomal multifunctional beta-oxidation protein {ECO:0000313|EMBL:KHJ31159.1};
GN ORFNames=EV44_g4439 {ECO:0000313|EMBL:KHJ31159.1};
OS Uncinula necator (Grape powdery mildew).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Erysiphales; Erysiphaceae; Erysiphe.
OX NCBI_TaxID=52586 {ECO:0000313|EMBL:KHJ31159.1, ECO:0000313|Proteomes:UP000030854};
RN [1] {ECO:0000313|EMBL:KHJ31159.1, ECO:0000313|Proteomes:UP000030854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=c {ECO:0000313|Proteomes:UP000030854};
RX PubMed=25487071;
RA Jones L., Riaz S., Morales-Cruz A., Amrine K.C., McGuire B., Gubler W.D.,
RA Walker M.A., Cantu D.;
RT "Adaptive genomic structural variation in the grape powdery mildew
RT pathogen, Erysiphe necator.";
RL BMC Genomics 15:1081-1081(2014).
CC -!- PATHWAY: Lipid metabolism; fatty acid beta-oxidation.
CC {ECO:0000256|ARBA:ARBA00005005}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the short-chain dehydrogenases/reductases (SDR)
CC family. {ECO:0000256|ARBA:ARBA00006484}.
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:KHJ31159.1}.
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DR EMBL; JNVN01003181; KHJ31159.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B1P3A4; -.
DR STRING; 52586.A0A0B1P3A4; -.
DR HOGENOM; CLU_010194_18_0_1; -.
DR OMA; WATKVHT; -.
DR OrthoDB; 2140828at2759; -.
DR UniPathway; UPA00659; -.
DR Proteomes; UP000030854; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:0006635; P:fatty acid beta-oxidation; IEA:UniProtKB-UniPathway.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR CDD; cd03448; HDE_HSD; 1.
DR CDD; cd05353; hydroxyacyl-CoA-like_DH_SDR_c-like; 2.
DR Gene3D; 3.10.129.10; Hotdog Thioesterase; 2.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
DR InterPro; IPR029069; HotDog_dom_sf.
DR InterPro; IPR002539; MaoC-like_dom.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR020904; Sc_DH/Rdtase_CS.
DR InterPro; IPR002347; SDR_fam.
DR PANTHER; PTHR45024; DEHYDROGENASES, SHORT CHAIN; 1.
DR PANTHER; PTHR45024:SF2; SCP2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00106; adh_short; 2.
DR Pfam; PF01575; MaoC_dehydratas; 1.
DR PRINTS; PR00081; GDHRDH.
DR PRINTS; PR00080; SDRFAMILY.
DR SMART; SM00822; PKS_KR; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF54637; Thioesterase/thiol ester dehydrase-isomerase; 2.
DR PROSITE; PS00061; ADH_SHORT; 1.
PE 3: Inferred from homology;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000030854}.
FT DOMAIN 786..897
FT /note="MaoC-like"
FT /evidence="ECO:0000259|Pfam:PF01575"
FT REGION 766..788
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 911 AA; 99061 MW; 8C73BB9AEF136102 CRC64;
MKQATMANLR YDNQVVVVTG AGGGLGKAYA LFFGSRGASV VVNDLGASFK GEGASSKAAD
VVVDEIKSSG GKAVANYDSV ENGNKIIETA IQNFGRIDIL INNAGILRDV SFKNMSDRDW
DLVIAVHVTG SFKCSRAAWP YFKKQKFGRV INTTSAAGLF GSFGQCNYSA AKLALVGFTE
TLAKEGAKYD IKANVIAPIA ASRMTETVMP PEILENLKPD WIVPLVAVLA HRENDENGAI
FEVGGGHIAK IRWERSKGLL LKPDDSYTPG AILKKWDQVK DFKDADYPNG VADFMGLLEK
GMRLPKNDPG EAIDLKGKVA LITGGGAGIG RSYCLAFAKY GASVVVNDLV DPSSVVQEIK
NLGAKAFGIK ASAEEGDLVV KAAIDAFGRI DIIINNAGIL RDKAFSNMDD KLWHDVMAVH
LRGTYKVTKA AWPYMLKQKY GRIVNTTSTS GIYGNFGQAN YAAAKCGILG FSRALAREGH
KYNIFVNTIA PNAGTAMTRT VLPEDMVQAF KPDYIAPLVI ALCSDKVPQP STGGLFEVGS
GWVSQTRWQR SGGHGFPIDE RLTPEAVREK WDRITDFLDG RADHPESAQD GLKSIMANFE
NRKAMTAKKE NSAKAANEQI LTNITESMKK TGEEIEFQYQ EKDIILYNLG IGAKSKDLRY
VFELDDNFQA LPTFGVIPFF LTTPPFSFSD IVPNFSPMML LHGEQYLEIL SYPIPTSATL
MSHAKLIEVV DKGNAAVVKI GTTTINKSTG ATLFYNENTI FIRGSGNFGG SRKPQDRGDA
TALNKPPHRK PDILIEEKTS EDLAAIYRLS GDFNPLHINP EFAAMGGFES PILHGLCTYG
IAGKHVYNSY GRFKSIKARF SGTVTPGQIL ITEMWKENNK VIFQVKVKET GKLAISNAAC
VLLDTDSKAK L
//
