ID   V9E8S2_PHYPR            Unreviewed;       501 AA.
AC   V9E8S2;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=FAD-binding PCMH-type domain-containing protein {ECO:0000259|PROSITE:PS51387};
GN   ORFNames=F443_18860 {ECO:0000313|EMBL:ETI34677.1};
OS   Phytophthora parasitica P1569.
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=1317065 {ECO:0000313|EMBL:ETI34677.1, ECO:0000313|Proteomes:UP000018721};
RN   [1] {ECO:0000313|EMBL:ETI34677.1, ECO:0000313|Proteomes:UP000018721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1569 {ECO:0000313|EMBL:ETI34677.1,
RC   ECO:0000313|Proteomes:UP000018721};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica P1569.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC       4 family. {ECO:0000256|ARBA:ARBA00008000}.
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:ETI34677.1}.
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DR   EMBL; ANIZ01003304; ETI34677.1; -; Genomic_DNA.
DR   AlphaFoldDB; V9E8S2; -.
DR   EnsemblProtists; ETI34677; ETI34677; F443_18860.
DR   eggNOG; KOG1232; Eukaryota.
DR   HOGENOM; CLU_017779_4_1_1; -.
DR   OrthoDB; 1664005at2759; -.
DR   Proteomes; UP000018721; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.70.2190; -; 1.
DR   Gene3D; 3.30.70.2740; -; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   PANTHER; PTHR43716; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43716:SF1; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000018721}.
FT   DOMAIN          74..253
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   501 AA;  55296 MW;  BA21FE59F9A669FE CRC64;
     MVMMLPTLLR TTRRQFGALS AARAFSTPAR NPAHASWTED DKAYFQQLLK PESVLTDVDD
     TETYTVDWLK KYKAQSNHQM VLKPKTTEQV SAILKYCNER NLPVVPQGGN TGLVGGSVPV
     YDEIVLSTSS MNSVISFDEV SGILVCEAGC ILENLDNYVA KHGYMMPLDL GAKGTCQIGG
     NVATNAGGLR LLRYGSLHGT VLGIEAVLAD GTVIDCLSTM RKDNTGYDLK QLFIGSEGTL
     GVVTKVSILT PPRSSSKNVA LLACEDFEAC QKAFVEAKKN LGEVLSAVEF MDRQSLDMVL
     TQQDWTKDPL ETPSPFYVLI ETSGSNSVHD MEKLEAYLED VMGSGVVVDG TVAQDEAQAQ
     KLFMLREDIS MSLSSRGYVY KYDISLPMDQ YYKIVEEVRE KMAPLGAEVV GFGHMGDCNL
     HLNISTLKYD EKVFNALEPY VFEWTSKYRG SISSEHGIGT HKPSYLHLSK SDNSIQLMRQ
     MKQMMDPKGI LNPYKVLPAS E
//