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Database: UniProt
Entry: A8N1W4_COPC7
LinkDB: A8N1W4_COPC7
Original site: A8N1W4_COPC7 
ID   A8N1W4_COPC7            Unreviewed;       517 AA.
AC   A8N1W4;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 2.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=D2HGD protein {ECO:0000313|EMBL:EAU92870.2};
GN   ORFNames=CC1G_03657 {ECO:0000313|EMBL:EAU92870.2};
OS   Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS   (Inky cap fungus) (Hormographiella aspergillata).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX   NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU92870.2, ECO:0000313|Proteomes:UP000001861};
RN   [1] {ECO:0000313|EMBL:EAU92870.2, ECO:0000313|Proteomes:UP000001861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC   {ECO:0000313|Proteomes:UP000001861};
RX   PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA   Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA   Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA   Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA   Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA   Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA   Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA   Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA   Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA   Zolan M.E., Pukkila P.J.;
RT   "Insights into evolution of multicellular fungi from the assembled
RT   chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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:EAU92870.2}.
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DR   EMBL; AACS02000001; EAU92870.2; -; Genomic_DNA.
DR   RefSeq; XP_001828863.2; XM_001828811.2.
DR   AlphaFoldDB; A8N1W4; -.
DR   STRING; 240176.A8N1W4; -.
DR   GeneID; 6005289; -.
DR   KEGG; cci:CC1G_03657; -.
DR   VEuPathDB; FungiDB:CC1G_03657; -.
DR   eggNOG; KOG1232; Eukaryota.
DR   HOGENOM; CLU_017779_4_1_1; -.
DR   InParanoid; A8N1W4; -.
DR   OMA; YNEDWMR; -.
DR   OrthoDB; 1664005at2759; -.
DR   Proteomes; UP000001861; 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:UP000001861}.
FT   DOMAIN          76..261
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   517 AA;  56458 MW;  D06B6BE4490C3378 CRC64;
     MLSSRVHRVA SRIPHRLLVN ARLASSVPQL NSVTPEDIAH FAKILPPSSI LSTLGPAASA
     TSEDLDIYNC DWIGRYKGHS TTVLKPKTTE QVSQILKWCN ERRIGVVPQG GNTGLVGGSV
     PVRDEVVLSL ANMNQVRTYD PVSGILVADA GCILQSLTDH VAPDHIMPID LGAKGRQVPA
     IFRTTPTMLT RSPFQLSDWR KCRNKCRRPE AASVVLADGT ILDQLTTLRK DNTGYDLKQL
     FIGAEGTLGV ITGVSILTPP APQSTNNVIL ALPSYKNVLP LFQKVKHHLS EILSAFEFID
     RTAYDLAVKH GQGRALSEDE VEGAECFVLV ETSGGRREHD EEKLNDLLES LLTADEPLIN
     TGVLAQNPAQ FASLWALREG VPEAVSKEGK AYKYDISIPV AKFQEVVDNT REHLRSKGLL
     HENAVKHVVG YGHVGDGNLH LNVVAHSFQP EIEAALEPYI YEVVQSLRGS ISAEHGIGAM
     KTHALPYSKS QASIDLMHKI KHIFDPNGIM NPGKVLE
//
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