ID W6Q9L9_PENRF Unreviewed; 475 AA.
AC W6Q9L9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=L-2-hydroxyglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00041137};
DE EC=1.1.99.2 {ECO:0000256|ARBA:ARBA00038878};
GN ORFNames=PROQFM164_S01g000276 {ECO:0000313|EMBL:CDM26467.1};
OS Penicillium roqueforti (strain FM164).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1365484 {ECO:0000313|EMBL:CDM26467.1};
RN [1] {ECO:0000313|EMBL:CDM26467.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FM164 {ECO:0000313|EMBL:CDM26467.1};
RX PubMed=24407037; DOI=10.1038/ncomms3876;
RA Cheeseman K., Ropars J., Renault P., Dupont J., Gouzy J., Branca A.,
RA Abraham A.L., Ceppi M., Conseiller E., Debuchy R., Malagnac F., Goarin A.,
RA Silar P., Lacoste S., Sallet E., Bensimon A., Giraud T., Brygoo Y.;
RT "Multiple recent horizontal transfers of a large genomic region in cheese
RT making fungi.";
RL Nat. Commun. 5:2876-2876(2014).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-2-hydroxyglutarate + A = 2-oxoglutarate + AH2;
CC Xref=Rhea:RHEA:21252, ChEBI:CHEBI:13193, ChEBI:CHEBI:16782,
CC ChEBI:CHEBI:16810, ChEBI:CHEBI:17499; EC=1.1.99.2;
CC Evidence={ECO:0000256|ARBA:ARBA00036066};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SIMILARITY: Belongs to the L2HGDH family.
CC {ECO:0000256|ARBA:ARBA00037941}.
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DR EMBL; HG792015; CDM26467.1; -; Genomic_DNA.
DR AlphaFoldDB; W6Q9L9; -.
DR STRING; 1365484.W6Q9L9; -.
DR OMA; GVHFTRM; -.
DR OrthoDB; 1815533at2759; -.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:UniProt.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR43104; L-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43104:SF4; L-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
FT DOMAIN 102..469
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 475 AA; 51416 MW; AC4B72F0D007D555 CRC64;
MMKDENLWFD ISIVPGSHTF EFQYMGLGIT PDVIPEVIPE VGGRMFLPKS HFRAPSLQAA
GQLRLPDMSA RALLKQQFKL INKLPTRCFS STRPTNADFT HAVIGAGVVG LAAARQLAAR
EGTSTILLER HDAPGTETSS RNSEVIHAGL YYPATSLKTQ LCIRGRNLLH DLCAQNNIPH
RNTKKWIVAQ NPTQWEACLK LHAHAQGLGD APTRLVGRDE AQQREPDVKA DAGIVESETS
GIVDSHSLMT YLHGDFEDRG GDVAFKTRVT GVEAIDGGRG GYKITAVSDE DGSVTSFTAE
TLINSAGHGA CDISNMLLPK ERHFVPHYAK GTYFSYAASR PRTSVLVYPV TLPGTGGLGT
HLTLDMAGRI RFGPDVEWVD SPDDLVPSAA RLEQALPEIK AYMPGVDVSA IALDYCGIRP
KLGRNGAVNE GKGFQDFIIQ EEEGLPGFVN LLGIESPGLT SCLAIGEMVD GILYR
//
