ID A0A179HZE2_PURLI Unreviewed; 448 AA.
AC A0A179HZE2;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=L-2-hydroxyglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00041137};
DE EC=1.1.99.2 {ECO:0000256|ARBA:ARBA00038878};
GN ORFNames=VFPFJ_00957 {ECO:0000313|EMBL:OAQ94848.1};
OS Purpureocillium lilacinum (Paecilomyces lilacinus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Purpureocillium.
OX NCBI_TaxID=33203 {ECO:0000313|EMBL:OAQ94848.1, ECO:0000313|Proteomes:UP000078340};
RN [1] {ECO:0000313|EMBL:OAQ94848.1, ECO:0000313|Proteomes:UP000078340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PLFJ-1 {ECO:0000313|EMBL:OAQ94848.1};
RA Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yin W., Xie B.;
RT "Biosynthesis of antibiotic leucinostatins and their inhibition on
RT Phytophthora in bio-control Purpureocillium lilacinum.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:OAQ94848.1}.
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DR EMBL; LSBI01000001; OAQ94848.1; -; Genomic_DNA.
DR RefSeq; XP_018183567.1; XM_018318042.1.
DR AlphaFoldDB; A0A179HZE2; -.
DR STRING; 33203.A0A179HZE2; -.
DR GeneID; 28883091; -.
DR KEGG; plj:VFPFJ_00957; -.
DR OMA; GVHFTRM; -.
DR OrthoDB; 1815533at2759; -.
DR Proteomes; UP000078340; Unassembled WGS sequence.
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;
KW Reference proteome {ECO:0000313|Proteomes:UP000078340}.
FT DOMAIN 41..437
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT REGION 224..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 448 AA; 46384 MW; 1CF4835655C6A166 CRC64;
MMLARRTVTA LPLRTGPACS RSSQRLQFSS TTAARADFTH VVIGGGVVGL AIARQLALRN
GAAASSSSST STTLLLERHG GVGTETSSRN SEVIHAGIYY GASSLKARLC VRGKQLLYGF
CAAHGVGHRR TGKWIVAQTR AQREALERIE RLCSGELGVP VRWVGDEEVR RAGEGVRAEE
GALESPTTGI VDAHGLMVAL QGLFEDAGGV VALNSPVTAI TPLGGGGGGG GGDGDASSSS
SPSPKGSAGW ELAVRDAATG ETSTITAETI INAAGLGAAD VHNMIVPPER RTRLHYAKGN
YFSYAAPLPR VSRLIYPAPE PGAGGLGTHL TLDLGGRMRF GPDVEWVESP EDLAVNGARM
ADAVAEIQKY LPGVDASCLA PDYAGIRPKL SPGGAVGTGK GFNDFIIRME DGYAGWVNLL
GIESPGLTSS LAIGEEVERL LYGSVTPS
//
