ID W3XAW2_PESFW Unreviewed; 420 AA.
AC W3XAW2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=L-2-hydroxyglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00041137};
DE EC=1.1.99.2 {ECO:0000256|ARBA:ARBA00038878};
GN ORFNames=PFICI_04458 {ECO:0000313|EMBL:ETS82582.1};
OS Pestalotiopsis fici (strain W106-1 / CGMCC3.15140).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Sporocadaceae; Pestalotiopsis.
OX NCBI_TaxID=1229662 {ECO:0000313|EMBL:ETS82582.1, ECO:0000313|Proteomes:UP000030651};
RN [1] {ECO:0000313|Proteomes:UP000030651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W106-1 / CGMCC3.15140 {ECO:0000313|Proteomes:UP000030651};
RX PubMed=25623211; DOI=10.1186/s12864-014-1190-9;
RA Wang X., Zhang X., Liu L., Xiang M., Wang W., Sun X., Che Y., Guo L.,
RA Liu G., Guo L., Wang C., Yin W.B., Stadler M., Zhang X., Liu X.;
RT "Genomic and transcriptomic analysis of the endophytic fungus
RT Pestalotiopsis fici reveals its lifestyle and high potential for synthesis
RT of natural products.";
RL BMC Genomics 16:28-28(2015).
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; KI912111; ETS82582.1; -; Genomic_DNA.
DR RefSeq; XP_007831230.1; XM_007833039.1.
DR AlphaFoldDB; W3XAW2; -.
DR STRING; 1229662.W3XAW2; -.
DR GeneID; 19269471; -.
DR KEGG; pfy:PFICI_04458; -.
DR eggNOG; KOG2665; Eukaryota.
DR HOGENOM; CLU_024775_1_0_1; -.
DR InParanoid; W3XAW2; -.
DR OMA; GVHFTRM; -.
DR OrthoDB; 1815533at2759; -.
DR Proteomes; UP000030651; 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:UP000030651}.
FT DOMAIN 35..410
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 420 AA; 45362 MW; 334312226731F285 CRC64;
MLGGSLRRQL LCNAQTRIWR SFSSTSPARA DFTHVVIGGG VVGLAVSQRL AAAHPASTTL
LLERHGHVGT ETSSRNSEVI HAGLYYGATS LKTRLCVRGK EQLYAFCEQH AVPHRRTGKW
IVAQTDDERD ALERLHVFAR DEIGVPTRWI DEEERRREDP EVTGRTGILE SPTSGIVDSH
SLMLALHGLF EEQGGVTALN SNVTAIEPLS GSGGKPGSGG WRITVRDSDT GEESSIETET
LVNCAGLGAA DVHNMIAPPE QHTRLYYAKG NYFSYAASHP RVKRLVYPMT MPGAGGLGTH
LTLDMAGRVR FGPDVEWVED PTDLQVSAAR LAPAVEAIHR YLPNVDVSAL AADYAGIRPK
LGKAGAVGQG KGFYDFHIKK EDGFEGWVNL LAIESPGLTS SLAIGDLVEQ LMYGSTTPES
//
