ID N4UYD0_COLOR Unreviewed; 408 AA.
AC N4UYD0;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=L-2-hydroxyglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00041137};
DE EC=1.1.99.2 {ECO:0000256|ARBA:ARBA00038878};
GN ORFNames=Cob_v004271 {ECO:0000313|EMBL:TDZ22720.1};
OS Colletotrichum orbiculare (strain 104-T / ATCC 96160 / CBS 514.97 / LARS
OS 414 / MAFF 240422) (Cucumber anthracnose fungus) (Colletotrichum
OS lagenarium).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum orbiculare species complex.
OX NCBI_TaxID=1213857 {ECO:0000313|EMBL:TDZ22720.1, ECO:0000313|Proteomes:UP000014480};
RN [1] {ECO:0000313|Proteomes:UP000014480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC {ECO:0000313|Proteomes:UP000014480};
RX PubMed=23252678; DOI=10.1111/nph.12085;
RA Gan P., Ikeda K., Irieda H., Narusaka M., O'Connell R.J., Narusaka Y.,
RA Takano Y., Kubo Y., Shirasu K.;
RT "Comparative genomic and transcriptomic analyses reveal the hemibiotrophic
RT stage shift of Colletotrichum fungi.";
RL New Phytol. 197:1236-1249(2013).
RN [2] {ECO:0000313|Proteomes:UP000014480}
RP GENOME REANNOTATION.
RC STRAIN=104-T / ATCC 96160 / CBS 514.97 / LARS 414 / MAFF 240422
RC {ECO:0000313|Proteomes:UP000014480};
RX PubMed=30893003; DOI=10.1094/MPMI-12-18-0352-A;
RA Gan P., Tsushima A., Narusaka M., Narusaka Y., Takano Y., Kubo Y.,
RA Shirasu K.;
RT "Genome sequence resources for four phytopathogenic fungi from the
RT Colletotrichum orbiculare species complex.";
RL Mol. Plant Microbe Interact. 32:1088-1090(2019).
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:TDZ22720.1}.
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DR EMBL; AMCV02000009; TDZ22720.1; -; Genomic_DNA.
DR AlphaFoldDB; N4UYD0; -.
DR STRING; 1213857.N4UYD0; -.
DR EnsemblFungi; ENH80808; ENH80808; Cob_10473.
DR eggNOG; KOG2665; Eukaryota.
DR HOGENOM; CLU_024775_1_0_1; -.
DR OrthoDB; 1815533at2759; -.
DR Proteomes; UP000014480; 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:UP000014480}.
FT DOMAIN 34..401
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 408 AA; 43546 MW; 4033433DEC737B7C CRC64;
MSLRPLCARS IGRLVQARRV SSSAASVKAD FTHVVVGGGA VGLATARALA QRPGTSTVLL
ERHGAVGTET SSRNSEVIHA GIYYGAGTLK TELCIRGKEL LYDFCRSRDV PHANTGKWIV
AQNDVQREAL QKIHDFCKND INVPVRWIGN EEAQRLEPGV RGETGILESP TTGIVDSHGL
MVALQGLFED AGGVVALSSA VTGVKPLGNK GSDGWEVRVR DSTTGEESTV TTEVLVNSAG
LGAIDINNMI LPAEEKRGMF YAKGNYFSYA SSSPKVSRLI YPAPEPGAGG LGTHLTLDLA
GRVRFGPDVE WVDSADDLAV NTSRMPLAVE AIKKYLPDLD ESCLEPDYAG IRPKLGKLGA
VAQGTGFHDF VIRREDGYEG WVNLLGIESP GLTSCLAIAE RVDKIVYG
//
