ID A0A2G5B5X8_COERN Unreviewed; 411 AA.
AC A0A2G5B5X8;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE RecName: Full=L-2-hydroxyglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00041137};
DE EC=1.1.99.2 {ECO:0000256|ARBA:ARBA00038878};
GN ORFNames=COEREDRAFT_10346 {ECO:0000313|EMBL:PIA14453.1};
OS Coemansia reversa (strain ATCC 12441 / NRRL 1564).
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Kickxellomycetes; Kickxellales; Kickxellaceae; Coemansia.
OX NCBI_TaxID=763665 {ECO:0000313|EMBL:PIA14453.1, ECO:0000313|Proteomes:UP000242474};
RN [1] {ECO:0000313|EMBL:PIA14453.1, ECO:0000313|Proteomes:UP000242474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 1564 {ECO:0000313|EMBL:PIA14453.1,
RC ECO:0000313|Proteomes:UP000242474};
RX PubMed=25977457; DOI=10.1093/gbe/evv090;
RA Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA Spatafora J.W., Berbee M.L.;
RT "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT Walls of Algal Ancestors of Land Plants.";
RL Genome Biol. Evol. 7:1590-1601(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KZ303517; PIA14453.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5B5X8; -.
DR STRING; 763665.A0A2G5B5X8; -.
DR OrthoDB; 1815533at2759; -.
DR Proteomes; UP000242474; 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:UP000242474}.
FT DOMAIN 33..406
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 411 AA; 44227 MW; BDCE20D10D84BFC9 CRC64;
MLRLRPCCRT VRAYTSAAQR LASCAVEDMT EIDYLVIGGG VVGLAIGRQL AARPATSTLV
VDKNRQPGME TSSRNSEVIH AGIHYPASSL RTKLCIEGKH LLYDYCRQHS VPHTKIGKWV
VAQDDTQTER LHTLARHCAD IGVPAQLLGR AHTAAEEPCV RARAVLASPT TGIVDSHALM
LALLQDLRDR SADYAPCAEV VAIHGESGGG YRALVATGDS DTPYMPIHAR AVVNAAGLWA
DRIAGMLVSD SHEWRTKYRL HFAKGCYYAY TPAPDATPIT VRRLVYPIPD EHATSLGTHL
TLDMAGAIRF GPDLEWISSN ADYAVDSAES TRSAAAAAIA TYLPQIRAQD LSPDYAGIRP
KLQPPGGAFR DFVVQEESAA GFPAFVNLVG IESPGLTASL AIARMVDGLL H
//
