ID V7C2A5_PHAVU Unreviewed; 447 AA.
AC V7C2A5;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=L-2-hydroxyglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00041137};
DE EC=1.1.99.2 {ECO:0000256|ARBA:ARBA00038878};
GN ORFNames=PHAVU_004G053400g {ECO:0000313|EMBL:ESW23508.1};
OS Phaseolus vulgaris (Kidney bean) (French bean).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW23508.1, ECO:0000313|Proteomes:UP000000226};
RN [1] {ECO:0000313|Proteomes:UP000000226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX PubMed=24908249; DOI=10.1038/ng.3008;
RA Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT "A reference genome for common bean and genome-wide analysis of dual
RT domestications.";
RL Nat. Genet. 46:707-713(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; CM002291; ESW23508.1; -; Genomic_DNA.
DR RefSeq; XP_007151514.1; XM_007151452.1.
DR AlphaFoldDB; V7C2A5; -.
DR STRING; 3885.V7C2A5; -.
DR EnsemblPlants; ESW23508; ESW23508; PHAVU_004G053400g.
DR GeneID; 18632100; -.
DR Gramene; ESW23508; ESW23508; PHAVU_004G053400g.
DR KEGG; pvu:PHAVU_004G053400g; -.
DR eggNOG; KOG2665; Eukaryota.
DR OMA; GVHFTRM; -.
DR OrthoDB; 1815533at2759; -.
DR Proteomes; UP000000226; Chromosome 4.
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 PRINTS; PR00411; PNDRDTASEI.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000000226}.
FT DOMAIN 61..443
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 447 AA; 48934 MW; E479512B52DD48CD CRC64;
MLKQAVQRFE GCISTSRRNG DVHMKWKKHL FGNWVRSMSS KPRSSNNRST WYSVPKERVE
CVVIGAGVVG IAVARALALK GREVLVVESA PTFGTGTSSR NSEVIHAGIY YPANSFKAVF
CVRGREMLYE YCSKHDIPHK QIGKLIVATR SSEIPKLCDI LNCGIQNGVG GLKMVDGVDA
MRMEPELQCM KAILSPLTGI VDSHSLMLSL VGEAENHGAT FTYNSTVIGG HVEGNDICVH
VTETDRLKEW KGTSILHPEL LLTSKLVVNS TGLSALALAK RFSGLKSEVV PSSYYARGCY
FTLSNTKASP FRHLIYPIPE DGGIGVHVTI DLNGQVKFGP NVEWIDSVDD ISSFQNKFDY
SVNPNRAEQF YPEIRKYFPN LKDGSLVAGY SGIRPKLSGP SQLPADFVIQ GEDIHGVPGL
INLFGIESPG LTSSMAIAEF ICKRFVG
//