ID A4IDW0_LEIIN Unreviewed; 522 AA.
AC A4IDW0; A0A2K4Z8X7; A0A381MXH8;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=L-2-hydroxyglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00041137};
DE EC=1.1.99.2 {ECO:0000256|ARBA:ARBA00038878};
GN ORFNames=LINJ_36_5700 {ECO:0000313|EMBL:CAM73045.1};
OS Leishmania infantum.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5671 {ECO:0000313|EMBL:CAM73045.1, ECO:0000313|Proteomes:UP000008153};
RN [1] {ECO:0000313|EMBL:CAM73045.1, ECO:0000313|Proteomes:UP000008153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCM5 {ECO:0000313|EMBL:CAM73045.1,
RC ECO:0000313|Proteomes:UP000008153};
RX PubMed=17572675; DOI=10.1038/ng2053;
RA Peacock C.S., Seeger K., Harris D., Murphy L., Ruiz J.C., Quail M.A.,
RA Peters N., Adlem E., Tivey A., Aslett M., Kerhornou A., Ivens A.,
RA Fraser A., Rajandream M.A., Carver T., Norbertczak H., Chillingworth T.,
RA Hance Z., Jagels K., Moule S., Ormond D., Rutter S., Squares R.,
RA Whitehead S., Rabbinowitsch E., Arrowsmith C., White B., Thurston S.,
RA Bringaud F., Baldauf S.L., Faulconbridge A., Jeffares D., Depledge D.P.,
RA Oyola S.O., Hilley J.D., Brito L.O., Tosi L.R., Barrell B., Cruz A.K.,
RA Mottram J.C., Smith D.F., Berriman M.;
RT "Comparative genomic analysis of three Leishmania species that cause
RT diverse human disease.";
RL Nat. Genet. 39:839-847(2007).
RN [2] {ECO:0000313|EMBL:CAM73045.1, ECO:0000313|Proteomes:UP000008153}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JPCM5 {ECO:0000313|EMBL:CAM73045.1,
RC ECO:0000313|Proteomes:UP000008153};
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
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; FR796468; CAM73045.1; -; Genomic_DNA.
DR RefSeq; XP_001469929.1; XM_001469892.1.
DR AlphaFoldDB; A4IDW0; -.
DR SMR; A4IDW0; -.
DR STRING; 5671.A4IDW0; -.
DR GeneID; 5074037; -.
DR KEGG; lif:LINJ_36_5700; -.
DR VEuPathDB; TriTrypDB:LINF_360064300; -.
DR eggNOG; KOG2665; Eukaryota.
DR InParanoid; A4IDW0; -.
DR OMA; FNCAFSK; -.
DR OrthoDB; 1815533at2759; -.
DR Proteomes; UP000008153; Chromosome 36.
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:SF2; 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 FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008153}.
FT DOMAIN 58..441
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 522 AA; 57398 MW; 14E25F3CE6D73661 CRC64;
MASVVGKVFS GMSQVAVVCG LVGAVYYRRE YGNMATDDAS TAHSLITFSR DDRRDIYDVA
IVGGGIVGVA TAREIRQKYP RKRVILIERE ADVAQHQSGH NSGCLHAGMF YPPGSAMARL
CPRGHSLIID YCKKNKLPYE LCGKIVVATE DSQRPTVQRM YDWGVANGVK GLEILEGEEA
IKKKEPLVTG VSALWSPVSG IIDFSEVTRC MLRELTAHAK NNFATQFQFD AQDFVGVSVT
KSKGAGTEEM VLIRGREKNH LGPEKTILAK NVITCCGLDS DVVAKHSGGI VEWLGKRVMQ
TYGFRGRYYQ LTPERRDMVR MHVYPCPDTR KGLSVGVHFT PTVDVRRGRQ VIIGPGSALA
LDRYGYTPYA IDLEYCFNCA FSKGGWVSLV SNFDVIFQTY YMDISKRQFL REAQKLIPSI
EAKDIVDSYC GVMAVGVAED GTLSMDLAME FARPRVTVPA TMDKKMLLEA IKDAPHSGKG
LEASDSSKPL ILNVRNAPSP AATASMAIAE DIVKAASSRF QW
//
