ID Q178E1_AEDAE Unreviewed; 511 AA.
AC Q178E1;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=D-2-hydroxyglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00039639};
DE EC=1.1.99.39 {ECO:0000256|ARBA:ARBA00039003};
GN Name=5567262 {ECO:0000313|EnsemblMetazoa:AAEL005921-PA};
OS Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Culicinae; Aedini; Aedes; Stegomyia.
OX NCBI_TaxID=7159 {ECO:0000313|EnsemblMetazoa:AAEL005921-PA, ECO:0000313|Proteomes:UP000008820};
RN [1] {ECO:0000313|EnsemblMetazoa:AAEL005921-PA, ECO:0000313|Proteomes:UP000008820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LVP_AGWG {ECO:0000313|EnsemblMetazoa:AAEL005921-PA,
RC ECO:0000313|Proteomes:UP000008820};
RG Aedes aegypti Genome Working Group (AGWG);
RA Matthews B.J.;
RT "Aedes aegypti genome working group (AGWG) sequencing and assembly.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AAEL005921-PA}
RP IDENTIFICATION.
RC STRAIN=LVP_AGWG {ECO:0000313|EnsemblMetazoa:AAEL005921-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-malate + A = AH2 + oxaloacetate; Xref=Rhea:RHEA:67460,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15588, ChEBI:CHEBI:16452,
CC ChEBI:CHEBI:17499; Evidence={ECO:0000256|ARBA:ARBA00035965};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67461;
CC Evidence={ECO:0000256|ARBA:ARBA00035965};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000256|ARBA:ARBA00008000}.
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DR RefSeq; XP_001651707.1; XM_001651657.1.
DR AlphaFoldDB; Q178E1; -.
DR STRING; 7159.Q178E1; -.
DR PaxDb; 7159-AAEL005921-PA; -.
DR EnsemblMetazoa; AAEL005921-RA; AAEL005921-PA; AAEL005921.
DR GeneID; 5567262; -.
DR KEGG; aag:5567262; -.
DR VEuPathDB; VectorBase:AAEL005921; -.
DR eggNOG; KOG1232; Eukaryota.
DR HOGENOM; CLU_017779_4_1_1; -.
DR InParanoid; Q178E1; -.
DR OMA; YNEDWMR; -.
DR OrthoDB; 1664005at2759; -.
DR Proteomes; UP000008820; Chromosome 3.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2190; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR PANTHER; PTHR43716; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43716:SF1; D-2-HYDROXYGLUTARATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000008820}.
FT DOMAIN 87..266
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 511 AA; 56537 MW; 90A65662D9CDA646 CRC64;
MFLLRSMPLK ASLSQKNVLP NLCRRLASSH REIPALTKER YPVKRGQYSE VTDRDVTKFE
SILGGSSRVL TQAEDTQGYN IDYLGSVRGY SRVVLKPKST EEVADIMKYC NERKLAVCPQ
GGNTGLVGGS VPVFDEVVLS LQLMDKIEQI DEYSGILVCQ SGCVLGTLEE KVNEKGLVMP
LDLGAKGSCH IGGNVSTNAG GLRLVRYGNL HGSVLGVEAV TAEGRVMDLM SNFKKDNTGY
HLKHLFIGSE GTLGIITKLS IFCPTASKSV NVAFLGLESY DAVKNTFLAA KRGLGEILSS
CEMIDEASLE SSTYHFNLQS PIEKYPFYML IETSGSNMAH DEEKLTNFLE SSMENGLVLD
GTVTNEPTKM RNIWKLRELI ADSLINDGYC FKYDISLPLD NFYDIVLAVR DRVGPLATKV
TGYGHIGDSN LHLNVSCAKF TPEIYKLLEP FVYEYTSNVR GSVSAEHGIG FLKTKYLKYS
KRPESLMLMQ QMKQLMDPNG ILNPYKVLPQ V
//
