ID E2C5C8_HARSA Unreviewed; 522 AA.
AC E2C5C8;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=D-2-hydroxyglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00039639};
DE EC=1.1.99.39 {ECO:0000256|ARBA:ARBA00039003};
GN ORFNames=EAI_16509 {ECO:0000313|EMBL:EFN76861.1};
OS Harpegnathos saltator (Jerdon's jumping ant).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Ponerinae; Ponerini; Harpegnathos.
OX NCBI_TaxID=610380 {ECO:0000313|Proteomes:UP000008237};
RN [1] {ECO:0000313|EMBL:EFN76861.1, ECO:0000313|Proteomes:UP000008237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R22 G/1 {ECO:0000313|EMBL:EFN76861.1,
RC ECO:0000313|Proteomes:UP000008237};
RX PubMed=20798317; DOI=10.1126/science.1192428;
RA Bonasio R., Zhang G., Ye C., Mutti N.S., Fang X., Qin N., Donahue G.,
RA Yang P., Li Q., Li C., Zhang P., Huang Z., Berger S.L., Reinberg D.,
RA Wang J., Liebig J.;
RT "Genomic comparison of the ants Camponotus floridanus and Harpegnathos
RT saltator.";
RL Science 329:1068-1071(2010).
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 EMBL; GL452770; EFN76861.1; -; Genomic_DNA.
DR RefSeq; XP_011151198.1; XM_011152896.2.
DR RefSeq; XP_011151199.1; XM_011152897.2.
DR RefSeq; XP_011151200.1; XM_011152898.2.
DR AlphaFoldDB; E2C5C8; -.
DR STRING; 610380.E2C5C8; -.
DR EnsemblMetazoa; XM_011152896.3; XP_011151198.1; LOC105190242.
DR EnsemblMetazoa; XM_011152897.3; XP_011151199.1; LOC105190242.
DR EnsemblMetazoa; XM_011152898.3; XP_011151200.1; LOC105190242.
DR GeneID; 105190242; -.
DR KEGG; hst:105190242; -.
DR InParanoid; E2C5C8; -.
DR OMA; YNEDWMR; -.
DR OrthoDB; 1664005at2759; -.
DR PhylomeDB; E2C5C8; -.
DR Proteomes; UP000008237; Unassembled WGS sequence.
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:UP000008237}.
FT DOMAIN 90..269
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 522 AA; 57754 MW; D8247F7CD4AA4907 CRC64;
MRTTPVSVLL RRCNDAVRQP TVKIASLSRR CYSANPKPEL TSIRYKVHRG PYASISTADV
RFFDGLLGSS RIITDPEECE MYNIDFPKTV RGNSQLILKP KSTEEVSAIL KYCNEKRLAV
CPQSGNTGLV GGSTPVFDEI VVSMKLMNKI LETNHLAGVL TCEAGCVLQD LDDHLTTVGL
MMPLDLGAKG SCLIGGCVST NAGGLRLLRY GNLHGNVLGV EAVKANGDVV DAMNTLKKNN
TGYHVKHLFI GSEGTLGIVT KVVIQCPPLP KAVNVAFLGL TNFNKVLETY HLAKKELGEI
LSSCEMMDRL SLDVSINHLG LKNPLTMHEN GHDFYMVIET SGSHSAHDEE KLSLFVEKAL
NQGIIEDGTL ANETTKVNHI WAMRERISEG VLRDGYVFKY DISLPLSSYY EIVEVLRERI
RDPRVVRISG YGHIGDGNIH VQVSIPEYYE DIAAQLEPFI FEYISQHKGS ISAEHGIGFK
KPKYLHLSRN SSEIEMMHDL KKLMDPNGIL NPYKVLQPVT TA
//
