ID A0A093JDI7_STRCA Unreviewed; 487 AA.
AC A0A093JDI7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=D-2-hydroxyglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00039639};
DE EC=1.1.99.39 {ECO:0000256|ARBA:ARBA00039003};
DE Flags: Fragment;
GN ORFNames=N308_04954 {ECO:0000313|EMBL:KFV76949.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV76949.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV76949.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV76949.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC 4 family. {ECO:0000256|ARBA:ARBA00008000}.
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DR EMBL; KL205920; KFV76949.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093JDI7; -.
DR STRING; 441894.ENSSCUP00000006137; -.
DR Proteomes; UP000053584; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000053584}.
FT DOMAIN 63..242
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV76949.1"
FT NON_TER 487
FT /evidence="ECO:0000313|EMBL:KFV76949.1"
SQ SEQUENCE 487 AA; 53347 MW; FC6A77C02EB01DB9 CRC64;
ALHPACPSFQ EVMLTSERYS VQRLPFSHVS NDDIAFFESI MPGRVITNPE ELKPFNVDWL
KSVRGCSKLL LKPQTAAEVS QVLRHCYERN LAVNPQGGNT GLVGGSVPVF DEVILSTVLM
SQIISFDKVS GILVCQAGCV LENLNQYLEG KGFIMPLDLG AKGSCHIGGN VATNAGGLRL
LRYGSLRGTV LGLEVVLADG SVLDCLASLR KDNTGYDLKQ LFIGSEGTLG VITAVSILCP
QKPKAVNLAF LGCQSFTQVL KTFTTCRAML GEILSAYEFM DNKCMELIER HLKLSSPVTG
SPFYVLIETS GSDSTHDEEK LNSFLEQVMA SGLVTNGTVA TDEKKIKMLW SLRERITEAL
THDGYVYKYD ISLPVGKLYD LVTDTRARLG QCAKNVVGYG HLGDGNLHLN ITAESYSHSL
LDAIEPFVYE WTARCNGSIS AEHGLGFKKK CFIQYSKPKE AVFLMQRFKA MLDPKGILNP
YKTLPSS
//
