ID A0A151MJU5_ALLMI Unreviewed; 820 AA.
AC A0A151MJU5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=D-2-hydroxyglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00039639};
DE EC=1.1.99.39 {ECO:0000256|ARBA:ARBA00039003};
GN Name=ING5 {ECO:0000313|EMBL:KYO24805.1};
GN ORFNames=Y1Q_0014101 {ECO:0000313|EMBL:KYO24805.1};
OS Alligator mississippiensis (American alligator).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Crocodylia; Alligatoridae; Alligatorinae;
OC Alligator.
OX NCBI_TaxID=8496 {ECO:0000313|EMBL:KYO24805.1};
RN [1] {ECO:0000313|EMBL:KYO24805.1, ECO:0000313|Proteomes:UP000050525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KSC_2009_1 {ECO:0000313|EMBL:KYO24805.1};
RX PubMed=22293439; DOI=10.1186/gb-2012-13-1-415;
RA St John J.A., Braun E.L., Isberg S.R., Miles L.G., Chong A.Y., Gongora J.,
RA Dalzell P., Moran C., Bed'hom B., Abzhanov A., Burgess S.C., Cooksey A.M.,
RA Castoe T.A., Crawford N.G., Densmore L.D., Drew J.C., Edwards S.V.,
RA Faircloth B.C., Fujita M.K., Greenwold M.J., Hoffmann F.G., Howard J.M.,
RA Iguchi T., Janes D.E., Khan S.Y., Kohno S., de Koning A.J., Lance S.L.,
RA McCarthy F.M., McCormack J.E., Merchant M.E., Peterson D.G., Pollock D.D.,
RA Pourmand N., Raney B.J., Roessler K.A., Sanford J.R., Sawyer R.H.,
RA Schmidt C.J., Triplett E.W., Tuberville T.D., Venegas-Anaya M.,
RA Howard J.T., Jarvis E.D., Guillette L.J.Jr., Glenn T.C., Green R.E.,
RA Ray D.A.;
RT "Sequencing three crocodilian genomes to illuminate the evolution of
RT archosaurs and amniotes.";
RL Genome Biol. 13:415-415(2012).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYO24805.1}.
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DR EMBL; AKHW03006003; KYO24805.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151MJU5; -.
DR STRING; 8496.A0A151MJU5; -.
DR Proteomes; UP000050525; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR CDD; cd16863; ING_ING5; 1.
DR CDD; cd15586; PHD_ING4_5; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2190; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR Gene3D; 6.10.140.1740; -; 1.
DR Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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; IPR024610; ING_N_histone-binding.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
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 Pfam; PF12998; ING; 1.
DR SMART; SM01408; ING; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000050525};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 368..547
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 114..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 820 AA; 91616 MW; B0C4AE87313B17FA CRC64;
MYLEHYLDSI ENLPCELQRN FQLMRELDQR TEDKKAEIDS LAAEYIASVK SMLPEQRVEH
IKKIQNAYSK CKEYSDDKVQ LAMQTYEMVD KHIRRLDADL ARFEADLKDK LEASDFESPG
GRGLKKGRSQ KDKRGSRGRG RRTSEEDTPK KKKLKGGSEF ADTILSVHPS DVLDMPVDPN
EPTYCLCHQV SYGEMIGCDN PDCPIEWFHF ACVDLTTKPK GKCRRKENRK EVGRSRSGSR
SRSAALPVSG YHGCIFSSPV SCGLVWFDPT KMANELPEQN LGSMDQCYSP VDTQAEQTCR
TTQDVKSQAI HLVEGWSPGQ ESSPYQLRQF TGSDADHDLA FFERIIPGGV ITDPEELKPF
NVDWLQSVRG SSKLLLRPRT TAEVSEILRY SNERNLAVNP QGGNTGLVGG SVPVFDEIIL
STALMNQVIS FDSVSGILVC QAGCILENLN RYLEELDFIM PLDLGAKGSC HIGGNVATNA
GGLRLLRYGS LRGTVLGLEV VLANGSVLNC LASLRKDNTG YDLKQLFIGS EGTLGVITAV
SILCPRKPMA VNLAFLGCQS FSQILETFTT CKRMLGEILS AYEFMDDRCM KLVVSHLKLS
NPVTESPFFI LIETSGSNST HDQEKLNNFL ECVMASGLVT DGTVATDDKK IKTLWALRER
ITEALTYDGY VFKYDISLPV EKLYDLVIDT RVRLARSAKN VVGYGHLGDG NLHLNITAES
YSHSLLDAIE PFVYEWTAKY RGSISAEHGL GFKKKHYIQY RMQSLLRELS ISTQTQTLWK
EETSAGHSYM GSSLDMKVHV ENRWFIYGTC HCSGNLYADL
//
