ID A0A016S584_9BILA Unreviewed; 943 AA.
AC A0A016S584;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=L-2-hydroxyglutarate dehydrogenase, mitochondrial {ECO:0000256|ARBA:ARBA00041137};
DE EC=1.1.99.2 {ECO:0000256|ARBA:ARBA00038878};
GN Name=Acey_s0290.g1530 {ECO:0000313|EMBL:EYB85803.1};
GN ORFNames=Y032_0290g1530 {ECO:0000313|EMBL:EYB85803.1};
OS Ancylostoma ceylanicum.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB85803.1, ECO:0000313|Proteomes:UP000024635};
RN [1] {ECO:0000313|Proteomes:UP000024635}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX PubMed=25730766; DOI=10.1038/ng.3237;
RA Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA Aroian R.V.;
RT "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT ceylanicum identify infection-specific gene families.";
RL Nat. Genet. 47:416-422(2015).
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}.
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:EYB85803.1}.
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DR EMBL; JARK01001626; EYB85803.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A016S584; -.
DR STRING; 53326.A0A016S584; -.
DR Proteomes; UP000024635; Unassembled WGS sequence.
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; 2.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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; 2.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
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:UP000024635}.
FT DOMAIN 80..445
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 537..935
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 943 AA; 105441 MW; B84C3695B602F73A CRC64;
MRSCRIRDMS LPCVLARSTH RLLLGHGIRC VSNAPSGSGT GKSSESAFRA AAAAPLSYSE
YRSAPWATDV TPFSFPPQFD IVVVGGGIVG SATARQLKIE HPEMSICMVE KESKLAPHQS
GNNSGVIHAG IYYTPGSLKA KLCVEGMDLA YKFFAEHNFP HKKTGKLIVA VEPEEIPRLD
ALFERALKNG CKDIKMIDGS QIKEYEPYCK GLKALWSPHT GIVDWGEVAK AFAADFQKRG
GTVYTNYPVK DITQSTHPMF PISVHSDWKS SRILTKYLVT CAGLHSDRVA QLTGCDPAPK
IVPFRGEYLL LKPEKRHIVK TNIYPVPDPR FPFLGVHFTP RMNGDVWLGP NAVLAYKREG
YSYFSISPTD LFESLTYSGM RKLVGKYFTY GMKELYRGIF IGAQVKQLQR FVPELKRSDV
TRGYSGVRAQ AMDPEGNLVD DFVFDSGHGP VNEYSITSWI HMMPHFFSCV SEYSTFEMHH
LLVQHQVWRS QKWWRKKIRG LSLSCALSRS THRLLVSHGL RCVSNAPPGY DFPPQFDMVV
VGGGIVGSAV ARQLKMEHPE MKICQVEKEG KLAPHQSGNN SGVIHAGIYY TPGTLKAKLC
VEGNDLAYKF FAENNFPHKK SGKLIVAVEP HEIPRLDNLY ERAQKNGCKD VKMIEGSQIK
EYEPYCKGLK ALWSPHTGIV EWGEVAKALS ADFEKKGGTV YVNYPVKNIT ASTHPMFPIS
IHSDWRNTRI LTKYLVTCCG LHSDRVAQLT GCNPAPKIIP FRGEYLLLRP EKKHIVKTNI
YPVPDPRLPF LGVHFTPRMN GDVWLGPNAV LAYKREGYSY FSVSPSDLYD SLMYSGMRKL
IFKYFAFGMK ELYRGVFIGA QVKQLQRFVP ELRRRDVTRG PAGVRAQAMD PQGNLVDDFV
FDSGTGPLSK RVLHVRNAPS PGATSSLAIA KMVAKEVKSR FSL
//
