ID   A0A0C9MTK0_9FUNG        Unreviewed;       535 AA.
AC   A0A0C9MTK0;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=D-lactate dehydrogenase 2, mitochondrial {ECO:0000313|EMBL:GAN06732.1};
GN   ORFNames=MAM1_0134c06220 {ECO:0000313|EMBL:GAN06732.1};
OS   Mucor ambiguus.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC   Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX   NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN06732.1};
RN   [1] {ECO:0000313|EMBL:GAN06732.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN06732.1};
RA   Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT   "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT   ambiguus NBRC6742.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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; DF836423; GAN06732.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C9MTK0; -.
DR   STRING; 91626.A0A0C9MTK0; -.
DR   OrthoDB; 1664005at2759; -.
DR   Proteomes; UP000053815; 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:UP000053815}.
FT   DOMAIN          101..280
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   535 AA;  59051 MW;  F0D7FA2F59540D81 CRC64;
     MLSIASRLRA ISSRVALTSI KPIAQKTAVK SVSIMCTRRT YATKEVSYTV DKFPGYVRNE
     NFKKLTAQDV EHFKTIVGEN GLIHDNQDDL FAFNTDWMHK FRGKSQLVLK PKTTQQVSDI
     MKYCNQQKLA VVPQGGNTGL VGGSVPVFDE VVLSLQGMNK IRGFDNVSGI LTADAGCVLE
     VLDNWLGEKG YMMPLDLGAK GSCHIGGNIA TNAGGLRLLR YGSLHGTVLG LEVVLPDGTI
     LDNMSTLRKD NTGYDLKQLF IGSEGTIGVI TGVSILTPHR SKAVNVALLG LNSFEDVQKA
     FKQSRVELSE ILSAFEFWDT NALQMFKKHA TPKDVMEKEY PFYVLIETSG SNKDHDDEKL
     TNYLENMMVD GVAEDGVVAQ DETQIRGLWS LREGFTEALG KEPAVYKYDI SMPVPKLYEC
     VEDMRQHLRD GGVFGQPDSP VTDVVAYGHV GDGNLHLNIA ASRLESRVSA LIEPYLFEWV
     ANHQGSISAE HGLGVAKNEF LGYSKSPVMI QMMKTMKNML DPNGIMNPYK YLPSN
//