ID G7Q1M9_MACFA Unreviewed; 507 AA.
AC G7Q1M9;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=EGM_11953 {ECO:0000313|EMBL:EHH60567.1};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
RN [1] {ECO:0000313|EMBL:EHH60567.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CE-4 {ECO:0000313|EMBL:EHH60567.1};
RX PubMed=22002653; DOI=10.1038/nbt.1992;
RA Yan G., Zhang G., Fang X., Zhang Y., Li C., Ling F., Cooper D.N., Li Q.,
RA Li Y., van Gool A.J., Du H., Chen J., Chen R., Zhang P., Huang Z.,
RA Thompson J.R., Meng Y., Bai Y., Wang J., Zhuo M., Wang T., Huang Y.,
RA Wei L., Li J., Wang Z., Hu H., Yang P., Le L., Stenson P.D., Li B., Liu X.,
RA Ball E.V., An N., Huang Q., Zhang Y., Fan W., Zhang X., Li Y., Wang W.,
RA Katze M.G., Su B., Nielsen R., Yang H., Wang J., Wang X., Wang J.;
RT "Genome sequencing and comparison of two nonhuman primate animal models,
RT the cynomolgus and Chinese rhesus macaques.";
RL Nat. Biotechnol. 29:1019-1023(2011).
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; CM001295; EHH60567.1; -; Genomic_DNA.
DR AlphaFoldDB; G7Q1M9; -.
DR eggNOG; KOG1231; Eukaryota.
DR Proteomes; UP000009130; Chromosome 20.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
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; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11748:SF111; D-LACTATE DEHYDROGENASE, MITOCHONDRIAL-RELATED; 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 Mitochondrion {ECO:0000256|ARBA:ARBA00023128}.
FT DOMAIN 62..265
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 507 AA; 54676 MW; 66334D5D0F4FDFC1 CRC64;
MARLLRAATW GLFPWRGYCS QKAKGELCRD FVEALKAVVG GSHVSTATVV REQHGRDESV
HRCEPPDAVV WPQNVEQVSR LAALCYRQGV PIIPFGTGTG LEGGVCAVQG GVCINLTHMD
RILELNLEDF SVVVEPGVTR KALNLHLRDS GLWFPVDPGA DASLCGMAAT GASGTNAVRY
GTMRDNVLNL EVVLPDGRLL HTAGQGRHFR LGFWSEIPHH TAWYSPCVSL GPRKSAAGYN
LTGLFVGSEG TLGLITATTL RLHPVPEAIV AATCAFPSVQ AAVDSTVHIL QAAVPVARIE
FLDEVMMDAC NRYSKLNCSV APTLFLEFHG SQQALEEQLQ RTEEIVQQNG ASDFSWAKAA
EERSQLWTAR HNAWYAALAM QPGCKGYSTD VCVPISRLPE ILVQTKEDLN ASGLTGSIVG
HVGDGNFHCI LLVNPDDAEE LGRVKAFAEQ LGRRALALHG TCTGEHGIGL GKRQLLREEV
GAVGVETMRQ LKAVLDPQGL MNPGKVL
//
