ID G1SGE9_RABIT Unreviewed; 484 AA.
AC G1SGE9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN Name=LDHD {ECO:0000313|Ensembl:ENSOCUP00000001653.2};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000001653.2, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000001653.2, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000001653.2,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000001653.2}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000001653.2};
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
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; AAGW02055362; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_002711769.1; XM_002711723.3.
DR AlphaFoldDB; G1SGE9; -.
DR STRING; 9986.ENSOCUP00000001653; -.
DR PaxDb; 9986-ENSOCUP00000001653; -.
DR Ensembl; ENSOCUT00000001918.2; ENSOCUP00000001653.2; ENSOCUG00000001913.2.
DR GeneID; 100341422; -.
DR KEGG; ocu:100341422; -.
DR CTD; 197257; -.
DR eggNOG; KOG1231; Eukaryota.
DR GeneTree; ENSGT00940000158705; -.
DR HOGENOM; CLU_017779_3_0_1; -.
DR InParanoid; G1SGE9; -.
DR OMA; CIMASFD; -.
DR OrthoDB; 1664005at2759; -.
DR TreeFam; TF314122; -.
DR Proteomes; UP000001811; Chromosome 5.
DR Bgee; ENSOCUG00000001913; Expressed in kidney and 18 other cell types or tissues.
DR GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:1903457; P:lactate catabolic process; IEA:Ensembl.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2740; -; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT DOMAIN 61..242
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 57..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 484 AA; 51735 MW; 8B60EF0CDEC9D309 CRC64;
MACLLRVARG GLSPWRGYCS KGTQGALSEG FVEALKAVVG SPHVSTAAVV REQHGHDESM
HRCQPPDAVS VAPEHRPGQP GWQPCNGQRV PIIPIGTGNG LEGGVCATQG GVCINLTHMD
RITELNPEDF SVVVEPGVTR KALNTHLRDS GLWFPVDPGA DASLCGMAAT GASGTNAVRY
GTMRDNVLNL EVVLPDGRLL HTAGRGRRSR KSAAGYDLTG LFVGSEGTLG LITAATLRLH
PVPEATVAAT CAFPSVQAAV DSTVQILQAA VPVARIEFLD DIMMDACNRY SKLNCSVAPT
LFLEFHGSKQ ALEEQVQRAE EIVQLNGASH FSWAKESEER SRLWAARHNA WYAVLALRPG
CKGYSTDVCV PISRLPEILV RTKEELKASG LTGAIVGHVG DGNFHCILLV DPEDADELQR
VEAFAEELGR RALALHGTCT GEHGIGLGKR QLLREEVGPV GLETMRQLKA TLDPRGLMNP
GKVL
//