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Database: UniProt
Entry: G1SGE9_RABIT
LinkDB: G1SGE9_RABIT
Original site: G1SGE9_RABIT 
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
//
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