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Database: UniProt
Entry: A5DXM0_LODEL
LinkDB: A5DXM0_LODEL
Original site: A5DXM0_LODEL 
ID   A5DXM0_LODEL            Unreviewed;       546 AA.
AC   A5DXM0;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   24-JAN-2024, entry version 78.
DE   SubName: Full=D-lactate dehydrogenase 2, mitochondrial {ECO:0000313|EMBL:EDK43928.1};
GN   ORFNames=LELG_02107 {ECO:0000313|EMBL:EDK43928.1};
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508 {ECO:0000313|EMBL:EDK43928.1, ECO:0000313|Proteomes:UP000001996};
RN   [1] {ECO:0000313|EMBL:EDK43928.1, ECO:0000313|Proteomes:UP000001996}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 /
RC   NRRL YB-4239 {ECO:0000313|Proteomes:UP000001996};
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W., Harris D., Hoyer L.L., Hube B., Klis F.M.,
RA   Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M., Nikolaou E.,
RA   Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F., Sherlock G.,
RA   Shah P., Silverstein K.A., Skrzypek M.S., Soll D., Staggs R.,
RA   Stansfield I., Stumpf M.P., Sudbery P.E., Srikantha T., Zeng Q., Berman J.,
RA   Berriman M., Heitman J., Gow N.A., Lorenz M.C., Birren B.W., Kellis M.,
RA   Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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; CH981525; EDK43928.1; -; Genomic_DNA.
DR   RefSeq; XP_001527278.1; XM_001527228.1.
DR   AlphaFoldDB; A5DXM0; -.
DR   STRING; 379508.A5DXM0; -.
DR   GeneID; 5233865; -.
DR   KEGG; lel:LELG_02107; -.
DR   VEuPathDB; FungiDB:LELG_02107; -.
DR   eggNOG; KOG1232; Eukaryota.
DR   HOGENOM; CLU_017779_4_1_1; -.
DR   InParanoid; A5DXM0; -.
DR   OMA; TPRTCGE; -.
DR   OrthoDB; 1664005at2759; -.
DR   Proteomes; UP000001996; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; 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:UP000001996}.
FT   DOMAIN          111..290
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   546 AA;  60404 MW;  2F9102D6FC4589F7 CRC64;
     MHRRAVTATV AKSTSRTTTT SRLVSLTSRR SFLLTKFSSI PSSRVSVAAY STAKTVPLTA
     ETYASKVQRD PRYKKLTASD LEFFKLVLPG NSIITDKDDL DFYNEDWMRK YKGQSQLVLK
     PKTVEQVSQI VKYCNQEKLA VVPQGGNTGL VGGSNPVFDE IILSLSSMNE IRSFDEASGI
     LKVDAGVILE TADQYLAERG FIFPLDLGAK GSCQIGGNVA CNAGGLRLLK YGSLHGSVLG
     LEVVLPDGTI YDSMHSLRKD NTGYDLKQLF IGSEGTLGVI TGVSILCPSR PQANNVAFLA
     VKDYETVTKV FNECKKELSE ILSAFEFMDL NSQKLTQQHL GVEQHPIESG EYPFYILIET
     SGSNKEHDDE KLETFLGNAM ENGLVEDGII AQDESQIQSL WSWRESIPEA STMNGGVYKY
     DVSIPLKDLY NLVEACNVEL DKAGIVDFED ASKPVVSAIG YGHIGDGNLH LNVCVRQYSK
     EIEKVLEPFV YEWISEKKGS ISAEHGLGFQ KKNYIGYSKN DQEISMIKSI KNHFDPEGIM
     NPYKYV
//
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