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
//