ID   YN53_SCHPO              Reviewed;         526 AA.
AC   Q9C1X2;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 122.
DE   RecName: Full=Putative D-lactate dehydrogenase C713.03, mitochondrial;
DE            EC=1.1.2.4;
DE   Flags: Precursor;
GN   ORFNames=SPBC713.03;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-lactate + 2 Fe(III)-[cytochrome c] = 2 Fe(II)-[cytochrome
CC         c] + 2 H(+) + pyruvate; Xref=Rhea:RHEA:13521, Rhea:RHEA-COMP:10350,
CC         Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16004, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.1.2.4;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000305};
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000269|PubMed:16823372}.
CC   -!- SIMILARITY: Belongs to the FAD-binding oxidoreductase/transferase type
CC       4 family. {ECO:0000305}.
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DR   EMBL; CU329671; CAC22604.1; -; Genomic_DNA.
DR   RefSeq; NP_595342.1; NM_001021250.2.
DR   AlphaFoldDB; Q9C1X2; -.
DR   SMR; Q9C1X2; -.
DR   BioGRID; 277666; 12.
DR   STRING; 4896.SPBC713.03.1; -.
DR   MaxQB; Q9C1X2; -.
DR   PaxDb; Q9C1X2; -.
DR   PRIDE; Q9C1X2; -.
DR   EnsemblFungi; SPBC713.03.1; SPBC713.03.1:pep; SPBC713.03.
DR   GeneID; 2541151; -.
DR   KEGG; spo:SPBC713.03; -.
DR   PomBase; SPBC713.03; -.
DR   VEuPathDB; FungiDB:SPBC713.03; -.
DR   eggNOG; KOG1232; Eukaryota.
DR   HOGENOM; CLU_017779_4_1_1; -.
DR   InParanoid; Q9C1X2; -.
DR   OMA; CNDNMLA; -.
DR   PhylomeDB; Q9C1X2; -.
DR   Reactome; R-SPO-880009; Interconversion of 2-oxoglutarate and 2-hydroxyglutarate.
DR   PRO; PR:Q9C1X2; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005759; C:mitochondrial matrix; ISO:PomBase.
DR   GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR   GO; GO:0099615; F:(D)-2-hydroxyglutarate-pyruvate transhydrogenase activity; ISO:PomBase.
DR   GO; GO:0004458; F:D-lactate dehydrogenase (cytochrome) activity; ISO:PomBase.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0006091; P:generation of precursor metabolites and energy; IC:PomBase.
DR   GO; GO:1903457; P:lactate catabolic process; ISO:PomBase.
DR   Gene3D; 1.10.45.10; -; 1.
DR   Gene3D; 3.30.43.10; -; 1.
DR   Gene3D; 3.30.465.10; -; 1.
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; IPR004113; FAD-linked_oxidase_C.
DR   InterPro; IPR006094; Oxid_FAD_bind_N.
DR   InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR   Pfam; PF02913; FAD-oxidase_C; 1.
DR   Pfam; PF01565; FAD_binding_4; 1.
DR   SUPFAM; SSF55103; SSF55103; 1.
DR   SUPFAM; SSF56176; SSF56176; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   FAD; Flavoprotein; Mitochondrion; Oxidoreductase; Reference proteome;
KW   Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           ?..526
FT                   /note="Putative D-lactate dehydrogenase C713.03,
FT                   mitochondrial"
FT                   /id="PRO_0000317236"
FT   DOMAIN          93..272
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
SQ   SEQUENCE   526 AA;  58473 MW;  00FAF5ABA81EBC11 CRC64;
     MHSLQCRRVI PFGKLSLSLH APRNALRFVH KPAFTFESYK SLHRDPKYAK LSEQDVQVFK
     SIIGKDGSLI DGLDKSTDPA DLDAFNIDWM NKYRGKTQLA LKPKTTQQVS EILKYCNQKK
     LAVVPQGGNT GLVGGSVPVF DEIVLNLGLM NQIHTFDEIS GVITLDSGVI LENADNFLAE
     KGYMFPLDLG AKGSCQVGGC AATAAGGLRL LRYGSLHGSI LGMEAVLPDG TILDNLVTLR
     KDNTGLDIKQ LFIGSEGYLG VITKLSVICP KRPSSTNVAF FGVPSYENVL KAFSETRSHL
     TEILSAFELM DNTSQTLVDK YSGTQRPLED EHPFYVLVET QGSNKEHDEQ KITALVEDLL
     EKEIISDGVL AQDESQLRVL WERREGITEC LAKAGSGVYK YDVSLPLPVL YDLVNDTKKR
     LIEFNLLDDT PEHPVIDVVG FGHMGDGNLH LNIAVRQFDK RVEKCLEPWV YEWVSRHRGS
     ISAEHGLGLL KKPFVGYSKS KEMIHLMKTL KNVFDPNGIM LPYKYV