(data stored in SCRATCH zone)

SWISSPROT: Q6BM17_DEBHA

ID   Q6BM17_DEBHA            Unreviewed;       346 AA.
AC   Q6BM17;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 2.
DT   08-MAY-2019, entry version 104.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|RuleBase:RU003405};
DE            EC=1.1.1.37 {ECO:0000256|RuleBase:RU003405};
GN   OrderedLocusNames=DEHA2F09020g {ECO:0000313|EMBL:CAG89095.2};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / JCM 1990 / NBRC
OS   0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG89095.2, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG89095.2, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / JCM 1990 / NBRC 0083 / IGC 2968
RC   {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S.,
RA   Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E.,
RA   Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V.,
RA   Barnay S., Blanchin S., Beckerich J.M., Beyne E., Bleykasten C.,
RA   Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A.,
RA   Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A.,
RA   Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R.,
RA   Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H.,
RA   Nicaud J.M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O.,
RA   Pellenz S., Potier S., Richard G.F., Straub M.L., Suleau A.,
RA   Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B.,
RA   Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate;
CC         Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.37; Evidence={ECO:0000256|RuleBase:RU003405};
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily.
CC       {ECO:0000256|RuleBase:RU003369}.
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DR   EMBL; CR382138; CAG89095.2; -; Genomic_DNA.
DR   RefSeq; XP_460754.2; XM_460754.1.
DR   STRING; 4959.XP_460754.2; -.
DR   EnsemblFungi; CAG89095; CAG89095; DEHA2F09020g.
DR   GeneID; 2903770; -.
DR   KEGG; dha:DEHA2F09020g; -.
DR   HOGENOM; HOG000213792; -.
DR   InParanoid; Q6BM17; -.
DR   KO; K00026; -.
DR   OMA; PRNHGFT; -.
DR   OrthoDB; 1204514at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:1990429; C:peroxisomal importomer complex; IEA:EnsemblFungi.
DR   GO; GO:0005782; C:peroxisomal matrix; IEA:EnsemblFungi.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003729; F:mRNA binding; IEA:EnsemblFungi.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006635; P:fatty acid beta-oxidation; IEA:EnsemblFungi.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0006735; P:NADH regeneration; IEA:EnsemblFungi.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.110.10; -; 1.
DR   InterPro; IPR001557; L-lactate/malate_DH.
DR   InterPro; IPR022383; Lactate/malate_DH_C.
DR   InterPro; IPR001236; Lactate/malate_DH_N.
DR   InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR   InterPro; IPR001252; Malate_DH_AS.
DR   InterPro; IPR010097; Malate_DH_type1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   TIGRFAMs; TIGR01772; MDH_euk_gproteo; 1.
DR   PROSITE; PS00068; MDH; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q6BM17.
DR   SWISS-2DPAGE; Q6BM17.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000599};
KW   NAD {ECO:0000256|RuleBase:RU003405};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003369};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000599};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU003405}.
FT   DOMAIN        2    150       Ldh_1_N. {ECO:0000259|Pfam:PF00056}.
FT   DOMAIN      152    341       Ldh_1_C. {ECO:0000259|Pfam:PF02866}.
FT   ACT_SITE    184    184       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000102-1}.
FT   BINDING      92     92       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000102-2}.
FT   BINDING     124    124       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000102-2}.
FT   BINDING     158    158       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000102-2}.
SQ   SEQUENCE   346 AA;  36388 MW;  5A2C5BFE711AA0D4 CRC64;
     MVKVTVCGAA GGIGQPLSLL LKLNPQVSEL SLFDVVNANG VAADLSHICS PAKVTGYQPS
     SKEDRDTIQK ALVNSDLVVI PAGVPRKPGM TRADLFNINA SIIRDIVGSI GKACPNAAIL
     IISNPVNSTV PIAAEVLKKL GVFNPKKLFG VTTLDSVRAE TFLGELIKET PTSLKGQISV
     IGGHSGDTIV PLVHATASVA KKVSGLSKSQ YNEFIHRVQF GGDEVVKAKN GAGSATLSMA
     YAGYRFAEKV IGSLNGQSES SSEIPDSSYI YLAGVPNGKE LSQKYLKNSE FFSVPVILEK
     GQIKAFVNPF DKLNVTSEES KLVDIALGGL QNSIDQGTTF VTGSKL
//

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