(data stored in SCRATCH zone)

SWISSPROT: B6HDG8_PENRW

ID   B6HDG8_PENRW            Unreviewed;       340 AA.
AC   B6HDG8;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   08-MAY-2019, entry version 71.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|RuleBase:RU003405};
DE            EC=1.1.1.37 {ECO:0000256|RuleBase:RU003405};
GN   ORFNames=Pc20g01610 {ECO:0000313|EMBL:CAP85490.1}, PCH_Pc20g01610
GN   {ECO:0000313|EMBL:CAP85490.1};
OS   Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 /
OS   Wisconsin 54-1255) (Penicillium chrysogenum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium;
OC   Penicillium chrysogenum species complex.
OX   NCBI_TaxID=500485 {ECO:0000313|EMBL:CAP85490.1, ECO:0000313|Proteomes:UP000000724};
RN   [1] {ECO:0000313|EMBL:CAP85490.1, ECO:0000313|Proteomes:UP000000724}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255
RC   {ECO:0000313|Proteomes:UP000000724};
RX   PubMed=18820685; DOI=10.1038/nbt.1498;
RA   van den Berg M.A., Albang R., Albermann K., Badger J.H., Daran J.-M.,
RA   Driessen A.J.M., Garcia-Estrada C., Fedorova N.D., Harris D.M.,
RA   Heijne W.H.M., Joardar V.S., Kiel J.A.K.W., Kovalchuk A., Martin J.F.,
RA   Nierman W.C., Nijland J.G., Pronk J.T., Roubos J.A.,
RA   van der Klei I.J., van Peij N.N.M.E., Veenhuis M., von Doehren H.,
RA   Wagner C., Wortman J.R., Bovenberg R.A.L.;
RT   "Genome sequencing and analysis of the filamentous fungus Penicillium
RT   chrysogenum.";
RL   Nat. Biotechnol. 26:1161-1168(2008).
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; AM920435; CAP85490.1; -; Genomic_DNA.
DR   RefSeq; XP_002562720.1; XM_002562674.1.
DR   STRING; 1108849.XP_002562720.1; -.
DR   EnsemblFungi; CAP85490; CAP85490; PCH_Pc20g01610.
DR   GeneID; 8312298; -.
DR   KEGG; pcs:Pc20g01610; -.
DR   eggNOG; KOG1494; Eukaryota.
DR   eggNOG; COG0039; LUCA.
DR   HOGENOM; HOG000213792; -.
DR   KO; K00026; -.
DR   OMA; QCTPKVE; -.
DR   OrthoDB; 976445at2759; -.
DR   BioCyc; PCHR:PC20G01610-MONOMER; -.
DR   Proteomes; UP000000724; Contig Pc00c20.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
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; B6HDG8.
DR   SWISS-2DPAGE; B6HDG8.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000724};
KW   NAD {ECO:0000256|RuleBase:RU003405};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003369};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000724};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU003405}.
FT   DOMAIN       25    168       Ldh_1_N. {ECO:0000259|Pfam:PF00056}.
FT   DOMAIN      170    336       Ldh_1_C. {ECO:0000259|Pfam:PF02866}.
FT   ACT_SITE    200    200       Proton acceptor. {ECO:0000256|PIRSR:
FT                                PIRSR000102-1}.
FT   BINDING     110    110       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000102-2}.
FT   BINDING     142    142       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000102-2}.
FT   BINDING     176    176       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR000102-2}.
SQ   SEQUENCE   340 AA;  35729 MW;  B244007299927EAA CRC64;
     MFAARRTVNL FQKRAFSASA INASKVSVLG AAGGIGQPLS LLLKLNPRVS ELALYDIRGG
     PGVAADLSHI NTNSTVTGYN PDASGLRDCL EGSEIILIPA GVPRKPGMTR DDLFNTNASI
     VRDLAKAAAE AAPKAHVLVI ANPVNSTVPI VAEVYKARNV YDPKRLFGVT TLDVVRASRF
     ISQVQNTNPA GEAVPVVGGH SGVTIVPLLS QSNHSSIAGQ ARDALVNRIQ FGGDEVVKAK
     DGAGSATLSM AMAGARFAES LLRAAQGEKG VIEPTFVDSP LYKDQGIDFF ASRVELGPNG
     VEKINSVGEV NEYEQGLLDA CLTDLKKNIQ KGVDFVKANP
//

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