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Database: UniProt
Entry: A0A0A2K9V2_PENIT
LinkDB: A0A0A2K9V2_PENIT
Original site: A0A0A2K9V2_PENIT 
ID   A0A0A2K9V2_PENIT        Unreviewed;       330 AA.
AC   A0A0A2K9V2;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   RecName: Full=malate dehydrogenase {ECO:0000256|ARBA:ARBA00012995};
DE            EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995};
GN   ORFNames=PITC_072210 {ECO:0000313|EMBL:KGO63668.1};
OS   Penicillium italicum (Blue mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=40296 {ECO:0000313|EMBL:KGO63668.1, ECO:0000313|Proteomes:UP000030104};
RN   [1] {ECO:0000313|EMBL:KGO63668.1, ECO:0000313|Proteomes:UP000030104}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHI-1 {ECO:0000313|EMBL:KGO63668.1,
RC   ECO:0000313|Proteomes:UP000030104};
RX   PubMed=25338147; DOI=10.1094/MPMI-09-14-0261-FI;
RA   Ballester A.R., Marcet-Houben M., Levin E., Sela N., Selma-Lazaro C.,
RA   Carmona L., Wisniewski M., Droby S., Gonzalez-Candelas L., Gabaldon T.;
RT   "Genome, transcriptome, and functional analyses of Penicillium expansum
RT   provide new insights into secondary metabolism and pathogenicity.";
RL   Mol. Plant Microbe Interact. 28:232-248(2015).
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; EC=1.1.1.37;
CC         Evidence={ECO:0000256|ARBA:ARBA00000774};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC       {ECO:0000256|ARBA:ARBA00008824}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGO63668.1}.
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DR   EMBL; JQGA01001628; KGO63668.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A2K9V2; -.
DR   STRING; 40296.A0A0A2K9V2; -.
DR   HOGENOM; CLU_047181_1_0_1; -.
DR   OMA; VECAFVQ; -.
DR   OrthoDB; 5059897at2759; -.
DR   PhylomeDB; A0A0A2K9V2; -.
DR   Proteomes; UP000030104; Unassembled WGS sequence.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
DR   CDD; cd01337; MDH_glyoxysomal_mitochondrial; 1.
DR   Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 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; IPR010097; Malate_DH_type1.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR01772; MDH_euk_gproteo; 1.
DR   PANTHER; PTHR11540; MALATE AND LACTATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11540:SF16; MALATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|PIRSR:PIRSR000102-3};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU003369};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030104};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT   DOMAIN          3..146
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          148..323
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        179
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         8..14
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         34
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         82
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         95
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         118..120
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         230
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
SQ   SEQUENCE   330 AA;  34167 MW;  68F2C03E9919B65A CRC64;
     MVKAVVLGAA GGIGQPLSLL LKASPLVDDL ALYDVVNTPG VAADLSHISS VAKITGYLPK
     DDGLKLALTG ADVVVIPAGI PRKPGMTRDD LFKVNAGIVK GLVESIAEFA PKAFILVISN
     PVNSTVPIAA EVLKAAGVFD PKRLFGVTTL DVVRAETFTQ EFSGVKNAAD ATVPVIGGHS
     GETIVPLFSK VSPNFQIPAD RYDALVNRVQ FGGDEVVKAK DGAGSATLSM AFAGFRFAEA
     VLKASKGEKG IVEPTFVYLP GVAGGDEIAK ATGLDFFSTP VELGPNGAEK AINILDGVTE
     QEKKLLEACI KGLQGNIEKG VEFAKNSAPK
//
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