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Database: UniProt
Entry: W7J7J9_9PSEU
LinkDB: W7J7J9_9PSEU
Original site: W7J7J9_9PSEU 
ID   W7J7J9_9PSEU            Unreviewed;       327 AA.
AC   W7J7J9; A0A8E3BHN3;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|ARBA:ARBA00020382, ECO:0000256|HAMAP-Rule:MF_01517};
DE            EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995, ECO:0000256|HAMAP-Rule:MF_01517};
GN   Name=mdh {ECO:0000256|HAMAP-Rule:MF_01517};
GN   ORFNames=DFQ13_103399 {ECO:0000313|EMBL:PWW64425.1}, UO65_2670
GN   {ECO:0000313|EMBL:EWC62034.1};
OS   Actinokineospora spheciospongiae.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Actinokineospora.
OX   NCBI_TaxID=909613 {ECO:0000313|EMBL:EWC62034.1, ECO:0000313|Proteomes:UP000019277};
RN   [1] {ECO:0000313|EMBL:EWC62034.1, ECO:0000313|Proteomes:UP000019277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EG49 {ECO:0000313|EMBL:EWC62034.1,
RC   ECO:0000313|Proteomes:UP000019277};
RX   PubMed=24604655;
RA   Harjes J., Ryu T., Abdelmohsen U.R., Moitinho-Silva L., Horn H., Ravasi T.,
RA   Hentschel U.;
RT   "Draft Genome Sequence of the Antitrypanosomally Active Sponge-Associated
RT   Bacterium Actinokineospora sp. Strain EG49.";
RL   Genome Announc. 2:e00160-14(2014).
RN   [2] {ECO:0000313|EMBL:PWW64425.1, ECO:0000313|Proteomes:UP000247287}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 8578 {ECO:0000313|EMBL:PWW64425.1,
RC   ECO:0000313|Proteomes:UP000247287};
RA   Whitman W.;
RT   "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT   soil and plant-associated and newly described type strains.";
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC       {ECO:0000256|HAMAP-Rule:MF_01517}.
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|HAMAP-Rule:MF_01517,
CC         ECO:0000256|RuleBase:RU000422};
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000256|ARBA:ARBA00009613, ECO:0000256|HAMAP-Rule:MF_01517}.
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:EWC62034.1}.
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DR   EMBL; AYXG01000092; EWC62034.1; -; Genomic_DNA.
DR   EMBL; QHCP01000003; PWW64425.1; -; Genomic_DNA.
DR   RefSeq; WP_035282188.1; NZ_QHCP01000003.1.
DR   AlphaFoldDB; W7J7J9; -.
DR   STRING; 909613.UO65_2670; -.
DR   PATRIC; fig|909613.9.peg.2670; -.
DR   eggNOG; COG0039; Bacteria.
DR   OrthoDB; 9802969at2; -.
DR   Proteomes; UP000019277; Unassembled WGS sequence.
DR   Proteomes; UP000247287; Unassembled WGS sequence.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   CDD; cd01338; MDH_choloroplast_like; 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   HAMAP; MF_01517; Malate_dehydrog_2; 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; IPR010945; Malate_DH_type2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR01759; MalateDH-SF1; 1.
DR   PANTHER; PTHR23382; MALATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR23382:SF0; MALATE DEHYDROGENASE 2, MITOCHONDRIAL-RELATED; 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.
DR   PROSITE; PS00068; MDH; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|PIRSR:PIRSR000102-3};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU003369};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019277};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU000422}.
FT   DOMAIN          5..144
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          155..320
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        186
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT                   ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         10..16
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT                   ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         104
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT                   ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         111
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01517"
FT   BINDING         128..130
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT                   ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         130
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
SQ   SEQUENCE   327 AA;  33955 MW;  F328F40AE0B22637 CRC64;
     MAPVNVTVTG AAGQIGYALL FRIASGALLG PDTKVNLRLL EIPAAVKAAE GTAMELDDCA
     FPLLAGIEVT DDAKKAFDGA NVALLVGARP RTKGMERGDL LEANGGIFKP QGEAINAGAA
     SDIKVLVVGN PANTNALIAQ QHAPDVPAGR FTAMTRLDHN RALSQLATKL GVTVEDIKKL
     TIWGNHSATQ YPDVFHAEVN GKNAAELVND EAWLADSFIP TVAKRGAAII EARGASSAAS
     AANAAIDHVH DWVLGTPAGD WTSMAIPSDG SYGVPEGIIS SFPVTCADGE YSIVQGLEVN
     EFSRARIDAS VAELVEERDA VKGLGLI
//
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