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Database: UniProt
Entry: J4UZH2_9GAMM
LinkDB: J4UZH2_9GAMM
Original site: J4UZH2_9GAMM 
ID   J4UZH2_9GAMM            Unreviewed;       332 AA.
AC   J4UZH2;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|ARBA:ARBA00020382, ECO:0000256|RuleBase:RU000422};
DE            EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995, ECO:0000256|RuleBase:RU000422};
GN   ORFNames=NT01SARS_0264 {ECO:0000313|EMBL:EJP71787.1};
OS   SAR86 cluster bacterium SAR86A.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; SAR86 cluster.
OX   NCBI_TaxID=1123866 {ECO:0000313|EMBL:EJP71787.1, ECO:0000313|Proteomes:UP000010305};
RN   [1] {ECO:0000313|EMBL:EJP71787.1, ECO:0000313|Proteomes:UP000010305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22170421; DOI=10.1038/ismej.2011.189;
RA   Dupont C.L., Rusch D.B., Yooseph S., Lombardo M.J., Richter R.A., Valas R.,
RA   Novotny M., Yee-Greenbaum J., Selengut J.D., Haft D.H., Halpern A.L.,
RA   Lasken R.S., Nealson K., Friedman R., Venter J.C.;
RT   "Genomic insights to SAR86, an abundant and uncultivated marine bacterial
RT   lineage.";
RL   ISME J. 6:1186-1199(2012).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC       {ECO:0000256|ARBA:ARBA00003966}.
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|RuleBase:RU000422};
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000256|ARBA:ARBA00009613}.
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DR   EMBL; JH611156; EJP71787.1; -; Genomic_DNA.
DR   AlphaFoldDB; J4UZH2; -.
DR   STRING; 1123866.NT01SARS_0264; -.
DR   HOGENOM; CLU_040727_2_3_6; -.
DR   Proteomes; UP000010305; Unassembled WGS sequence.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
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; 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; 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|PIRSR:PIRSR000102-3, ECO:0000256|RuleBase:RU000422};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003369};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010305};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU000422}.
FT   DOMAIN          5..152
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          160..329
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        191
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         103
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         110
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         134..136
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         166
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
SQ   SEQUENCE   332 AA;  35995 MW;  A109AE7A889450A5 CRC64;
     MSKSIKVVVT GAAGQIAYSL IPRLVDGKTF GDKIVNLALV EIPQVVDKLE GLVMELEDSY
     FPNMGEVTYT DNFEEASKDA DWFLLVGSIP RGIVYNGKKI EERSDLLSIN GGIFVDQGIA
     IGRYGKKNAK ILVVGNPANT NAFIGKHAAN NDSQLWMAMT MLDANRAKSI LAKKTNNNVS
     DIKNMIIWGN HSPTMYPDSE NVQILGELGS SVINDINWVE SDFIPKVQQR GKAVIDARGA
     SSATSAAKAA IDTVIACENP TDPGDCFSAA IASDGSYDVP KGIICGYPLM TLEDGSIEIK
     RDISLSEFAK NKFQISIDEL LSEREAVKHL MQ
//
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