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Database: UniProt
Entry: E1RJ09_METP4
LinkDB: E1RJ09_METP4
Original site: E1RJ09_METP4 
ID   E1RJ09_METP4            Unreviewed;       288 AA.
AC   E1RJ09;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 63.
DE   RecName: Full=malate dehydrogenase {ECO:0000256|ARBA:ARBA00012995};
DE            EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995};
GN   OrderedLocusNames=Mpet_1928 {ECO:0000313|EMBL:ADN36679.1};
OS   Methanolacinia petrolearia (strain DSM 11571 / OCM 486 / SEBR 4847)
OS   (Methanoplanus petrolearius).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanomicrobiaceae; Methanolacinia.
OX   NCBI_TaxID=679926 {ECO:0000313|EMBL:ADN36679.1, ECO:0000313|Proteomes:UP000006565};
RN   [1] {ECO:0000313|EMBL:ADN36679.1, ECO:0000313|Proteomes:UP000006565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11571 / OCM 486 / SEBR 4847
RC   {ECO:0000313|Proteomes:UP000006565};
RX   PubMed=21304750;
RA   Brambilla E., Djao O.D., Daligault H., Lapidus A., Lucas S., Hammon N.,
RA   Nolan M., Tice H., Cheng J.F., Han C., Tapia R., Goodwin L., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M.,
RA   Spring S., Sikorski J., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Methanoplanus petrolearius type strain (SEBR
RT   4847).";
RL   Stand. Genomic Sci. 3:203-211(2010).
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|ARBA:ARBA00000774};
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily.
CC       {ECO:0000256|ARBA:ARBA00008104, ECO:0000256|RuleBase:RU003369}.
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DR   EMBL; CP002117; ADN36679.1; -; Genomic_DNA.
DR   RefSeq; WP_013329856.1; NC_014507.1.
DR   AlphaFoldDB; E1RJ09; -.
DR   STRING; 679926.Mpet_1928; -.
DR   GeneID; 9744405; -.
DR   KEGG; mpi:Mpet_1928; -.
DR   eggNOG; arCOG00246; Archaea.
DR   HOGENOM; CLU_045401_1_2_2; -.
DR   OMA; CYIIVLT; -.
DR   OrthoDB; 2596at2157; -.
DR   Proteomes; UP000006565; Chromosome.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
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; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1.
DR   PANTHER; PTHR43128:SF16; L-LACTATE DEHYDROGENASE; 1.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   PRINTS; PR00086; LLDHDRGNASE.
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|ARBA:ARBA00023027, ECO:0000256|PIRSR:PIRSR000102-3};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003369};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006565}.
FT   DOMAIN          5..135
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          139..283
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        166
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         8..13
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         33
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         76
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         90
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         111..113
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         144
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
SQ   SEQUENCE   288 AA;  31150 MW;  D11F51F2380BAA97 CRC64;
     MTVLSILGAG KIGGEVAFLS AATGIAGEIN LFDINKPLLE AQKLDLLHTG LDITIDTDPE
     NIRNSDIILF AAGMARNPQI KTRADLLDVN IRVASECMKC ISGFDGVFIT VTNPMDALNY
     YLCTKGGIER EKCIGFGGQL DTARLHLFLK EKGIAPDNTA QALGEHGEFQ VPIFSGLEDE
     VPTDLREEIL IKMRGASMPV IKGKGGTVFG PAQNIVDLIR IISQDLRETV PCSCALDGEY
     GISSCSIGVP AVIGREGILR IEETNLDEWE TNKMKEAAEH LKTLCGRF
//
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