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Database: UniProt
Entry: A0A0Q0W1M6_9EURY
LinkDB: A0A0Q0W1M6_9EURY
Original site: A0A0Q0W1M6_9EURY 
ID   A0A0Q0W1M6_9EURY        Unreviewed;       323 AA.
AC   A0A0Q0W1M6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=malate dehydrogenase {ECO:0000256|ARBA:ARBA00012995};
DE            EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995};
GN   ORFNames=APR55_00885 {ECO:0000313|EMBL:KQC07479.1};
OS   Methanolinea sp. SDB.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanoregulaceae; Methanolinea.
OX   NCBI_TaxID=1735327 {ECO:0000313|EMBL:KQC07479.1, ECO:0000313|Proteomes:UP000050878};
RN   [1] {ECO:0000313|EMBL:KQC07479.1, ECO:0000313|Proteomes:UP000050878}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SDB {ECO:0000313|EMBL:KQC07479.1};
RA   Wawrik B., Marks C.R., Davidova I.A., Mcinerney M.J., Pruitt S., Duncan K.,
RA   Suflita J.M., Callaghan A.V.;
RT   "Metagenomic Analysis of a Methanogenic Paraffin-Utilizing Consortium.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KQC07479.1}.
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DR   EMBL; LKUF01000276; KQC07479.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q0W1M6; -.
DR   Proteomes; UP000050878; Unassembled WGS sequence.
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   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}.
FT   DOMAIN          3..145
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          148..308
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        178
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         85
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         98
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         121..123
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         123
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
SQ   SEQUENCE   323 AA;  34706 MW;  45012252B028831B CRC64;
     MAKVTIIGAT GQVGTYSAHT ISAIPHVSEI LLFGRTGREN LLAGITQDLV DSFAACGTGM
     ELGWTTDMED IAESDIVVLS AGIPRKPGQD RLDLAIANAR IVAELSRQIA EVSPSSMILV
     VTNPVDVMTS VALQYSGMDE QQVFGLGTHL DSMRLKSLIA SYFKVHVSEV HTRIIGEHGE
     SMVPLWSATT IGGIQISNLP AFSRIPIQDM VEMVRTGGEN IIRNRGATIF GPGEAIATLV
     RTILGNENRI LTVSAYVKSE VHDIGDVCIG VPARINRSGV FPVPIKIDPV EVKSFRESVE
     KIRSITGEVT SMLEKNGMPI GMQ
//
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