ID   D2RHB2_ARCPA            Unreviewed;       294 AA.
AC   D2RHB2;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 72.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|ARBA:ARBA00020382};
DE            EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995};
GN   OrderedLocusNames=Arcpr_0622 {ECO:0000313|EMBL:ADB57687.1};
OS   Archaeoglobus profundus (strain DSM 5631 / JCM 9629 / NBRC 100127 / Av18).
OC   Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC   Archaeoglobus.
OX   NCBI_TaxID=572546 {ECO:0000313|EMBL:ADB57687.1, ECO:0000313|Proteomes:UP000001901};
RN   [1] {ECO:0000313|EMBL:ADB57687.1, ECO:0000313|Proteomes:UP000001901}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5631 / JCM 9629 / NBRC 100127 / Av18
RC   {ECO:0000313|Proteomes:UP000001901};
RX   PubMed=21304717;
RA   von Jan M., Lapidus A., Del Rio T.G., Copeland A., Tice H., Cheng J.F.,
RA   Lucas S., Chen F., Nolan M., Goodwin L., Han C., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Ovchinnikova G., Chertkov O., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Saunders E.,
RA   Brettin T., Detter J.C., Chain P., Eichinger K., Huber H., Spring S.,
RA   Rohde M., Goker M., Wirth R., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Archaeoglobus profundus type strain (AV18).";
RL   Stand. Genomic Sci. 2:327-346(2010).
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily.
CC       {ECO:0000256|ARBA:ARBA00008104, ECO:0000256|RuleBase:RU003369}.
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DR   EMBL; CP001857; ADB57687.1; -; Genomic_DNA.
DR   RefSeq; WP_012940023.1; NC_013741.1.
DR   AlphaFoldDB; D2RHB2; -.
DR   STRING; 572546.Arcpr_0622; -.
DR   PaxDb; 572546-Arcpr_0622; -.
DR   GeneID; 8739281; -.
DR   KEGG; apo:Arcpr_0622; -.
DR   eggNOG; arCOG00246; Archaea.
DR   HOGENOM; CLU_045401_2_1_2; -.
DR   OrthoDB; 2596at2157; -.
DR   Proteomes; UP000001901; Chromosome.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   CDD; cd01339; LDH-like_MDH; 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; IPR011275; Malate_DH_type3.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR43128; L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+)); 1.
DR   PANTHER; PTHR43128:SF34; 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|PIRSR:PIRSR000102-3};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003369};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001901}.
FT   DOMAIN          2..141
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          146..291
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        171
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         7..12
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         32
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         87
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         94
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         117..119
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         119
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         150
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
SQ   SEQUENCE   294 AA;  32228 MW;  37D8D9FFE8756B59 CRC64;
     MKLGFVGAGR IGSTTAFTCI QHLDLDEVVL VDIVEDLAVG EAMDLSHAIV GLDKYAKIVG
     GSDYSLLKGC DLIVVSAGLA RKPGMTRLDL AKKNAEIMRS VAKNIVKHAS DSKILVVTNP
     LDVMTYVMWK ETGKDRREVF GMGSLLDTVR LKERIIALGG KPRRIFMMGE HGDSMFCPKS
     LAEVEGEVDL DRAIEETRGV AMEVIKRKGA TFYAPAVCIY RMVKAVLEDT KEEIPTSVVL
     QGEYGISDVA LGVPAILGRD GVERIVEYDL TDEEKAMLMK SAEILKERLK ELGY
//