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Database: UniProt
Entry: G7VGW9_9CREN
LinkDB: G7VGW9_9CREN
Original site: G7VGW9_9CREN 
ID   G7VGW9_9CREN            Unreviewed;       309 AA.
AC   G7VGW9;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|ARBA:ARBA00020382};
GN   ORFNames=P186_0500 {ECO:0000313|EMBL:AET31952.1};
OS   Pyrobaculum ferrireducens.
OC   Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=1104324 {ECO:0000313|EMBL:AET31952.1, ECO:0000313|Proteomes:UP000005867};
RN   [1] {ECO:0000313|EMBL:AET31952.1, ECO:0000313|Proteomes:UP000005867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1860 {ECO:0000313|EMBL:AET31952.1,
RC   ECO:0000313|Proteomes:UP000005867};
RX   PubMed=22247528; DOI=10.1128/JB.06465-11;
RA   Mardanov A.V., Gumerov V.M., Slobodkina G.B., Beletsky A.V.,
RA   Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.;
RT   "Complete genome sequence of strain 1860, a crenarchaeon of the genus
RT   pyrobaculum able to grow with various electron acceptors.";
RL   J. Bacteriol. 194:727-728(2012).
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily.
CC       {ECO:0000256|ARBA:ARBA00008104, ECO:0000256|RuleBase:RU003369}.
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DR   EMBL; CP003098; AET31952.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7VGW9; -.
DR   STRING; 1104324.P186_0500; -.
DR   KEGG; pyr:P186_0500; -.
DR   eggNOG; arCOG00246; Archaea.
DR   HOGENOM; CLU_045401_2_1_2; -.
DR   OrthoDB; 2596at2157; -.
DR   BioCyc; PSP1104324:GJSN-488-MONOMER; -.
DR   Proteomes; UP000005867; 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   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}.
FT   DOMAIN          2..140
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          145..298
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        173
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         6..11
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         31
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         80
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         86
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         93
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
SQ   SEQUENCE   309 AA;  33319 MW;  7F021CC313F1D563 CRC64;
     MITIIGSGRV GAAAAIIMGL MKIDTKILLI DIVKGLPQGE ALDMNHMSSI LGLDVEYVGS
     NEYRDMEGSD LVVVTAGLPR KPGMTREQLL EANAKIVAEI GREIRKYAPN SVVILTTNPL
     DAMTYVMWKA TGFPRERVIG FSGVLDAGRL AYYAAKKLGA SPASILPIVL GQHGESMFPV
     PSKSFLHGVP LSKLLTEEQL REVVEDTVKA GARITELRGF SSNWGPGAGL AIMAEAVKRD
     AKRSLIASVV LQGEYGVRDI PVEVPLILGR GGVVKILEVE LTEEEKQKFM QSVEAVRKLV
     ASIPPAYLQ
//
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