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Database: UniProt
Entry: G4R6B6_PELHB
LinkDB: G4R6B6_PELHB
Original site: G4R6B6_PELHB 
ID   G4R6B6_PELHB            Unreviewed;       320 AA.
AC   G4R6B6;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 69.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00487};
DE            EC=1.1.1.37 {ECO:0000256|HAMAP-Rule:MF_00487};
GN   Name=mdh {ECO:0000256|HAMAP-Rule:MF_00487};
GN   OrderedLocusNames=KKY_3192 {ECO:0000313|EMBL:AEQ53181.1};
OS   Pelagibacterium halotolerans (strain DSM 22347 / JCM 15775 / CGMCC 1.7692 /
OS   B2).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Devosiaceae; Pelagibacterium.
OX   NCBI_TaxID=1082931 {ECO:0000313|EMBL:AEQ53181.1, ECO:0000313|Proteomes:UP000008850};
RN   [1] {ECO:0000313|EMBL:AEQ53181.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=B2 {ECO:0000313|EMBL:AEQ53181.1};
RA   Huo Y.-Y., Cheng H., Wu M.;
RL   Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEQ53181.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B2 {ECO:0000313|EMBL:AEQ53181.1};
RX   PubMed=22156395; DOI=10.1128/JB.06343-11;
RA   Huo Y.Y., Cheng H., Han X.F., Jiang X.W., Sun C., Zhang X.Q., Zhu X.F.,
RA   Liu Y.F., Li P.F., Ni P.X., Wu M.;
RT   "Complete genome sequence of Pelagibacterium halotolerans B2T.";
RL   J. Bacteriol. 194:197-198(2012).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC       {ECO:0000256|ARBA:ARBA00003966, ECO:0000256|HAMAP-Rule:MF_00487}.
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|HAMAP-Rule:MF_00487};
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 3 family.
CC       {ECO:0000256|HAMAP-Rule:MF_00487}.
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DR   EMBL; CP003075; AEQ53181.1; -; Genomic_DNA.
DR   RefSeq; WP_014132327.1; NC_016078.1.
DR   AlphaFoldDB; G4R6B6; -.
DR   STRING; 1082931.KKY_3192; -.
DR   KEGG; phl:KKY_3192; -.
DR   PATRIC; fig|1082931.4.peg.3145; -.
DR   eggNOG; COG0039; Bacteria.
DR   HOGENOM; CLU_045401_2_1_5; -.
DR   OMA; MGWTSQA; -.
DR   Proteomes; UP000008850; Chromosome.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
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   HAMAP; MF_00487; Malate_dehydrog_3; 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   NCBIfam; TIGR01763; MalateDH_bact; 1.
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|HAMAP-Rule:MF_00487};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00487,
KW   ECO:0000256|RuleBase:RU003369};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008850};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP-
KW   Rule:MF_00487}.
FT   DOMAIN          5..143
FT                   /note="Lactate/malate dehydrogenase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00056"
FT   DOMAIN          148..304
FT                   /note="Lactate/malate dehydrogenase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02866"
FT   ACT_SITE        176
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT                   ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         10..15
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT                   ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         34
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT                   ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         89
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         96
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT                   ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         119..121
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT                   ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         121
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00487,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
SQ   SEQUENCE   320 AA;  33864 MW;  A009D29F96A4955A CRC64;
     MARKKIALIG AGQIGGTLAH LVALKELGDV MLFDIVDGVP QGKALDLAQS GPVEGYNSTL
     KGTSEYKDIE GADVVIVTAG VPRKPGMSRD DLLEINLKVM EQVGAGISKY APDAFVICIT
     NPLDAMVWAL QKFSGLPAEK VVGMAGVLDS ARFRHFIADE LNVSVQDVTA FVMGGHGDTM
     VPLARYSTVA GIPLPDMVKM GWMSKDKLDE IIQRTRDGGA EIVGLLKTGS AFYAPAASAV
     EMAECYLKDK KRILPCAAHL TGQFGLSDTY VGVPVVIGAG GVERIVEIEL NASEKKMFDA
     SVQSVDGLVE ACKKIAPKLA
//
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