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Database: UniProt
Entry: A0A0Q7PUI9_9GAMM
LinkDB: A0A0Q7PUI9_9GAMM
Original site: A0A0Q7PUI9_9GAMM 
ID   A0A0Q7PUI9_9GAMM        Unreviewed;       328 AA.
AC   A0A0Q7PUI9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01517};
DE            EC=1.1.1.37 {ECO:0000256|HAMAP-Rule:MF_01517};
GN   Name=mdh {ECO:0000256|HAMAP-Rule:MF_01517};
GN   ORFNames=ASD14_15275 {ECO:0000313|EMBL:KQY49145.1};
OS   Lysobacter sp. Root494.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=1736549 {ECO:0000313|EMBL:KQY49145.1, ECO:0000313|Proteomes:UP000051738};
RN   [1] {ECO:0000313|EMBL:KQY49145.1, ECO:0000313|Proteomes:UP000051738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root494 {ECO:0000313|EMBL:KQY49145.1,
RC   ECO:0000313|Proteomes:UP000051738};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQY49145.1, ECO:0000313|Proteomes:UP000051738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root494 {ECO:0000313|EMBL:KQY49145.1,
RC   ECO:0000313|Proteomes:UP000051738};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC       {ECO:0000256|ARBA:ARBA00003966, ECO:0000256|HAMAP-Rule:MF_01517}.
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_01517};
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000256|ARBA:ARBA00009613, ECO:0000256|HAMAP-Rule:MF_01517}.
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:KQY49145.1}.
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DR   EMBL; LMFH01000010; KQY49145.1; -; Genomic_DNA.
DR   RefSeq; WP_056135936.1; NZ_LMFH01000010.1.
DR   AlphaFoldDB; A0A0Q7PUI9; -.
DR   STRING; 1736549.ASD14_15275; -.
DR   OrthoDB; 9802969at2; -.
DR   Proteomes; UP000051738; Unassembled WGS sequence.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   CDD; cd01338; MDH_choloroplast_like; 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_01517; Malate_dehydrog_2; 1.
DR   InterPro; IPR003652; Ataxin_AXH_dom.
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; IPR010945; Malate_DH_type2.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR01759; MalateDH-SF1; 1.
DR   PANTHER; PTHR23382; MALATE DEHYDROGENASE; 1.
DR   PANTHER; PTHR23382:SF0; MALATE DEHYDROGENASE 2, MITOCHONDRIAL-RELATED; 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.
DR   PROSITE; PS51148; AXH; 1.
PE   3: Inferred from homology;
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|PIRSR:PIRSR000102-3};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU003369};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051738};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   DOMAIN          269..328
FT                   /note="AXH"
FT                   /evidence="ECO:0000259|PROSITE:PS51148"
FT   ACT_SITE        189
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT                   ECO:0000256|PIRSR:PIRSR000102-1"
FT   BINDING         11..17
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT                   ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         107
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT                   ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         114
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01517"
FT   BINDING         131..133
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT                   ECO:0000256|PIRSR:PIRSR000102-3"
FT   BINDING         133
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
FT   BINDING         164
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT                   ECO:0000256|PIRSR:PIRSR000102-2"
SQ   SEQUENCE   328 AA;  35005 MW;  1DE40404C207AC3A CRC64;
     MKTPVRVAVT GAAGQIGYAL LFRIASGEML GKDQPVILQM LELPMEKAQA ALKGVMMELE
     DCAFPLLAGM VGTDDPKVAF KDADYALLVG AMPRGPGMER KDLLLKNAEI FTVQGKALNE
     VASRNVKVLV VGNPANTNAY IAMKSAPQLP AKNFTAMLRL DHNRALSQLA SKAGVAVKDI
     KNMVVWGNHS PTMYPDYRFA TVANGISLKD KINDADWNAN TFIPVVGKRG AAIIEARGLS
     SAASAANAAI DHMRDWALGT NGEWVTMGVP SDGSYGIPEG VMYGVPVTCA NGEYTRVEGL
     PVDDFSRAAM DKTLAELEEE RAGVAHLL
//
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