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Database: UniProt
Entry: T0J6K9_9SPHN
LinkDB: T0J6K9_9SPHN
Original site: T0J6K9_9SPHN 
ID   T0J6K9_9SPHN            Unreviewed;       321 AA.
AC   T0J6K9;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 48.
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   ORFNames=M529_09530 {ECO:0000313|EMBL:EQB32477.1};
OS   Sphingobium ummariense RL-3.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1346791 {ECO:0000313|EMBL:EQB32477.1, ECO:0000313|Proteomes:UP000015523};
RN   [1] {ECO:0000313|EMBL:EQB32477.1, ECO:0000313|Proteomes:UP000015523}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RL-3 {ECO:0000313|EMBL:EQB32477.1,
RC   ECO:0000313|Proteomes:UP000015523};
RX   PubMed=24233594;
RA   Kohli P., Dua A., Sangwan N., Oldach P., Khurana J.P., Lal R.;
RT   "Draft Genome Sequence of Sphingobium ummariense Strain RL-3, a
RT   Hexachlorocyclohexane-Degrading Bacterium.";
RL   Genome Announc. 1:e00956-13(2013).
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}.
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:EQB32477.1}.
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DR   EMBL; AUWY01000071; EQB32477.1; -; Genomic_DNA.
DR   RefSeq; WP_021317732.1; NZ_AUWY01000071.1.
DR   AlphaFoldDB; T0J6K9; -.
DR   STRING; 1346791.M529_09530; -.
DR   PATRIC; fig|1346791.3.peg.1829; -.
DR   eggNOG; COG0039; Bacteria.
DR   OrthoDB; 9802969at2; -.
DR   Proteomes; UP000015523; Unassembled WGS sequence.
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:UP000015523};
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..308
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   321 AA;  33611 MW;  70772C3F77AB3968 CRC64;
     MARKKIALIG AGNIGGTLAH LAALKGLGDI VLFDVVEGVP QGKALDLSQC GPVEGFDAKI
     TGSNDYADIA GADVIIVTAG VARKPGMSRD DLLGINLKVM KAVGEGIKAN APDAFVICIT
     NPLDAMVWAL REFSGLPHNK VVGMAGVLDS ARFSHFIAEE FDVSVKDVNT FVLGGHGDTM
     VPVVQYSTVS GIPVPDLIEQ GRSTKERIDA IVQRTRSGGG EIVGLLKTGS AYYAPATSGI
     AMAEAYLYDQ KRLLPCAAFV EGKYGLDEGL YVGVPVIIGK DGVEQIVEIK LDDEAKANLQ
     VSVDAVKELL VACKGIDESL A
//
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