ID E7RWD5_9BURK Unreviewed; 326 AA.
AC E7RWD5;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
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=HMPREF0551_0798 {ECO:0000313|EMBL:EFV95310.1};
OS Lautropia mirabilis ATCC 51599.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Lautropia.
OX NCBI_TaxID=887898 {ECO:0000313|EMBL:EFV95310.1, ECO:0000313|Proteomes:UP000011021};
RN [1] {ECO:0000313|EMBL:EFV95310.1, ECO:0000313|Proteomes:UP000011021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51599 {ECO:0000313|EMBL:EFV95310.1,
RC ECO:0000313|Proteomes:UP000011021};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (DEC-2010) 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:EFV95310.1}.
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DR EMBL; AEQP01000003; EFV95310.1; -; Genomic_DNA.
DR RefSeq; WP_005672960.1; NZ_GL636062.1.
DR AlphaFoldDB; E7RWD5; -.
DR STRING; 887898.HMPREF0551_0798; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_040727_2_0_4; -.
DR Proteomes; UP000011021; Unassembled WGS sequence.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule.
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; 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.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|PIRSR:PIRSR000102-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01517}; Reference proteome {ECO:0000313|Proteomes:UP000011021};
KW Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517}.
FT DOMAIN 6..152
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 157..321
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 187
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 BINDING 42
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 105
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 112
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517"
FT BINDING 129..131
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 131
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01517,
FT ECO:0000256|PIRSR:PIRSR000102-2"
SQ SEQUENCE 326 AA; 34947 MW; E2FFD8403DF90B9D CRC64;
MKAPKRVAVT GAAGQIAYSL LFRIANGDML GKDQPVILQL LDITPAMAAV KGVVMELEDC
AFPLLAGIVV TDDPNVAFKD ADYALLVGAR PRSKGMERKD LLEANGAIFT VQGKALNDHA
SRDVKVLVVG NPANTNAYIA MKSAPDLPAK NFTAMLRLDH NRALSQLAAK TGRTVDSIEK
LVVWGNHSPT MYPDIRFASS NGDAMPKLVN DEAWVKDTFI PTVGKRGAAI IEARGLSSAA
SAANAAIDHM RDWALGTNGK WVTMGVPSQG DYEIPEGVIY GMPVTCQNGD YTIVKGLDID
AFSRERMNAT LEELEGERNG VKHLLG
//
