MDH_FLAFR
ID MDH_FLAFR Reviewed; 311 AA.
AC Q25QU7;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=Malate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00487, ECO:0000303|PubMed:16306697};
DE EC=1.1.1.37 {ECO:0000255|HAMAP-Rule:MF_00487, ECO:0000269|PubMed:16306697};
GN Name=mdh {ECO:0000255|HAMAP-Rule:MF_00487, ECO:0000303|PubMed:16306697};
OS Flavobacterium frigidimaris.
OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=262320;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-17; 57-67 AND
RP 137-151, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=DSM 15937 / CIP 109029 / JCM 12218 / KUC-1;
RX PubMed=16306697; DOI=10.1271/bbb.69.2146;
RA Oikawa T., Yamamoto N., Shimoke K., Uesato S., Ikeuchi T., Fujioka T.;
RT "Purification, characterization, and overexpression of psychrophilic and
RT thermolabile malate dehydrogenase of a novel antarctic psychrotolerant,
RT Flavobacterium frigidimaris KUC-1.";
RL Biosci. Biotechnol. Biochem. 69:2146-2154(2005).
RN [2]
RP CRYSTALLIZATION, AND SUBUNIT.
RC STRAIN=DSM 15937 / CIP 109029 / JCM 12218 / KUC-1;
RX PubMed=18007057; DOI=10.1107/s1744309107051524;
RA Fujii T., Oikawa T., Muraoka I., Soda K., Hata Y.;
RT "Crystallization and preliminary X-ray diffraction studies of tetrameric
RT malate dehydrogenase from the novel Antarctic psychrophile Flavobacterium
RT frigidimaris KUC-1.";
RL Acta Crystallogr. F 63:983-986(2007).
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC Can use both NAD and NADP for malate oxidation, but NADPH cannot be
CC used for oxaloacetate reduction. {ECO:0000269|PubMed:16306697}.
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:0000255|HAMAP-Rule:MF_00487,
CC ECO:0000269|PubMed:16306697};
CC -!- ACTIVITY REGULATION: Strongly inhibited by iodoacetic acid and CuCl(2).
CC Completely inhibited by N-ethylmaleimide and HgCl(2).
CC {ECO:0000269|PubMed:16306697}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.740 mM for L-malate (at 40 degrees Celsius)
CC {ECO:0000269|PubMed:16306697};
CC KM=0.0382 mM for NAD(+) (at 40 degrees Celsius)
CC {ECO:0000269|PubMed:16306697};
CC Vmax=456 umol/min/mg enzyme (at 40 degrees Celsius)
CC {ECO:0000269|PubMed:16306697};
CC Note=kcat is 138 sec(-1). {ECO:0000269|PubMed:16306697};
CC pH dependence:
CC Optimum pH is 10.5 for malate oxidation and 8.0 for oxaloacetate
CC reduction. {ECO:0000269|PubMed:16306697};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:16306697};
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16306697,
CC ECO:0000269|PubMed:18007057}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 3 family.
CC {ECO:0000255|HAMAP-Rule:MF_00487, ECO:0000305}.
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DR EMBL; AB161423; BAE91927.2; -; Genomic_DNA.
DR AlphaFoldDB; Q25QU7; -.
DR SMR; Q25QU7; -.
DR STRING; 262320.SAMN05444481_103297; -.
DR BRENDA; 1.1.1.37; 8533.
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; -; 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 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; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
DR TIGRFAMs; TIGR01763; MalateDH_bact; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT CHAIN 1..311
FT /note="Malate dehydrogenase"
FT /id="PRO_0000436025"
FT ACT_SITE 175
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 7..12
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 32
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 82
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 95
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 118..120
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT CONFLICT 15
FT /note="C -> T (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 17
FT /note="D -> F (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="D -> N (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="M -> V (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 311 AA; 32610 MW; 7693C700FE143722 CRC64;
MKVTIVGAGN VGATCADVIS YRGIASEVVL LDIKEGFAEG KALDIMQCAT NTGFNTKVSG
VTNDYSKTAG SDVVVITSGI PRKPGMTREE LIGINAGIVK TVAENVLKHS PNTIIVVVSN
PMDTMTYLAL KATGVPKNRI IGMGGALDSS RFRTYLSLAL DKPANDISAM VIGGHGDTTM
IPLTRLASYN GIPVTEFLSE EVLQKVAADT MVGGATLTGL LGTSAWYAPG ASVAYLVDSI
LNDQKKMIAC SVFVEGEYGQ NDICIGVPCI IGKNGVEEIL DIKLNDQEKA LFAKSADAVR
GMNDALKSIL V
