MDH_HYDS0
ID MDH_HYDS0 Reviewed; 332 AA.
AC B4U831;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Malate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00487};
DE EC=1.1.1.37 {ECO:0000255|HAMAP-Rule:MF_00487};
GN Name=mdh {ECO:0000255|HAMAP-Rule:MF_00487};
GN OrderedLocusNames=HY04AAS1_0605;
OS Hydrogenobaculum sp. (strain Y04AAS1).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Hydrogenobaculum;
OC unclassified Hydrogenobaculum.
OX NCBI_TaxID=380749;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y04AAS1;
RX PubMed=19136599; DOI=10.1128/jb.01645-08;
RA Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT "Complete and draft genome sequences of six members of the Aquificales.";
RL J. Bacteriol. 191:1992-1993(2009).
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_00487};
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 3 family.
CC {ECO:0000255|HAMAP-Rule:MF_00487}.
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DR EMBL; CP001130; ACG57292.1; -; Genomic_DNA.
DR RefSeq; WP_012513648.1; NC_011126.1.
DR AlphaFoldDB; B4U831; -.
DR SMR; B4U831; -.
DR STRING; 380749.HY04AAS1_0605; -.
DR EnsemblBacteria; ACG57292; ACG57292; HY04AAS1_0605.
DR KEGG; hya:HY04AAS1_0605; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_045401_2_1_0; -.
DR OMA; ASCAEYI; -.
DR OrthoDB; 870724at2; -.
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.
PE 3: Inferred from homology;
KW NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT CHAIN 1..332
FT /note="Malate dehydrogenase"
FT /id="PRO_1000126137"
FT ACT_SITE 190
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 11..16
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 110
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 133..135
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 166
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
SQ SEQUENCE 332 AA; 35909 MW; 0C2FCF9618291C80 CRC64;
MGHKKTVSII GAGNVGEHIA SLLVLKGAVN IRLFDLPKKD GEKLYAHVKG KALDMLQMAC
ALGIDTDISG FVVDQNGNGY EALEGSDIVV ITAGFPRKPG MSRDDLLGIN ISIMNTISEQ
IKKYAKNSIV IVVTNPVDIM TYAVYKLLGC NRKRVIGMAG VLDSSRFRTF ISLELNVSPK
DVHAYVIGGH GDEMVPLAGV SNVGGIPIST LIDEKKIKEL VERTRFGGGE IVDYMGTSAY
HAPAASVVEM IESVALNAKR VLTCSVLLDE EASKYYEAEN LCVGVPVKLG ENGVEKIVKV
PMTDFERDLW MKSVASVKKN IAIADEFVSK YI
