(data stored in ACNUC7421 zone)

SWISSPROT: MDH_RHOPS

ID   MDH_RHOPS               Reviewed;         322 AA.
AC   Q13DR6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 84.
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=RPD_0535;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to
CC       oxaloacetate. {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;
CC         EC=1.1.1.37; 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}.
DR   EMBL; CP000283; ABE37773.1; -; Genomic_DNA.
DR   RefSeq; WP_011500960.1; NC_007958.1.
DR   SMR; Q13DR6; -.
DR   STRING; 316057.RPD_0535; -.
DR   EnsemblBacteria; ABE37773; ABE37773; RPD_0535.
DR   KEGG; rpd:RPD_0535; -.
DR   eggNOG; ENOG4105C80; Bacteria.
DR   eggNOG; COG0039; LUCA.
DR   HOGENOM; HOG000213794; -.
DR   KO; K00024; -.
DR   OMA; MDLMQTA; -.
DR   OrthoDB; 870724at2; -.
DR   BioCyc; RPAL316057:RPD_RS02740-MONOMER; -.
DR   Proteomes; UP000001818; Chromosome.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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   3: Inferred from homology;
DR   PRODOM; Q13DR6.
DR   SWISS-2DPAGE; Q13DR6.
KW   Complete proteome; NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT   CHAIN         1    322       Malate dehydrogenase.
FT                                /FTId=PRO_1000026485.
FT   NP_BIND      10     15       NAD. {ECO:0000255|HAMAP-Rule:MF_00487}.
FT   NP_BIND     119    121       NAD. {ECO:0000255|HAMAP-Rule:MF_00487}.
FT   ACT_SITE    176    176       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00487}.
FT   BINDING      34     34       NAD. {ECO:0000255|HAMAP-Rule:MF_00487}.
FT   BINDING      83     83       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00487}.
FT   BINDING      89     89       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00487}.
FT   BINDING      96     96       NAD. {ECO:0000255|HAMAP-Rule:MF_00487}.
FT   BINDING     121    121       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00487}.
FT   BINDING     152    152       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00487}.
SQ   SEQUENCE   322 AA;  33941 MW;  54488F77251A0A17 CRC64;
     MARDKIALIG SGQIGGTLAH MIGLKELGDV VLFDIAEGVP QGKALDIAES SPVDGFDAKF
     TGANSYEAIE GASVVIVTAG VPRKPGMSRD DLLSINLKVM EQVGAGIKKY APDAFVICIT
     NPLDAMVWAL QKASGMPAKK VVGMAGVLDS ARFRYFLADE FNVSVEDVTA FVLGGHGDTM
     VPLVKYSTVA GIPLPDLVKI GWTSQARLDE IVDRTRNGGA EIVNLLKTGS AFYAPAASAV
     AMAESYLRDK KRVLPVAAYL NGEYGIKDTY VGVPVVIGAK GVERIVEIEL AGKDREAFDK
     SVGAVQGLID ACKKIAPDLL GR
//

If you have problems or comments...

PBIL Back to PBIL home page