(data stored in ACNUC30630 zone)

SWISSPROT: MDH_RHOPT

ID   MDH_RHOPT               Reviewed;         322 AA.
AC   B3Q761;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   11-DEC-2019, entry version 69.
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}; OrderedLocusNames=Rpal_0187;
OS   Rhodopseudomonas palustris (strain TIE-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=395960;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TIE-1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Emerson D.,
RA   Newman D.K., Roden E., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris TIE-1.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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}.
DR   EMBL; CP001096; ACE98749.1; -; Genomic_DNA.
DR   RefSeq; WP_012493973.1; NC_011004.1.
DR   SMR; B3Q761; -.
DR   EnsemblBacteria; ACE98749; ACE98749; Rpal_0187.
DR   KEGG; rpt:Rpal_0187; -.
DR   HOGENOM; HOG000213794; -.
DR   KO; K00024; -.
DR   OMA; MDLMQTA; -.
DR   OrthoDB; 870724at2; -.
DR   BioCyc; RPAL395960:RPAL_RS00940-MONOMER; -.
DR   Proteomes; UP000001725; 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; B3Q761.
DR   SWISS-2DPAGE; B3Q761.
KW   NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT   CHAIN           1..322
FT                   /note="Malate dehydrogenase"
FT                   /id="PRO_1000126149"
FT   NP_BIND         10..15
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   NP_BIND         119..121
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   ACT_SITE        176
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         34
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         83
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         89
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         96
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         121
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         152
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
SQ   SEQUENCE   322 AA;  33968 MW;  1641556B89B2C330 CRC64;
     MARDKIALIG SGQIGGTLAH LVGLKELGDV VLFDIAEGVP QGKALDIAES SPVDGFDSKL
     TGANSYEAIE GARVVIVTAG VPRKPGMSRD DLLSINLKVM EQVGAGIKKY APDAFVICIT
     NPLDAMVWAL QKASGLPAKK VVGMAGVLDS ARFRYFLADE FNVSVEDVTA FVLGGHGDTM
     VPLVKYSTVA GIPLPDLVKM GWTSQARLDE IVDRTRNGGA EIVNLLKTGS AFYAPASSAI
     AMAESYLKDK KRVVPVAAHL NGEYGVKDMY VGVPVVIGDK GVERIVEIEL AGKDKEAFDK
     SVAAVQGLVE ACKKIAPDLL GR
//

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