ID MDH_ACICJ Reviewed; 327 AA.
AC A5G320;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 01-MAY-2013, entry version 46.
DE RecName: Full=Malate dehydrogenase;
DE EC=1.1.1.37;
GN Name=mdh; OrderedLocusNames=Acry_3063;
OS Acidiphilium cryptum (strain JF-5).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidiphilium.
OX NCBI_TaxID=349163;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JF-5;
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., Sims D., Brettin T., Bruce D., Han C., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Magnuson T.,
RA Richardson P.;
RT "Complete sequence of chromosome of Acidiphilium cryptum JF-5.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to
CC oxaloacetate (By similarity).
CC -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
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DR EMBL; CP000697; ABQ32252.1; -; Genomic_DNA.
DR RefSeq; YP_001236171.1; NC_009484.1.
DR ProteinModelPortal; A5G320; -.
DR SMR; A5G320; 3-325.
DR STRING; 349163.Acry_3063; -.
DR EnsemblBacteria; ABQ32252; ABQ32252; Acry_3063.
DR GeneID; 5161153; -.
DR KEGG; acr:Acry_3063; -.
DR PATRIC; 20651264; VBIAciCry6074_3587.
DR eggNOG; COG0039; -.
DR HOGENOM; HOG000220953; -.
DR KO; K00024; -.
DR OMA; NCLIASK; -.
DR ProtClustDB; PRK05442; -.
DR BioCyc; ACRY349163:GHET-3117-MONOMER; -.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:HAMAP.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0044262; P:cellular carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:HAMAP.
DR Gene3D; 3.40.50.720; -; 1.
DR Gene3D; 3.90.110.10; -; 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; IPR016040; NAD(P)-bd_dom.
DR PANTHER; PTHR23382; PTHR23382; 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; Lactate_DH/Glyco_hydro_4_C; 1.
DR TIGRFAMs; TIGR01759; MalateDH-SF1; 1.
DR PROSITE; PS00068; MDH; FALSE_NEG.
PE 3: Inferred from homology;
KW Complete proteome; NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT CHAIN 1 327 Malate dehydrogenase.
FT /FTId=PRO_1000068598.
FT NP_BIND 12 18 NAD (By similarity).
FT NP_BIND 130 132 NAD (By similarity).
FT ACT_SITE 188 188 Proton acceptor (By similarity).
FT BINDING 93 93 Substrate (By similarity).
FT BINDING 99 99 Substrate (By similarity).
FT BINDING 106 106 NAD (By similarity).
FT BINDING 113 113 NAD (By similarity).
FT BINDING 132 132 Substrate (By similarity).
FT BINDING 163 163 Substrate (By similarity).
SQ SEQUENCE 327 AA; 34474 MW; F60BC6BF6DD37EFB CRC64;
MAKSPVRIAV TGAAGQIAYA LVFRIASGAL LGPDQPVILH LLDLPQMQGA LGGVMMELED
CAFPLLAGMV ATDDPKVAFK DIDIGFLVGA RPRGKGMERK DLLGANAEIF TVQGRALNEV
AKRSARVLVV GNPANTNAYI AMKSAPDLSP DCFSAMIRLD HNRAASMLAA KAGVNVGDVG
KLIVWGNHSP TMYPDYRFAE AGGRKLAEAI NDEAWNRDVF IPTVGKRGAA VIEARGASSA
ASAANAAIDQ VRDWVVGSDG RWVSMAIPSD GSYGIPEGIM FGVPVTTQGG VVTRVPNLAI
DAFAQSRLDI TLNELKEERE AIAHLLA
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