ID C6D8B2_PAESJ Unreviewed; 313 AA.
AC C6D8B2;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 01-MAY-2013, entry version 31.
DE RecName: Full=Malate dehydrogenase;
DE EC=1.1.1.37;
DE Flags: Precursor;
GN Name=mdh; OrderedLocusNames=Pjdr2_4471;
OS Paenibacillus sp. (strain JDR-2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC Paenibacillus.
OX NCBI_TaxID=324057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JDR-2;
RX PubMed=22675593; DOI=10.4056/sigs.2374349;
RA Chow V., Nong G., St John F.J., Rice J.D., Dickstein E., Chertkov O.,
RA Bruce D., Detter C., Brettin T., Han J., Woyke T., Pitluck S.,
RA Nolan M., Pati A., Martin J., Copeland A., Land M.L., Goodwin L.,
RA Jones J.B., Ingram L.O., Shanmugam K.T., Preston J.F.;
RT "Complete genome sequence of Paenibacillus sp. strain JDR-2.";
RL Stand. Genomic Sci. 6:1-10(2012).
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to
CC oxaloacetate (By similarity).
CC -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 3 family.
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DR EMBL; CP001656; ACT03092.1; -; Genomic_DNA.
DR RefSeq; YP_003013178.1; NC_012914.1.
DR ProteinModelPortal; C6D8B2; -.
DR SMR; C6D8B2; 5-310.
DR STRING; 324057.Pjdr2_4471; -.
DR EnsemblBacteria; ACT03092; ACT03092; Pjdr2_4471.
DR GeneID; 8124407; -.
DR KEGG; pjd:Pjdr2_4471; -.
DR PATRIC; 22839501; VBIPaeSp118865_4457.
DR eggNOG; COG0039; -.
DR HOGENOM; HOG000213794; -.
DR KO; K00024; -.
DR OMA; DAMTYVM; -.
DR ProtClustDB; CLSK2551411; -.
DR BioCyc; PSP324057:GH5H-4570-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_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; IPR016040; NAD(P)-bd_dom.
DR PANTHER; PTHR11540; PTHR11540; 1.
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; SSF56327; Lactate_DH/Glyco_hydro_4_C; 1.
DR TIGRFAMs; TIGR01763; MalateDH_bact; 1.
PE 3: Inferred from homology;
KW Complete proteome; NAD; Oxidoreductase; Signal;
KW Tricarboxylic acid cycle.
FT SIGNAL 1 25 Potential.
FT CHAIN 26 313 Potential.
FT /FTId=PRO_5000485664.
FT NP_BIND 12 17 NAD (By similarity).
FT NP_BIND 123 125 NAD (By similarity).
FT ACT_SITE 180 180 Proton acceptor (By similarity).
FT BINDING 36 36 NAD (By similarity).
FT BINDING 87 87 Substrate (By similarity).
FT BINDING 93 93 Substrate (By similarity).
FT BINDING 100 100 NAD (By similarity).
FT BINDING 125 125 Substrate (By similarity).
FT BINDING 156 156 Substrate (By similarity).
SQ SEQUENCE 313 AA; 33285 MW; DF37716268958356 CRC64;
MAIKRRKITV VGAGFTGATT ALMAAQKELG DIVLVDIPQL ENPTKGKALD MLESTPVQGL
DANITGTSNY DETKDSDVVI ITAGIARKPG MSRDDLVNTN AGIVRSVCES VKATSPNAYV
IILSNPVDAM TYVAYQTLGF PKNRVIGQSG VLDTARYCTF IAQELNVSVE DVRGFVLGGH
GDDMVPLVRY SNVGGIPIEK LIPSDRIEAI VQRSRVGGGE IVNLLGNGSA YYAPAASLVQ
MTEAILKDKK RILPVIALLE GEYGYNNLFM GVPTIIGGDG IEKVIELELT SEEKAALDKS
AESVQNVIKV VTG
//
