ID MDH_SHEFN Reviewed; 311 AA.
AC Q07YA5;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 01-MAY-2013, entry version 47.
DE RecName: Full=Malate dehydrogenase;
DE EC=1.1.1.37;
GN Name=mdh; OrderedLocusNames=Sfri_3173;
OS Shewanella frigidimarina (strain NCIMB 400).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318167;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 400;
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., Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T.,
RA Nealson K.H., Newman D., Tiedje J.M., Zhou J., Romine M.F.,
RA Culley D.E., Serres M., Chertkov O., Brettin T., Bruce D., Han C.,
RA Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL Submitted (AUG-2006) 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 1 family.
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DR EMBL; CP000447; ABI73009.1; -; Genomic_DNA.
DR RefSeq; YP_751848.1; NC_008345.1.
DR ProteinModelPortal; Q07YA5; -.
DR SMR; Q07YA5; 1-310.
DR STRING; 318167.Sfri_3173; -.
DR PRIDE; Q07YA5; -.
DR EnsemblBacteria; ABI73009; ABI73009; Sfri_3173.
DR GeneID; 4280075; -.
DR KEGG; sfr:Sfri_3173; -.
DR PATRIC; 23500495; VBISheFri14343_3288.
DR eggNOG; COG0039; -.
DR HOGENOM; HOG000213792; -.
DR KO; K00024; -.
DR OMA; VEVKGFA; -.
DR ProtClustDB; PRK05086; -.
DR BioCyc; SFRI318167:GIXS-3287-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_01516; Malate_dehydrog_1; 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; IPR001252; Malate_DH_AS.
DR InterPro; IPR010097; Malate_DH_type1.
DR InterPro; IPR023958; Malate_DH_type1_bac.
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 SUPFAM; SSF56327; Lactate_DH/Glyco_hydro_4_C; 1.
DR TIGRFAMs; TIGR01772; MDH_euk_gproteo; 1.
DR PROSITE; PS00068; MDH; 1.
PE 3: Inferred from homology;
KW Complete proteome; NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT CHAIN 1 311 Malate dehydrogenase.
FT /FTId=PRO_0000294302.
FT NP_BIND 7 13 NAD (By similarity).
FT NP_BIND 117 119 NAD (By similarity).
FT ACT_SITE 177 177 Proton acceptor (By similarity).
FT BINDING 34 34 NAD (By similarity).
FT BINDING 81 81 Substrate (By similarity).
FT BINDING 87 87 Substrate (By similarity).
FT BINDING 94 94 NAD (By similarity).
FT BINDING 119 119 Substrate (By similarity).
FT BINDING 153 153 Substrate (By similarity).
FT BINDING 227 227 NAD (By similarity).
SQ SEQUENCE 311 AA; 32143 MW; E448B2067BCC2F02 CRC64;
MKVAVLGAAG GIGQALALLL KTQLPAGSKL SLYDIAPVTP GVAVDLSHIP TDVEVKGFAG
QDPTDALVGA DVVLMSAGVA RKPGMDRSDL FNINAGIVRN LMEKVAVTCP KALVGIITNP
VNTTVAIAAE VLKNAGVYDK NRLFGITTLD VIRSETFIAE LKGLNVADVK VNVIGGHSGV
TILPLLSQVE GVTFTDEEVA AMTTRIQNAG TEVVEAKAGG GSATLSMGQA ACRFGLSLVR
GLQGEANVVE CAYVDGGSEH ATFFAQPILL GKNGVEKVLP YGEISAFEAN ARDAMLDTLK
GDIKLGVEFV K
//
