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Database: UniProt
Entry: Q07YA5
LinkDB: Q07YA5
Original site: Q07YA5 
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   29-OCT-2014, entry version 55.
DE   RecName: Full=Malate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01516};
DE            EC=1.1.1.37 {ECO:0000255|HAMAP-Rule:MF_01516};
GN   Name=mdh {ECO:0000255|HAMAP-Rule:MF_01516};
GN   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. {ECO:0000255|HAMAP-Rule:MF_01516}.
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH.
CC       {ECO:0000255|HAMAP-Rule:MF_01516}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01516}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01516}.
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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   OrthoDB; EOG6091FG; -.
DR   BioCyc; SFRI318167:GIXS-3287-MONOMER; -.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-HAMAP.
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:UniProtKB-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; SSF56327; 1.
DR   TIGRFAMs; TIGR01772; MDH_euk_gproteo; 1.
DR   PROSITE; PS00068; MDH; 1.
PE   3: Inferred from homology;
KW   Complete proteome; NAD; Oxidoreductase; Reference proteome;
KW   Tricarboxylic acid cycle.
FT   CHAIN         1    311       Malate dehydrogenase.
FT                                /FTId=PRO_0000294302.
FT   NP_BIND       7     13       NAD. {ECO:0000255|HAMAP-Rule:MF_01516}.
FT   NP_BIND     117    119       NAD. {ECO:0000255|HAMAP-Rule:MF_01516}.
FT   ACT_SITE    177    177       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01516}.
FT   BINDING      34     34       NAD. {ECO:0000255|HAMAP-Rule:MF_01516}.
FT   BINDING      81     81       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01516}.
FT   BINDING      87     87       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01516}.
FT   BINDING      94     94       NAD. {ECO:0000255|HAMAP-Rule:MF_01516}.
FT   BINDING     119    119       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01516}.
FT   BINDING     153    153       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01516}.
FT   BINDING     227    227       NAD. {ECO:0000255|HAMAP-Rule:MF_01516}.
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
//
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