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Database: UniProt/TrEMBL
Entry: F0RNN9_DEIPM
LinkDB: F0RNN9_DEIPM
Original site: F0RNN9_DEIPM 
ID   F0RNN9_DEIPM            Unreviewed;       328 AA.
AC   F0RNN9;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   25-OCT-2017, entry version 52.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|SAAS:SAAS00369716};
DE            EC=1.1.1.37 {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|SAAS:SAAS00369716};
GN   Name=mdh {ECO:0000256|HAMAP-Rule:MF_01517};
GN   OrderedLocusNames=Deipr_0097 {ECO:0000313|EMBL:ADY25272.1};
OS   Deinococcus proteolyticus (strain ATCC 35074 / DSM 20540 / JCM 6276 /
OS   NBRC 101906 / NCIMB 13154 / VKM Ac-1939 / CCM 2703 / MRP).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales;
OC   Deinococcaceae; Deinococcus.
OX   NCBI_TaxID=693977 {ECO:0000313|EMBL:ADY25272.1, ECO:0000313|Proteomes:UP000007718};
RN   [1] {ECO:0000313|Proteomes:UP000007718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35074 / DSM 20540 / JCM 6276 / NBRC 101906 / NCIMB 13154 /
RC   VKM Ac-1939 / CCM 2703 / MRP {ECO:0000313|Proteomes:UP000007718};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Ovchinnikova G.,
RA   Zeytun A., Detter J.C., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R., Steenblock K.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete sequence of chromosome of Deinococcus proteolyticus DSM
RT   20540.";
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to
CC       oxaloacetate. {ECO:0000256|HAMAP-Rule:MF_01517,
CC       ECO:0000256|SAAS:SAAS00755561}.
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH.
CC       {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|SAAS:SAAS00369698}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000256|HAMAP-Rule:MF_01517}.
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DR   EMBL; CP002536; ADY25272.1; -; Genomic_DNA.
DR   RefSeq; WP_013613881.1; NC_015161.1.
DR   STRING; 693977.Deipr_0097; -.
DR   PRIDE; F0RNN9; -.
DR   EnsemblBacteria; ADY25272; ADY25272; Deipr_0097.
DR   KEGG; dpt:Deipr_0097; -.
DR   eggNOG; ENOG4105D9Z; Bacteria.
DR   eggNOG; COG0039; LUCA.
DR   KO; K00024; -.
DR   OMA; RPRTKGM; -.
DR   OrthoDB; POG091H03R4; -.
DR   Proteomes; UP000007718; 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:0006108; P:malate metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
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; IPR036291; NAD(P)-bd_dom_sf.
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; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   TIGRFAMs; TIGR01759; MalateDH-SF1; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000007718};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01517};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU003369, ECO:0000313|EMBL:ADY25272.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007718};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   DOMAIN        5    150       Ldh_1_N. {ECO:0000259|Pfam:PF00056}.
FT   DOMAIN      157    321       Ldh_1_C. {ECO:0000259|Pfam:PF02866}.
FT   NP_BIND      11     17       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   NP_BIND     129    131       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   ACT_SITE    187    187       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517, ECO:0000256|PIRSR:PIRSR000102-
FT                                1}.
FT   BINDING      92     92       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
FT   BINDING      98     98       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
FT   BINDING     105    105       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   BINDING     112    112       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   BINDING     131    131       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
FT   BINDING     162    162       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
SQ   SEQUENCE   328 AA;  35238 MW;  7AC866895BCA1406 CRC64;
     MKEPVRVAVT GAAGQIGYSL LFRIAAGDML GKDQPVILQL LEITPALKAL EGVVMELRDG
     AFPLLADVIT SDDPEVAFKD ADYALLVGAM PRKQGMERGD LLSANGGIFK PQGEALNKVA
     SRNVKVLVVG NPANTNALIA QQNAPDLDPR CFTAMVRLDH NRAISQLAEK TGKPVTDIKN
     VTIWGNHSST QYPDLSQTTV GGEKALDLVD QNWYESEYIP TVAKRGAAII EARGLSSAAS
     AASAAIDHMR DWALGTKEGE WVSMGIPSDG SYGIPEGLIY GFPVTVKDGK YEIVQGLEVS
     DFSRGKMDAT AKELEEERDE VRKLGLVK
//
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