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Database: UniProt/TrEMBL
Entry: D3PQL0_MEIRD
LinkDB: D3PQL0_MEIRD
Original site: D3PQL0_MEIRD 
ID   D3PQL0_MEIRD            Unreviewed;       329 AA.
AC   D3PQL0;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-SEP-2017, entry version 65.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|RuleBase:RU004066, ECO:0000256|SAAS:SAAS00369716};
DE            EC=1.1.1.37 {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|RuleBase:RU004066, ECO:0000256|SAAS:SAAS00369716};
GN   Name=mdh {ECO:0000256|HAMAP-Rule:MF_01517};
GN   ORFNames=K649_04530 {ECO:0000313|EMBL:AGK04208.1};
OS   Meiothermus ruber (strain ATCC 35948 / DSM 1279 / VKM B-1258 / 21)
OS   (Thermus ruber).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
OC   Meiothermus.
OX   NCBI_TaxID=504728 {ECO:0000313|EMBL:AGK04208.1, ECO:0000313|Proteomes:UP000013026};
RN   [1] {ECO:0000313|EMBL:AGK04208.1, ECO:0000313|Proteomes:UP000013026}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 1279 {ECO:0000313|EMBL:AGK04208.1,
RC   ECO:0000313|Proteomes:UP000013026};
RA   Chin J., Alexander D.H., Marks P., Korlach J., Clum A., Copeland A.;
RL   Submitted (APR-2013) 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|RuleBase:RU004066,
CC       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; CP005385; AGK04208.1; -; Genomic_DNA.
DR   RefSeq; WP_013013262.1; NC_021081.1.
DR   ProteinModelPortal; D3PQL0; -.
DR   STRING; 504728.Mrub_0978; -.
DR   EnsemblBacteria; AGK04208; AGK04208; K649_04530.
DR   KEGG; mrb:Mrub_0978; -.
DR   KEGG; mre:K649_04530; -.
DR   PATRIC; fig|504728.9.peg.936; -.
DR   eggNOG; ENOG4105D9Z; Bacteria.
DR   eggNOG; COG0039; LUCA.
DR   HOGENOM; HOG000220953; -.
DR   KO; K00024; -.
DR   OMA; RPRTKGM; -.
DR   Proteomes; UP000013026; 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   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; IPR001252; Malate_DH_AS.
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; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   TIGRFAMs; TIGR01759; MalateDH-SF1; 1.
DR   PROSITE; PS00068; MDH; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000013026};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|RuleBase:RU000422};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU004066, ECO:0000313|EMBL:AGK04208.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000013026};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU000422}.
FT   DOMAIN        5    150       Ldh_1_N. {ECO:0000259|Pfam:PF00056}.
FT   DOMAIN      156    323       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   329 AA;  35340 MW;  C57E56BF6A0CC7DB CRC64;
     MKPPVRVAVT GAAGQIGYSL LFRIAAGEML GKDQPVILQL LEITPALKAL GGVIMELEDC
     AFPTLAGIVA TDDPNIAFGD ADYALLVGAM PRKQGMERAD LLQANGAIFT AQGRALSENA
     RKHVKVLVVG NPANTNALIT YKNAPNLSPR QIHAMTRLDH NRAISQLAAR LKVPVSEIKK
     MTIWGNHSLT QYPDLFHCEV GGRNAYELVG DHDWYANTYI PKVAKRGAEI IEARGASSAA
     SAASAAIDHM RDWALGTPAG DWVSMAIPSD GSYGIPEGLV YSYPCVCKDG DFEIVQGLEI
     NEFSRSKMDA SAKELADERD AVLQLGLIK
//
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