GenomeNet

Database: UniProt/TrEMBL
Entry: D7BFP3_MEISD
LinkDB: D7BFP3_MEISD
Original site: D7BFP3_MEISD 
ID   D7BFP3_MEISD            Unreviewed;       329 AA.
AC   D7BFP3;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   22-NOV-2017, entry version 55.
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   OrderedLocusNames=Mesil_1713 {ECO:0000313|EMBL:ADH63596.1};
OS   Meiothermus silvanus (strain ATCC 700542 / DSM 9946 / VI-R2) (Thermus
OS   silvanus).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
OC   Meiothermus.
OX   NCBI_TaxID=526227 {ECO:0000313|EMBL:ADH63596.1, ECO:0000313|Proteomes:UP000001916};
RN   [1] {ECO:0000313|EMBL:ADH63596.1, ECO:0000313|Proteomes:UP000001916}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700542 / DSM 9946 / VI-R2
RC   {ECO:0000313|Proteomes:UP000001916};
RX   PubMed=21304690;
RA   Sikorski J., Tindall B.J., Lowry S., Lucas S., Nolan M., Copeland A.,
RA   Glavina Del Rio T., Tice H., Cheng J.F., Han C., Pitluck S.,
RA   Liolios K., Ivanova N., Mavromatis K., Mikhailova N., Pati A.,
RA   Goodwin L., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Rohde M., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Meiothermus silvanus type strain (VI-
RT   R2).";
RL   Stand. Genomic Sci. 3:37-46(2010).
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP002042; ADH63596.1; -; Genomic_DNA.
DR   RefSeq; WP_013158156.1; NC_014212.1.
DR   ProteinModelPortal; D7BFP3; -.
DR   STRING; 526227.Mesil_1713; -.
DR   EnsemblBacteria; ADH63596; ADH63596; Mesil_1713.
DR   KEGG; msv:Mesil_1713; -.
DR   eggNOG; ENOG4105D9Z; Bacteria.
DR   eggNOG; COG0039; LUCA.
DR   HOGENOM; HOG000220953; -.
DR   KO; K00024; -.
DR   OMA; RPRTKGM; -.
DR   OrthoDB; POG091H03R4; -.
DR   Proteomes; UP000001916; 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; IPR001252; Malate_DH_AS.
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.
DR   PROSITE; PS00068; MDH; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000001916};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|RuleBase:RU000422};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU003369, ECO:0000313|EMBL:ADH63596.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001916};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU000422}.
FT   DOMAIN        5    149       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, ECO:0000256|PIRSR:PIRSR000102-
FT                                2}.
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, ECO:0000256|PIRSR:PIRSR000102-
FT                                2}.
FT   BINDING     162    162       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517, ECO:0000256|PIRSR:PIRSR000102-
FT                                2}.
SQ   SEQUENCE   329 AA;  35156 MW;  6DCC0CAF50529242 CRC64;
     MKSPVRVAVT GAAGQIGYSL LFRIAAGEML GKDQPVILQL LEITPALKAL QGVVMELEDC
     AFPTLAGVVQ TDDPNIAFAD ADYALLVGAM PRKAGMERAD LLQANGAIFT AQGKALSENA
     KKSVKVLVVG NPANTNALIA YHNAPGLSPR QFHAMTRLDH NRAISQLAAR VKKPVTSIKK
     MTIWGNHSLT QYPDLFHCEV DGQNAYELVG DPEWYANTYI PTVAKRGAAI IEARGASSAA
     SAASAAIDHM RDWALGTPEG DWVSMAIPSD GSYGIPEGLV YSYPCVCKGG DFTIVQGLEI
     NDFSRQKMDA SAKELADERD AVKQLGLIK
//
DBGET integrated database retrieval system