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Database: UniProt/TrEMBL
Entry: K7R4L0_THEOS
LinkDB: K7R4L0_THEOS
Original site: K7R4L0_THEOS 
ID   K7R4L0_THEOS            Unreviewed;       327 AA.
AC   K7R4L0;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   05-JUL-2017, entry version 36.
DE   RecName: Full=Malate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|RuleBase:RU000422, ECO:0000256|SAAS:SAAS00369716};
DE            EC=1.1.1.37 {ECO:0000256|HAMAP-Rule:MF_01517, ECO:0000256|RuleBase:RU000422, ECO:0000256|SAAS:SAAS00369716};
GN   Name=mdh {ECO:0000256|HAMAP-Rule:MF_01517};
GN   ORFNames=Theos_0764 {ECO:0000313|EMBL:AFV75824.1};
OS   Thermus oshimai JL-2.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
OC   Thermus.
OX   NCBI_TaxID=751945 {ECO:0000313|EMBL:AFV75824.1, ECO:0000313|Proteomes:UP000000211};
RN   [1] {ECO:0000313|EMBL:AFV75824.1, ECO:0000313|Proteomes:UP000000211}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JL-2 {ECO:0000313|EMBL:AFV75824.1,
RC   ECO:0000313|Proteomes:UP000000211};
RX   PubMed=23405355; DOI=10.1128/genomeA.00106-12;
RA   Murugapiran S.K., Huntemann M., Wei C.L., Han J., Detter J.C.,
RA   Han C.S., Erkkila T.H., Teshima H., Chen A., Kyrpides N.,
RA   Mavrommatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Lam J.,
RA   McDonald A.I., Dodsworth J.A., Pati A., Goodwin L., Peters L.,
RA   Pitluck S., Woyke T., Hedlund B.P.;
RT   "Whole Genome Sequencing of Thermus oshimai JL-2 and Thermus
RT   thermophilus JL-18, Incomplete Denitrifiers from the United States
RT   Great Basin.";
RL   Genome Announc. 1:E00106-E00112(2013).
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:RU000422,
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; CP003249; AFV75824.1; -; Genomic_DNA.
DR   RefSeq; WP_016329017.1; NC_019386.1.
DR   EnsemblBacteria; AFV75824; AFV75824; Theos_0764.
DR   KEGG; tos:Theos_0764; -.
DR   PATRIC; fig|751945.3.peg.751; -.
DR   KO; K00024; -.
DR   OrthoDB; POG091H03R4; -.
DR   Proteomes; UP000000211; Chromosome.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-HAMAP.
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-HAMAP.
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:UP000000211};
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};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU000422}.
FT   DOMAIN        5    152       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   327 AA;  35572 MW;  FDA6D4B757156376 CRC64;
     MKAPVRVAVT GAAGQIGYSL LFRIAAGEML GKDQPIVLQL LEIPQAMKAL EGVIMELEDC
     AFPLLAGIEA SDDPKVAFRD ADYALLVGAA PRKAGMERRD LLEMNGRIFT EQGRALAEVA
     KREVKVLVVG NPANTNALIA YKNAEGLDPR NFTAMTRLDH NRAKAQLSKK TGVPVDRIRK
     LAVWGNHSST MFPDLFHAEV DGRPALELVD MEWYEKVFIP TVAQRGAAII QARGASSAAS
     AANAAIEHIR DWALGTPEGD FVSMAVPSRG EYGIPEDIVY SFPVTAKDGV YTVVEGLEIT
     PFARERMEIT ARELLDEMEQ VKALGLI
//
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