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Database: UniProt/TrEMBL
Entry: B7A6J5_THEAQ
LinkDB: B7A6J5_THEAQ
Original site: B7A6J5_THEAQ 
ID   B7A6J5_THEAQ            Unreviewed;       327 AA.
AC   B7A6J5;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-SEP-2017, entry version 57.
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=TaqDRAFT_4444 {ECO:0000313|EMBL:EED10884.1};
OS   Thermus aquaticus Y51MC23.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
OC   Thermus.
OX   NCBI_TaxID=498848 {ECO:0000313|EMBL:EED10884.1, ECO:0000313|Proteomes:UP000005403};
RN   [1] {ECO:0000313|EMBL:EED10884.1, ECO:0000313|Proteomes:UP000005403}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y51MC23 {ECO:0000313|EMBL:EED10884.1,
RC   ECO:0000313|Proteomes:UP000005403};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L.,
RA   Hauser L., Saunders E., Tapia R., Green L., Rogers Y., Detter J.C.,
RA   Brettin T.S., Mead D.;
RT   "Sequencing of the draft genome and assembly of Thermus aquaticus
RT   Y51MC23.";
RL   Submitted (DEC-2008) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EED10884.1}.
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DR   EMBL; ABVK02000002; EED10884.1; -; Genomic_DNA.
DR   RefSeq; WP_003044995.1; NZ_CP010822.1.
DR   ProteinModelPortal; B7A6J5; -.
DR   STRING; 498848.TaqDRAFT_4444; -.
DR   EnsemblBacteria; EED10884; EED10884; TaqDRAFT_4444.
DR   KEGG; taq:TO73_1768; -.
DR   eggNOG; ENOG4105D9Z; Bacteria.
DR   eggNOG; COG0039; LUCA.
DR   KO; K00024; -.
DR   OrthoDB; POG091H03R4; -.
DR   Proteomes; UP000005403; Unassembled WGS sequence.
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:UP000005403};
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};
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;  35543 MW;  1FC0BD19AFCEDB57 CRC64;
     MKSPVRVAVT GAAGQIGYSL LFRIAAGEML GKDQPVILQL LEIPQAMRAL EGVVMELEDC
     AFPLLAGLEA SDDPKVAFKD ADYALLVGAA PRKAGMERRD LLELNGRIFT EQGRALAEVA
     KKDVKVLVVG NPANTNALIA YKNAPGLNPR NFTAMTRLDH NRAKAQLSKK TGVSVDRIRR
     ITVWGNHSST MFPDLFHAEV DGRPALELVD MEWYEEVFIP TVAQRGAAII QARGASSAAS
     AANAAIEHIR DWALGTPEGD FVSMAVPSQG EYGIPEEIVY SFPVTAKDGV YRIVEGLEIN
     EFARKRMEIT AQELLDEMAQ VKALGLI
//
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