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Database: UniProt/TrEMBL
Entry: A0A172T7E1_9DEIO
LinkDB: A0A172T7E1_9DEIO
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ID   A0A172T7E1_9DEIO        Unreviewed;       330 AA.
AC   A0A172T7E1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-SEP-2017, entry version 10.
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   ORFNames=SU48_02680 {ECO:0000313|EMBL:ANE42846.1};
OS   Deinococcus puniceus.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales;
OC   Deinococcaceae; Deinococcus.
OX   NCBI_TaxID=1182568 {ECO:0000313|EMBL:ANE42846.1, ECO:0000313|Proteomes:UP000077363};
RN   [1] {ECO:0000313|EMBL:ANE42846.1, ECO:0000313|Proteomes:UP000077363}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY1 {ECO:0000313|EMBL:ANE42846.1,
RC   ECO:0000313|Proteomes:UP000077363};
RA   Kim M.K., Srinivasan S., Lee J.-J.;
RT   "Deinococcus puniceus/DY1/ whole genome sequencing.";
RL   Submitted (JAN-2015) 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; CP011387; ANE42846.1; -; Genomic_DNA.
DR   RefSeq; WP_064013901.1; NZ_CP011387.1.
DR   EnsemblBacteria; ANE42846; ANE42846; SU48_02680.
DR   KEGG; dpu:SU48_02680; -.
DR   PATRIC; fig|1182568.3.peg.561; -.
DR   KO; K00024; -.
DR   Proteomes; UP000077363; 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; 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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000077363};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01517};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU003369, ECO:0000313|EMBL:ANE42846.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077363};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   DOMAIN        7    147       Ldh_1_N. {ECO:0000259|Pfam:PF00056}.
FT   DOMAIN      159    323       Ldh_1_C. {ECO:0000259|Pfam:PF02866}.
FT   NP_BIND      13     19       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   NP_BIND     131    133       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   ACT_SITE    189    189       Proton acceptor. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517, ECO:0000256|PIRSR:PIRSR000102-
FT                                1}.
FT   BINDING      94     94       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
FT   BINDING     100    100       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
FT   BINDING     107    107       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   BINDING     114    114       NAD. {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   BINDING     133    133       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
FT   BINDING     164    164       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517}.
SQ   SEQUENCE   330 AA;  35119 MW;  F6BFBEAF7323370D CRC64;
     MTTKPPVRVA VTGAAGQIGY SLLFRIASGD MLGKDQPVIL HLLEITPALK ALNGVVMELR
     DCAFPLLADI VTSDDPMVAF KDIDYALLVG AMPRKAGMER GDLLSANGGI FKPQGEALNA
     VASRNVKVLV VGNPANTNAL IAQQNAPDLN PGQFTAMVRL DHNRAISQLA EQTGKPVSSI
     QNLTIWGNHS STQYPDLSAA TVDGQPALDL VERDWYENSY ISTVAKRGAA IIEARGLSSA
     ASAASAAIDH MRDWALGTPE GQWVSMGIPS DGSYGVPAGL IYGFPVTCKN GQYEIVQGLE
     VSDFSRGKMD ATAQELTEER DEVRKLGLVK
//
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