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Database: UniProt/TrEMBL
Entry: H8GS29_DEIGI
LinkDB: H8GS29_DEIGI
Original site: H8GS29_DEIGI 
ID   H8GS29_DEIGI            Unreviewed;       330 AA.
AC   H8GS29;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   28-MAR-2018, entry version 43.
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   ECO:0000313|EMBL:AFD26420.1};
GN   OrderedLocusNames=DGo_CA2493 {ECO:0000313|EMBL:AFD26420.1};
OS   Deinococcus gobiensis (strain DSM 21396 / JCM 16679 / CGMCC 1.7299 /
OS   I-0).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales;
OC   Deinococcaceae; Deinococcus.
OX   NCBI_TaxID=745776 {ECO:0000313|EMBL:AFD26420.1, ECO:0000313|Proteomes:UP000007575};
RN   [1] {ECO:0000313|EMBL:AFD26420.1, ECO:0000313|Proteomes:UP000007575}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21396 / JCM 16679 / CGMCC 1.7299 / I-0
RC   {ECO:0000313|Proteomes:UP000007575};
RX   PubMed=22470573; DOI=10.1371/journal.pone.0034458;
RA   Yuan M., Chen M., Zhang W., Lu W., Wang J., Yang M., Zhao P., Tang R.,
RA   Li X., Hao Y., Zhou Z., Zhan Y., Yu H., Teng C., Yan Y., Ping S.,
RA   Wang Y., Lin M.;
RT   "Genome sequence and transcriptome analysis of the radioresistant
RT   bacterium Deinococcus gobiensis: insights into the extreme
RT   environmental adaptations.";
RL   PLoS ONE 7:E34458-E34458(2012).
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; CP002191; AFD26420.1; -; Genomic_DNA.
DR   RefSeq; WP_014685902.1; NC_017790.1.
DR   EnsemblBacteria; AFD26420; AFD26420; DGo_CA2493.
DR   KEGG; dgo:DGo_CA2493; -.
DR   PATRIC; fig|745776.4.peg.2559; -.
DR   KO; K00024; -.
DR   OMA; RPRTKGM; -.
DR   OrthoDB; POG091H03R4; -.
DR   Proteomes; UP000007575; 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; 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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000007575};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01517};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01517,
KW   ECO:0000256|RuleBase:RU003369};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007575};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   DOMAIN        7    148       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, ECO:0000256|PIRSR:PIRSR000102-
FT                                2}.
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, ECO:0000256|PIRSR:PIRSR000102-
FT                                2}.
FT   BINDING     164    164       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01517, ECO:0000256|PIRSR:PIRSR000102-
FT                                2}.
SQ   SEQUENCE   330 AA;  35252 MW;  6C740D97265272FC CRC64;
     MANKQPVRVA VTGAAGQIGY SLLFRIASGD MLGKDQPVIL QLLEITPALK ALGGVVMELR
     DCAFPLLADI VVSDDPMVAF KDADYALLVG AMPRKAGMER GDLLGANGGI FKPQGEALNA
     VASRDVKVLV VGNPANTNAL IAQQNAPDLD PKQFTAMVRL DHNRAVSQLA EKTGQPVSEI
     KNMTIWGNHS STQYPDLSQT TVGGQPALDL VERDWYEQTY IPTVAKRGAA IIEARGLSSA
     ASAASAAIDH MRDWALGTRE GEWVSMGIPS DGSYGIPEGL IYGFPVRTSG GKYEIVQGLD
     ISDFSRGKMD ATAQELSEER DEVRKLGLVK
//
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