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Database: UniProt/TrEMBL
Entry: E0TBC2_PARBH
LinkDB: E0TBC2_PARBH
Original site: E0TBC2_PARBH 
ID   E0TBC2_PARBH            Unreviewed;       326 AA.
AC   E0TBC2;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   20-DEC-2017, entry version 54.
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   OrderedLocusNames=PB2503_01232 {ECO:0000313|EMBL:ADM08326.1};
OS   Parvularcula bermudensis (strain ATCC BAA-594 / HTCC2503 /
OS   KCTC 12087).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Parvularculales;
OC   Parvularculaceae; Parvularcula.
OX   NCBI_TaxID=314260 {ECO:0000313|EMBL:ADM08326.1, ECO:0000313|Proteomes:UP000001302};
RN   [1] {ECO:0000313|Proteomes:UP000001302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-594 / HTCC2503 / KCTC 12087
RC   {ECO:0000313|Proteomes:UP000001302};
RA   Kang D.-M., Oh H.-M., Cho J.-C.;
RT   "Genome sequence of Parvularcula bermudensis HTCC2503.";
RL   Submitted (AUG-2010) 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; CP002156; ADM08326.1; -; Genomic_DNA.
DR   RefSeq; WP_013299300.1; NC_014414.1.
DR   ProteinModelPortal; E0TBC2; -.
DR   STRING; 314260.PB2503_01232; -.
DR   EnsemblBacteria; ADM08326; ADM08326; PB2503_01232.
DR   KEGG; pbr:PB2503_01232; -.
DR   eggNOG; ENOG4105D9Z; Bacteria.
DR   eggNOG; COG0039; LUCA.
DR   HOGENOM; HOG000220953; -.
DR   KO; K00024; -.
DR   OMA; RPRTKGM; -.
DR   OrthoDB; POG091H03R4; -.
DR   Proteomes; UP000001302; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001302};
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:UP000001302};
KW   Tricarboxylic acid cycle {ECO:0000256|HAMAP-Rule:MF_01517}.
FT   DOMAIN        6    144       Ldh_1_N. {ECO:0000259|Pfam:PF00056}.
FT   DOMAIN      157    321       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   COILED      300    320       {ECO:0000256|SAM:Coils}.
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   326 AA;  34460 MW;  D077322E0527378A CRC64;
     MKSPVTVTVT GAAGQIGYAL LFRIASGDML GKDQPVILNL LEITPAMGAL EGVAMELNDC
     AFPLLQGLNP TDDAERAFDK CDYGLLVGAM PRKQGMERKD LLSANGGIFG PQGKALNKGA
     SRDVKVLVVG NPANTNALIA SANAPDLDPS CFNAMMRLDH NRAISQLAEK TGAATTDISG
     VTIWGNHSST QFPDLYHAKV GGAEALSKID EEWYKDDFIP TVQQRGAAII KARGASSAAS
     AASAAIDHMR NWALGTEGSE WVSMAVPADG SYGIEPGIMF GYPCTCANGK YEIVQGLDLN
     DFAKEKIAAT EAELREERAA VEHLLS
//
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