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Database: UniProt/SWISS-PROT
Entry: MDH_HALHL
LinkDB: MDH_HALHL
Original site: MDH_HALHL 
ID   MDH_HALHL               Reviewed;         326 AA.
AC   A1WV94;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   28-FEB-2018, entry version 70.
DE   RecName: Full=Malate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01517};
DE            EC=1.1.1.37 {ECO:0000255|HAMAP-Rule:MF_01517};
GN   Name=mdh {ECO:0000255|HAMAP-Rule:MF_01517};
GN   OrderedLocusNames=Hhal_0830;
OS   Halorhodospira halophila (strain DSM 244 / SL1) (Ectothiorhodospira
OS   halophila (strain DSM 244 / SL1)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Halorhodospira.
OX   NCBI_TaxID=349124;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 244 / SL1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Hoff W., Richardson P.;
RT   "Complete sequence of Halorhodospira halophila SL1.";
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to
CC       oxaloacetate. {ECO:0000255|HAMAP-Rule:MF_01517}.
CC   -!- CATALYTIC ACTIVITY: (S)-malate + NAD(+) = oxaloacetate + NADH.
CC       {ECO:0000255|HAMAP-Rule:MF_01517}.
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC       {ECO:0000255|HAMAP-Rule:MF_01517}.
DR   EMBL; CP000544; ABM61606.1; -; Genomic_DNA.
DR   RefSeq; WP_011813629.1; NC_008789.1.
DR   ProteinModelPortal; A1WV94; -.
DR   SMR; A1WV94; -.
DR   STRING; 349124.Hhal_0830; -.
DR   PRIDE; A1WV94; -.
DR   EnsemblBacteria; ABM61606; ABM61606; Hhal_0830.
DR   KEGG; hha:Hhal_0830; -.
DR   eggNOG; ENOG4105D9Z; Bacteria.
DR   eggNOG; COG0039; LUCA.
DR   HOGENOM; HOG000220953; -.
DR   KO; K00024; -.
DR   OMA; RPRTKGM; -.
DR   OrthoDB; POG091H03R4; -.
DR   Proteomes; UP000000647; Chromosome.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
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-KW.
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; IPR001252; Malate_DH_AS.
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.
DR   PROSITE; PS00068; MDH; 1.
PE   3: Inferred from homology;
KW   Complete proteome; NAD; Oxidoreductase; Reference proteome;
KW   Tricarboxylic acid cycle.
FT   CHAIN         1    326       Malate dehydrogenase.
FT                                /FTId=PRO_0000294387.
FT   NP_BIND      11     17       NAD. {ECO:0000255|HAMAP-Rule:MF_01517}.
FT   NP_BIND     129    131       NAD. {ECO:0000255|HAMAP-Rule:MF_01517}.
FT   ACT_SITE    187    187       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01517}.
FT   BINDING      92     92       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01517}.
FT   BINDING      98     98       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01517}.
FT   BINDING     105    105       NAD. {ECO:0000255|HAMAP-Rule:MF_01517}.
FT   BINDING     112    112       NAD. {ECO:0000255|HAMAP-Rule:MF_01517}.
FT   BINDING     131    131       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01517}.
FT   BINDING     162    162       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01517}.
SQ   SEQUENCE   326 AA;  34688 MW;  0C0E16BC467880D8 CRC64;
     MKAPVRVAVT GAAGQIGYSL LFRIAAGEML GKDQPVTLQL LEIPQAQEAL QGTVMELEDC
     AFPLVDGIIA TDSAEEAFRD ADYVLLVGAK PRGPGMERKD LLEANAAIFS AQGQALNAVA
     KRDVKVLAVG NPANTNALIT QRNAPDLDPR NFTAMTRLDH NRALAQLSNK VGCHSTEIRG
     LAVWGNHSAT QYPDISHCTI QGRPAADQVE HAWVKDTFIP TVQQRGAAII KARGASSAAS
     AASAAIDHMR DWALGTPEGE WTSMAVPSDG SYGIEAGLIY SFPVTCRGGD YKIVSGLSVD
     DFSRARMDQT AAELAEERDA VAHLLP
//
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