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Database: UniProt/SWISS-PROT
Entry: MDH_PSYWF
LinkDB: MDH_PSYWF
Original site: MDH_PSYWF 
ID   MDH_PSYWF               Reviewed;         327 AA.
AC   A5WGM2;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   07-JUN-2017, entry version 71.
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=PsycPRwf_1873;
OS   Psychrobacter sp. (strain PRwf-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Psychrobacter.
OX   NCBI_TaxID=349106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PRwf-1;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome of Psychrobacter sp. PRwf-1.";
RL   Submitted (MAY-2007) 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; CP000713; ABQ94813.1; -; Genomic_DNA.
DR   RefSeq; WP_011961090.1; NC_009524.1.
DR   ProteinModelPortal; A5WGM2; -.
DR   SMR; A5WGM2; -.
DR   STRING; 349106.PsycPRwf_1873; -.
DR   EnsemblBacteria; ABQ94813; ABQ94813; PsycPRwf_1873.
DR   KEGG; prw:PsycPRwf_1873; -.
DR   eggNOG; ENOG4105D9Z; Bacteria.
DR   eggNOG; COG0039; LUCA.
DR   HOGENOM; HOG000220953; -.
DR   KO; K00024; -.
DR   OMA; RPRTKGM; -.
DR   OrthoDB; POG091H03R4; -.
DR   Proteomes; UP000001993; 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   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; NAD; Oxidoreductase; Reference proteome;
KW   Tricarboxylic acid cycle.
FT   CHAIN         1    327       Malate dehydrogenase.
FT                                /FTId=PRO_0000319846.
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   327 AA;  35366 MW;  9FDD02BB8CAD08EB CRC64;
     MKQPVRVAVT GAAGNISYAM LFRIASGEML GKDQPVILQL LEITPALDAL KGVVMELEDC
     AFPLLAGVVQ TDDATVAFKD ADYALLVGAR PRGPGMERKD LLEANAAIFS AQGKALNEVA
     SRDVKVLVVG NPANTNALIA QRNAPDLDPR NFTAMTRLDH NRGMAQLAEE TNSTVNDVKK
     MIIWGNHSST QYPDLTECTV NGKPALEQVD RDWYENSYIP SVQKRGAAII EARGASSAAS
     AANAAIAHMR TWALGTDEND WVSMGVYSQG EYGIAKGLIY SFPCTCSNGD WKIVEGLDTS
     SDFSQEKMKA TEQELSEERD AVEHLLP
//
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