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Database: UniProt/SWISS-PROT
Entry: MDH_ALCBS
LinkDB: MDH_ALCBS
Original site: MDH_ALCBS 
ID   MDH_ALCBS               Reviewed;         328 AA.
AC   Q0VQ52;
DT   10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   25-OCT-2017, entry version 82.
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=ABO_1248;
OS   Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689
OS   / SK2).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2;
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(2006).
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; AM286690; CAL16696.1; -; Genomic_DNA.
DR   ProteinModelPortal; Q0VQ52; -.
DR   SMR; Q0VQ52; -.
DR   STRING; 393595.ABO_1248; -.
DR   PRIDE; Q0VQ52; -.
DR   EnsemblBacteria; CAL16696; CAL16696; ABO_1248.
DR   KEGG; abo:ABO_1248; -.
DR   eggNOG; ENOG4105C80; Bacteria.
DR   eggNOG; COG0039; LUCA.
DR   HOGENOM; HOG000220953; -.
DR   KO; K00024; -.
DR   OMA; RPRTKGM; -.
DR   OrthoDB; POG091H03R4; -.
DR   Proteomes; UP000008871; 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    328       Malate dehydrogenase.
FT                                /FTId=PRO_0000294372.
FT   NP_BIND      13     19       NAD. {ECO:0000255|HAMAP-Rule:MF_01517}.
FT   NP_BIND     131    133       NAD. {ECO:0000255|HAMAP-Rule:MF_01517}.
FT   ACT_SITE    189    189       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01517}.
FT   BINDING      94     94       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01517}.
FT   BINDING     100    100       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01517}.
FT   BINDING     107    107       NAD. {ECO:0000255|HAMAP-Rule:MF_01517}.
FT   BINDING     114    114       NAD. {ECO:0000255|HAMAP-Rule:MF_01517}.
FT   BINDING     133    133       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01517}.
FT   BINDING     164    164       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01517}.
SQ   SEQUENCE   328 AA;  35407 MW;  B9EB0E5352E4CBBA CRC64;
     MFMKAPVRVA VTGAAGQISY SLLFRIASGD MLGKDQPVIL QLLEITPALE ALNGVIMELE
     DCAFPLVAGI TGTDDANVAF KDADYALLVG ARPRGPGMER KDLLEANAAI FSAQGKAIND
     NASKGIKVLV VGNPANTNAL IAQRNAPDID PRQFTAMTRL DHNRAMAQLA NKLGKTVNDV
     KKMLIWGNHS STQYPDLHHC EVDGKVAIDQ VEQDWYENDY IPTVQQRGAA IIKARGASSA
     ASAANAAVDH MRSWALGTDE GDWVSMGIYS DGSYGIQEGL IYSFPCTCKN GDWTIVQGLE
     VNDFSRGKMQ ATEQELAEER DAVSHLLP
//
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