(data stored in ACNUC7421 zone)

SWISSPROT: MDH_RUEPO

ID   MDH_RUEPO               Reviewed;         320 AA.
AC   Q5LXE1;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   11-DEC-2019, entry version 101.
DE   RecName: Full=Malate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00487};
DE            EC=1.1.1.37 {ECO:0000255|HAMAP-Rule:MF_00487};
GN   Name=mdh {ECO:0000255|HAMAP-Rule:MF_00487}; OrderedLocusNames=SPO0349;
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter
OS   pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M.,
RA   Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine
RT   environment.";
RL   Nature 432:910-913(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3;
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC       {ECO:0000255|HAMAP-Rule:MF_00487}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate + NAD(+) = H(+) + NADH + oxaloacetate;
CC         Xref=Rhea:RHEA:21432, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589,
CC         ChEBI:CHEBI:16452, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.37;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00487};
CC   -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 3 family.
CC       {ECO:0000255|HAMAP-Rule:MF_00487}.
DR   EMBL; CP000031; AAV93667.1; -; Genomic_DNA.
DR   RefSeq; WP_011046110.1; NC_003911.12.
DR   SMR; Q5LXE1; -.
DR   STRING; 246200.SPO0349; -.
DR   EnsemblBacteria; AAV93667; AAV93667; SPO0349.
DR   KEGG; sil:SPO0349; -.
DR   eggNOG; ENOG4105C80; Bacteria.
DR   eggNOG; COG0039; LUCA.
DR   HOGENOM; HOG000213794; -.
DR   KO; K00024; -.
DR   OMA; KVCGMAG; -.
DR   OrthoDB; 870724at2; -.
DR   BioCyc; RPOM246200:G1G48-356-MONOMER; -.
DR   Proteomes; UP000001023; Chromosome.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; ISS:TIGR.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; ISS:TIGR.
DR   CDD; cd01339; LDH-like_MDH; 1.
DR   Gene3D; 3.90.110.10; -; 1.
DR   HAMAP; MF_00487; Malate_dehydrog_3; 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; IPR011275; Malate_DH_type3.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF02866; Ldh_1_C; 1.
DR   Pfam; PF00056; Ldh_1_N; 1.
DR   PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR   PRINTS; PR00086; LLDHDRGNASE.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   SUPFAM; SSF56327; SSF56327; 1.
DR   TIGRFAMs; TIGR01763; MalateDH_bact; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q5LXE1.
DR   SWISS-2DPAGE; Q5LXE1.
KW   NAD; Oxidoreductase; Reference proteome; Tricarboxylic acid cycle.
FT   CHAIN           1..320
FT                   /note="Malate dehydrogenase"
FT                   /id="PRO_0000113471"
FT   NP_BIND         10..15
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   NP_BIND         119..121
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   ACT_SITE        176
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         34
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         83
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         89
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         96
FT                   /note="NAD"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         121
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         152
FT                   /note="Substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
SQ   SEQUENCE   320 AA;  33535 MW;  5205FB65543FE4B7 CRC64;
     MARPKIALIG AGQIGGTLAH LVALKELGDV VLFDIAEGTP EGKALDIAES GPSEGFDAKL
     KGTQSYADIA GADVCIVTAG VPRKPGMSRD DLLGINLKVM KSVGEGIRDN APDAFVICIT
     NPLDAMVWAL QQFSGLPANK VCGMAGVLDS ARFRHFLAEE FNVSMKDVTA FVLGGHGDTM
     VPSVRYSTVA GIPLPDLIKM GWTSQEKLDA IVQRTRDGGA EIVGLLKTGS AYYAPATSAI
     EMAEAYLKDQ KRVLPCAAYC NGELGVKGMY VGVPTVIGAG GIERIIDVSL TKEEQDMFDN
     SVNAVKGLVE ACKGIDGSLA
//

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