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Database: UniProt
Entry: O67655
LinkDB: O67655
Original site: O67655 
ID   MDH1_AQUAE              Reviewed;         335 AA.
AC   O67655;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   16-JAN-2019, entry version 130.
DE   RecName: Full=Malate dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_00487};
DE            EC=1.1.1.37 {ECO:0000255|HAMAP-Rule:MF_00487};
GN   Name=mdh1; Synonyms=mdh; OrderedLocusNames=aq_1782;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex
RT   aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- FUNCTION: Catalyzes the reversible oxidation of malate to
CC       oxaloacetate. {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;
CC         EC=1.1.1.37; 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; AE000657; AAC07619.1; -; Genomic_DNA.
DR   PIR; E70453; E70453.
DR   RefSeq; NP_214221.1; NC_000918.1.
DR   RefSeq; WP_010881158.1; NC_000918.1.
DR   ProteinModelPortal; O67655; -.
DR   SMR; O67655; -.
DR   STRING; 224324.aq_1782; -.
DR   EnsemblBacteria; AAC07619; AAC07619; aq_1782.
DR   GeneID; 1193462; -.
DR   KEGG; aae:aq_1782; -.
DR   PATRIC; fig|224324.8.peg.1378; -.
DR   eggNOG; ENOG4105C80; Bacteria.
DR   eggNOG; COG0039; LUCA.
DR   HOGENOM; HOG000213794; -.
DR   InParanoid; O67655; -.
DR   KO; K00024; -.
DR   OMA; MDLMQTA; -.
DR   OrthoDB; 870724at2; -.
DR   BioCyc; AAEO224324:G1G15-1273-MONOMER; -.
DR   Proteomes; UP000000798; 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:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
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;
KW   Complete proteome; NAD; Oxidoreductase; Reference proteome;
KW   Tricarboxylic acid cycle.
FT   CHAIN         1    335       Malate dehydrogenase 1.
FT                                /FTId=PRO_0000113422.
FT   NP_BIND      11     16       NAD. {ECO:0000255|HAMAP-Rule:MF_00487}.
FT   NP_BIND     133    135       NAD. {ECO:0000255|HAMAP-Rule:MF_00487}.
FT   ACT_SITE    190    190       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00487}.
FT   BINDING      35     35       NAD. {ECO:0000255|HAMAP-Rule:MF_00487}.
FT   BINDING      97     97       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00487}.
FT   BINDING     103    103       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00487}.
FT   BINDING     110    110       NAD. {ECO:0000255|HAMAP-Rule:MF_00487}.
FT   BINDING     135    135       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00487}.
FT   BINDING     166    166       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00487}.
SQ   SEQUENCE   335 AA;  36675 MW;  E02FA4C339237118 CRC64;
     MRMKKTVAVI GAGNVGEHVA SLILLKNLAN VKMFDLPRKT EEKVFEPVKG KALDMKQMLA
     AMDIDARVEG YTVTPEGEGY EPLEGSDIVV ITAGFPRRPG MSREDLLEAN IRIISVIADR
     IKRYAPDAIV IVVTNPVDVM TYVAYKLLNF PKNRVMGMAG VLDSARFKTF ISEELMVSPK
     DIHAYVIGGH GDEMVPLISI SNVGGIPLKD LLPKEKLEKI IERTRFGGGE IVNLMGTSAY
     YAPAAAIVDM IEALVQNSKR ILPCSVYLDG EAGEYYGVQG FCVGVPVKLG SNGVEEIIKV
     PMIEEEREMW RRSVESVKKT VEVAEGILSA GSSRQ
//
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