位置:首页 > 蛋白库 > MDH_EHRRG
MDH_EHRRG
ID   MDH_EHRRG               Reviewed;         317 AA.
AC   Q5FGT9;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 107.
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};
GN   OrderedLocusNames=ERGA_CDS_04180;
OS   Ehrlichia ruminantium (strain Gardel).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Ehrlichia.
OX   NCBI_TaxID=302409;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Gardel;
RX   PubMed=16547041; DOI=10.1128/jb.188.7.2533-2542.2006;
RA   Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y.,
RA   Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D.;
RT   "Comparative genomic analysis of three strains of Ehrlichia ruminantium
RT   reveals an active process of genome size plasticity.";
RL   J. Bacteriol. 188:2533-2542(2006).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR925677; CAI27870.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5FGT9; -.
DR   SMR; Q5FGT9; -.
DR   EnsemblBacteria; CAI27870; CAI27870; ERGA_CDS_04180.
DR   KEGG; erg:ERGA_CDS_04180; -.
DR   HOGENOM; CLU_045401_2_1_5; -.
DR   OMA; ASCAEYI; -.
DR   BioCyc; ERUM302409:ERGA_RS02160-MON; -.
DR   Proteomes; UP000000533; Chromosome.
DR   GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0019752; P:carboxylic acid 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   NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT   CHAIN           1..317
FT                   /note="Malate dehydrogenase"
FT                   /id="PRO_0000113450"
FT   ACT_SITE        181
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         15..20
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         39
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         94
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         101
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         124..126
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         126
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT   BINDING         157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
SQ   SEQUENCE   317 AA;  34263 MW;  8774003F1FA8CADE CRC64;
     MRDMMIQSKK IALIGSGNIG GMIAYLIRLK NLGDVVLLDI NDGMAKGKAL DIAESSPIGK
     YNGEIFGTNN YADIENADAI IVTAGITRKP GMSRDDLIST NVNIIKEIAT NIAKYAPNAF
     VIVVTNPLDV MVLAMYRYSH LPSNMIVGMA GVLDSARFSY FIAKELNVSV ESVDSLVLGG
     HGDIMLPLIR YSSVSGVSIA DLIKLGMITH DKVTEIVERT RKGGEEIVSL LKTGSAYYAP
     AESAVLMLDS YLNDKKLMLP CSAYLKGEYG VHDLFVGVPI IIGKNGVEKI VELQLTEEEN
     SIFNNSVALI QNLVANI
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024