MDH_RICAH
ID MDH_RICAH Reviewed; 314 AA.
AC A8GN82;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=A1C_02825;
OS Rickettsia akari (strain Hartford).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=293614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hartford;
RA Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S.,
RA Sanchez A., Whiting M., Dasch G., Eremeeva M.;
RT "Complete genome sequence of Rickettsia akari.";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP000847; ABV74857.1; -; Genomic_DNA.
DR RefSeq; WP_012149490.1; NC_009881.1.
DR AlphaFoldDB; A8GN82; -.
DR SMR; A8GN82; -.
DR STRING; 293614.A1C_02825; -.
DR PRIDE; A8GN82; -.
DR EnsemblBacteria; ABV74857; ABV74857; A1C_02825.
DR KEGG; rak:A1C_02825; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_045401_2_1_5; -.
DR OMA; MGWTSQA; -.
DR Proteomes; UP000006830; 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..314
FT /note="Malate dehydrogenase"
FT /id="PRO_1000026488"
FT ACT_SITE 177
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 11..16
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 35
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 97
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 120..122
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
SQ SEQUENCE 314 AA; 33607 MW; F1EFCACB6F90D245 CRC64;
MKKNPKISLI GSGNIGGTLA HLISLRELGD IVLFDVAEGV PQGKALDLMQ ASTIAGSDIK
ITGTNDYKDI EGSDAIIITA GLPRKPGMSR DDLISINTGI MKNVAENVKK YAPDAFVIVI
TNPLDVMVYV MLKASGLPHN QVIGMAGVLD SSRFNLFLAE EFKVSVSNVN STVLGGHGDA
MVPLARYSTI SGIPIPDLIK MGLSSNENIE KIIDRTRNGG GDIVALLKTG SAYYAPAASA
IEMLEAYLKD KRQMLTCAAY LQGEYGVHDL YVGVPIIIGK EGVIKVVELQ LTKEEKTLFD
KSVEGVKTLI ETIQ
