MDH_BACAN
ID MDH_BACAN Reviewed; 312 AA.
AC Q6HSF4; Q6KLP9; Q81KZ7;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 134.
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=BA_4837, GBAA_4837, BAS4486;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) 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; AE016879; AAP28526.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT33956.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT56784.1; -; Genomic_DNA.
DR RefSeq; NP_847040.1; NC_003997.3.
DR RefSeq; WP_000153232.1; NZ_WXXJ01000026.1.
DR RefSeq; YP_030734.1; NC_005945.1.
DR PDB; 3TL2; X-ray; 1.70 A; A=1-312.
DR PDBsum; 3TL2; -.
DR AlphaFoldDB; Q6HSF4; -.
DR SMR; Q6HSF4; -.
DR STRING; 260799.BAS4486; -.
DR DNASU; 1083988; -.
DR EnsemblBacteria; AAP28526; AAP28526; BA_4837.
DR EnsemblBacteria; AAT33956; AAT33956; GBAA_4837.
DR GeneID; 59154822; -.
DR GeneID; 64203187; -.
DR GeneID; 67468888; -.
DR KEGG; ban:BA_4837; -.
DR KEGG; bar:GBAA_4837; -.
DR KEGG; bat:BAS4486; -.
DR PATRIC; fig|198094.11.peg.4798; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_045401_2_1_9; -.
DR OMA; CYIIVLT; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; 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 1: Evidence at protein level;
KW 3D-structure; NAD; Oxidoreductase; Phosphoprotein; Reference proteome;
KW Tricarboxylic acid cycle.
FT CHAIN 1..312
FT /note="Malate dehydrogenase"
FT /id="PRO_0000113424"
FT ACT_SITE 180
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 12..17
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 36
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 100
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 123..125
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00487"
FT STRAND 7..11
FT /evidence="ECO:0007829|PDB:3TL2"
FT HELIX 15..26
FT /evidence="ECO:0007829|PDB:3TL2"
FT STRAND 31..35
FT /evidence="ECO:0007829|PDB:3TL2"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:3TL2"
FT HELIX 41..58
FT /evidence="ECO:0007829|PDB:3TL2"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:3TL2"
FT HELIX 70..73
FT /evidence="ECO:0007829|PDB:3TL2"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:3TL2"
FT HELIX 93..114
FT /evidence="ECO:0007829|PDB:3TL2"
FT STRAND 119..122
FT /evidence="ECO:0007829|PDB:3TL2"
FT HELIX 127..138
FT /evidence="ECO:0007829|PDB:3TL2"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:3TL2"
FT STRAND 145..147
FT /evidence="ECO:0007829|PDB:3TL2"
FT HELIX 150..165
FT /evidence="ECO:0007829|PDB:3TL2"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:3TL2"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:3TL2"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:3TL2"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:3TL2"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:3TL2"
FT HELIX 204..215
FT /evidence="ECO:0007829|PDB:3TL2"
FT HELIX 217..225
FT /evidence="ECO:0007829|PDB:3TL2"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:3TL2"
FT HELIX 232..246
FT /evidence="ECO:0007829|PDB:3TL2"
FT STRAND 251..261
FT /evidence="ECO:0007829|PDB:3TL2"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:3TL2"
FT STRAND 266..277
FT /evidence="ECO:0007829|PDB:3TL2"
FT STRAND 280..284
FT /evidence="ECO:0007829|PDB:3TL2"
FT HELIX 291..308
FT /evidence="ECO:0007829|PDB:3TL2"
SQ SEQUENCE 312 AA; 33498 MW; 615A61C61CA217FD CRC64;
MTIKRKKVSV IGAGFTGATT AFLLAQKELA DVVLVDIPQL ENPTKGKALD MLEASPVQGF
DANIIGTSDY ADTADSDVVV ITAGIARKPG MSRDDLVATN SKIMKSITRD IAKHSPNAII
VVLTNPVDAM TYSVFKEAGF PKERVIGQSG VLDTARFRTF IAQELNLSVK DITGFVLGGH
GDDMVPLVRY SYAGGIPLET LIPKERLEAI VERTRKGGGE IVGLLGNGSA YYAPAASLVE
MTEAILKDQR RVLPAIAYLE GEYGYSDLYL GVPVILGGNG IEKIIELELL ADEKEALDRS
VESVRNVMKV LV
