MDH_BURP1
ID MDH_BURP1 Reviewed; 327 AA.
AC Q3JKE9;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Malate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01517};
DE EC=1.1.1.37 {ECO:0000255|HAMAP-Rule:MF_01517};
GN Name=mdh {ECO:0000255|HAMAP-Rule:MF_01517};
GN OrderedLocusNames=BURPS1710b_A0795;
OS Burkholderia pseudomallei (strain 1710b).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320372;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1710b;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(2010).
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC {ECO:0000255|HAMAP-Rule:MF_01517}.
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_01517};
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 2 family.
CC {ECO:0000255|HAMAP-Rule:MF_01517}.
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DR EMBL; CP000125; ABA52700.1; -; Genomic_DNA.
DR RefSeq; WP_004187735.1; NC_007435.1.
DR PDB; 3D5T; X-ray; 2.51 A; A/B/C/D=1-327.
DR PDBsum; 3D5T; -.
DR AlphaFoldDB; Q3JKE9; -.
DR SMR; Q3JKE9; -.
DR EnsemblBacteria; ABA52700; ABA52700; BURPS1710b_A0795.
DR GeneID; 56598079; -.
DR KEGG; bpm:BURPS1710b_A0795; -.
DR HOGENOM; CLU_040727_2_0_4; -.
DR OMA; TKGMERG; -.
DR OrthoDB; 870724at2; -.
DR EvolutionaryTrace; Q3JKE9; -.
DR Proteomes; UP000002700; Chromosome II.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.110.10; -; 1.
DR HAMAP; MF_01517; Malate_dehydrog_2; 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; IPR010945; Malate_DH_type2.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23382; PTHR23382; 1.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 1.
DR TIGRFAMs; TIGR01759; MalateDH-SF1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NAD; Oxidoreductase; Tricarboxylic acid cycle.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..327
FT /note="Malate dehydrogenase"
FT /id="PRO_0000294380"
FT ACT_SITE 188
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 12..18
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 99
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 106
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 113
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 130..132
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 132
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT BINDING 163
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01517"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:3D5T"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:3D5T"
FT TURN 27..31
FT /evidence="ECO:0007829|PDB:3D5T"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:3D5T"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:3D5T"
FT HELIX 48..59
FT /evidence="ECO:0007829|PDB:3D5T"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:3D5T"
FT HELIX 75..79
FT /evidence="ECO:0007829|PDB:3D5T"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:3D5T"
FT HELIX 99..120
FT /evidence="ECO:0007829|PDB:3D5T"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:3D5T"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:3D5T"
FT HELIX 134..143
FT /evidence="ECO:0007829|PDB:3D5T"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:3D5T"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:3D5T"
FT HELIX 158..172
FT /evidence="ECO:0007829|PDB:3D5T"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:3D5T"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:3D5T"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:3D5T"
FT HELIX 206..210
FT /evidence="ECO:0007829|PDB:3D5T"
FT HELIX 214..218
FT /evidence="ECO:0007829|PDB:3D5T"
FT HELIX 220..225
FT /evidence="ECO:0007829|PDB:3D5T"
FT HELIX 227..235
FT /evidence="ECO:0007829|PDB:3D5T"
FT HELIX 240..256
FT /evidence="ECO:0007829|PDB:3D5T"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:3D5T"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:3D5T"
FT STRAND 280..288
FT /evidence="ECO:0007829|PDB:3D5T"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:3D5T"
FT HELIX 302..319
FT /evidence="ECO:0007829|PDB:3D5T"
FT TURN 320..322
FT /evidence="ECO:0007829|PDB:3D5T"
SQ SEQUENCE 327 AA; 35015 MW; 2E919ABA6D3F67B3 CRC64;
MAKPAKRVAV TGAAGQIAYS LLFRIANGDL LGKDQPVILQ LLDLPQAQAA VKGVVMELDD
CAFPLLAGVV ITDDPKVAFK DADVALLVGA RPRSKGMERK DLLSANAEIF TVQGAALNEV
ASRDVKVLVV GNPANTNAYI AMKSAPDLPK KNFTAMLRLD HNRALSQLAA KSGKPVASIE
KLAVWGNHSP TMYPDFRFAT AEGESLLKLI NDDVWNRDTF IPTVGKRGAA IIEARGLSSA
ASAANAAIDH VRDWVLGTNG KWVTMGIPSD GSYGIPEDII YGVPVICENG EYKRVEGLEI
DAFSREKMDG TLAELLEERD GVAHLLK
