MDH_LEGPH
ID MDH_LEGPH Reviewed; 330 AA.
AC Q5ZT13;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 94.
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}; OrderedLocusNames=lpg2352;
OS Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC
OS 33152 / DSM 7513).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=272624;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX PubMed=15448271; DOI=10.1126/science.1099776;
RA Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M., Asamani G.,
RA Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J., Steshenko V.,
RA Park S.H., Zhao B., Teplitskaya E., Edwards J.R., Pampou S., Georghiou A.,
RA Chou I.-C., Iannuccilli W., Ulz M.E., Kim D.H., Geringer-Sameth A.,
RA Goldsberry C., Morozov P., Fischer S.G., Segal G., Qu X., Rzhetsky A.,
RA Zhang P., Cayanis E., De Jong P.J., Ju J., Kalachikov S., Shuman H.A.,
RA Russo J.J.;
RT "The genomic sequence of the accidental pathogen Legionella pneumophila.";
RL Science 305:1966-1968(2004).
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; AE017354; AAU28414.1; -; Genomic_DNA.
DR RefSeq; WP_010948058.1; NC_002942.5.
DR RefSeq; YP_096361.1; NC_002942.5.
DR PDB; 6PBL; X-ray; 1.85 A; A/B=1-330.
DR PDBsum; 6PBL; -.
DR AlphaFoldDB; Q5ZT13; -.
DR SMR; Q5ZT13; -.
DR STRING; 272624.lpg2352; -.
DR PaxDb; Q5ZT13; -.
DR PRIDE; Q5ZT13; -.
DR EnsemblBacteria; AAU28414; AAU28414; lpg2352.
DR GeneID; 66491480; -.
DR KEGG; lpn:lpg2352; -.
DR PATRIC; fig|272624.6.peg.2473; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_040727_2_0_6; -.
DR OMA; TKGMERG; -.
DR Proteomes; UP000000609; Chromosome.
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; IPR001252; Malate_DH_AS.
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.
DR PROSITE; PS00068; MDH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; NAD; Oxidoreductase; Reference proteome;
KW Tricarboxylic acid cycle.
FT CHAIN 1..330
FT /note="Malate dehydrogenase"
FT /id="PRO_0000113372"
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 5..10
FT /evidence="ECO:0007829|PDB:6PBL"
FT TURN 11..14
FT /evidence="ECO:0007829|PDB:6PBL"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:6PBL"
FT TURN 27..31
FT /evidence="ECO:0007829|PDB:6PBL"
FT STRAND 36..42
FT /evidence="ECO:0007829|PDB:6PBL"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:6PBL"
FT HELIX 48..59
FT /evidence="ECO:0007829|PDB:6PBL"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:6PBL"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:6PBL"
FT HELIX 75..79
FT /evidence="ECO:0007829|PDB:6PBL"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:6PBL"
FT HELIX 99..120
FT /evidence="ECO:0007829|PDB:6PBL"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:6PBL"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:6PBL"
FT HELIX 134..143
FT /evidence="ECO:0007829|PDB:6PBL"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:6PBL"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:6PBL"
FT HELIX 158..171
FT /evidence="ECO:0007829|PDB:6PBL"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:6PBL"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:6PBL"
FT TURN 196..198
FT /evidence="ECO:0007829|PDB:6PBL"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:6PBL"
FT HELIX 206..210
FT /evidence="ECO:0007829|PDB:6PBL"
FT HELIX 213..218
FT /evidence="ECO:0007829|PDB:6PBL"
FT HELIX 220..225
FT /evidence="ECO:0007829|PDB:6PBL"
FT HELIX 227..235
FT /evidence="ECO:0007829|PDB:6PBL"
FT HELIX 240..255
FT /evidence="ECO:0007829|PDB:6PBL"
FT STRAND 264..269
FT /evidence="ECO:0007829|PDB:6PBL"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:6PBL"
FT STRAND 281..289
FT /evidence="ECO:0007829|PDB:6PBL"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:6PBL"
FT HELIX 303..325
FT /evidence="ECO:0007829|PDB:6PBL"
SQ SEQUENCE 330 AA; 36007 MW; 3C36348E4E1BCAEA CRC64;
MTNNRVRVAV TGAAGQIGYA LVFRIASGQM FGPNTEVELN LLELEPALPS LEGVAMELDD
CAFPLLKRIV CTADLNKAMD GVNWALLVGS VPRKQGMERS DLLQINGGIF TKQGQAINDY
ASDDVRVFVV GNPCNTNCLI AMNHAKDVPS DRFYAMTTLD ELRARTQLAK KAGVDITAVT
QMTIWGNHSA TQYPDFYNAK INGTSAAQVI NDETWLKETF VSTVQQRGAA VIKARGSSSA
ASAANAIITG VNHLVTDTPA GESFSMCRRS KGEYGVDEGL IFSFPCRREH GELKVVENLE
FNDFGRERFN TTLNELRSER DTVKSLGLLD
