ID K7AAK2_9ALTE Unreviewed; 311 AA.
AC K7AAK2;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 73.
DE RecName: Full=Malate dehydrogenase {ECO:0000256|ARBA:ARBA00020382, ECO:0000256|HAMAP-Rule:MF_01516};
DE EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995, ECO:0000256|HAMAP-Rule:MF_01516};
GN Name=mdh {ECO:0000256|HAMAP-Rule:MF_01516};
GN ORFNames=C427_5153 {ECO:0000313|EMBL:AGH47252.1};
OS Paraglaciecola psychrophila 170.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=1129794 {ECO:0000313|EMBL:AGH47252.1, ECO:0000313|Proteomes:UP000011864};
RN [1] {ECO:0000313|EMBL:AGH47252.1, ECO:0000313|Proteomes:UP000011864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:AGH47252.1,
RC ECO:0000313|Proteomes:UP000011864};
RX PubMed=23640379;
RA Yin J., Chen J., Liu G., Yu Y., Song L., Wang X., Qu X.;
RT "Complete Genome Sequence of Glaciecola psychrophila Strain 170T.";
RL Genome Announc. 1:E00199-13(2013).
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC {ECO:0000256|ARBA:ARBA00003966, ECO:0000256|HAMAP-Rule:MF_01516}.
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:0000256|ARBA:ARBA00000774, ECO:0000256|HAMAP-
CC Rule:MF_01516, ECO:0000256|RuleBase:RU000422};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_01516}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC {ECO:0000256|ARBA:ARBA00008824, ECO:0000256|HAMAP-Rule:MF_01516}.
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DR EMBL; CP003837; AGH47252.1; -; Genomic_DNA.
DR RefSeq; WP_007638066.1; NZ_BAES01000044.1.
DR AlphaFoldDB; K7AAK2; -.
DR SMR; K7AAK2; -.
DR STRING; 1129794.C427_5153; -.
DR KEGG; gps:C427_5153; -.
DR PATRIC; fig|1129794.4.peg.5138; -.
DR eggNOG; COG0039; Bacteria.
DR HOGENOM; CLU_047181_1_0_6; -.
DR OrthoDB; 9802969at2; -.
DR Proteomes; UP000011864; 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 CDD; cd01337; MDH_glyoxysomal_mitochondrial; 1.
DR Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR HAMAP; MF_01516; Malate_dehydrog_1; 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; IPR010097; Malate_DH_type1.
DR InterPro; IPR023958; Malate_DH_type1_bac.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR01772; MDH_euk_gproteo; 1.
DR PANTHER; PTHR11540; MALATE AND LACTATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11540:SF16; MALATE DEHYDROGENASE, MITOCHONDRIAL; 1.
DR Pfam; PF02866; Ldh_1_C; 1.
DR Pfam; PF00056; Ldh_1_N; 1.
DR PIRSF; PIRSF000102; Lac_mal_DH; 1.
DR SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00068; MDH; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|HAMAP-Rule:MF_01516, ECO:0000256|PIRSR:PIRSR000102-3};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01516}; Reference proteome {ECO:0000313|Proteomes:UP000011864};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP-
KW Rule:MF_01516}.
FT DOMAIN 1..145
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 147..308
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 177
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 7..13
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 34
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 87
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 94
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 117..119
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 119
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 227
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01516,
FT ECO:0000256|PIRSR:PIRSR000102-3"
SQ SEQUENCE 311 AA; 32464 MW; 879CDC180D32DF0B CRC64;
MKIAVLGAAG GIGQALSLLL KVQLPAGSEL SLYDVAPVVP GVAVDLSHIP TDVKVQGYGK
DDLADALTGC DIVLIPAGVP RKPGMDRSDL FNINAGIVRN LVDAIADNCP EACTCIITNP
VNTTVAIAAE ALKAKGVYNK NKLFGVTTLD VIRSETFVGN LKGLNPANVH VPVIGGHSGT
TILPLLSQVQ GVDFTDEEVA SLTTRIQNAG TEVVEAKAGG GSATLSMGHA AARFCLSLVD
AMRGENVVEY TYVETNSDDA EFFAHPVRLG KNGVEEILSY GELSEFEENA KNAMLEGLRS
DIAMGVKFVT G
//