ID Q9K327_ECOLX Unreviewed; 282 AA.
AC Q9K327;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 130.
DE RecName: Full=Malate dehydrogenase {ECO:0000256|ARBA:ARBA00020382, ECO:0000256|RuleBase:RU000422};
DE EC=1.1.1.37 {ECO:0000256|ARBA:ARBA00012995, ECO:0000256|RuleBase:RU000422};
DE Flags: Fragment;
GN Name=mdh {ECO:0000313|EMBL:AAF97152.1};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:AAF97152.1};
RN [1] {ECO:0000313|EMBL:AAF97152.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B170 {ECO:0000313|EMBL:AAF97152.1}, DEC11a
RC {ECO:0000313|EMBL:AAF97150.1}, DEC12a {ECO:0000313|EMBL:AAF97151.1},
RC DEC1a {ECO:0000313|EMBL:AAF97140.1}, DEC2a
RC {ECO:0000313|EMBL:AAF97141.1}, and E2348/69
RC {ECO:0000313|EMBL:AAF97139.1};
RX PubMed=10894541; DOI=10.1038/35017546;
RA Reid S.D., Herbelin C.J., Bumbaugh A.C., Selander R.K., Whittam T.S.;
RT "Parallel evolution of virulence in pathogenic Escherichia coli.";
RL Nature 406:64-67(2000).
CC -!- FUNCTION: Catalyzes the reversible oxidation of malate to oxaloacetate.
CC {ECO:0000256|ARBA:ARBA00003966}.
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,
CC ECO:0000256|RuleBase:RU000422};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. MDH type 1 family.
CC {ECO:0000256|ARBA:ARBA00008824}.
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DR EMBL; AF267599; AAF97139.1; -; Genomic_DNA.
DR EMBL; AF267600; AAF97140.1; -; Genomic_DNA.
DR EMBL; AF267601; AAF97141.1; -; Genomic_DNA.
DR EMBL; AF267610; AAF97150.1; -; Genomic_DNA.
DR EMBL; AF267611; AAF97151.1; -; Genomic_DNA.
DR EMBL; AF267612; AAF97152.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9K327; -.
DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
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|PIRSR:PIRSR000102-3, ECO:0000256|RuleBase:RU000422};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003369};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW ECO:0000256|RuleBase:RU000422}.
FT DOMAIN 1..129
FT /note="Lactate/malate dehydrogenase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00056"
FT DOMAIN 131..281
FT /note="Lactate/malate dehydrogenase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02866"
FT ACT_SITE 161
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-1"
FT BINDING 18
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 65
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 71
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 78
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 101..103
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT BINDING 103
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-2"
FT BINDING 211
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000256|PIRSR:PIRSR000102-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AAF97152.1"
FT NON_TER 282
FT /evidence="ECO:0000313|EMBL:AAF97152.1"
SQ SEQUENCE 282 AA; 29314 MW; 535EA5C89CDAB97B CRC64;
ALLLKTQLPS GSELSLYDIA PVTPGVAVDL SHIPTAVKIK GFSGEDATPA LEGADVVLIS
AGVARKPGMD RSDLFNVNAG IVKNLVQQVA KTCPKACIGI ITNPVNTTVA IAAEVLKKAG
VYDKNKLFGV TTLDIIRSNT FVAELKGKQP GEVEVPVIGG HSGVTILPLL SQVPGVSFTE
QEVADLTKRI QNAGTEVVEA KAGGGSATLS MGQAAARFGL SLVRALQGEQ GVVECAYVEG
DGQYARFFSQ PLLLGKNGVE ERKSIGTLSA FEQNALEGML DT
//
