A7ZSD0 (MDH_ECO24) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Malate dehydrogenase
EC=1.1.1.37

Gene names

Name:	mdh
Ordered Locus Names:	EcE24377A_3719

Organism

Escherichia coli O139:H28 (strain E24377A / ETEC) [Complete proteome] [HAMAP]

Taxonomic identifier

331111 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	312 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the reversible oxidation of malate to oxaloacetate By similarity. HAMAP MF_01516
Catalytic activity	(S)-malate + NAD+ = oxaloacetate + NADH. HAMAP MF_01516
Subunit structure	Homodimer By similarity. HAMAP MF_01516
Sequence similarities	Belongs to the LDH/MDH superfamily. MDH type 1 family.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cellular carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro malate metabolic process Inferred from electronic annotation. Source: InterPro tricarboxylic acid cycle Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	L-malate dehydrogenase activity Inferred from electronic annotation. Source: EC nucleotide binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 312	312	Malate dehydrogenase HAMAP MF_01516		PRO_1000068585
Regions
	Nucleotide binding	7 – 13	7	NAD By similarity
	Nucleotide binding	117 – 119	3	NAD By similarity
Sites
	Active site	177	1	Proton acceptor By similarity
	Binding site	34	1	NAD By similarity
	Binding site	81	1	Substrate By similarity
	Binding site	87	1	Substrate By similarity
	Binding site	94	1	NAD By similarity
	Binding site	119	1	Substrate By similarity
	Binding site	153	1	Substrate By similarity
	Binding site	227	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	A7ZSD0 [UniParc]. Last modified October 23, 2007. Version 1. Checksum: 17741A3B5AD068BA	FASTA	312	32,337
	10 20 30 40 50 60 MKVAVLGAAG GIGQALALLL KTQLPSGSEL SLYDIAPVTP GVAVDLSHIP TAVKIKGFSG 70 80 90 100 110 120 EDATPALEGA DVVLISAGVA RKPGMDRSDL FNVNAGIVKN LVQQVAKTCP KACIGIITNP 130 140 150 160 170 180 VNTTVAIAAE VLKKAGVYDK NKLFGVTTLD IIRSNTFVAE LKGKQPGEVE VPVIGGHSGV 190 200 210 220 230 240 TILPLLSQVP GVSFTEQEVA DLTKRIQNAG TEVVEAKAGG GSATLSMGQA AARFGLSLVR 250 260 270 280 290 300 ALQGEQGVVE CAYVEGDGQY ARFFSQPLLL GKNGVEERKS IGTLSAFEQN ALEGMLDTLK 310 KDIALGEEFV NK

References

[1]

"The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates." Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J. J. Bacteriol. 190:6881-6893(2008) [PubMed: 18676672] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: E24377A / ETEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000800 Genomic DNA. Translation: ABV17436.1.
RefSeq	YP_001464709.1. NC_009801.1.
3D structure databases
ProteinModelPortal	A7ZSD0.
SMR	A7ZSD0. Positions 1-312.
ModBase	Search...
Protein-protein interaction databases
STRING	A7ZSD0.
Proteomic databases
PRIDE	A7ZSD0.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000020034; EBESCP00000019096; EBESCG00000019088.
GeneID	5586293.
GenomeReviews	Gene locus EcE24377A_3719 in contig CP000800_GR.
KEGG	ecw:EcE24377A_3719.
PATRIC	18296722. VBIEscCol31211_3973.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0039.
GeneTree	EBGT00050000011757.
HOGENOM	HBG566126.
OMA	LVEKCAA.
ProtClustDB	PRK05086.
Enzyme and pathway databases
BioCyc	ECOL331111:ECE24377A_3719-MONOMER.
Family and domain databases
HAMAP	MF_01516. Malate_dehydrog_1. [Tree]
InterPro	IPR001557. L-lactate/malate_DH. IPR022383. Lactate/malate_DH_C. IPR001236. Lactate/malate_DH_N. IPR015955. Lactate_DH/Glyco_Ohase_4_C. IPR001252. Malate_DH_AS. IPR010097. Malate_DH_type1. IPR023958. Malate_DH_type1_bac. IPR016040. NAD(P)-bd_dom. [Graphical view]
Gene3D	G3DSA:3.90.110.10. lact_mal_DH. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K00024.
Pfam	PF02866. Ldh_1_C. 1 hit. PF00056. Ldh_1_N. 1 hit. [Graphical view]
PIRSF	PIRSF000102. Lac_mal_DH. 1 hit.
SUPFAM	SSF56327. Lactate_DH/Glyco_hydro_4_C. 1 hit.
TIGRFAMs	TIGR01772. MDH_euk_gproteo. 1 hit.
PROSITE	PS00068. MDH. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MDH_ECO24

Accession

Primary (citable) accession number: A7ZSD0

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	October 23, 2007
Last modified:	January 25, 2012
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program