A0LFF8 (MDH_SYNFM) 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:	Sfum_0460

Organism

Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB) [Complete proteome] [HAMAP]

Taxonomic identifier

335543 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Deltaproteobacteria › Syntrophobacterales › Syntrophobacteraceae › Syntrophobacter › Syntrophobacter fumaroxidans

Protein attributes

Sequence length	329 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the reversible oxidation of malate to oxaloacetate. Catalyzes the reduction of oxaloacetate more efficiently than the oxidation of malate. Ref.2
Catalytic activity	(S)-malate + NAD+ = oxaloacetate + NADH. Ref.2
Enzyme regulation	Substrate inhibition is observed at high concentrations of oxaloacetate. Ref.2
Subunit structure	Homodimer. Ref.2
Sequence similarities	Belongs to the LDH/MDH superfamily. MDH type 2 family.
Biophysicochemical properties	Kinetic parameters: KM=50 µM for oxaloacetate (at 37 degrees Celsius and pH 7.5) Ref.2 KM=30 µM for NADH (at 37 degrees Celsius and pH 7.5) KM=4 mM for L-malate (at 37 degrees Celsius and pH 9.0) KM=1.1 mM for NAD (at 37 degrees Celsius and pH 9.0) pH dependence: Optimum pH is 8.5 with oxaloacetate as substrate. Temperature dependence: Optimum temperature is 60 degrees Celsius with oxaloacetate as substrate.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing
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: HAMAP
Molecular_function	L-malate dehydrogenase activity Inferred from electronic annotation. Source: HAMAP 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
	Initiator methionine	1	1	Removed Ref.2
	Chain	2 – 329	328	Malate dehydrogenase HAMAP-Rule MF_01517		PRO_0000292376
Regions
	Nucleotide binding	12 – 18	7	NAD By similarity
	Nucleotide binding	132 – 134	3	NAD By similarity
Sites
	Active site	190	1	Proton acceptor By similarity
	Binding site	95	1	Substrate By similarity
	Binding site	101	1	Substrate By similarity
	Binding site	108	1	NAD By similarity
	Binding site	115	1	NAD By similarity
	Binding site	134	1	Substrate By similarity
	Binding site	165	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	A0LFF8 [UniParc]. Last modified December 12, 2006. Version 1. Checksum: 1BE66E683446BE07	FASTA	329	35,690
	10 20 30 40 50 60 MAKKPVRVTV TGAAGQIGYA LLFRVASGQM LGPDQPIILQ MLELPIDKVQ AALKGVMMEL 70 80 90 100 110 120 EDCAFPLLAD MIGTGDPKVA FKDSDYALLV GARPRGPGME RKDLLLENAK IFIEQGKAMN 130 140 150 160 170 180 AVASRDIRVI VVGNPANTNA WIAMKSAPDL PKGNFTAMLR LDHNRAKSQL ATRTGKPVAS 190 200 210 220 230 240 VEKMIVWGNH SPTMYPDIRF CTVDGQPAVK LVNDEAWYRN EYIPKVGKRG AAIIEARGLS 250 260 270 280 290 300 SAASAANAAI DHMHDWALGT NGKWVTMGLP SDGSYGIPEG TMYGVPVTCT PGKYERVKGL 310 320 EIDAFSREKM DFTLKELTEE QAGVKEMVK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequence of Syntrophobacter fumaroxidans MPOB." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G., Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Boone D.R. , Brockman F., Culley D., Ferry J., Gunsalus R., McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J., Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P. Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 10017 / MPOB.
[2]	"Purification and characterization of malate dehydrogenase from the syntrophic propionate-oxidizing bacterium strain MPOB." van Kuijk B.L.M., Stams A.J.M. FEMS Microbiol. Lett. 144:141-144(1996) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-22, FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000478 Genomic DNA. Translation: ABK16160.1.
RefSeq	YP_844595.1. NC_008554.1.
3D structure databases
ProteinModelPortal	A0LFF8.
SMR	A0LFF8. Positions 3-327.
ModBase	Search...
Protein-protein interaction databases
STRING	335543.Sfum_0460.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABK16160; ABK16160; Sfum_0460.
GeneID	4460269.
KEGG	sfu:Sfum_0460.
PATRIC	23845877. VBISynFum78438_0536.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0039.
HOGENOM	HOG000220953.
KO	K00024.
OMA	NCLIASK.
ProtClustDB	PRK05442.
Enzyme and pathway databases
BioCyc	SFUM335543:GH6P-524-MONOMER.
Family and domain databases
Gene3D	3.40.50.720. 1 hit. 3.90.110.10. 1 hit.
HAMAP	MF_01517. Malate_dehydrog_2.
InterPro	IPR001557. L-lactate/malate_DH. IPR022383. Lactate/malate_DH_C. IPR001236. Lactate/malate_DH_N. IPR015955. Lactate_DH/Glyco_Ohase_4_C. IPR010945. Malate_DH_type2. IPR016040. NAD(P)-bd_dom. [Graphical view]
PANTHER	PTHR23382. PTHR23382. 1 hit.
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	TIGR01759. MalateDH-SF1. 1 hit.
PROSITE	PS00068. MDH. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MDH_SYNFM

Accession

Primary (citable) accession number: A0LFF8
Secondary accession number(s): P80648

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 26, 2007
Last sequence update:	December 12, 2006
Last modified:	May 1, 2013
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program