P80536 (MDH_BURPS) 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:	BPSS1722

Organism

Burkholderia pseudomallei (strain K96243) [Reference proteome] [HAMAP]

Taxonomic identifier

272560 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group › Burkholderia pseudomallei

Protein attributes

Sequence length	327 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 By similarity. HAMAP-Rule MF_01517
Catalytic activity	(S)-malate + NAD+ = oxaloacetate + NADH. HAMAP-Rule MF_01517
Subunit structure	Homodimer By similarity. HAMAP-Rule MF_01517
Sequence similarities	Belongs to the LDH/MDH superfamily. MDH type 2 family.

Ontologies

Keywords
Biological process	Tricarboxylic acid cycle
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Direct protein sequencing Reference 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: HAMAP
Molecular_function	L-malate dehydrogenase activity Inferred from electronic annotation. Source: HAMAP
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 – 327	326	Malate dehydrogenase HAMAP-Rule MF_01517		PRO_0000113354
Regions
	Nucleotide binding	12 – 18	7	NAD By similarity
	Nucleotide binding	130 – 132	3	NAD By similarity
Sites
	Active site	188	1	Proton acceptor By similarity
	Binding site	93	1	Substrate By similarity
	Binding site	99	1	Substrate By similarity
	Binding site	106	1	NAD By similarity
	Binding site	113	1	NAD By similarity
	Binding site	132	1	Substrate By similarity
	Binding site	163	1	Substrate By similarity
Experimental info
	Sequence conflict	24	1	R → K AA sequence Ref.2
	Sequence conflict	29	1	D → K AA sequence Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P80536 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 2E919ABA6D3F67B3	FASTA	327	35,015
	10 20 30 40 50 60 MAKPAKRVAV TGAAGQIAYS LLFRIANGDL LGKDQPVILQ LLDLPQAQAA VKGVVMELDD 70 80 90 100 110 120 CAFPLLAGVV ITDDPKVAFK DADVALLVGA RPRSKGMERK DLLSANAEIF TVQGAALNEV 130 140 150 160 170 180 ASRDVKVLVV GNPANTNAYI AMKSAPDLPK KNFTAMLRLD HNRALSQLAA KSGKPVASIE 190 200 210 220 230 240 KLAVWGNHSP TMYPDFRFAT AEGESLLKLI NDDVWNRDTF IPTVGKRGAA IIEARGLSSA 250 260 270 280 290 300 ASAANAAIDH VRDWVLGTNG KWVTMGIPSD GSYGIPEDII YGVPVICENG EYKRVEGLEI 310 320 DAFSREKMDG TLAELLEERD GVAHLLK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Genomic plasticity of the causative agent of melioidosis, Burkholderia pseudomallei." Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F., Challis G.L. , Cherevach I., Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J. Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K96243.
[2]	"Structural studies of malate dehydrogenases (MDHs): MDHs in Brevundimonas species are the first reported MDHs in Proteobacteria which resemble lactate dehydrogenases in primary structure." Charnock C. J. Bacteriol. 179:4066-4070(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-30. Strain: ATCC 23343.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX571966 Genomic DNA. Translation: CAH39196.1.
RefSeq	YP_111728.1. NC_006351.1.
3D structure databases
ProteinModelPortal	P80536.
SMR	P80536. Positions 3-325.
ModBase	Search...
Protein-protein interaction databases
STRING	272560.BPSS1722.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3095126.
KEGG	bps:BPSS1722.
PATRIC	19271718. VBIBurPse99623_6030.
Phylogenomic databases
eggNOG	COG0039.
HOGENOM	HOG000220953.
KO	K00024.
OMA	NCLIASK.
ProtClustDB	PRK05442.
Enzyme and pathway databases
BioCyc	BPSE272560:GJNI-5293-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_BURPS

Accession

Primary (citable) accession number: P80536
Secondary accession number(s): Q63JJ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	January 23, 2007
Last modified:	May 29, 2013
This is version 89 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program