Q0BAF9 (MDH_BURCM) 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:	Bamb_3309

Organism

Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia (strain AMMD)) [Complete proteome] [HAMAP]

Taxonomic identifier

339670 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia cepacia complex › Burkholderia ambifaria

Protein attributes

Sequence length	328 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology

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.
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
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 By similarity
	Chain	2 – 328	327	Malate dehydrogenase HAMAP-Rule MF_01517		PRO_0000294378
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

Sequences

	Sequence		Length	Mass (Da)
	Q0BAF9 [UniParc]. Last modified October 17, 2006. Version 1. Checksum: 93DE88B218FE3F67	FASTA	328	35,115
	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 YGVPVVCENG EYKRVEGLEI 310 320 DAFSREKMDG TLAELLEERD GVAHLLKN

References

[1]

"Complete sequence of chromosome 2 of Burkholderia cepacia AMMD." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L. , Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K., Ramette A., Tiedje J., Richardson P. Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-244 / AMMD.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000441 Genomic DNA. Translation: ABI88864.1.
RefSeq	YP_775198.1. NC_008391.1.
3D structure databases
ProteinModelPortal	Q0BAF9.
SMR	Q0BAF9. Positions 3-325.
ModBase	Search...
Protein-protein interaction databases
STRING	339670.Bamb_3309.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABI88864; ABI88864; Bamb_3309.
GeneID	4312311.
KEGG	bam:Bamb_3309.
PATRIC	19022411. VBIBurAmb61564_3463.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0039.
HOGENOM	HOG000220953.
KO	K00024.
OMA	NCLIASK.
ProtClustDB	PRK05442.
Enzyme and pathway databases
BioCyc	BAMB339670:GH48-1121-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_BURCM

Accession

Primary (citable) accession number: Q0BAF9

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 10, 2007
Last sequence update:	October 17, 2006
Last modified:	May 1, 2013
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program