A9IIS3 (MDH_BORPD) 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:	Bpet1818

Organism

Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448) [Complete proteome] [HAMAP]

Taxonomic identifier

340100 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	329 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_01517
Catalytic activity	(S)-malate + NAD+ = oxaloacetate + NADH. HAMAP MF_01517
Subunit structure	Homodimer By similarity. HAMAP 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
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 – 329	329	Malate dehydrogenase HAMAP MF_01517		PRO_1000191609
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)
	A9IIS3 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: 505EAFF3AF09D1CF	FASTA	329	35,440
	10 20 30 40 50 60 MSKPAMRVAV TGAAGQIGYA LLFRIASGEM LGKDQPVILQ LLEIPDEKAQ KALKGVIMEL 70 80 90 100 110 120 DDCAFPLLQE VTAHSDPRTA FKDADVALLV GARPRGPGME RKDLLSVNAQ IFTAQGKALN 130 140 150 160 170 180 DVASRNVKVL VVGNPANTNA YIAMKSAPDL PAKNFTAMLR LDHNRALSQL AAKSGKAVAD 190 200 210 220 230 240 IEKLVVWGNH SPTMYPDYRF ATVGGQSLAK LINDDAWNRD TFIPTVGKRG AAIIEARGLS 250 260 270 280 290 300 SAASAANAAI DHVRDWVLGS NGKWVTMGIP SDGSYGIPEG IIYGVPVTTE NGEYKRVEGL 310 320 EIDAFSRERL DFTLKELLEE RDGVKDLLK

References

[1]

"The missing link: Bordetella petrii is endowed with both the metabolic versatility of environmental bacteria and virulence traits of pathogenic Bordetellae." Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H., Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V., Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S., Linke B., Meyer F. , Mormann S., Nakunst D., Rueckert C., Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T., Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O., Martinez-Arias R. BMC Genomics 9:449-449(2008) [PubMed: 18826580] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-461 / DSM 12804 / CCUG 43448.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AM902716 Genomic DNA. Translation: CAP42157.1.
RefSeq	YP_001630426.1. NC_010170.1.
3D structure databases
ProteinModelPortal	A9IIS3.
SMR	A9IIS3. Positions 3-328.
ModBase	Search...
Protein-protein interaction databases
STRING	A9IIS3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	5820459.
GenomeReviews	Gene locus Bpet1818 in contig AM902716_GR.
KEGG	bpt:Bpet1818.
PATRIC	21165089. VBIBorPet31633_1809.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG289884.
OMA	DPNVAFK.
ProtClustDB	PRK05442.
Enzyme and pathway databases
BioCyc	BPET94624:BPET1818-MONOMER.
Family and domain databases
HAMAP	MF_01517. Malate_dehydrog_2. [Tree]
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]
Gene3D	G3DSA:3.90.110.10. lact_mal_DH. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KO	K00024.
PANTHER	PTHR23382. MDH_SF1. 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_BORPD

Accession

Primary (citable) accession number: A9IIS3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	February 5, 2008
Last modified:	January 25, 2012
This is version 40 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program