Q7WD94 (MDH_BORBR) 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:	BB3684

Organism

Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50) (Alcaligenes bronchisepticus) [Complete proteome] [HAMAP]

Taxonomic identifier

257310 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella › Bordetella bronchiseptica

Protein attributes

Sequence length	329 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 – 329	328	Malate dehydrogenase HAMAP-Rule MF_01517		PRO_0000113349
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)
	Q7WD94 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 29F3BECAD6F6C3F4	FASTA	329	35,664
	10 20 30 40 50 60 MSKPALRVAV TGAAGQIGYA LLFRIASGEM LGKDQPVILQ LLEIPDEKAQ KALKGVIMEL 70 80 90 100 110 120 EDCAFPLLHE VTAHSDPRTA FKDADVALLV GARPRGPGME RKDLLSVNAQ IFTAQGRALN 130 140 150 160 170 180 DVASRNVKVL VVGNPANTNA YIAMKSAPDL PAKNFTAMLR LDHNRALSQL SAKSGKRVAD 190 200 210 220 230 240 IEKLIVWGNH SPTMYPDFRF ATVGGQGLTQ LINDDAWNRD TFIPTVGKRG AAIIEARGLS 250 260 270 280 290 300 SAASAANAAI DHVRDWVLGS NGKWVTMGIP SDGSYGIPEG IIYGFPVVTE NGEYKMIKDL 310 320 EIDAFSRERL DFTLKELLEE RDGVKDLLK

References

[1]

"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-588 / NCTC 13252 / RB50.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX640448 Genomic DNA. Translation: CAE35657.1.
RefSeq	NP_890219.1. NC_002927.3.
3D structure databases
ProteinModelPortal	Q7WD94.
SMR	Q7WD94. Positions 3-328.
ModBase	Search...
Protein-protein interaction databases
STRING	257310.BB3684.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAE35657; CAE35657; BB3684.
GeneID	2659043.
KEGG	bbr:BB3684.
PATRIC	21140745. VBIBorBro124907_3733.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0039.
HOGENOM	HOG000220953.
KO	K00024.
OMA	AINDHAA.
ProtClustDB	PRK05442.
Enzyme and pathway databases
BioCyc	BBRO257310:BB3684-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_BORBR

Accession

Primary (citable) accession number: Q7WD94

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2004
Last sequence update:	October 1, 2003
Last modified:	May 1, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program