Q5HBC0 (MDH_EHRRW) 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:	Erum4090, ERWE_CDS_04240

Organism

Ehrlichia ruminantium (strain Welgevonden) [Complete proteome] [HAMAP]

Taxonomic identifier

254945 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Alphaproteobacteria › Rickettsiales › Anaplasmataceae › Ehrlichia › canis group › Ehrlichia ruminantium

Protein attributes

Sequence length	313 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the reversible oxidation of malate to oxaloacetate By similarity. HAMAP-Rule MF_00487
Catalytic activity	(S)-malate + NAD+ = oxaloacetate + NADH. HAMAP-Rule MF_00487
Sequence similarities	Belongs to the LDH/MDH superfamily. MDH type 3 family.
Sequence caution	The sequence CAH58132.1 differs from that shown. Reason: Erroneous initiation.

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
	Chain	1 – 313	313	Malate dehydrogenase HAMAP-Rule MF_00487		PRO_0000241949
Regions
	Nucleotide binding	11 – 16	6	NAD By similarity
	Nucleotide binding	120 – 122	3	NAD By similarity
Sites
	Active site	177	1	Proton acceptor By similarity
	Binding site	35	1	NAD By similarity
	Binding site	84	1	Substrate By similarity
	Binding site	90	1	Substrate By similarity
	Binding site	97	1	NAD By similarity
	Binding site	122	1	Substrate By similarity
	Binding site	153	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5HBC0 [UniParc]. Last modified June 27, 2006. Version 2. Checksum: AE339233CEC06E2F	FASTA	313	33,729
	10 20 30 40 50 60 MIQSKKIALI GSGNIGGMIA YLIRLKNLGD VVLLDINDGM AKGKALDIAE SSPIGKYNGE 70 80 90 100 110 120 IFGTNNYADI ENADAIIVTA GITRKPGMSR DDLISTNVNI IKEIATNIAK YAPNAFVIVV 130 140 150 160 170 180 TNPLDVMVLA MYRYSHLPSN MIVGMAGVLD SARFSYFIAK ELNVSVESVD SLVLGGHGDI 190 200 210 220 230 240 MLPLIRYSSV SGVSIADLIK LGMITHDKVT EIVERTRKGG EEIVSLLKTG SAYYAPAESA 250 260 270 280 290 300 VLMLDSYLND KKLMLPCSAY LKGEYGVHDL FVGVPIIIGK NGVEKIVELQ LTEEENSIFN 310 NSVALIQNLV ANI

References

[1]

"The genome of the heartwater agent Ehrlichia ruminantium contains multiple tandem repeats of actively variable copy number." Collins N.E., Liebenberg J., de Villiers E.P., Brayton K.A., Louw E., Pretorius A., Faber F.E., van Heerden H., Josemans A., van Kleef M., Steyn H.C., van Strijp M.F., Zweygarth E., Jongejan F., Maillard J.C., Berthier D., Botha M., Joubert F. , Corton C.H., Thomson N.R., Allsopp M.T., Allsopp B.A. Proc. Natl. Acad. Sci. U.S.A. 102:838-843(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Welgevonden.

[2]

"Comparative genomic analysis of three strains of Ehrlichia ruminantium reveals an active process of genome size plasticity." Frutos R., Viari A., Ferraz C., Morgat A., Eychenie S., Kandassamy Y., Chantal I., Bensaid A., Coissac E., Vachiery N., Demaille J., Martinez D. J. Bacteriol. 188:2533-2542(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Welgevonden.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CR767821 Genomic DNA. Translation: CAH58132.1. Different initiation. CR925678 Genomic DNA. Translation: CAI26918.1.
RefSeq	YP_180274.1. NC_005295.2. YP_197300.1. NC_006832.1.
3D structure databases
ProteinModelPortal	Q5HBC0.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAH58132; CAH58132; Erum4090. CAI26918; CAI26918; ERWE_CDS_04240.
GeneID	3233406. 3260940.
KEGG	eru:Erum4090. erw:ERWE_CDS_04240.
PATRIC	20580669. VBIEhrRum92411_0450.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0039.
HOGENOM	HOG000213794.
KO	K00024.
OMA	NYKDIEG.
ProtClustDB	PRK06223.
Enzyme and pathway databases
BioCyc	ERUM254945:GJ2L-448-MONOMER.
Family and domain databases
Gene3D	3.40.50.720. 1 hit. 3.90.110.10. 1 hit.
HAMAP	MF_00487. Malate_dehydrog_3.
InterPro	IPR001557. L-lactate/malate_DH. IPR022383. Lactate/malate_DH_C. IPR001236. Lactate/malate_DH_N. IPR015955. Lactate_DH/Glyco_Ohase_4_C. IPR011275. Malate_DH_type3. IPR016040. NAD(P)-bd_dom. [Graphical view]
PANTHER	PTHR11540. PTHR11540. 1 hit.
Pfam	PF02866. Ldh_1_C. 1 hit. PF00056. Ldh_1_N. 1 hit. [Graphical view]
PIRSF	PIRSF000102. Lac_mal_DH. 1 hit.
PRINTS	PR00086. LLDHDRGNASE.
SUPFAM	SSF56327. Lactate_DH/Glyco_hydro_4_C. 1 hit.
TIGRFAMs	TIGR01763. MalateDH_bact. 1 hit.
ProtoNet	Search...

Entry information

Entry name

MDH_EHRRW

Accession

Primary (citable) accession number: Q5HBC0
Secondary accession number(s): Q5FEX9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 27, 2006
Last sequence update:	June 27, 2006
Last modified:	May 1, 2013
This is version 58 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program