P61975 (MDH_LEPIC) 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:	LIC_11781

Organism

Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130) [Complete proteome] [HAMAP]

Taxonomic identifier

267671 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Spirochaetes › Spirochaetia › Spirochaetales › Leptospiraceae › Leptospira › Leptospira interrogans › Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni

Protein attributes

Sequence length	326 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_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.
Sequence caution	The sequence AAS70370.1 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 – 326	326	Malate dehydrogenase HAMAP-Rule MF_01517		PRO_0000113374
Regions
	Nucleotide binding	11 – 17	7	NAD By similarity
	Nucleotide binding	129 – 131	3	NAD By similarity
Sites
	Active site	187	1	Proton acceptor By similarity
	Binding site	92	1	Substrate By similarity
	Binding site	98	1	Substrate By similarity
	Binding site	105	1	NAD By similarity
	Binding site	112	1	NAD By similarity
	Binding site	131	1	Substrate By similarity
	Binding site	162	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	P61975 [UniParc]. Last modified June 7, 2004. Version 1. Checksum: 40F511F4AE1014FB	FASTA	326	34,918
	10 20 30 40 50 60 MSKTVKVAVT GAAGQIGYSL LFRIASGQMF GADTAVEIQM LELEAAIPAA KGVIMELEDC 70 80 90 100 110 120 AFPLLQKVTV SSDLDTAFKE INWALLVGSV PRKAGMERGD LLKINGGIFV NQGKAIEKNA 130 140 150 160 170 180 ASDVRILVVG NPCNTNCLIA MNNAKGISQD RWFAMTKLDE NRAKSQLASK AGVPVKEVTH 190 200 210 220 230 240 LGIWGNHSAT QYPDFYNTKI SGKPVTDVIS DHEWLKGDFI KNVQQRGAEI IKARGASSAA 250 260 270 280 290 300 SAANGVVDTV RGIITPTAPG DCFSAAVVSD GSYGAEKGLI FGFPLKSDGK KVEIIQGISL 310 320 NDFAKEKFKI THEELVSERN EVKEML

References

[1]

"Comparative genomics of two Leptospira interrogans serovars reveals novel insights into physiology and pathogenesis." Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B., Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V., Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L., Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S. , Ferro M.I.T., Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H., Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M., Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L., Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A., Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A., Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A. J. Bacteriol. 186:2164-2172(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Fiocruz L1-130.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016823 Genomic DNA. Translation: AAS70370.1. Different initiation.
RefSeq	YP_001733.2. NC_005823.1.
3D structure databases
ProteinModelPortal	P61975.
ModBase	Search...
Protein-protein interaction databases
STRING	267671.LIC11781.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAS70370; AAS70370; LIC_11781.
GeneID	2772594.
KEGG	lic:LIC11781.
Organism-specific databases
CMR	Search...
Phylogenomic databases
KO	K00024.
OMA	AINDHAA.
ProtClustDB	PRK05442.
Enzyme and pathway databases
BioCyc	LINT267671:GHQI-2046-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. IPR001252. Malate_DH_AS. 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. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

MDH_LEPIC

Accession

Primary (citable) accession number: P61975

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2004
Last sequence update:	June 7, 2004
Last modified:	May 1, 2013
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program