B0SF41 (MDH_LEPBA) 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:	LBF_1102

Organism

Leptospira biflexa serovar Patoc (strain Patoc 1 / Ames) [Complete proteome] [HAMAP]

Taxonomic identifier

355278 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Spirochaetes › Spirochaetia › Spirochaetales › Leptospiraceae › Leptospira › Leptospira biflexa › Leptospira biflexa serovar Patoc

Protein attributes

Sequence length	327 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.

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 – 327	327	Malate dehydrogenase HAMAP-Rule MF_01517		PRO_1000191623
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)
	B0SF41 [UniParc]. Last modified April 8, 2008. Version 1. Checksum: A0CE4ACD82D54BE4	FASTA	327	34,931
	10 20 30 40 50 60 MSKKVKVAVT GAAGQIGYAL LFRIASGQMF GPDTAVELQL LELEQAIPAA KGVIMELDDC 70 80 90 100 110 120 AFPLLEKVSV SSNIDEAFRD INWALLVGSV PRKAGMERGD LLKINGGIFT TQGKAIEKNA 130 140 150 160 170 180 ASDVRVLVVG NPCNTNALIA MNNAKGVPSD RWFAMTGLDE NRAKTQLAQK AGVLVKDVSN 190 200 210 220 230 240 VAIWGNHSAT QYPDFFNAKV NGKPATDVIS DHDWLKGDFI STVQKRGAAI IAARGASSAA 250 260 270 280 290 300 SAANAVVDTV HNIVTPTKPG DWFSAACHSN GEYGVDKGLI FGYPLKSDGK KVEIVTGLEI 310 320 NAFGKEKFDI THNELKEERN EVKDMLG

References

[1]

"Genome sequence of the saprophyte Leptospira biflexa provides insights into the evolution of Leptospira and the pathogenesis of leptospirosis." Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N., Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A., Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L., Rood J.I., Lajus A. , Davies J.K., Medigue C., Adler B. PLoS ONE 3:E1607-E1607(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Patoc 1 / Ames.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000777 Genomic DNA. Translation: ABZ93628.1.
RefSeq	YP_001962206.1. NC_010842.1.
3D structure databases
ProteinModelPortal	B0SF41.
SMR	B0SF41. Positions 3-325.
ModBase	Search...
Protein-protein interaction databases
STRING	355278.LBF_1102.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	ABZ93628; ABZ93628; LBF_1102.
GeneID	6388414.
KEGG	lbf:LBF_1102.
PATRIC	22341205. VBILepBif95142_1171.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0039.
HOGENOM	HOG000220953.
KO	K00024.
OMA	AINDHAA.
ProtClustDB	PRK05442.
Enzyme and pathway databases
BioCyc	LBIF355278:GHTJ-1425-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_LEPBA

Accession

Primary (citable) accession number: B0SF41

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	April 8, 2008
Last modified:	May 1, 2013
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program