Malate dehydrogenase - Herminiimonas arsenicoxydans

Preferred order of sections

Names and origin

Protein names

Recommended name:
Malate dehydrogenase
EC=1.1.1.37

Gene names

Name:	mdh
Ordered Locus Names:	HEAR1780

Organism

Herminiimonas arsenicoxydans [Complete proteome] [HAMAP]

Taxonomic identifier

204773 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Oxalobacteraceae › Herminiimonas

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-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 – 329

329

Malate dehydrogenase HAMAP-Rule MF_01517

PRO_1000068603

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)

Tools

A4G5Z9 [UniParc].

Last modified April 17, 2007. Version 1.
Checksum: C2337E4EA65B698D
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FASTA

329

35,365

        10         20         30         40         50         60 
MAKAPMRVAV TGAAGQIGYS LLFRIANGDL LGKDQPVILQ LLEIDNEKAQ NALKGVIMEI 

        70         80         90        100        110        120 
DDCAFPLLAG VSAHSDPMTA FKDVDIALLV GARPRGPGME RKDLLEANAQ IFTVQGKALD 

       130        140        150        160        170        180 
AVASRNVKVL VVGNPANTNA YIAMKSAPNL PAKNFTAMLR LDHNRALSQI AAKTGKPVTA 

       190        200        210        220        230        240 
IEKLTVWGNH SPTMYPDYRF ATIDGKSVKE AINDEVWNKD VFLPTVGKRG AAIIEARGVS 

       250        260        270        280        290        300 
SAASAANAAI DHVRDWVLGT NGKWVTMGIP SDGSYGIPKD TMFGFPVTTE NGEYKIVQGL 

       310        320 
EIDAFSQERI NLTLKELSEE REGVKHLLA

« Hide

References

[1]

"A tale of two oxidation states: bacterial colonization of arsenic-rich environments."
Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E., Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M., Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E., Lieutaud A.

Bertin P.N.
PLoS Genet. 3:518-530(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ULPAs1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU207211 Genomic DNA. Translation: CAL61936.1.
RefSeq	YP_001100061.1. NC_009138.1.
3D structure databases
ProteinModelPortal	A4G5Z9.
SMR	A4G5Z9. Positions 3-329.
ModBase	Search...
Protein-protein interaction databases
STRING	204773.HEAR1780.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAL61936; CAL61936; HEAR1780.
GeneID	4932101.
KEGG	har:HEAR1780.
PATRIC	22113618. VBIHerArs17568_1681.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0039.
HOGENOM	HOG000220953.
KO	K00024.
OMA	AINDHAA.
ProtClustDB	PRK05442.
Enzyme and pathway databases
BioCyc	HARS204773:GJCA-1716-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_HERAR

Accession

Primary (citable) accession number: A4G5Z9

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	April 17, 2007
Last modified:	May 1, 2013
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents