Q0QLE1 (DMDB_EUBBA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
2,3-dimethylmalate dehydratase small subunit
EC=4.2.1.85

Gene names

Name:

DmdB

Organism

Eubacterium barkeri (Clostridium barkeri)

Taxonomic identifier

1528 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Clostridia › Clostridiales › Eubacteriaceae › Eubacterium

Protein attributes

Sequence length	163 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	(2R,3S)-2,3-dimethylmalate = dimethylmaleate + H2O. Ref.2
Pathway	Cofactor degradation; nicotinate degradation; propanoate and pyruvate from 6-hydroxynicotinate: step 7/8. Ref.1
Subunit structure	Heterodimer of a large and a small subunit By similarity.
Induction	By nicotinic acid. Ref.2
Sequence similarities	Belongs to the LeuD family. LeuD type 2 subfamily.
Biophysicochemical properties	Kinetic parameters: KM=3.1 mM for dimethylmaleate Ref.2 pH dependence: Highly active between pH 6.5 and 9.0. Retains 50% and 10% of maximum activity at pH 5.0 and 4.5 respectively.

Ontologies

Keywords
Molecular function	Lyase
Gene Ontology (GO)
Biological_process	cofactor catabolic process Inferred from direct assay Ref.2. Source: UniProtKB leucine biosynthetic process Inferred from electronic annotation. Source: HAMAP
Cellular_component	3-isopropylmalate dehydratase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	3-isopropylmalate dehydratase activity Inferred from electronic annotation. Source: HAMAP dimethylmaleate hydratase activity Inferred from direct assay Ref.2. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 163	163	2,3-dimethylmalate dehydratase small subunit HAMAP-Rule MF_01032		PRO_0000403995

Sequences

	Sequence		Length	Mass (Da)
	Q0QLE1 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 6A2E9CBA57AEF3EE	FASTA	163	17,369
	10 20 30 40 50 60 MKAKGSVFRY GDNVDTDVII PARFLNTSDP LELAAHCMED IDADFSSKVN AGDIIVADDN 70 80 90 100 110 120 FGCGSSREHA PISIKASGVS CVIANSFARI FYRNAINIGL PILECPEAVA VIEAGDEVEV 130 140 150 160 DFDSGVITDV TKGQSFQGQA FPEFMQTLIA AGGLVNYINA TEK

References

[1]	"Molecular and functional analysis of nicotinate catabolism in Eubacterium barkeri." Alhapel A., Darley D.J., Wagener N., Eckel E., Elsner N., Pierik A.J. Proc. Natl. Acad. Sci. U.S.A. 103:12341-12346(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PATHWAY. Strain: ATCC 25849 / DSM 1223 / JCM 1389 / NCIB 10623.
[2]	"Nicotinic acid metabolism. Dimethylmaleate hydratase." Kollmann-Koch A., Eggerer H. Hoppe-Seyler's Z. Physiol. Chem. 365:847-857(1984) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION. Strain: ATCC 25849 / DSM 1223 / JCM 1389 / NCIB 10623.

Cross-references

Sequence databases
EMBL GenBank DDBJ	DQ310789 Genomic DNA. Translation: ABC88409.1.
3D structure databases
ProteinModelPortal	Q0QLE1.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-13677.
UniPathway	UPA01010; UER01018.
Family and domain databases
Gene3D	3.20.19.10. 1 hit.
HAMAP	MF_01032. LeuD_type2.
InterPro	IPR015937. Acoase/IPM_deHydtase. IPR015928. Aconitase/3IPM_dehydase_swvl. IPR000573. AconitaseA/IPMdHydase_ssu_swvl. IPR011827. IsopropMal_deHydtase_ssu. IPR011824. IsopropMal_deHydtase_ssu_bac. [Graphical view]
PANTHER	PTHR11670. PTHR11670. 1 hit.
Pfam	PF00694. Aconitase_C. 1 hit. [Graphical view]
SUPFAM	SSF52016. Aconitase/3IPM_dehydase_swvl. 1 hit.
TIGRFAMs	TIGR02084. leud. 1 hit. TIGR02087. LEUD_arch. 1 hit.
ProtoNet	Search...

Entry information

Entry name

DMDB_EUBBA

Accession

Primary (citable) accession number: Q0QLE1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 8, 2011
Last sequence update:	September 5, 2006
Last modified:	April 3, 2013
This is version 37 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program