Q0QLE2 (DMDA_EUBBA) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Gene names

Name:

dmdA

Organism

Eubacterium barkeri (Clostridium barkeri)

Taxonomic identifier

1528 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	420 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	(2R,3S)-2,3-dimethylmalate = dimethylmaleate + H2O. Ref.2
Cofactor	Binds 1 4Fe-4S cluster per subunit By similarity. UniProtKB A6LPX4
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. UniProtKB A6LPX4
Induction	By nicotinic acid. Ref.2
Sequence similarities	Belongs to the aconitase/IPM isomerase family. LeuC 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. Ref.2

Ontologies

Keywords
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
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
Molecular_function	3-isopropylmalate dehydratase activity Inferred from electronic annotation. Source: HAMAP 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW dimethylmaleate hydratase activity Inferred from direct assay Ref.2. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 420	420	2,3-dimethylmalate dehydratase large subunit		PRO_0000403994
Sites
	Metal binding	301	1	Iron-sulfur (4Fe-4S) By similarity UniProtKB A6LPX4
	Metal binding	361	1	Iron-sulfur (4Fe-4S) By similarity UniProtKB A6LPX4
	Metal binding	364	1	Iron-sulfur (4Fe-4S) By similarity UniProtKB A6LPX4

Sequences

	Sequence		Length	Mass (Da)
	Q0QLE2 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: 7A709C21B776B48C	FASTA	420	44,821
	10 20 30 40 50 60 MGMTMTQKIL AAHASLDSVK AGDLIMADLD MVLANDITGP VAINVFGTID KEKVFDKDKI 70 80 90 100 110 120 ALVPDHFAPA KDIKSAQQCK QVRCFACDQE ITNYFEIGEM GIEHALLPEK GLVAAGDVVI 130 140 150 160 170 180 GADSHTCTYG ALGAFSTGVG STDMAVGMAT GKAWFKVPAA LRFNLTGTLN KNVSGKDLIL 190 200 210 220 230 240 HIIGMIGVDG ALYRSMEFTG PGVACLSMDD RFTISNMAIE AGGKNGIFPV DDQTISYMEE 250 260 270 280 290 300 HGSGDYKVYA ADADAVYEKT FDIDLSQLKS TVAFPHLPEN TKTVDAIEEP VTIDQVVIGS 310 320 330 340 350 360 CTNGRFEDLK RAADILRGKH VKKGVRMLVI PATHKIYLDA MEAGYLREFI EAGATISTPT 370 380 390 400 410 420 CGPCLGGYMG ILAEGERCVS TTNRNFVGRM GHVDSEVYLA SPEVAAASAI LGRIATPDEL

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: ABC88408.1.
3D structure databases
ProteinModelPortal	Q0QLE2.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-13676.
UniPathway	UPA01010; UER01018.
Family and domain databases
Gene3D	3.30.499.10. 2 hits. 3.40.1060.10. 1 hit.
HAMAP	MF_01027. LeuC_type2.
InterPro	IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3. IPR015937. Acoase/IPM_deHydtase. IPR001030. Acoase/IPM_deHydtase_lsu_aba. IPR015932. Aconitase/IPMdHydase_lsu_aba_2. IPR018136. Aconitase_4Fe-4S_BS. IPR011826. HAcnase/IPMdehydase_lsu_prok. IPR006251. Homoacnase/IPMdehydase_lsu. IPR011823. IsopropMal_deHydtase_lsu_bac. [Graphical view]
PANTHER	PTHR11670. PTHR11670. 1 hit. PTHR11670:SF6. PTHR11670:SF6. 1 hit.
Pfam	PF00330. Aconitase. 2 hits. [Graphical view]
PRINTS	PR00415. ACONITASE.
SUPFAM	SSF53732. Aconitase_N. 1 hit.
TIGRFAMs	TIGR01343. hacA_fam. 1 hit. TIGR02086. IPMI_arch. 1 hit. TIGR02083. LEU2. 1 hit.
PROSITE	PS00450. ACONITASE_1. 1 hit. PS01244. ACONITASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

DMDA_EUBBA

Accession

Primary (citable) accession number: Q0QLE2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 8, 2011
Last sequence update:	September 5, 2006
Last modified:	April 3, 2013
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program