Reviewed, UniProtKB/Swiss-Prot Q8RSQ2 (BAR_RHOER)

Names and origin

Protein names

Recommended name:
    Barbiturase
    EC=3.5.2.1

Gene names

Name:

bar

Organism

Rhodococcus erythropolis

Taxonomic identifier

1833 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus

Protein attributes

Sequence length	369 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Cleaves the barbituric acid ring to yield ureidomalonic acid. Ref.1 Ref.2
Catalytic activity	Barbiturate + H2O = 3-oxo-3-ureidopropanoate. Ref.1 Ref.2
Cofactor	Binds 1 zinc ion per subunit. Ref.1
Pathway	Pyrimidine metabolism; uracil degradation via oxidative pathway; malonate and urea from uracil: step 2/3. Ref.2
Subunit structure	Homotetramer. Ref.1
biophysicochemical properties	Kinetic parameters: KM=1.0 mM for barbituric acid Vmax=2.5 µmol/min/mg enzyme

Ontologies

Keywords
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Molecular function	barbiturase activity Inferred from electronic annotation. Source: EC zinc 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
	Initiator methionine	1	1	Removed Ref.1
	Chain	2 – 369	368	Barbiturase		PRO_0000064828
Sites
	Metal binding	322	1	Zinc Potential
	Metal binding	324	1	Zinc Potential

Sequences

	Sequence		Length	Mass (Da)
	Q8RSQ2-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: E8C6419B71EFF38E	FASTA	369	38,998
	10 20 30 40 50 60 MPEAIEVRKV PLHSVSDASE LAKLIDDGVL EADRVIAVIG KTEGNGGVND YTRIIADRAF 70 80 90 100 110 120 REVLSAKGNR SPEEVAEVPI VWSGGTDGVI SPHATIFATV PADKVTKTDE PRLTVGVAMS 130 140 150 160 170 180 EQLLPEDIGR TAMITKVAAA VKDAMADAGI TDPADVHYVQ TKTPLLTIHT IRDAKSRGKT 190 200 210 220 230 240 VWTEQTHESM DLSNGGTALG IAVALGEIDM PTDEDVMHSR ELFSSVASCS SGVELDRAQI 250 260 270 280 290 300 VVVGNARGVG GRYRIGHSVM KDPLDQDGIW AAIRDAGLEL PERPHSNDLD GQLVNVFLKC 310 320 330 340 350 360 EASQDGTVRG RRNAMLDDSD VHWHRQIKSC VGGVTAAVTG DPAVFVSVSA AHQGPEGGGP VAAIVDLGQ

References

[1]

"Barbiturase, a novel zinc-containing amidohydrolase involved in oxidative pyrimidine metabolism." Soong C.-L., Ogawa J., Sakuradani E., Shimizu S. J. Biol. Chem. 277:7051-7058(2002) [PubMed: 11748240] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-37; 68-101; 108-136; 163-175; 262-295 AND 301-328, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT. Strain: ATCC 11048 / DSM 43060 / JCM 3132 / NCIMB 8147 / NCTC 8036.

[2]

"Novel amidohydrolytic reactions in oxidative pyrimidine metabolism: analysis of the barbiturase reaction and discovery of a novel enzyme, ureidomalonase." Soong C.-L., Ogawa J., Shimizu S. Biochem. Biophys. Res. Commun. 286:222-226(2001) [PubMed: 11485332] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, PATHWAY. Strain: ATCC 11048 / DSM 43060 / JCM 3132 / NCIMB 8147 / NCTC 8036.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ320520 Genomic DNA. Translation: CAC86669.1.
3D structure databases
ModBase	Search...
Enzyme and pathway databases
BRENDA	3.5.2.1. 1430.
Family and domain databases
InterPro	IPR014086. Amidohydrolase_AtzD/TrzD. [Graphical view]
Pfam	PF09663. Amido_AtzD_TrzD. 1 hit. [Graphical view]
TIGRFAMs	TIGR02714. amido_AtzD_TrzD. 1 hit.
ProtoNet	Search...

Entry information

Entry name

BAR_RHOER

Accession

Primary (citable) accession number: Q8RSQ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	January 23, 2007
Last modified:	March 24, 2009
This is version 30 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)