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Reviewed, UniProtKB/Swiss-Prot Q03248 (BUP1_RAT)

Last modified June 16, 2009. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Beta-ureidopropionase
    EC=3.5.1.6
Alternative name(s):
    Beta-alanine synthase
    N-carbamoyl-beta-alanine amidohydrolase
Gene names
Name: Upb1
Synonyms: Bup1
OrganismRattus norvegicus (Rat)
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length393 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Converts N-carbamyl-beta-aminoisobutyric acid and N-carbamyl-beta-alanine to, respectively, beta-aminoisobutyric acid and beta-alanine, ammonia and carbon dioxide.

Catalytic activity

N-carbamoyl-beta-alanine + H2O = beta-alanine + CO2 + NH3.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Enzyme regulation

Allosteric enzyme with positive cooperativity toward the substrate N-carbamoyl-beta-alanine.

Pathway

Amino-acid biosynthesis; beta-alanine biosynthesis.

Subunit structure

In the absence of ligands, the enzyme exists as a stable homohexamer, although this is not the most active form of the enzyme. This native hexamer dissociates to an inactive trimer in response to the product, beta-alanine, or associates to the more active homododecamer in response to the substrate.

Subcellular location

Cytoplasm.

Post-translational modification

The N-terminus is blocked.

Sequence similarities

Belongs to the CN hydrolase family. BUP subfamily.

Contains 1 CN hydrolase domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termAllosteric enzyme
Direct protein sequencing
Gene Ontology (GO)
   Biological processbeta-alanine biosynthetic process Ref.1

Traceable author statement. Source: RGD

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

soluble fraction

Inferred from direct assay. Source: RGD

   Molecular functionbeta-ureidopropionase activity Ref.1

Inferred from direct assay. Source: RGD

zinc ion binding Ref.1

Inferred from direct assay. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 393393Beta-ureidopropionase
PRO_0000204054

Regions

Domain72 – 366295CN hydrolase

Sites

Metal binding971Zinc Potential
Metal binding1581Zinc Potential
Metal binding2801Zinc Potential
Metal binding2931Zinc Potential
Metal binding3071Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
Q03248-1 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 723E5AF5B01E3AAD

FASTA39344,042
        10         20         30         40         50         60 
MAGPEWQSLE QCLEKHLPPD DLSQVKRILY GKQTRNLDLP RKALEAASER NFELKGYAFG 

        70         80         90        100        110        120 
AAKEQQRCPQ IVRVGLVQNR IPLPTSAPVA EQVSALHKRI EEIAEVAAMC GVNIICFQEA 

       130        140        150        160        170        180 
WNMPFAFCTR EKLPWTEFAE SAEDGLTTRF CQKLAKKHNM VVISPILERD RDHGGVLWNT 

       190        200        210        220        230        240 
AVVISNSGLV MGKTRKNHIP RVGDFNESTY YMEGNLGHPV FQTQFGRIAV NICYGRHHPL 

       250        260        270        280        290        300 
NWLMYSVNGA EIIFNPSATI GELSESMWPI EARNAAIANH CFTCALNRVG QEHYPNEFTS 

       310        320        330        340        350        360 
GDGKKAHHDL GYFYGSSYVA APDGSRTPGL SRNQDGLLVT ELNLNLCQQI NDFWTFKMTG 

       370        380        390 
RLEMYARELA EAVKPNYSPN IVKEDLVLAP SSG 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, sequencing, and expression of a cDNA encoding beta-alanine synthase from rat liver."
Kvalnes-Krick K.L., Traut T.W.
J. Biol. Chem. 268:5686-5693(1993) [PubMed: 8449931] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 202-212, CHARACTERIZATION.
Tissue: Liver.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

M97662 mRNA. Translation: AAA40804.1.
BC078767 mRNA. Translation: AAH78767.1.
IPIIPI00208970.
PIRS27881. A46624.
RefSeqNP_446297.1.
UniGeneRn.11110

3D structure databases

ModBaseSearch...

Proteomic databases

PRIDEQ03248.

Genome annotation databases

GeneID116593.
KEGGrno:116593.

Organism-specific databases

RGD620091. Upb1.

Phylogenomic databases

HOVERGENQ03248.

Enzyme and pathway databases

BRENDA3.5.1.6. 248.

Family and domain databases

InterProIPR003010. Ntlse/CNhydtse.
[Graphical view]
Gene3DG3DSA:3.60.110.10. Ntlse/CNhydtse. 1 hit.
PfamPF00795. CN_hydrolase. 1 hit.
[Graphical view]
PROSITEPS50263. CN_HYDROLASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio619283.

Entry information

Entry nameBUP1_RAT
AccessionPrimary (citable) accession number: Q03248
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 16, 2009
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents