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Reviewed, UniProtKB/Swiss-Prot Q5RBM6 (BUP1_PONAB)

Last modified June 16, 2009. Version 28. 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
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length384 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript 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 By similarity.

Catalytic activity

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

Cofactor

Binds 1 zinc ion per subunit By similarity.

Enzyme regulation

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

Pathway

Amino-acid biosynthesis; beta-alanine biosynthesis.

Subcellular location

Cytoplasm By similarity.

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
Gene Ontology (GO)
   Biological processnitrogen compound metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionbeta-ureidopropionase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 384384Beta-ureidopropionase
PRO_0000204053

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
Q5RBM6-1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 8F7B1BC8E25077BA

FASTA38443,098
        10         20         30         40         50         60 
MAGAEWKSLE ECLEKHLPLP DLQEVKRVLY GKELRKLDLP REAFEAASRE DFELQGYAFE 

        70         80         90        100        110        120 
AAEEQLRRPR IVHVGLVQNR IPLPANAPVA EQVSALHRRI KAIVEVAAMC GVNIICFQEA 

       130        140        150        160        170        180 
WTMPFAFCTR EKLPWTEFAE SAEDGPTTRF CQKLAKNHDM VVVSPILERD SEHGDVLWNT 

       190        200        210        220        230        240 
AVVISNSGAV LGKTRKNHIP RVGDFNESTY YMEGNLGHPV FQTQFGRIAV NICYGRHHPL 

       250        260        270        280        290        300 
NWLMYSINGA EIIFNPSATI GALSESLWSI EARNAAIANH CFTCAINRVG TEHFPNEFTS 

       310        320        330        340        350        360 
GDGKKAHQDF GYFYGSSYVA APDGSRTPGL SRSQDGLLVA KLDLNLCQQV NDVWNFKMTG 

       370        380 
RYEMYARELA EAVKSNYSPT IVKE 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

CR858612 mRNA. Translation: CAH90834.1.
RefSeqNP_001125476.1.
UniGenePab.13051

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID100172385.

Phylogenomic databases

HOVERGENQ5RBM6.

Enzyme and pathway databases

BRENDA3.5.1.6. 269192.

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...

Entry information

Entry nameBUP1_PONAB
AccessionPrimary (citable) accession number: Q5RBM6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2005
Last sequence update: December 21, 2004
Last modified: June 16, 2009
This is version 28 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