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Protein

Beta-ureidopropionase

Gene

Upb1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Converts N-carbamoyl-beta-aminoisobutyrate and N-carbamoyl-beta-alanine (3-ureidopropanoate) to, respectively, beta-aminoisobutyrate and beta-alanine, ammonia and carbon dioxide.1 Publication

Catalytic activityi

3-ureidopropanoate + H2O = beta-alanine + CO2 + NH3.1 Publication

Cofactori

Zn2+1 PublicationNote: Binds 2 Zn2+ ions per subunit.1 Publication

Enzyme regulationi

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

Pathwayi: beta-alanine biosynthesis

This protein is involved in the pathway beta-alanine biosynthesis, which is part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the pathway beta-alanine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi97 – 971ZincSequence analysis
Active sitei119 – 1191Proton acceptorPROSITE-ProRule annotation
Metal bindingi158 – 1581ZincSequence analysis
Active sitei196 – 1961Proton donorPROSITE-ProRule annotation
Active sitei233 – 2331NucleophilePROSITE-ProRule annotation
Metal bindingi280 – 2801ZincSequence analysis
Metal bindingi293 – 2931ZincSequence analysis
Metal bindingi307 – 3071ZincSequence analysis

GO - Molecular functioni

  • beta-ureidopropionase activity Source: RGD
  • zinc ion binding Source: RGD

GO - Biological processi

  • beta-alanine biosynthetic process Source: RGD
  • beta-alanine metabolic process Source: RGD
  • in utero embryonic development Source: RGD
  • liver development Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15401.
SABIO-RKQ03248.
UniPathwayiUPA00131.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-ureidopropionase (EC:3.5.1.61 Publication)
Alternative name(s):
Beta-alanine synthase
N-carbamoyl-beta-alanine amidohydrolase
Gene namesi
Name:Upb1
Synonyms:Bup1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620091. Upb1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 393393Beta-ureidopropionasePRO_0000204054Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei378 – 3781PhosphoserineCombined sources

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ03248.

PTM databases

iPTMnetiQ03248.
PhosphoSiteiQ03248.

Interactioni

Subunit structurei

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.

Structurei

3D structure databases

ProteinModelPortaliQ03248.
SMRiQ03248. Positions 5-384.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini72 – 366295CN hydrolasePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 CN hydrolase domain.PROSITE-ProRule annotation

Phylogenomic databases

HOVERGENiHBG018848.
InParanoidiQ03248.
KOiK01431.
PhylomeDBiQ03248.

Family and domain databases

Gene3Di3.60.110.10. 1 hit.
InterProiIPR003010. C-N_Hydrolase.
[Graphical view]
PfamiPF00795. CN_hydrolase. 1 hit.
[Graphical view]
SUPFAMiSSF56317. SSF56317. 1 hit.
PROSITEiPS50263. CN_HYDROLASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q03248-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGPEWQSLE QCLEKHLPPD DLSQVKRILY GKQTRNLDLP RKALEAASER
60 70 80 90 100
NFELKGYAFG AAKEQQRCPQ IVRVGLVQNR IPLPTSAPVA EQVSALHKRI
110 120 130 140 150
EEIAEVAAMC GVNIICFQEA WNMPFAFCTR EKLPWTEFAE SAEDGLTTRF
160 170 180 190 200
CQKLAKKHNM VVISPILERD RDHGGVLWNT AVVISNSGLV MGKTRKNHIP
210 220 230 240 250
RVGDFNESTY YMEGNLGHPV FQTQFGRIAV NICYGRHHPL NWLMYSVNGA
260 270 280 290 300
EIIFNPSATI GELSESMWPI EARNAAIANH CFTCALNRVG QEHYPNEFTS
310 320 330 340 350
GDGKKAHHDL GYFYGSSYVA APDGSRTPGL SRNQDGLLVT ELNLNLCQQI
360 370 380 390
NDFWTFKMTG RLEMYARELA EAVKPNYSPN IVKEDLVLAP SSG
Length:393
Mass (Da):44,042
Last modified:October 1, 1993 - v1
Checksum:i723E5AF5B01E3AAD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97662 mRNA. Translation: AAA40804.1.
BC078767 mRNA. Translation: AAH78767.1.
PIRiA46624. S27881.
RefSeqiNP_446297.1. NM_053845.1.
UniGeneiRn.11110.

Genome annotation databases

GeneIDi116593.
KEGGirno:116593.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97662 mRNA. Translation: AAA40804.1.
BC078767 mRNA. Translation: AAH78767.1.
PIRiA46624. S27881.
RefSeqiNP_446297.1. NM_053845.1.
UniGeneiRn.11110.

3D structure databases

ProteinModelPortaliQ03248.
SMRiQ03248. Positions 5-384.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiQ03248.
PhosphoSiteiQ03248.

Proteomic databases

PRIDEiQ03248.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi116593.
KEGGirno:116593.

Organism-specific databases

CTDi51733.
RGDi620091. Upb1.

Phylogenomic databases

HOVERGENiHBG018848.
InParanoidiQ03248.
KOiK01431.
PhylomeDBiQ03248.

Enzyme and pathway databases

UniPathwayiUPA00131.
BioCyciMetaCyc:MONOMER-15401.
SABIO-RKQ03248.

Miscellaneous databases

PROiQ03248.

Family and domain databases

Gene3Di3.60.110.10. 1 hit.
InterProiIPR003010. C-N_Hydrolase.
[Graphical view]
PfamiPF00795. CN_hydrolase. 1 hit.
[Graphical view]
SUPFAMiSSF56317. SSF56317. 1 hit.
PROSITEiPS50263. CN_HYDROLASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 202-212, FUNCTION, CATALYTIC ACTIVITY, COFACTOR.
    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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Kidney.
  3. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiBUP1_RAT
AccessioniPrimary (citable) accession number: Q03248
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 8, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.