Q03248 (BUP1_RAT) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	393 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Cytoplasm
Ligand	Metal-binding Zinc
Molecular function	Hydrolase
Technical term	Allosteric enzyme Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	beta-alanine biosynthetic process Traceable author statement Ref.1. Source: RGD embryo development Inferred from expression pattern. Source: RGD
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell soluble fraction Inferred from direct assay. Source: RGD
Molecular function	beta-ureidopropionase activity Inferred from direct assay Ref.1. Source: RGD zinc ion binding Inferred from direct assay Ref.1. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 393	393	Beta-ureidopropionase		PRO_0000204054
Regions
	Domain	72 – 366	295	CN hydrolase
Sites
	Metal binding	97	1	Zinc Potential
	Metal binding	158	1	Zinc Potential
	Metal binding	280	1	Zinc Potential
	Metal binding	293	1	Zinc Potential
	Metal binding	307	1	Zinc Potential

Sequences

	Sequence		Length	Mass (Da)
	Q03248 [UniParc]. Last modified October 1, 1993. Version 1. Checksum: 723E5AF5B01E3AAD	FASTA	393	44,042
	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

References

	« Hide 'large scale' referencesShow '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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M97662 mRNA. Translation: AAA40804.1. BC078767 mRNA. Translation: AAH78767.1.
IPI	IPI00208970.
PIR	S27881. A46624.
RefSeq	NP_446297.1. NM_053845.1.
UniGene	Rn.11110.
3D structure databases
ProteinModelPortal	Q03248.
SMR	Q03248. Positions 5-384.
ModBase	Search...
Proteomic databases
PRIDE	Q03248.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	116593.
KEGG	rno:116593.
Organism-specific databases
CTD	51733.
RGD	620091. Upb1.
Phylogenomic databases
eggNOG	roNOG04713.
HOVERGEN	HBG018848.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-15401.
Gene expression databases
Genevestigator	Q03248.
Family and domain databases
InterPro	IPR003010. Ntlse/CNhydtse. [Graphical view]
Gene3D	G3DSA:3.60.110.10. Ntlse/CNhydtse. 1 hit.
KO	K01431.
Pfam	PF00795. CN_hydrolase. 1 hit. [Graphical view]
SUPFAM	SSF56317. Ntlse/CNhydtse. 1 hit.
PROSITE	PS50263. CN_HYDROLASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	619283.

Entry information

Entry name

BUP1_RAT

Accession

Primary (citable) accession number: Q03248

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	October 1, 1993
Last modified:	November 16, 2011
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program