ID   BUP1_PONAB              Reviewed;         384 AA.
AC   Q5RBM6;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 78.
DE   RecName: Full=Beta-ureidopropionase;
DE            EC=3.5.1.6;
DE   AltName: Full=Beta-alanine synthase;
DE   AltName: Full=N-carbamoyl-beta-alanine amidohydrolase;
GN   Name=UPB1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes a late step in pyrimidine degradation. Converts N-
CC       carbamoyl-beta-alanine (3-ureidopropanoate) into beta-alanine, ammonia
CC       and carbon dioxide. Likewise, converts N-carbamoyl-beta-
CC       aminoisobutyrate (3-ureidoisobutyrate) into beta-aminoisobutyrate,
CC       ammonia and carbon dioxide. {ECO:0000250|UniProtKB:Q9UBR1}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-(carbamoylamino)propanoate + 2 H(+) + H2O = beta-alanine +
CC         CO2 + NH4(+); Xref=Rhea:RHEA:11184, ChEBI:CHEBI:11892,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:57966; EC=3.5.1.6;
CC         Evidence={ECO:0000250|UniProtKB:Q9UBR1};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3-(carbamoylamino)-2-methylpropanoate + 2 H(+) + H2O = (R)-3-
CC         amino-2-methylpropanoate + CO2 + NH4(+); Xref=Rhea:RHEA:37339,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:57731, ChEBI:CHEBI:74414; EC=3.5.1.6;
CC         Evidence={ECO:0000250|UniProtKB:Q9UBR1};
CC   -!- PATHWAY: Amino-acid biosynthesis; beta-alanine biosynthesis.
CC       {ECO:0000250|UniProtKB:Q9UBR1}.
CC   -!- SUBUNIT: Homodimer, homotetramer, homooctamer; can also form higher
CC       homooligomers. {ECO:0000250|UniProtKB:Q9UBR1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily. BUP
CC       family. {ECO:0000305}.
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DR   EMBL; CR858612; CAH90834.1; -; mRNA.
DR   RefSeq; NP_001125476.1; NM_001132004.1.
DR   AlphaFoldDB; Q5RBM6; -.
DR   SMR; Q5RBM6; -.
DR   STRING; 9601.ENSPPYP00000012992; -.
DR   GeneID; 100172385; -.
DR   KEGG; pon:100172385; -.
DR   CTD; 51733; -.
DR   eggNOG; KOG0808; Eukaryota.
DR   InParanoid; Q5RBM6; -.
DR   UniPathway; UPA00131; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003837; F:beta-ureidopropionase activity; ISS:UniProtKB.
DR   GO; GO:0033396; P:beta-alanine biosynthetic process via 3-ureidopropionate; ISS:UniProtKB.
DR   GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
DR   GO; GO:0046135; P:pyrimidine nucleoside catabolic process; ISS:UniProtKB.
DR   Gene3D; 3.60.110.10; -; 1.
DR   InterPro; IPR003010; C-N_Hydrolase.
DR   InterPro; IPR036526; C-N_Hydrolase_sf.
DR   Pfam; PF00795; CN_hydrolase; 1.
DR   SUPFAM; SSF56317; SSF56317; 1.
DR   PROSITE; PS50263; CN_HYDROLASE; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Phosphoprotein; Reference proteome.
FT   CHAIN           1..384
FT                   /note="Beta-ureidopropionase"
FT                   /id="PRO_0000204053"
FT   DOMAIN          72..344
FT                   /note="CN hydrolase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        119
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        196
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   ACT_SITE        233
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT   MOD_RES         378
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q03248"
SQ   SEQUENCE   384 AA;  43098 MW;  8F7B1BC8E25077BA CRC64;
     MAGAEWKSLE ECLEKHLPLP DLQEVKRVLY GKELRKLDLP REAFEAASRE DFELQGYAFE
     AAEEQLRRPR IVHVGLVQNR IPLPANAPVA EQVSALHRRI KAIVEVAAMC GVNIICFQEA
     WTMPFAFCTR EKLPWTEFAE SAEDGPTTRF CQKLAKNHDM VVVSPILERD SEHGDVLWNT
     AVVISNSGAV LGKTRKNHIP RVGDFNESTY YMEGNLGHPV FQTQFGRIAV NICYGRHHPL
     NWLMYSINGA EIIFNPSATI GALSESLWSI EARNAAIANH CFTCAINRVG TEHFPNEFTS
     GDGKKAHQDF GYFYGSSYVA APDGSRTPGL SRSQDGLLVA KLDLNLCQQV NDVWNFKMTG
     RYEMYARELA EAVKSNYSPT IVKE