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 22-FEB-2023, entry version 80.
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 OrthoDB; 177430at2759; -.
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 CDD; cd07587; ML_beta-AS; 1.
DR Gene3D; 3.60.110.10; Carbon-nitrogen hydrolase; 1.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR PANTHER; PTHR43674:SF2; BETA-UREIDOPROPIONASE; 1.
DR PANTHER; PTHR43674; NITRILASE C965.09-RELATED; 1.
DR Pfam; PF00795; CN_hydrolase; 1.
DR SUPFAM; SSF56317; Carbon-nitrogen hydrolase; 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
//
