BUP1_DICDI
ID BUP1_DICDI Reviewed; 391 AA.
AC Q964D8; Q554Z2;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Beta-ureidopropionase;
DE EC=3.5.1.6 {ECO:0000269|PubMed:11454750};
DE AltName: Full=Beta-alanine synthase;
DE AltName: Full=N-carbamoyl-beta-alanine amidohydrolase;
GN Name=pyd3; Synonyms=bup1, upb1; ORFNames=DDB_G0274123;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11454750; DOI=10.1093/genetics/158.3.999;
RA Gojkovic Z., Sandrini M.P., Piskur J.;
RT "Eukaryotic beta-alanine synthases are functionally related but have a high
RT degree of structural diversity.";
RL Genetics 158:999-1011(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [4]
RP PROTEIN SEQUENCE OF 2-14; 62-70; 277-291 AND 371-391, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=AX2;
RA Bienvenut W.V., Ura S., Insall R.H.;
RL Submitted (JUL-2009) to UniProtKB.
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 (PubMed:11454750). Likewise, converts N-carbamoyl-
CC beta-aminoisobutyrate (3-ureidoisobutyrate) into beta-aminoisobutyrate,
CC ammonia and carbon dioxide (By similarity).
CC {ECO:0000250|UniProtKB:Q9UBR1, ECO:0000269|PubMed:11454750}.
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:0000269|PubMed:11454750};
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:0000269|PubMed:11454750}.
CC -!- SUBUNIT: Homodimer and higher homooligomers.
CC {ECO:0000250|UniProtKB:Q9UBR1}.
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily. BUP
CC family. {ECO:0000305}.
CC -!- CAUTION: Lacks the zinc-binding sites found in mammalian orthologs.
CC {ECO:0000305}.
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DR EMBL; AF333186; AAK60519.1; -; mRNA.
DR EMBL; AAFI02000012; EAL69954.1; -; Genomic_DNA.
DR RefSeq; XP_644181.1; XM_639089.1.
DR AlphaFoldDB; Q964D8; -.
DR SMR; Q964D8; -.
DR STRING; 44689.DDB0185221; -.
DR PaxDb; Q964D8; -.
DR EnsemblProtists; EAL69954; EAL69954; DDB_G0274123.
DR GeneID; 8619610; -.
DR KEGG; ddi:DDB_G0274123; -.
DR dictyBase; DDB_G0274123; pyd3.
DR eggNOG; KOG0808; Eukaryota.
DR HOGENOM; CLU_030130_4_1_1; -.
DR InParanoid; Q964D8; -.
DR OMA; AVKPNYS; -.
DR PhylomeDB; Q964D8; -.
DR Reactome; R-DDI-73621; Pyrimidine catabolism.
DR UniPathway; UPA00131; -.
DR PRO; PR:Q964D8; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0045335; C:phagocytic vesicle; HDA:dictyBase.
DR GO; GO:0003837; F:beta-ureidopropionase activity; IBA:GO_Central.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IBA:GO_Central.
DR GO; GO:0033396; P:beta-alanine biosynthetic process via 3-ureidopropionate; IBA:GO_Central.
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 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Hydrolase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 2..391
FT /note="Beta-ureidopropionase"
FT /id="PRO_0000327637"
FT DOMAIN 75..347
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 122
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 199
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 236
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.4"
SQ SEQUENCE 391 AA; 44089 MW; C851253D45FC0948 CRC64;
MSKQFESVQA TLEKYIPAEE LSEVKRILYG YNRGHHVKSL PICQEALDLA NKNNFEIVAS
KVEADPEQLR KPRIVRLGII QNSIGAETTA PIQDQYLAIE AKIEKMIDAA GAMGVNVLCL
QETWHMPFAF CTREKYPWVE FAESASTGQS IKFIQRMARK YNMVIISPML ERDDVHASTI
HNTAVVVGNN GNIIGKSRKN HIPRTGDFNE STYYMESTLG HPVFETIYGK IAINICYGRH
HNLNWLAYGL NGAEIVFNPS ATVGELSEPM WGVEARNAAM TNNYFVGSIN RVGTEHFPNE
FTSGNGKPAH KDFGHFYGSS YFSSPDNCCT PSLSRVSDGL NISEVDLNLC QQVKDKWNFQ
MTARYELYAK FLTDYINPNY QPNIIKDPSM K
