BUP1_ARATH
ID BUP1_ARATH Reviewed; 408 AA.
AC Q8H183; Q9FMF2;
DT 01-APR-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Beta-ureidopropionase {ECO:0000303|PubMed:11161056};
DE EC=3.5.1.6 {ECO:0000269|PubMed:11161056, ECO:0000269|PubMed:19413687};
DE AltName: Full=N-carbamoyl-beta-alanine amidohydrolase {ECO:0000303|Ref.1};
DE AltName: Full=Protein PYRIMIDINE 3 {ECO:0000303|Ref.1};
GN Name=PYD3 {ECO:0000303|Ref.1};
GN Synonyms=BETA-UP {ECO:0000303|PubMed:11161056};
GN OrderedLocusNames=At5g64370 {ECO:0000312|Araport:AT5G64370};
GN ORFNames=MSJ1.21 {ECO:0000312|EMBL:BAB09868.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702 {ECO:0000312|EMBL:AAN17428.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Gojkovic Z., Sandrini M.P.B., Piskur J.;
RT "Eukaryotic beta-alanine synthases.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9501997; DOI=10.1093/dnares/4.6.401;
RA Nakamura Y., Sato S., Kaneko T., Kotani H., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. III. Sequence
RT features of the regions of 1,191,918 bp covered by seventeen physically
RT assigned P1 clones.";
RL DNA Res. 4:401-414(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 17-408, FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=11161056; DOI=10.1104/pp.125.2.1001;
RA Walsh T.A., Green S.B., Larrinua I.M., Schmitzer P.R.;
RT "Characterization of plant beta-ureidopropionase and functional
RT overexpression in Escherichia coli.";
RL Plant Physiol. 125:1001-1011(2001).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, INDUCTION BY NITROGEN
RP LIMITATION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia;
RX PubMed=19413687; DOI=10.1111/j.1469-8137.2009.02843.x;
RA Zrenner R., Riegler H., Marquard C.R., Lange P.R., Geserick C.,
RA Bartosz C.E., Chen C.T., Slocum R.D.;
RT "A functional analysis of the pyrimidine catabolic pathway in
RT Arabidopsis.";
RL New Phytol. 183:117-132(2009).
CC -!- FUNCTION: Catalyzes a late step in pyrimidine degradation. Converts N-
CC carbamoyl-beta-aminoisobutyrate and N-carbamoyl-beta-alanine (3-
CC ureidopropanoate) to, respectively, beta-aminoisobutyrate and beta-
CC alanine, ammonia and carbon dioxide. Involved in the recycling of
CC nitrogen from nucleobases to general nitrogen metabolism.
CC {ECO:0000269|PubMed:11161056, ECO:0000269|PubMed:19413687}.
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:11161056, ECO:0000269|PubMed:19413687};
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:11161056, ECO:0000269|PubMed:19413687}.
CC -!- SUBUNIT: Homodimer, homotetramer, homooctamer; can also form higher
CC homooligomers. {ECO:0000250|UniProtKB:Q9UBR1}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19413687}.
CC -!- DEVELOPMENTAL STAGE: Up-regulated between days 3 and 5 after
CC germination and during senescence. {ECO:0000269|PubMed:19413687}.
CC -!- INDUCTION: Up-regulated by nitrogen limitation.
CC {ECO:0000269|PubMed:19413687}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, but unable to grow on
CC uracil as sole nitrogen source. {ECO:0000269|PubMed:19413687}.
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily. BUP
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB09868.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF465754; AAO33358.1; -; mRNA.
DR EMBL; AB008268; BAB09868.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002688; AED97881.1; -; Genomic_DNA.
DR EMBL; BT000451; AAN17428.1; -; mRNA.
DR EMBL; BT008503; AAP37862.1; -; mRNA.
DR RefSeq; NP_201242.2; NM_125833.5.
DR AlphaFoldDB; Q8H183; -.
DR SMR; Q8H183; -.
DR STRING; 3702.AT5G64370.1; -.
DR PaxDb; Q8H183; -.
DR PRIDE; Q8H183; -.
DR ProteomicsDB; 240369; -.
DR EnsemblPlants; AT5G64370.1; AT5G64370.1; AT5G64370.
DR GeneID; 836558; -.
DR Gramene; AT5G64370.1; AT5G64370.1; AT5G64370.
DR KEGG; ath:AT5G64370; -.
DR Araport; AT5G64370; -.
DR TAIR; locus:2173348; AT5G64370.
DR eggNOG; KOG0808; Eukaryota.
DR HOGENOM; CLU_030130_4_1_1; -.
DR InParanoid; Q8H183; -.
DR OMA; AVKPNYS; -.
DR OrthoDB; 996578at2759; -.
DR PhylomeDB; Q8H183; -.
DR BioCyc; ARA:AT5G64370-MON; -.
DR BioCyc; MetaCyc:MON-9543; -.
DR BRENDA; 3.5.1.6; 399.
DR SABIO-RK; Q8H183; -.
DR UniPathway; UPA00131; -.
DR PRO; PR:Q8H183; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8H183; baseline and differential.
DR Genevisible; Q8H183; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0003837; F:beta-ureidopropionase activity; IDA:TAIR.
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 GO; GO:0043562; P:cellular response to nitrogen levels; IEP:TAIR.
DR GO; GO:0006212; P:uracil catabolic process; IMP:TAIR.
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 Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1..408
FT /note="Beta-ureidopropionase"
FT /id="PRO_0000432456"
FT DOMAIN 90..360
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 137
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 212
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 249
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ SEQUENCE 408 AA; 45553 MW; B294ECBAEFB9C40E CRC64;
MDHMISENGE TSAEGSICGY DSLHQLLSAN LKPELYQEVN RLLLGRNCGR SLEQIVLPES
AKALSSKHDF DLQAASFSAD KEQMRNPRVV RVGLIQNSIA LPTTAPFSDQ TRGIFDKLKP
IIDAAGVAGV NILCLQEAWT MPFAFCTRER RWCEFAEPVD GESTKFLQEL AKKYNMVIVS
PILERDIDHG EVLWNTAVII GNNGNIIGKH RKNHIPRVGD FNESTYYMEG DTGHPVFETV
FGKIAVNICY GRHHPLNWLA FGLNGAEIVF NPSATVGELS EPMWPIEARN AAIANSYFVG
SINRVGTEVF PNPFTSGDGK PQHNDFGHFY GSSHFSAPDA SCTPSLSRYK DGLLISDMDL
NLCRQYKDKW GFRMTARYEV YADLLAKYIK PDFKPQVVSD PLLHKNST
