DUR1_LACKL
ID DUR1_LACKL Reviewed; 1830 AA.
AC A5H0J2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Urea amidolyase;
DE AltName: Full=Pyrimidine-degrading protein 13,15;
DE AltName: Full=Uracil catabolism protein 3,5;
DE Includes:
DE RecName: Full=Urea carboxylase;
DE EC=6.3.4.6;
DE Includes:
DE RecName: Full=Allophanate hydrolase;
DE EC=3.5.1.54;
GN Name=DUR1,2; Synonyms=PYD13,15, URC3,5;
OS Lachancea kluyveri (Yeast) (Saccharomyces kluyveri).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=4934;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=18550080; DOI=10.1016/j.jmb.2008.05.029;
RA Andersen G., Bjoernberg O., Polakova S., Pynyaha Y., Rasmussen A.,
RA Moeller K., Hofer A., Moritz T., Sandrini M.P., Merico A.M., Compagno C.,
RA Aekerlund H.E., Gojkovic Z., Piskur J.;
RT "A second pathway to degrade pyrimidine nucleic acid precursors in
RT eukaryotes.";
RL J. Mol. Biol. 380:656-666(2008).
CC -!- FUNCTION: Involved in uracil catabolism. Hydrolysis of urea to ammonia
CC and CO(2). {ECO:0000269|PubMed:18550080}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + hydrogencarbonate + urea = ADP + H(+) + phosphate +
CC urea-1-carboxylate; Xref=Rhea:RHEA:20896, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15832, ChEBI:CHEBI:16199, ChEBI:CHEBI:17544,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=6.3.4.6;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 H(+) + H2O + urea-1-carboxylate = 2 CO2 + 2 NH4(+);
CC Xref=Rhea:RHEA:19029, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15832, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938; EC=3.5.1.54;
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586; Evidence={ECO:0000250};
CC -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC urea (allophanate route): step 1/2.
CC -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC urea (allophanate route): step 2/2.
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DUR1,2 family. {ECO:0000305}.
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DR EMBL; DQ512718; ABF58890.1; -; Genomic_DNA.
DR AlphaFoldDB; A5H0J2; -.
DR SMR; A5H0J2; -.
DR PRIDE; A5H0J2; -.
DR UniPathway; UPA00258; UER00371.
DR UniPathway; UPA00258; UER00372.
DR GO; GO:0004039; F:allophanate hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004847; F:urea carboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0043419; P:urea catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.40.100.10; -; 2.
DR Gene3D; 3.90.1300.10; -; 1.
DR InterPro; IPR014085; Allophanate_hydrolase.
DR InterPro; IPR023631; Amidase_dom.
DR InterPro; IPR036928; AS_sf.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR003778; CT_A_B.
DR InterPro; IPR003833; CT_C_D.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR InterPro; IPR014084; Urea_COase.
DR Pfam; PF01425; Amidase; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF02626; CT_A_B; 1.
DR Pfam; PF02682; CT_C_D; 1.
DR SMART; SM00796; AHS1; 1.
DR SMART; SM00797; AHS2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF50891; SSF50891; 2.
DR SUPFAM; SSF51230; SSF51230; 1.
DR SUPFAM; SSF51246; SSF51246; 1.
DR SUPFAM; SSF52440; SSF52440; 1.
DR SUPFAM; SSF75304; SSF75304; 1.
DR TIGRFAMs; TIGR02713; allophanate_hyd; 1.
DR TIGRFAMs; TIGR00724; urea_amlyse_rel; 1.
DR TIGRFAMs; TIGR02712; urea_carbox; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Biotin; Hydrolase; Ligase; Multifunctional enzyme;
KW Nucleotide-binding.
FT CHAIN 1..1830
FT /note="Urea amidolyase"
FT /id="PRO_0000367271"
FT DOMAIN 625..1068
FT /note="Biotin carboxylation"
FT DOMAIN 744..941
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 1752..1830
FT /note="Biotinyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT BINDING 115..122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 740
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 823
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 858
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 1796
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
SQ SEQUENCE 1830 AA; 201131 MW; C5D1ED66A5F4F10D CRC64;
MSVDTLGWSA QDWIDFHGKS TPEHSYNTLL SLLKSQKSAP EDPAWISLIN EANLAHQWKV
LQSKANKQQL PLYGVPIAVK DNIDSKGSPT TAACPAFEYN PSADSTVVAL LKDAGAIVIG
KTNLDQFATG LVGTRSPYGK TPCVFSDKHV SGGSSAGSAS AVGRGIVPIA LGTDTAGSGR
VPAALNNLIG LKPTKGLFSC SGVVPACKSL DCVSVFAMNL SDAERCFKVM AKPDLENDEY
SRPLPSNPLQ KYPKNVTIAI PKEVPWYGET ENPKLYAKAI ENLKVAGASI VTIDFEPLLA
LARCLYEGAW VAERYEATKD FFATNPPESS LDPTVTSIIK TATKYDAADS FRYEYQRQGI
LQKVDQTLKD IDVLCVPTCP LNPTFEEVAA EPVLVNSRQG TWTNFVNLAD MAALAVPAGF
RPDGLPQGVT LIGKKFTDFA LLELANRYFK VAFPQGSRTF GKFIDRQVTT KDDELRGPDI
SPEDSVKLAV VGAHLKGLPL YWQLEKVNAT YLGSPKTSKN YKLYALPKTG PILKPGLRRV
GEETGSQIQL EVYSVPKENF GEFISMVPEP LGIGSVELES GEWVKSFICE EFGYTQKGTV
DITKYGGFKK YIDFLKQEEA KVKKPFETVL IANRGEIAVR IIKTLKKLNI RSVAVYSDPD
KYSQHVIDAD LGVALNGRTA AETYLDIDKI IKAAKDTNAQ AIIPGYGFLS ENAEFADKCV
EEGIVFVGPS GEAIRKLGLK HSAREIAEKA GVPLVPGSGL VTSAKEAKEI ANKLEYPVMV
KSTAGGGGIG LQKVDSENEI ERVFETVQHQ GKAYFGDSGV FLERFVENAR HVEIQMMGDG
YGKAIAIGER DCSLQRRNQK IIEETPAPNL GETTRTKMRQ AAESLGSLLK YKCAGTVEFI
YDERRDEFYF LEVNARLQVE HPITEMVTGL DLVEWMLRIA ADDAPDFESA NIVVTGASIE
ARLYAENPAK DFRPSPGLLT DVHFPEWARV DTWVSKGTTV SAEYDPTLAK IIVHGKDRND
AIMKMNKALN ETVVYGCITN IDYLRSIASS EMFKTAKVAT KILDSYDYKP CAFEVTSPGA
YTTVQDYPGR VGYWRIGVPP SGPMDAYSFR LANRIVGNHY KAPAIELTLN GPKILFHTET
IIAISGGIAA CSLNDKPIEQ NKPIQVNRGD HLAIGKLSVG CRAYLAIRGG IDVPEYLGSR
STFALGNMGG YNGRVLKLGD VLFLNQPELA SSSLPGPAYE PQAPPANLLP KISDDKEWTI
GVTCGPHGSP DFFKPESVEE FFSEKWKVHY NSNRFGVRLI GPKPKWARKD GGEGGLHPSN
AHDYVYSLGA INFTGDEPVI ITSDGPSLGG FVCQAVVPEA ELWKVGQVKP GDSIQFVPIS
YQVARQLKES QDAAIETLED GKLQTLTSDL ILPTYEDPVL VQLPKKSNLS PKVTYRQAGD
RYILVEYGEN QMDLNIAYRI NQLINLVGKH KTVGIVEMSQ GVRSVLIEYD GYKISQGALL
DTLVAYESEI QFDKNWSIKS KIFKLPLAFE DSKTLECVTR YQETIRSKAP WLPNNVDFVA
EVNDITHKDV ENMLYSARFL VLGLGDVFLG APCAVPLDPR HRFLGSKYNP SRTYTKNGVV
GIGGMYMCIY AMDSPGGYQL VGRTIPIWDK LKLGSHSQEH PWLLTPFDQV EFYPVSEEEL
DRFTEDCENG KFPVQVEESV FDHKNYLKWI NENIESITEF QKSQGGAKAD EFARLIQVAN
QELESSTTNK SAVEEEYPED AEMVYSEYSG RFWKPMVSAG DTVTKGDGLV IVEAMKTEMV
VPAKKSGKVL KIVHKNGDMV DAGDLVAVIQ
