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   13-SEP-2023, entry version 83.
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   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   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 1.20.58.1700; -; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.30.1360.40; -; 1.
DR   Gene3D; 3.90.1300.10; Amidase signature (AS) domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   Gene3D; 2.40.100.10; Cyclophilin-like; 2.
DR   Gene3D; 3.10.490.10; Gamma-glutamyl cyclotransferase-like; 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   NCBIfam; TIGR02713; allophanate_hyd; 1.
DR   NCBIfam; TIGR00724; urea_amlyse_rel; 1.
DR   NCBIfam; TIGR02712; urea_carbox; 1.
DR   PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR   PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
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; SSF75304; Amidase signature (AS) enzymes; 1.
DR   SUPFAM; SSF50891; Cyclophilin-like; 2.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF160467; PH0987 N-terminal domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 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
//