DUR1_YEAST
ID DUR1_YEAST Reviewed; 1835 AA.
AC P32528; D6VQK5;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Urea amidolyase;
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; OrderedLocusNames=YBR208C; ORFNames=YBR1448;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1802034; DOI=10.3109/10425179109008435;
RA Genbauffe F.S., Cooper T.G.;
RT "The urea amidolyase (DUR1,2) gene of Saccharomyces cerevisiae.";
RL DNA Seq. 2:19-32(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA Mewes H.-W., Kleine K.;
RT "Complete DNA sequence of yeast chromosome II.";
RL EMBO J. 13:5795-5809(1994).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1487-1835.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8368014; DOI=10.1002/yea.320090714;
RA Bussereau F., Mallet L., Gaillon L., Jacquet M.;
RT "A 12.8 kb segment, on the right arm of chromosome II from Saccharomyces
RT cerevisiae including part of the DUR1,2 gene, contains five putative new
RT genes.";
RL Yeast 9:797-806(1993).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-803, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Hydrolysis of urea to ammonia and CO(2).
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;
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.
CC -!- INDUCTION: By allophanate or its non-metabolized analog oxalurate.
CC Repressed in the presence of readily used nitrogen sources.
CC -!- MISCELLANEOUS: Present with 952 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
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DR EMBL; M64926; AAC41643.1; -; Genomic_DNA.
DR EMBL; Z36077; CAA85172.1; -; Genomic_DNA.
DR EMBL; Z21487; CAA79695.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07325.1; -; Genomic_DNA.
DR PIR; S46082; S46082.
DR RefSeq; NP_009767.1; NM_001178556.1.
DR AlphaFoldDB; P32528; -.
DR SMR; P32528; -.
DR BioGRID; 32904; 40.
DR DIP; DIP-6296N; -.
DR IntAct; P32528; 9.
DR STRING; 4932.YBR208C; -.
DR iPTMnet; P32528; -.
DR MaxQB; P32528; -.
DR PaxDb; P32528; -.
DR PRIDE; P32528; -.
DR EnsemblFungi; YBR208C_mRNA; YBR208C; YBR208C.
DR GeneID; 852507; -.
DR KEGG; sce:YBR208C; -.
DR SGD; S000000412; DUR1,2.
DR VEuPathDB; FungiDB:YBR208C; -.
DR eggNOG; KOG0238; Eukaryota.
DR eggNOG; KOG1211; Eukaryota.
DR HOGENOM; CLU_002162_4_1_1; -.
DR InParanoid; P32528; -.
DR OMA; HDCEYAI; -.
DR BioCyc; MetaCyc:YBR208C-MON; -.
DR BioCyc; YEAST:YBR208C-MON; -.
DR BRENDA; 3.5.1.54; 984.
DR BRENDA; 6.3.4.6; 984.
DR UniPathway; UPA00258; UER00371.
DR UniPathway; UPA00258; UER00372.
DR PRO; PR:P32528; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P32528; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004039; F:allophanate hydrolase activity; IMP:SGD.
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; IMP:SGD.
DR GO; GO:0000256; P:allantoin catabolic process; TAS:SGD.
DR GO; GO:0043419; P:urea catabolic process; IMP:SGD.
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 1: Evidence at protein level;
KW ATP-binding; Biotin; Hydrolase; Ligase; Multifunctional enzyme;
KW Nucleotide-binding; Phosphoprotein; Reference proteome.
FT CHAIN 1..1835
FT /note="Urea amidolyase"
FT /id="PRO_0000146832"
FT DOMAIN 632..1075
FT /note="Biotin carboxylation"
FT DOMAIN 751..948
FT /note="ATP-grasp"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT DOMAIN 1754..1832
FT /note="Biotinyl-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT BINDING 122..129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT BINDING 747
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 830
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 865
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 803
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1798
FT /note="N6-biotinyllysine"
FT /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT ProRule:PRU01066"
FT CONFLICT 96
FT /note="P -> R (in Ref. 1; AAC41643)"
FT /evidence="ECO:0000305"
FT CONFLICT 256..258
FT /note="LKK -> KKN (in Ref. 1; AAC41643)"
FT /evidence="ECO:0000305"
FT CONFLICT 459
FT /note="I -> M (in Ref. 1; AAC41643)"
FT /evidence="ECO:0000305"
FT CONFLICT 830
FT /note="E -> K (in Ref. 1; AAC41643)"
FT /evidence="ECO:0000305"
FT CONFLICT 1395
FT /note="D -> E (in Ref. 1; AAC41643)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1835 AA; 201832 MW; F52B0DD0FE42CD65 CRC64;
MTVSSDTTAE ISLGWSIQDW IDFHKSSSSQ ASLRLLESLL DSQNVAPVDN AWISLISKEN
LLHQFQILKS RENKETLPLY GVPIAVKDNI DVRGLPTTAA CPSFAYEPSK DSKVVELLRN
AGAIIVGKTN LDQFATGLVG TRSPYGKTPC AFSKEHVSGG SSAGSASVVA RGIVPIALGT
DTAGSGRVPA ALNNLIGLKP TKGVFSCQGV VPACKSLDCV SIFALNLSDA ERCFRIMCQP
DPDNDEYSRP YVSNPLKKFS SNVTIAIPKN IPWYGETKNP VLFSNAVENL SRTGANVIEI
DFEPLLELAR CLYEGTWVAE RYQAIQSFLD SKPPKESLDP TVISIIEGAK KYSAVDCFSF
EYKRQGILQK VRRLLESVDV LCVPTCPLNP TMQQVADEPV LVNSRQGTWT NFVNLADLAA
LAVPAGFRDD GLPNGITLIG KKFTDYALLE LANRYFQNIF PNGSRTYGTF TSSSVKPAND
QLVGPDYDPS TSIKLAVVGA HLKGLPLHWQ LEKVNATYLC TTKTSKAYQL FALPKNGPVL
KPGLRRVQDS NGSQIELEVY SVPKELFGAF ISMVPEPLGI GSVELESGEW IKSFICEESG
YKAKGTVDIT KYGGFRAYFE MLKKKESQKK KLFDTVLIAN RGEIAVRIIK TLKKLGIRSV
AVYSDPDKYS QHVTDADVSV PLHGTTAAQT YLDMNKIIDA AKQTNAQAII PGYGFLSENA
DFSDACTSAG ITFVGPSGDI IRGLGLKHSA RQIAQKAGVP LVPGSLLITS VEEAKKVAAE
LEYPVMVKST AGGGGIGLQK VDSEEDIEHI FETVKHQGET FFGDAGVFLE RFIENARHVE
VQLMGDGFGK AIALGERDCS LQRRNQKVIE ETPAPNLPEK TRLALRKAAE SLGSLLNYKC
AGTVEFIYDE KKDEFYFLEV NTRLQVEHPI TEMVTGLDLV EWMIRIAAND APDFDSTKVE
VNGVSMEARL YAENPLKNFR PSPGLLVDVK FPDWARVDTW VKKGTNISPE YDPTLAKIIV
HGKDRDDAIS KLNQALEETK VYGCITNIDY LKSIITSDFF AKAKVSTNIL NSYQYEPTAI
EITLPGAHTS IQDYPGRVGY WRIGVPPSGP MDAYSFRLAN RIVGNDYRTP AIEVTLTGPS
IVFHCETVIA ITGGTALCTL DGQEIPQHKP VEVKRGSTLS IGKLTSGCRA YLGIRGGIDV
PKYLGSYSTF TLGNVGGYNG RVLKLGDVLF LPSNEENKSV ECLPQNIPQS LIPQISETKE
WRIGVTCGPH GSPDFFKPES IEEFFSEKWK VHYNSNRFGV RLIGPKPKWA RSNGGEGGMH
PSNTHDYVYS LGAINFTGDE PVIITCDGPS LGGFVCQAVV PEAELWKVGQ VKPGDSIQFV
PLSYESSRSL KESQDVAIKS LDGTKLRRLD SVSILPSFET PILAQMEKVN ELSPKVVYRQ
AGDRYVLVEY GDNEMNFNIS YRIECLISLV KKNKTIGIVE MSQGVRSVLI EFDGYKVTQK
ELLKVLVAYE TEIQFDENWK ITSNIIRLPM AFEDSKTLAC VQRYQETIRS SAPWLPNNVD
FIANVNGISR NEVYDMLYSA RFMVLGLGDV FLGSPCAVPL DPRHRFLGSK YNPSRTYTER
GAVGIGGMYM CIYAANSPGG YQLVGRTIPI WDKLCLAASS EVPWLMNPFD QVEFYPVSEE
DLDKMTEDCD NGVYKVNIEK SVFDHQEYLR WINANKDSIT AFQEGQLGER AEEFAKLIQN
ANSELKESVT VKPDEEEDFP EGAEIVYSEY SGRFWKSIAS VGDVIEAGQG LLIIEAMKAE
MIISAPKSGK IIKICHGNGD MVDSGDIVAV IETLA
