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P32528

- DUR1_YEAST

UniProt

P32528 - DUR1_YEAST

Protein

Urea amidolyase

Gene

DUR1,2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 2 (01 Oct 1994)
      Previous versions | rss
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    Functioni

    Hydrolysis of urea to ammonia and CO2.

    Catalytic activityi

    ATP + urea + HCO3- = ADP + phosphate + urea-1-carboxylate.
    Urea-1-carboxylate + H2O = 2 CO2 + 2 NH3.

    Cofactori

    Biotin.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei747 – 7471ATPBy similarity
    Binding sitei830 – 8301ATPBy similarity
    Binding sitei865 – 8651ATPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi122 – 1298ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. allophanate hydrolase activity Source: SGD
    2. ATP binding Source: UniProtKB-KW
    3. biotin carboxylase activity Source: InterPro
    4. carbon-nitrogen ligase activity, with glutamine as amido-N-donor Source: InterPro
    5. metal ion binding Source: InterPro
    6. urea carboxylase activity Source: SGD

    GO - Biological processi

    1. allantoin catabolic process Source: SGD
    2. arginine metabolic process Source: UniProtKB-KW
    3. urea catabolic process Source: SGD

    Keywords - Molecular functioni

    Hydrolase, Ligase

    Keywords - Biological processi

    Arginine metabolism

    Keywords - Ligandi

    ATP-binding, Biotin, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:YBR208C-MONOMER.
    YEAST:YBR208C-MONOMER.
    BRENDAi6.3.4.6. 984.
    UniPathwayiUPA00258; UER00371.
    UPA00258; UER00372.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Urea amidolyase
    Including the following 2 domains:
    Urea carboxylase (EC:6.3.4.6)
    Allophanate hydrolase (EC:3.5.1.54)
    Gene namesi
    Name:DUR1,2
    Ordered Locus Names:YBR208C
    ORF Names:YBR1448
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome II

    Organism-specific databases

    CYGDiYBR208c.
    SGDiS000000412. DUR1,2.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 18351835Urea amidolyasePRO_0000146832Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei803 – 8031Phosphoserine1 Publication
    Modified residuei1798 – 17981N6-biotinyllysineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP32528.
    PaxDbiP32528.
    PeptideAtlasiP32528.

    Expressioni

    Inductioni

    By allophanate or its non-metabolized analog oxalurate. Repressed in the presence of readily used nitrogen sources.

    Gene expression databases

    GenevestigatoriP32528.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    BioGridi32904. 18 interactions.
    DIPiDIP-6296N.
    IntActiP32528. 2 interactions.
    MINTiMINT-664989.
    STRINGi4932.YBR208C.

    Structurei

    3D structure databases

    ProteinModelPortaliP32528.
    SMRiP32528. Positions 10-623, 630-1379, 1437-1680, 1735-1832.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini632 – 1075444Biotin carboxylationAdd
    BLAST
    Domaini751 – 948198ATP-graspPROSITE-ProRule annotationAdd
    BLAST
    Domaini1755 – 183581Biotinyl-bindingAdd
    BLAST

    Sequence similaritiesi

    Contains 1 ATP-grasp domain.PROSITE-ProRule annotation
    Contains 1 biotin carboxylation domain.Curated
    Contains 1 biotinyl-binding domain.Curated

    Phylogenomic databases

    eggNOGiCOG0511.
    GeneTreeiENSGT00550000074675.
    HOGENOMiHOG000251581.
    KOiK14541.
    OMAiVEWMVRQ.
    OrthoDBiEOG7PGDZZ.

    Family and domain databases

    Gene3Di2.40.100.10. 2 hits.
    3.30.1360.40. 1 hit.
    3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.20. 1 hit.
    3.90.1300.10. 1 hit.
    InterProiIPR003833. Allophan_hydro_1.
    IPR003778. Allophan_hydro_2.
    IPR014085. Allophanate_hydrolase.
    IPR000120. Amidase.
    IPR023631. Amidase_dom.
    IPR024946. Arg_repress_C-like.
    IPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR001882. Biotin_BS.
    IPR011764. Biotin_carboxylation_dom.
    IPR005482. Biotin_COase_C.
    IPR000089. Biotin_lipoyl.
    IPR005481. CarbamoylP_synth_lsu_N.
    IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
    IPR029000. Cyclophilin-like_dom.
    IPR016185. PreATP-grasp_dom.
    IPR011054. Rudment_hybrid_motif.
    IPR011053. Single_hybrid_motif.
    IPR014084. Urea_COase.
    [Graphical view]
    PfamiPF02682. AHS1. 1 hit.
    PF02626. AHS2. 1 hit.
    PF01425. Amidase. 1 hit.
    PF02785. Biotin_carb_C. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF00289. CPSase_L_chain. 1 hit.
    PF02786. CPSase_L_D2. 1 hit.
    [Graphical view]
    SMARTiSM00796. AHS1. 1 hit.
    SM00797. AHS2. 1 hit.
    SM00878. Biotin_carb_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF50891. SSF50891. 2 hits.
    SSF51230. SSF51230. 1 hit.
    SSF51246. SSF51246. 1 hit.
    SSF52440. SSF52440. 1 hit.
    SSF75304. SSF75304. 1 hit.
    TIGRFAMsiTIGR02713. allophanate_hyd. 1 hit.
    TIGR00724. urea_amlyse_rel. 1 hit.
    TIGR02712. urea_carbox. 1 hit.
    PROSITEiPS50975. ATP_GRASP. 1 hit.
    PS50979. BC. 1 hit.
    PS00188. BIOTIN. 1 hit.
    PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00866. CPSASE_1. 1 hit.
    PS00867. CPSASE_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P32528-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTVSSDTTAE ISLGWSIQDW IDFHKSSSSQ ASLRLLESLL DSQNVAPVDN     50
    AWISLISKEN LLHQFQILKS RENKETLPLY GVPIAVKDNI DVRGLPTTAA 100
    CPSFAYEPSK DSKVVELLRN AGAIIVGKTN LDQFATGLVG TRSPYGKTPC 150
    AFSKEHVSGG SSAGSASVVA RGIVPIALGT DTAGSGRVPA ALNNLIGLKP 200
    TKGVFSCQGV VPACKSLDCV SIFALNLSDA ERCFRIMCQP DPDNDEYSRP 250
    YVSNPLKKFS SNVTIAIPKN IPWYGETKNP VLFSNAVENL SRTGANVIEI 300
    DFEPLLELAR CLYEGTWVAE RYQAIQSFLD SKPPKESLDP TVISIIEGAK 350
    KYSAVDCFSF EYKRQGILQK VRRLLESVDV LCVPTCPLNP TMQQVADEPV 400
    LVNSRQGTWT NFVNLADLAA LAVPAGFRDD GLPNGITLIG KKFTDYALLE 450
    LANRYFQNIF PNGSRTYGTF TSSSVKPAND QLVGPDYDPS TSIKLAVVGA 500
    HLKGLPLHWQ LEKVNATYLC TTKTSKAYQL FALPKNGPVL KPGLRRVQDS 550
    NGSQIELEVY SVPKELFGAF ISMVPEPLGI GSVELESGEW IKSFICEESG 600
    YKAKGTVDIT KYGGFRAYFE MLKKKESQKK KLFDTVLIAN RGEIAVRIIK 650
    TLKKLGIRSV AVYSDPDKYS QHVTDADVSV PLHGTTAAQT YLDMNKIIDA 700
    AKQTNAQAII PGYGFLSENA DFSDACTSAG ITFVGPSGDI IRGLGLKHSA 750
    RQIAQKAGVP LVPGSLLITS VEEAKKVAAE LEYPVMVKST AGGGGIGLQK 800
    VDSEEDIEHI FETVKHQGET FFGDAGVFLE RFIENARHVE VQLMGDGFGK 850
    AIALGERDCS LQRRNQKVIE ETPAPNLPEK TRLALRKAAE SLGSLLNYKC 900
    AGTVEFIYDE KKDEFYFLEV NTRLQVEHPI TEMVTGLDLV EWMIRIAAND 950
    APDFDSTKVE VNGVSMEARL YAENPLKNFR PSPGLLVDVK FPDWARVDTW 1000
    VKKGTNISPE YDPTLAKIIV HGKDRDDAIS KLNQALEETK VYGCITNIDY 1050
    LKSIITSDFF AKAKVSTNIL NSYQYEPTAI EITLPGAHTS IQDYPGRVGY 1100
    WRIGVPPSGP MDAYSFRLAN RIVGNDYRTP AIEVTLTGPS IVFHCETVIA 1150
    ITGGTALCTL DGQEIPQHKP VEVKRGSTLS IGKLTSGCRA YLGIRGGIDV 1200
    PKYLGSYSTF TLGNVGGYNG RVLKLGDVLF LPSNEENKSV ECLPQNIPQS 1250
    LIPQISETKE WRIGVTCGPH GSPDFFKPES IEEFFSEKWK VHYNSNRFGV 1300
    RLIGPKPKWA RSNGGEGGMH PSNTHDYVYS LGAINFTGDE PVIITCDGPS 1350
    LGGFVCQAVV PEAELWKVGQ VKPGDSIQFV PLSYESSRSL KESQDVAIKS 1400
    LDGTKLRRLD SVSILPSFET PILAQMEKVN ELSPKVVYRQ AGDRYVLVEY 1450
    GDNEMNFNIS YRIECLISLV KKNKTIGIVE MSQGVRSVLI EFDGYKVTQK 1500
    ELLKVLVAYE TEIQFDENWK ITSNIIRLPM AFEDSKTLAC VQRYQETIRS 1550
    SAPWLPNNVD FIANVNGISR NEVYDMLYSA RFMVLGLGDV FLGSPCAVPL 1600
    DPRHRFLGSK YNPSRTYTER GAVGIGGMYM CIYAANSPGG YQLVGRTIPI 1650
    WDKLCLAASS EVPWLMNPFD QVEFYPVSEE DLDKMTEDCD NGVYKVNIEK 1700
    SVFDHQEYLR WINANKDSIT AFQEGQLGER AEEFAKLIQN ANSELKESVT 1750
    VKPDEEEDFP EGAEIVYSEY SGRFWKSIAS VGDVIEAGQG LLIIEAMKAE 1800
    MIISAPKSGK IIKICHGNGD MVDSGDIVAV IETLA 1835
    Length:1,835
    Mass (Da):201,832
    Last modified:October 1, 1994 - v2
    Checksum:iF52B0DD0FE42CD65
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti96 – 961P → R in AAC41643. (PubMed:1802034)Curated
    Sequence conflicti256 – 2583LKK → KKN in AAC41643. (PubMed:1802034)Curated
    Sequence conflicti459 – 4591I → M in AAC41643. (PubMed:1802034)Curated
    Sequence conflicti830 – 8301E → K in AAC41643. (PubMed:1802034)Curated
    Sequence conflicti1395 – 13951D → E in AAC41643. (PubMed:1802034)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64926 Genomic DNA. Translation: AAC41643.1.
    Z36077 Genomic DNA. Translation: CAA85172.1.
    Z21487 Genomic DNA. Translation: CAA79695.1.
    BK006936 Genomic DNA. Translation: DAA07325.1.
    PIRiS46082.
    RefSeqiNP_009767.1. NM_001178556.1.

    Genome annotation databases

    EnsemblFungiiYBR208C; YBR208C; YBR208C.
    GeneIDi852507.
    KEGGisce:YBR208C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M64926 Genomic DNA. Translation: AAC41643.1 .
    Z36077 Genomic DNA. Translation: CAA85172.1 .
    Z21487 Genomic DNA. Translation: CAA79695.1 .
    BK006936 Genomic DNA. Translation: DAA07325.1 .
    PIRi S46082.
    RefSeqi NP_009767.1. NM_001178556.1.

    3D structure databases

    ProteinModelPortali P32528.
    SMRi P32528. Positions 10-623, 630-1379, 1437-1680, 1735-1832.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32904. 18 interactions.
    DIPi DIP-6296N.
    IntActi P32528. 2 interactions.
    MINTi MINT-664989.
    STRINGi 4932.YBR208C.

    Proteomic databases

    MaxQBi P32528.
    PaxDbi P32528.
    PeptideAtlasi P32528.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YBR208C ; YBR208C ; YBR208C .
    GeneIDi 852507.
    KEGGi sce:YBR208C.

    Organism-specific databases

    CYGDi YBR208c.
    SGDi S000000412. DUR1,2.

    Phylogenomic databases

    eggNOGi COG0511.
    GeneTreei ENSGT00550000074675.
    HOGENOMi HOG000251581.
    KOi K14541.
    OMAi VEWMVRQ.
    OrthoDBi EOG7PGDZZ.

    Enzyme and pathway databases

    UniPathwayi UPA00258 ; UER00371 .
    UPA00258 ; UER00372 .
    BioCyci MetaCyc:YBR208C-MONOMER.
    YEAST:YBR208C-MONOMER.
    BRENDAi 6.3.4.6. 984.

    Miscellaneous databases

    NextBioi 971522.

    Gene expression databases

    Genevestigatori P32528.

    Family and domain databases

    Gene3Di 2.40.100.10. 2 hits.
    3.30.1360.40. 1 hit.
    3.30.1490.20. 1 hit.
    3.30.470.20. 1 hit.
    3.40.50.20. 1 hit.
    3.90.1300.10. 1 hit.
    InterProi IPR003833. Allophan_hydro_1.
    IPR003778. Allophan_hydro_2.
    IPR014085. Allophanate_hydrolase.
    IPR000120. Amidase.
    IPR023631. Amidase_dom.
    IPR024946. Arg_repress_C-like.
    IPR011761. ATP-grasp.
    IPR013815. ATP_grasp_subdomain_1.
    IPR013816. ATP_grasp_subdomain_2.
    IPR001882. Biotin_BS.
    IPR011764. Biotin_carboxylation_dom.
    IPR005482. Biotin_COase_C.
    IPR000089. Biotin_lipoyl.
    IPR005481. CarbamoylP_synth_lsu_N.
    IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
    IPR029000. Cyclophilin-like_dom.
    IPR016185. PreATP-grasp_dom.
    IPR011054. Rudment_hybrid_motif.
    IPR011053. Single_hybrid_motif.
    IPR014084. Urea_COase.
    [Graphical view ]
    Pfami PF02682. AHS1. 1 hit.
    PF02626. AHS2. 1 hit.
    PF01425. Amidase. 1 hit.
    PF02785. Biotin_carb_C. 1 hit.
    PF00364. Biotin_lipoyl. 1 hit.
    PF00289. CPSase_L_chain. 1 hit.
    PF02786. CPSase_L_D2. 1 hit.
    [Graphical view ]
    SMARTi SM00796. AHS1. 1 hit.
    SM00797. AHS2. 1 hit.
    SM00878. Biotin_carb_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50891. SSF50891. 2 hits.
    SSF51230. SSF51230. 1 hit.
    SSF51246. SSF51246. 1 hit.
    SSF52440. SSF52440. 1 hit.
    SSF75304. SSF75304. 1 hit.
    TIGRFAMsi TIGR02713. allophanate_hyd. 1 hit.
    TIGR00724. urea_amlyse_rel. 1 hit.
    TIGR02712. urea_carbox. 1 hit.
    PROSITEi PS50975. ATP_GRASP. 1 hit.
    PS50979. BC. 1 hit.
    PS00188. BIOTIN. 1 hit.
    PS50968. BIOTINYL_LIPOYL. 1 hit.
    PS00866. CPSASE_1. 1 hit.
    PS00867. CPSASE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The urea amidolyase (DUR1,2) gene of Saccharomyces cerevisiae."
      Genbauffe F.S., Cooper T.G.
      DNA Seq. 2:19-32(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Complete DNA sequence of yeast chromosome II."
      Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C., Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M., Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M., Cziepluch C.
      , Demolis N., Delaveau T., Doignon F., Domdey H., Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D., Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.
      EMBO J. 13:5795-5809(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. "A 12.8 kb segment, on the right arm of chromosome II from Saccharomyces cerevisiae including part of the DUR1,2 gene, contains five putative new genes."
      Bussereau F., Mallet L., Gaillon L., Jacquet M.
      Yeast 9:797-806(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1487-1835.
      Strain: ATCC 204508 / S288c.
    5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    6. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-803, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiDUR1_YEAST
    AccessioniPrimary (citable) accession number: P32528
    Secondary accession number(s): D6VQK5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1994
    Last modified: October 1, 2014
    This is version 147 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 952 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome II
      Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

    External Data

    Dasty 3