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A5H0J2

- DUR1_LACKL

UniProt

A5H0J2 - DUR1_LACKL

Protein

Urea amidolyase

Gene

DUR1,2

Organism
Lachancea kluyveri (Yeast) (Saccharomyces kluyveri)
Status
Reviewed - Annotation score: 4 out of 5- Protein inferred from homologyi
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    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (12 Jun 2007)
      Previous versions | rss
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    Functioni

    Involved in uracil catabolism. Hydrolysis of urea to ammonia and CO2.1 Publication

    Catalytic activityi

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

    Cofactori

    Biotin.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei740 – 7401ATPBy similarity
    Binding sitei823 – 8231ATPBy similarity
    Binding sitei858 – 8581ATPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi115 – 1228ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. allophanate hydrolase activity Source: UniProtKB-EC
    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: UniProtKB-EC

    GO - Biological processi

    1. arginine metabolic process Source: UniProtKB-KW
    2. urea catabolic process Source: UniProtKB-UniPathway

    Keywords - Molecular functioni

    Hydrolase, Ligase

    Keywords - Biological processi

    Arginine metabolism

    Keywords - Ligandi

    ATP-binding, Biotin, Nucleotide-binding

    Enzyme and pathway databases

    UniPathwayiUPA00258; UER00371.
    UPA00258; UER00372.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Urea amidolyase
    Alternative name(s):
    Pyrimidine-degrading protein 13,15
    Uracil catabolism protein 3,5
    Including the following 2 domains:
    Urea carboxylase (EC:6.3.4.6)
    Allophanate hydrolase (EC:3.5.1.54)
    Gene namesi
    Name:DUR1,2
    Synonyms:PYD13,15, URC3,5
    OrganismiLachancea kluyveri (Yeast) (Saccharomyces kluyveri)
    Taxonomic identifieri4934 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeLachancea

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 18301830Urea amidolyasePRO_0000367271Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1796 – 17961N6-biotinyllysineBy similarity

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliA5H0J2.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini625 – 1068444Biotin carboxylationAdd
    BLAST
    Domaini744 – 941198ATP-graspPROSITE-ProRule annotationAdd
    BLAST
    Domaini1753 – 182977Biotinyl-bindingAdd
    BLAST

    Sequence similaritiesi

    Belongs to the DUR1,2 family.Curated
    Contains 1 ATP-grasp domain.PROSITE-ProRule annotation
    Contains 1 biotin carboxylation domain.Curated
    Contains 1 biotinyl-binding domain.Curated

    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.

    A5H0J2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSVDTLGWSA QDWIDFHGKS TPEHSYNTLL SLLKSQKSAP EDPAWISLIN     50
    EANLAHQWKV LQSKANKQQL PLYGVPIAVK DNIDSKGSPT TAACPAFEYN 100
    PSADSTVVAL LKDAGAIVIG KTNLDQFATG LVGTRSPYGK TPCVFSDKHV 150
    SGGSSAGSAS AVGRGIVPIA LGTDTAGSGR VPAALNNLIG LKPTKGLFSC 200
    SGVVPACKSL DCVSVFAMNL SDAERCFKVM AKPDLENDEY SRPLPSNPLQ 250
    KYPKNVTIAI PKEVPWYGET ENPKLYAKAI ENLKVAGASI VTIDFEPLLA 300
    LARCLYEGAW VAERYEATKD FFATNPPESS LDPTVTSIIK TATKYDAADS 350
    FRYEYQRQGI LQKVDQTLKD IDVLCVPTCP LNPTFEEVAA EPVLVNSRQG 400
    TWTNFVNLAD MAALAVPAGF RPDGLPQGVT LIGKKFTDFA LLELANRYFK 450
    VAFPQGSRTF GKFIDRQVTT KDDELRGPDI SPEDSVKLAV VGAHLKGLPL 500
    YWQLEKVNAT YLGSPKTSKN YKLYALPKTG PILKPGLRRV GEETGSQIQL 550
    EVYSVPKENF GEFISMVPEP LGIGSVELES GEWVKSFICE EFGYTQKGTV 600
    DITKYGGFKK YIDFLKQEEA KVKKPFETVL IANRGEIAVR IIKTLKKLNI 650
    RSVAVYSDPD KYSQHVIDAD LGVALNGRTA AETYLDIDKI IKAAKDTNAQ 700
    AIIPGYGFLS ENAEFADKCV EEGIVFVGPS GEAIRKLGLK HSAREIAEKA 750
    GVPLVPGSGL VTSAKEAKEI ANKLEYPVMV KSTAGGGGIG LQKVDSENEI 800
    ERVFETVQHQ GKAYFGDSGV FLERFVENAR HVEIQMMGDG YGKAIAIGER 850
    DCSLQRRNQK IIEETPAPNL GETTRTKMRQ AAESLGSLLK YKCAGTVEFI 900
    YDERRDEFYF LEVNARLQVE HPITEMVTGL DLVEWMLRIA ADDAPDFESA 950
    NIVVTGASIE ARLYAENPAK DFRPSPGLLT DVHFPEWARV DTWVSKGTTV 1000
    SAEYDPTLAK IIVHGKDRND AIMKMNKALN ETVVYGCITN IDYLRSIASS 1050
    EMFKTAKVAT KILDSYDYKP CAFEVTSPGA YTTVQDYPGR VGYWRIGVPP 1100
    SGPMDAYSFR LANRIVGNHY KAPAIELTLN GPKILFHTET IIAISGGIAA 1150
    CSLNDKPIEQ NKPIQVNRGD HLAIGKLSVG CRAYLAIRGG IDVPEYLGSR 1200
    STFALGNMGG YNGRVLKLGD VLFLNQPELA SSSLPGPAYE PQAPPANLLP 1250
    KISDDKEWTI GVTCGPHGSP DFFKPESVEE FFSEKWKVHY NSNRFGVRLI 1300
    GPKPKWARKD GGEGGLHPSN AHDYVYSLGA INFTGDEPVI ITSDGPSLGG 1350
    FVCQAVVPEA ELWKVGQVKP GDSIQFVPIS YQVARQLKES QDAAIETLED 1400
    GKLQTLTSDL ILPTYEDPVL VQLPKKSNLS PKVTYRQAGD RYILVEYGEN 1450
    QMDLNIAYRI NQLINLVGKH KTVGIVEMSQ GVRSVLIEYD GYKISQGALL 1500
    DTLVAYESEI QFDKNWSIKS KIFKLPLAFE DSKTLECVTR YQETIRSKAP 1550
    WLPNNVDFVA EVNDITHKDV ENMLYSARFL VLGLGDVFLG APCAVPLDPR 1600
    HRFLGSKYNP SRTYTKNGVV GIGGMYMCIY AMDSPGGYQL VGRTIPIWDK 1650
    LKLGSHSQEH PWLLTPFDQV EFYPVSEEEL DRFTEDCENG KFPVQVEESV 1700
    FDHKNYLKWI NENIESITEF QKSQGGAKAD EFARLIQVAN QELESSTTNK 1750
    SAVEEEYPED AEMVYSEYSG RFWKPMVSAG DTVTKGDGLV IVEAMKTEMV 1800
    VPAKKSGKVL KIVHKNGDMV DAGDLVAVIQ 1830
    Length:1,830
    Mass (Da):201,131
    Last modified:June 12, 2007 - v1
    Checksum:iC5D1ED66A5F4F10D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ512718 Genomic DNA. Translation: ABF58890.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    DQ512718 Genomic DNA. Translation: ABF58890.1 .

    3D structure databases

    ProteinModelPortali A5H0J2.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    UniPathwayi UPA00258 ; UER00371 .
    UPA00258 ; UER00372 .

    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. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.

    Entry informationi

    Entry nameiDUR1_LACKL
    AccessioniPrimary (citable) accession number: A5H0J2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 24, 2009
    Last sequence update: June 12, 2007
    Last modified: October 1, 2014
    This is version 56 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Multifunctional enzyme

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3