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A5H0J2 (DUR1_LACKL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Urea amidolyase
Alternative name(s):
Pyrimidine-degrading protein 13,15
Uracil catabolism protein 3,5

Including the following 2 domains:

  1. Urea carboxylase
    EC=6.3.4.6
  2. Allophanate hydrolase
    EC=3.5.1.54
Gene names
Name:DUR1,2
Synonyms:PYD13,15, URC3,5
OrganismLachancea kluyveri (Yeast) (Saccharomyces kluyveri)
Taxonomic identifier4934 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeLachancea

Protein attributes

Sequence length1830 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

ATP + urea + HCO3- = ADP + phosphate + urea-1-carboxylate.

Urea-1-carboxylate + H2O = 2 CO2 + 2 NH3.

Cofactor

Biotin By similarity.

Pathway

Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (allophanate route): step 1/2.

Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (allophanate route): step 2/2.

Subunit structure

Monomer By similarity.

Sequence similarities

Belongs to the DUR1,2 family.

Contains 1 ATP-grasp domain.

Contains 1 biotin carboxylation domain.

Contains 1 biotinyl-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18301830Urea amidolyase
PRO_0000367271

Regions

Domain625 – 1068444Biotin carboxylation
Domain744 – 941198ATP-grasp
Domain1753 – 182977Biotinyl-binding
Nucleotide binding115 – 1228ATP Potential

Sites

Binding site7401ATP By similarity
Binding site8231ATP By similarity
Binding site8581ATP By similarity

Amino acid modifications

Modified residue17961N6-biotinyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A5H0J2 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: C5D1ED66A5F4F10D

FASTA1,830201,131
        10         20         30         40         50         60 
MSVDTLGWSA QDWIDFHGKS TPEHSYNTLL SLLKSQKSAP EDPAWISLIN EANLAHQWKV 

        70         80         90        100        110        120 
LQSKANKQQL PLYGVPIAVK DNIDSKGSPT TAACPAFEYN PSADSTVVAL LKDAGAIVIG 

       130        140        150        160        170        180 
KTNLDQFATG LVGTRSPYGK TPCVFSDKHV SGGSSAGSAS AVGRGIVPIA LGTDTAGSGR 

       190        200        210        220        230        240 
VPAALNNLIG LKPTKGLFSC SGVVPACKSL DCVSVFAMNL SDAERCFKVM AKPDLENDEY 

       250        260        270        280        290        300 
SRPLPSNPLQ KYPKNVTIAI PKEVPWYGET ENPKLYAKAI ENLKVAGASI VTIDFEPLLA 

       310        320        330        340        350        360 
LARCLYEGAW VAERYEATKD FFATNPPESS LDPTVTSIIK TATKYDAADS FRYEYQRQGI 

       370        380        390        400        410        420 
LQKVDQTLKD IDVLCVPTCP LNPTFEEVAA EPVLVNSRQG TWTNFVNLAD MAALAVPAGF 

       430        440        450        460        470        480 
RPDGLPQGVT LIGKKFTDFA LLELANRYFK VAFPQGSRTF GKFIDRQVTT KDDELRGPDI 

       490        500        510        520        530        540 
SPEDSVKLAV VGAHLKGLPL YWQLEKVNAT YLGSPKTSKN YKLYALPKTG PILKPGLRRV 

       550        560        570        580        590        600 
GEETGSQIQL EVYSVPKENF GEFISMVPEP LGIGSVELES GEWVKSFICE EFGYTQKGTV 

       610        620        630        640        650        660 
DITKYGGFKK YIDFLKQEEA KVKKPFETVL IANRGEIAVR IIKTLKKLNI RSVAVYSDPD 

       670        680        690        700        710        720 
KYSQHVIDAD LGVALNGRTA AETYLDIDKI IKAAKDTNAQ AIIPGYGFLS ENAEFADKCV 

       730        740        750        760        770        780 
EEGIVFVGPS GEAIRKLGLK HSAREIAEKA GVPLVPGSGL VTSAKEAKEI ANKLEYPVMV 

       790        800        810        820        830        840 
KSTAGGGGIG LQKVDSENEI ERVFETVQHQ GKAYFGDSGV FLERFVENAR HVEIQMMGDG 

       850        860        870        880        890        900 
YGKAIAIGER DCSLQRRNQK IIEETPAPNL GETTRTKMRQ AAESLGSLLK YKCAGTVEFI 

       910        920        930        940        950        960 
YDERRDEFYF LEVNARLQVE HPITEMVTGL DLVEWMLRIA ADDAPDFESA NIVVTGASIE 

       970        980        990       1000       1010       1020 
ARLYAENPAK DFRPSPGLLT DVHFPEWARV DTWVSKGTTV SAEYDPTLAK IIVHGKDRND 

      1030       1040       1050       1060       1070       1080 
AIMKMNKALN ETVVYGCITN IDYLRSIASS EMFKTAKVAT KILDSYDYKP CAFEVTSPGA 

      1090       1100       1110       1120       1130       1140 
YTTVQDYPGR VGYWRIGVPP SGPMDAYSFR LANRIVGNHY KAPAIELTLN GPKILFHTET 

      1150       1160       1170       1180       1190       1200 
IIAISGGIAA CSLNDKPIEQ NKPIQVNRGD HLAIGKLSVG CRAYLAIRGG IDVPEYLGSR 

      1210       1220       1230       1240       1250       1260 
STFALGNMGG YNGRVLKLGD VLFLNQPELA SSSLPGPAYE PQAPPANLLP KISDDKEWTI 

      1270       1280       1290       1300       1310       1320 
GVTCGPHGSP DFFKPESVEE FFSEKWKVHY NSNRFGVRLI GPKPKWARKD GGEGGLHPSN 

      1330       1340       1350       1360       1370       1380 
AHDYVYSLGA INFTGDEPVI ITSDGPSLGG FVCQAVVPEA ELWKVGQVKP GDSIQFVPIS 

      1390       1400       1410       1420       1430       1440 
YQVARQLKES QDAAIETLED GKLQTLTSDL ILPTYEDPVL VQLPKKSNLS PKVTYRQAGD 

      1450       1460       1470       1480       1490       1500 
RYILVEYGEN QMDLNIAYRI NQLINLVGKH KTVGIVEMSQ GVRSVLIEYD GYKISQGALL 

      1510       1520       1530       1540       1550       1560 
DTLVAYESEI QFDKNWSIKS KIFKLPLAFE DSKTLECVTR YQETIRSKAP WLPNNVDFVA 

      1570       1580       1590       1600       1610       1620 
EVNDITHKDV ENMLYSARFL VLGLGDVFLG APCAVPLDPR HRFLGSKYNP SRTYTKNGVV 

      1630       1640       1650       1660       1670       1680 
GIGGMYMCIY AMDSPGGYQL VGRTIPIWDK LKLGSHSQEH PWLLTPFDQV EFYPVSEEEL 

      1690       1700       1710       1720       1730       1740 
DRFTEDCENG KFPVQVEESV FDHKNYLKWI NENIESITEF QKSQGGAKAD EFARLIQVAN 

      1750       1760       1770       1780       1790       1800 
QELESSTTNK SAVEEEYPED AEMVYSEYSG RFWKPMVSAG DTVTKGDGLV IVEAMKTEMV 

      1810       1820       1830 
VPAKKSGKVL KIVHKNGDMV DAGDLVAVIQ 

« Hide

References

[1]"A second pathway to degrade pyrimidine nucleic acid precursors in eukaryotes."
Andersen G., Bjoernberg O., Polakova S., Pynyaha Y., Rasmussen A., Moeller K., Hofer A., Moritz T., Sandrini M.P., Merico A.M., Compagno C., Aekerlund H.E., Gojkovic Z., Piskur J.
J. Mol. Biol. 380:656-666(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ512718 Genomic DNA. Translation: ABF58890.1.

3D structure databases

ProteinModelPortalA5H0J2.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00258; UER00371.
UPA00258; UER00372.

Family and domain databases

Gene3D3.30.1360.40. 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.
InterProIPR003833. 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.
IPR016185. PreATP-grasp_dom.
IPR011054. Rudment_hybrid_motif.
IPR011053. Single_hybrid_motif.
IPR014084. Urea_COase.
[Graphical view]
PfamPF02682. 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]
SMARTSM00796. AHS1. 1 hit.
SM00797. AHS2. 1 hit.
SM00878. Biotin_carb_C. 1 hit.
[Graphical view]
SUPFAMSSF51230. SSF51230. 1 hit.
SSF51246. SSF51246. 1 hit.
SSF52440. SSF52440. 1 hit.
SSF75304. SSF75304. 1 hit.
TIGRFAMsTIGR02713. allophanate_hyd. 1 hit.
TIGR00724. urea_amlyse_rel. 1 hit.
TIGR02712. urea_carbox. 1 hit.
PROSITEPS50975. 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]
ProtoNetSearch...

Entry information

Entry nameDUR1_LACKL
AccessionPrimary (citable) accession number: A5H0J2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: June 12, 2007
Last modified: April 16, 2014
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways