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P32528 (DUR1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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

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
Ordered Locus Names:YBR208C
ORF Names:YBR1448
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length1835 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolysis of urea to ammonia and CO2.

Catalytic activity

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

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

Cofactor

Biotin.

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.

Induction

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

Miscellaneous

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

Sequence similarities

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 – 18351835Urea amidolyase
PRO_0000146832

Regions

Domain632 – 1075444Biotin carboxylation
Domain751 – 948198ATP-grasp
Domain1755 – 183581Biotinyl-binding
Nucleotide binding122 – 1298ATP Potential

Sites

Binding site7471ATP By similarity
Binding site8301ATP By similarity
Binding site8651ATP By similarity

Amino acid modifications

Modified residue8031Phosphoserine Ref.6
Modified residue17981N6-biotinyllysine

Experimental info

Sequence conflict961P → R in AAC41643. Ref.1
Sequence conflict256 – 2583LKK → KKN in AAC41643. Ref.1
Sequence conflict4591I → M in AAC41643. Ref.1
Sequence conflict8301E → K in AAC41643. Ref.1
Sequence conflict13951D → E in AAC41643. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P32528 [UniParc].

Last modified October 1, 1994. Version 2.
Checksum: F52B0DD0FE42CD65

FASTA1,835201,832
        10         20         30         40         50         60 
MTVSSDTTAE ISLGWSIQDW IDFHKSSSSQ ASLRLLESLL DSQNVAPVDN AWISLISKEN 

        70         80         90        100        110        120 
LLHQFQILKS RENKETLPLY GVPIAVKDNI DVRGLPTTAA CPSFAYEPSK DSKVVELLRN 

       130        140        150        160        170        180 
AGAIIVGKTN LDQFATGLVG TRSPYGKTPC AFSKEHVSGG SSAGSASVVA RGIVPIALGT 

       190        200        210        220        230        240 
DTAGSGRVPA ALNNLIGLKP TKGVFSCQGV VPACKSLDCV SIFALNLSDA ERCFRIMCQP 

       250        260        270        280        290        300 
DPDNDEYSRP YVSNPLKKFS SNVTIAIPKN IPWYGETKNP VLFSNAVENL SRTGANVIEI 

       310        320        330        340        350        360 
DFEPLLELAR CLYEGTWVAE RYQAIQSFLD SKPPKESLDP TVISIIEGAK KYSAVDCFSF 

       370        380        390        400        410        420 
EYKRQGILQK VRRLLESVDV LCVPTCPLNP TMQQVADEPV LVNSRQGTWT NFVNLADLAA 

       430        440        450        460        470        480 
LAVPAGFRDD GLPNGITLIG KKFTDYALLE LANRYFQNIF PNGSRTYGTF TSSSVKPAND 

       490        500        510        520        530        540 
QLVGPDYDPS TSIKLAVVGA HLKGLPLHWQ LEKVNATYLC TTKTSKAYQL FALPKNGPVL 

       550        560        570        580        590        600 
KPGLRRVQDS NGSQIELEVY SVPKELFGAF ISMVPEPLGI GSVELESGEW IKSFICEESG 

       610        620        630        640        650        660 
YKAKGTVDIT KYGGFRAYFE MLKKKESQKK KLFDTVLIAN RGEIAVRIIK TLKKLGIRSV 

       670        680        690        700        710        720 
AVYSDPDKYS QHVTDADVSV PLHGTTAAQT YLDMNKIIDA AKQTNAQAII PGYGFLSENA 

       730        740        750        760        770        780 
DFSDACTSAG ITFVGPSGDI IRGLGLKHSA RQIAQKAGVP LVPGSLLITS VEEAKKVAAE 

       790        800        810        820        830        840 
LEYPVMVKST AGGGGIGLQK VDSEEDIEHI FETVKHQGET FFGDAGVFLE RFIENARHVE 

       850        860        870        880        890        900 
VQLMGDGFGK AIALGERDCS LQRRNQKVIE ETPAPNLPEK TRLALRKAAE SLGSLLNYKC 

       910        920        930        940        950        960 
AGTVEFIYDE KKDEFYFLEV NTRLQVEHPI TEMVTGLDLV EWMIRIAAND APDFDSTKVE 

       970        980        990       1000       1010       1020 
VNGVSMEARL YAENPLKNFR PSPGLLVDVK FPDWARVDTW VKKGTNISPE YDPTLAKIIV 

      1030       1040       1050       1060       1070       1080 
HGKDRDDAIS KLNQALEETK VYGCITNIDY LKSIITSDFF AKAKVSTNIL NSYQYEPTAI 

      1090       1100       1110       1120       1130       1140 
EITLPGAHTS IQDYPGRVGY WRIGVPPSGP MDAYSFRLAN RIVGNDYRTP AIEVTLTGPS 

      1150       1160       1170       1180       1190       1200 
IVFHCETVIA ITGGTALCTL DGQEIPQHKP VEVKRGSTLS IGKLTSGCRA YLGIRGGIDV 

      1210       1220       1230       1240       1250       1260 
PKYLGSYSTF TLGNVGGYNG RVLKLGDVLF LPSNEENKSV ECLPQNIPQS LIPQISETKE 

      1270       1280       1290       1300       1310       1320 
WRIGVTCGPH GSPDFFKPES IEEFFSEKWK VHYNSNRFGV RLIGPKPKWA RSNGGEGGMH 

      1330       1340       1350       1360       1370       1380 
PSNTHDYVYS LGAINFTGDE PVIITCDGPS LGGFVCQAVV PEAELWKVGQ VKPGDSIQFV 

      1390       1400       1410       1420       1430       1440 
PLSYESSRSL KESQDVAIKS LDGTKLRRLD SVSILPSFET PILAQMEKVN ELSPKVVYRQ 

      1450       1460       1470       1480       1490       1500 
AGDRYVLVEY GDNEMNFNIS YRIECLISLV KKNKTIGIVE MSQGVRSVLI EFDGYKVTQK 

      1510       1520       1530       1540       1550       1560 
ELLKVLVAYE TEIQFDENWK ITSNIIRLPM AFEDSKTLAC VQRYQETIRS SAPWLPNNVD 

      1570       1580       1590       1600       1610       1620 
FIANVNGISR NEVYDMLYSA RFMVLGLGDV FLGSPCAVPL DPRHRFLGSK YNPSRTYTER 

      1630       1640       1650       1660       1670       1680 
GAVGIGGMYM CIYAANSPGG YQLVGRTIPI WDKLCLAASS EVPWLMNPFD QVEFYPVSEE 

      1690       1700       1710       1720       1730       1740 
DLDKMTEDCD NGVYKVNIEK SVFDHQEYLR WINANKDSIT AFQEGQLGER AEEFAKLIQN 

      1750       1760       1770       1780       1790       1800 
ANSELKESVT VKPDEEEDFP EGAEIVYSEY SGRFWKSIAS VGDVIEAGQG LLIIEAMKAE 

      1810       1820       1830 
MIISAPKSGK IIKICHGNGD MVDSGDIVAV IETLA 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
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]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M64926 Genomic DNA. Translation: AAC41643.1.
Z36077 Genomic DNA. Translation: CAA85172.1.
Z21487 Genomic DNA. Translation: CAA79695.1.
BK006936 Genomic DNA. Translation: DAA07325.1.
PIRS46082.
RefSeqNP_009767.1. NM_001178556.1.

3D structure databases

ProteinModelPortalP32528.
SMRP32528. Positions 10-623, 630-1379, 1437-1680, 1735-1832.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid32904. 18 interactions.
DIPDIP-6296N.
IntActP32528. 2 interactions.
MINTMINT-664989.
STRING4932.YBR208C.

Proteomic databases

MaxQBP32528.
PaxDbP32528.
PeptideAtlasP32528.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYBR208C; YBR208C; YBR208C.
GeneID852507.
KEGGsce:YBR208C.

Organism-specific databases

CYGDYBR208c.
SGDS000000412. DUR1,2.

Phylogenomic databases

eggNOGCOG0511.
GeneTreeENSGT00550000074675.
HOGENOMHOG000251581.
KOK14541.
OMAVEWMVRQ.
OrthoDBEOG7PGDZZ.

Enzyme and pathway databases

BioCycMetaCyc:YBR208C-MONOMER.
YEAST:YBR208C-MONOMER.
BRENDA6.3.4.6. 984.
UniPathwayUPA00258; UER00371.
UPA00258; UER00372.

Gene expression databases

GenevestigatorP32528.

Family and domain databases

Gene3D2.40.100.10. 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.
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.
IPR029000. Cyclophilin-like_dom.
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]
SUPFAMSSF50891. SSF50891. 2 hits.
SSF51230. 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...

Other

NextBio971522.

Entry information

Entry nameDUR1_YEAST
AccessionPrimary (citable) accession number: P32528
Secondary accession number(s): D6VQK5
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1994
Last modified: June 11, 2014
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome II

Yeast (Saccharomyces cerevisiae) chromosome II: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways