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P32528

- DUR1_YEAST

UniProt

P32528 - DUR1_YEAST

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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

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
Complete GO annotation...

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.
InParanoidiP32528.
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

        10         20         30         40         50
MTVSSDTTAE ISLGWSIQDW IDFHKSSSSQ ASLRLLESLL DSQNVAPVDN
60 70 80 90 100
AWISLISKEN LLHQFQILKS RENKETLPLY GVPIAVKDNI DVRGLPTTAA
110 120 130 140 150
CPSFAYEPSK DSKVVELLRN AGAIIVGKTN LDQFATGLVG TRSPYGKTPC
160 170 180 190 200
AFSKEHVSGG SSAGSASVVA RGIVPIALGT DTAGSGRVPA ALNNLIGLKP
210 220 230 240 250
TKGVFSCQGV VPACKSLDCV SIFALNLSDA ERCFRIMCQP DPDNDEYSRP
260 270 280 290 300
YVSNPLKKFS SNVTIAIPKN IPWYGETKNP VLFSNAVENL SRTGANVIEI
310 320 330 340 350
DFEPLLELAR CLYEGTWVAE RYQAIQSFLD SKPPKESLDP TVISIIEGAK
360 370 380 390 400
KYSAVDCFSF EYKRQGILQK VRRLLESVDV LCVPTCPLNP TMQQVADEPV
410 420 430 440 450
LVNSRQGTWT NFVNLADLAA LAVPAGFRDD GLPNGITLIG KKFTDYALLE
460 470 480 490 500
LANRYFQNIF PNGSRTYGTF TSSSVKPAND QLVGPDYDPS TSIKLAVVGA
510 520 530 540 550
HLKGLPLHWQ LEKVNATYLC TTKTSKAYQL FALPKNGPVL KPGLRRVQDS
560 570 580 590 600
NGSQIELEVY SVPKELFGAF ISMVPEPLGI GSVELESGEW IKSFICEESG
610 620 630 640 650
YKAKGTVDIT KYGGFRAYFE MLKKKESQKK KLFDTVLIAN RGEIAVRIIK
660 670 680 690 700
TLKKLGIRSV AVYSDPDKYS QHVTDADVSV PLHGTTAAQT YLDMNKIIDA
710 720 730 740 750
AKQTNAQAII PGYGFLSENA DFSDACTSAG ITFVGPSGDI IRGLGLKHSA
760 770 780 790 800
RQIAQKAGVP LVPGSLLITS VEEAKKVAAE LEYPVMVKST AGGGGIGLQK
810 820 830 840 850
VDSEEDIEHI FETVKHQGET FFGDAGVFLE RFIENARHVE VQLMGDGFGK
860 870 880 890 900
AIALGERDCS LQRRNQKVIE ETPAPNLPEK TRLALRKAAE SLGSLLNYKC
910 920 930 940 950
AGTVEFIYDE KKDEFYFLEV NTRLQVEHPI TEMVTGLDLV EWMIRIAAND
960 970 980 990 1000
APDFDSTKVE VNGVSMEARL YAENPLKNFR PSPGLLVDVK FPDWARVDTW
1010 1020 1030 1040 1050
VKKGTNISPE YDPTLAKIIV HGKDRDDAIS KLNQALEETK VYGCITNIDY
1060 1070 1080 1090 1100
LKSIITSDFF AKAKVSTNIL NSYQYEPTAI EITLPGAHTS IQDYPGRVGY
1110 1120 1130 1140 1150
WRIGVPPSGP MDAYSFRLAN RIVGNDYRTP AIEVTLTGPS IVFHCETVIA
1160 1170 1180 1190 1200
ITGGTALCTL DGQEIPQHKP VEVKRGSTLS IGKLTSGCRA YLGIRGGIDV
1210 1220 1230 1240 1250
PKYLGSYSTF TLGNVGGYNG RVLKLGDVLF LPSNEENKSV ECLPQNIPQS
1260 1270 1280 1290 1300
LIPQISETKE WRIGVTCGPH GSPDFFKPES IEEFFSEKWK VHYNSNRFGV
1310 1320 1330 1340 1350
RLIGPKPKWA RSNGGEGGMH PSNTHDYVYS LGAINFTGDE PVIITCDGPS
1360 1370 1380 1390 1400
LGGFVCQAVV PEAELWKVGQ VKPGDSIQFV PLSYESSRSL KESQDVAIKS
1410 1420 1430 1440 1450
LDGTKLRRLD SVSILPSFET PILAQMEKVN ELSPKVVYRQ AGDRYVLVEY
1460 1470 1480 1490 1500
GDNEMNFNIS YRIECLISLV KKNKTIGIVE MSQGVRSVLI EFDGYKVTQK
1510 1520 1530 1540 1550
ELLKVLVAYE TEIQFDENWK ITSNIIRLPM AFEDSKTLAC VQRYQETIRS
1560 1570 1580 1590 1600
SAPWLPNNVD FIANVNGISR NEVYDMLYSA RFMVLGLGDV FLGSPCAVPL
1610 1620 1630 1640 1650
DPRHRFLGSK YNPSRTYTER GAVGIGGMYM CIYAANSPGG YQLVGRTIPI
1660 1670 1680 1690 1700
WDKLCLAASS EVPWLMNPFD QVEFYPVSEE DLDKMTEDCD NGVYKVNIEK
1710 1720 1730 1740 1750
SVFDHQEYLR WINANKDSIT AFQEGQLGER AEEFAKLIQN ANSELKESVT
1760 1770 1780 1790 1800
VKPDEEEDFP EGAEIVYSEY SGRFWKSIAS VGDVIEAGQG LLIIEAMKAE
1810 1820 1830
MIISAPKSGK IIKICHGNGD MVDSGDIVAV IETLA
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.
InParanoidi P32528.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 148 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