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Protein

Protein URA2

Gene

URA2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

This protein is a "fusion" protein encoding three enzymatic activities of the pyrimidine pathway (GATase, CPSase, and ATCase).

Miscellaneous

GATase (glutamine amidotransferase) and CPSase (carbamoyl phosphate synthase) form together the glutamine-dependent CPSase (GD-CPSase) (EC 6.3.5.5).
In eukaryotes EC 6.3.5.5 is synthesized by two pathway-specific (arginine and pyrimidine) genes under separate control.
Present with 11000 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

2 ATP + L-glutamine + HCO3- + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate.
Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate.

Pathwayi: UMP biosynthesis via de novo pathway

This protein is involved in step 1 and 2 of the subpathway that synthesizes (S)-dihydroorotate from bicarbonate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Protein URA2 (URA2)
  2. Protein URA2 (URA2)
  3. Dihydroorotase (URA4)
This subpathway is part of the pathway UMP biosynthesis via de novo pathway, which is itself part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-dihydroorotate from bicarbonate, the pathway UMP biosynthesis via de novo pathway and in Pyrimidine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei302For GATase activityBy similarity1
Active sitei386For GATase activityBy similarity1
Active sitei388For GATase activityBy similarity1

GO - Molecular functioni

GO - Biological processi

  • 'de novo' pyrimidine nucleobase biosynthetic process Source: SGD
  • 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
  • arginine biosynthetic process Source: GO_Central
  • glutamine metabolic process Source: SGD
  • negative regulation of pyrimidine nucleobase metabolic process Source: SGD
  • urea cycle Source: GO_Central

Keywordsi

Molecular functionLigase, Multifunctional enzyme, Transferase
Biological processPyrimidine biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:YJL130C-MONOMER
YEAST:YJL130C-MONOMER
BRENDAi6.3.5.5 984
UniPathwayiUPA00070; UER00115
UPA00070; UER00116

Protein family/group databases

MEROPSiC26.956

Names & Taxonomyi

Protein namesi
Recommended name:
Protein URA2
Including the following 2 domains:
Glutamine-dependent carbamoyl-phosphate synthase (EC:6.3.5.5)
Aspartate carbamoyltransferase (EC:2.1.3.2)
Gene namesi
Name:URA2
Ordered Locus Names:YJL130C
ORF Names:J0686
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome X

Organism-specific databases

EuPathDBiFungiDB:YJL130C
SGDiS000003666 URA2

Subcellular locationi

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001995112 – 2214Protein URA2Add BLAST2213

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1
Cross-linki1853Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Modified residuei1857Phosphoserine; by PKACombined sources1 Publication1

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP07259
PaxDbiP07259
PRIDEiP07259

PTM databases

CarbonylDBiP07259
iPTMnetiP07259

Interactioni

Protein-protein interaction databases

BioGridi33626, 170 interactors
DIPiDIP-7215N
IntActiP07259, 463 interactors
MINTiP07259
STRINGi4932.YJL130C

Structurei

3D structure databases

SMRiP07259
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini228 – 413Glutamine amidotransferase type-1Add BLAST186
Domaini562 – 754ATP-grasp 1Add BLAST193
Domaini1099 – 1290ATP-grasp 2Add BLAST192
Domaini1356 – 1508MGS-likePROSITE-ProRule annotationAdd BLAST153

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 400GATase (Glutamine amidotransferase)Add BLAST399
Regioni401 – 440LinkerAdd BLAST40
Regioni441 – 1482CPSase (Carbamoyl-phosphate synthase)Add BLAST1042
Regioni1483 – 1492Linker10
Regioni1493 – 1821Defective DHOase domainAdd BLAST329
Regioni1822 – 1909LinkerAdd BLAST88
Regioni1910 – 2214ATCase (Aspartate transcarbamylase)Add BLAST305

Domaini

The DHOase domain is defective.

Sequence similaritiesi

In the central section; belongs to the metallo-dependent hydrolases superfamily. DHOase family. CAD subfamily.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

GeneTreeiENSGT00910000145257
HOGENOMiHOG000234584
InParanoidiP07259
KOiK11541
OMAiNIPCTSM
OrthoDBiEOG092C0957

Family and domain databases

CDDicd01744 GATase1_CPSase, 1 hit
Gene3Di1.10.1030.10, 1 hit
3.30.1490.20, 1 hit
3.40.50.1370, 3 hits
3.40.50.1380, 1 hit
3.40.50.880, 1 hit
3.50.30.20, 1 hit
HAMAPiMF_00001 Asp_carb_tr, 1 hit
MF_01209 CPSase_S_chain, 1 hit
InterProiView protein in InterPro
IPR006132 Asp/Orn_carbamoyltranf_P-bd
IPR006130 Asp/Orn_carbamoylTrfase
IPR036901 Asp/Orn_carbamoylTrfase_sf
IPR002082 Asp_carbamoyltransf
IPR006131 Asp_carbamoyltransf_Asp/Orn-bd
IPR011761 ATP-grasp
IPR013815 ATP_grasp_subdomain_1
IPR006275 CarbamoylP_synth_lsu
IPR005480 CarbamoylP_synth_lsu_oligo
IPR036897 CarbamoylP_synth_lsu_oligo_sf
IPR006274 CarbamoylP_synth_ssu
IPR002474 CarbamoylP_synth_ssu_N
IPR036480 CarbP_synth_ssu_N_sf
IPR005479 CbamoylP_synth_lsu-like_ATP-bd
IPR005483 CbamoylP_synth_lsu_CPSase_dom
IPR029062 Class_I_gatase-like
IPR035686 CPSase_GATase1
IPR017926 GATASE
IPR032466 Metal_Hydrolase
IPR011607 MGS-like_dom
IPR036914 MGS-like_dom_sf
IPR016185 PreATP-grasp_dom_sf
PfamiView protein in Pfam
PF02786 CPSase_L_D2, 2 hits
PF02787 CPSase_L_D3, 1 hit
PF00988 CPSase_sm_chain, 1 hit
PF00117 GATase, 1 hit
PF02142 MGS, 1 hit
PF00185 OTCace, 1 hit
PF02729 OTCace_N, 1 hit
PRINTSiPR00100 AOTCASE
PR00101 ATCASE
PR00098 CPSASE
SMARTiView protein in SMART
SM01096 CPSase_L_D3, 1 hit
SM01097 CPSase_sm_chain, 1 hit
SM00851 MGS, 1 hit
SUPFAMiSSF48108 SSF48108, 1 hit
SSF51556 SSF51556, 1 hit
SSF52021 SSF52021, 1 hit
SSF52317 SSF52317, 1 hit
SSF52335 SSF52335, 1 hit
SSF52440 SSF52440, 2 hits
SSF53671 SSF53671, 1 hit
TIGRFAMsiTIGR00670 asp_carb_tr, 1 hit
TIGR01369 CPSaseII_lrg, 1 hit
TIGR01368 CPSaseIIsmall, 1 hit
PROSITEiView protein in PROSITE
PS50975 ATP_GRASP, 2 hits
PS00097 CARBAMOYLTRANSFERASE, 1 hit
PS00866 CPSASE_1, 2 hits
PS00867 CPSASE_2, 2 hits
PS51273 GATASE_TYPE_1, 1 hit
PS51855 MGS, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P07259-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATIAPTAPI TPPMESTGDR LVTLELKDGT VLQGYSFGAE KSVAGELVFQ
60 70 80 90 100
TGMVGYPESV TDPSYEGQIL VITYPLVGNY GVPDMHLRDE LVEELPRYFE
110 120 130 140 150
SNRIHIAGLV ISHYTDEYSH YLAKSSLGKW LQNEGIPAVY GVDTRSLTKH
160 170 180 190 200
LRDAGSMLGR LSLEKSGSDR TISRSSSWRS AFDVPEWVDP NVQNLVSKVS
210 220 230 240 250
INEPKLYVPP ADNKHIELQT GPDGKVLRIL AIDVGMKYNQ IRCFIKRGVE
260 270 280 290 300
LKVVPWNYDF TKEDYDGLFI SNGPGDPSVL DDLSQRLSNV LEAKKTPVFG
310 320 330 340 350
ICLGHQLIAR AAGASTLKLK FGNRGHNIPC TSTISGRCYI TSQNHGFAVD
360 370 380 390 400
VDTLTSGWKP LFVNANDDSN EGIYHSELPY FSVQFHPEST PGPRDTEFLF
410 420 430 440 450
DVFIQAVKEF KYTQVLKPIA FPGGLLEDNV KAHPRIEAKK VLVLGSGGLS
460 470 480 490 500
IGQAGEFDYS GSQAIKALKE EGIYTILINP NIATIQTSKG LADKVYFVPV
510 520 530 540 550
TAEFVRKVIL HERPDAIYVT FGGQTALSVG IAMKDEFEAL GVKVLGTPID
560 570 580 590 600
TIITTEDREL FSNAIDEINE KCAKSQAANS VDEALAAVKE IGFPVIVRAA
610 620 630 640 650
YALGGLGSGF ANNEKELVDL CNVAFSSSPQ VLVEKSMKGW KEVEYEVVRD
660 670 680 690 700
AFDNCITVCN MENFDPLGIH TGDSIVVAPS QTLSDEDYNM LRTTAVNVIR
710 720 730 740 750
HLGVVGECNI QYALNPVSKD YCIIEVNARL SRSSALASKA TGYPLAYTAA
760 770 780 790 800
KLGLNIPLNE VKNSVTKSTC ACFEPSLDYC VVKMPRWDLK KFTRVSTELS
810 820 830 840 850
SSMKSVGEVM SIGRTFEEAI QKAIRSTEYA NLGFNETDLD IDIDYELNNP
860 870 880 890 900
TDMRVFAIAN AFAKKGYSVD KVWEMTRIDK WFLNKLHDLV QFAEKISSFG
910 920 930 940 950
TKEELPSLVL RQAKQLGFDD RQIARFLDSN EVAIRRLRKE YGITPFVKQI
960 970 980 990 1000
DTVAAEFPAY TNYLYMTYNA DSHDLSFDDH GVMVLGSGVY RIGSSVEFDW
1010 1020 1030 1040 1050
CAVTAVRTLR ANNIKTIMVN YNPETVSTDY DEADRLYFET INLERVLDIY
1060 1070 1080 1090 1100
EIENSSGVVV SMGGQTSNNI AMTLHRENVK ILGTSPDMID SAENRYKFSR
1110 1120 1130 1140 1150
MLDQIGVDQP AWKELTSMDE AESFAEKVGY PVLVRPSYVL SGAAMNTVYS
1160 1170 1180 1190 1200
KNDLESYLNQ AVEVSRDYPV VITKYIENAK EIEMDAVARN GELVMHVVSE
1210 1220 1230 1240 1250
HVENAGVHSG DATLIVPPQD LAPETVDRIV VATAKIGKAL KITGPYNIQF
1260 1270 1280 1290 1300
IAKDNEIKVI ECNVRASRSF PFISKVVGVN LIELATKAIM GLPLTPYPVE
1310 1320 1330 1340 1350
KLPDDYVAVK VPQFSFPRLA GADPVLGVEM ASTGEVATFG HSKYEAYLKS
1360 1370 1380 1390 1400
LLATGFKLPK KNILLSIGSY KEKQELLSSV QKLYNMGYKL FATSGTADFL
1410 1420 1430 1440 1450
SEHGIAVQYL EVLNKDDDDQ KSEYSLTQHL ANNEIDLYIN LPSANRFRRP
1460 1470 1480 1490 1500
ASYVSKGYKT RRLAVDYSVP LVTNVKCAKL LIEAISRNIT LDVSERDAQT
1510 1520 1530 1540 1550
SHRTITLPGL INIATYVPNA SHVIKGPAEL KETTRLFLES GFTYCQLMPR
1560 1570 1580 1590 1600
SISGPVITDV ASLKAANSVS QDSSYTDFSF TIAGTAHNAH SVTQSASKVT
1610 1620 1630 1640 1650
ALFLPLRELK NKITAVAELL NQWPTEKQVI AEAKTADLAS VLLLTSLQNR
1660 1670 1680 1690 1700
SIHITGVSNK EDLALIMTVK AKDPRVTCDV NIYSLFIAQD DYPEAVFLPT
1710 1720 1730 1740 1750
KEDQEFFWNN LDSIDAFSVG ALPVALANVT GNKVDVGMGI KDSLPLLLAA
1760 1770 1780 1790 1800
VEEGKLTIDD IVLRLHDNPA KIFNIPTQDS VVEIDLDYSF RRNKRWSPFN
1810 1820 1830 1840 1850
KDMNGGIERV VYNGETLVLS GELVSPGAKG KCIVNPSPAS ITASAELQST
1860 1870 1880 1890 1900
SAKRRFSITE EAIADNLDAA EDAIPEQPLE QKLMSSRPPR ELVAPGAIQN
1910 1920 1930 1940 1950
LIRSNNPFRG RHILSIKQFK RSDFHVLFAV AQELRAAVAR EGVLDLMKGH
1960 1970 1980 1990 2000
VITTIFFEPS TRTCSSFIAA MERLGGRIVN VNPLVSSVKK GETLQDTIRT
2010 2020 2030 2040 2050
LACYSDAIVM RHSEEMSVHI AAKYSPVPII NGGNGSREHP TQAFLDLFTI
2060 2070 2080 2090 2100
REEIGTVNGI TVTFMGDLKH GRTVHSLCRL LMHYQVRINL VSPPELRLPE
2110 2120 2130 2140 2150
GLREELRKAG LLGVESIELT PHIISKTDVL YCTRVQEERF NSPEEYARLK
2160 2170 2180 2190 2200
DTYIVDNKIL AHAKENMAIM HPLPRVNEIK EEVDYDHRAA YFRQMKYGLF
2210
VRMALLAMVM GVDM
Length:2,214
Mass (Da):245,041
Last modified:September 21, 2011 - v5
Checksum:iD5A47F4E42A9B1A7
GO

Sequence cautioni

The sequence ABI95879 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti86H → D in CAA29068 (PubMed:3039294).Curated1
Sequence conflicti123A → R in CAA89425 (PubMed:8641269).Curated1
Sequence conflicti250 – 257ELKVVPWN → RIESCSMD in CAA29068 (PubMed:3039294).Curated8
Sequence conflicti270I → Y in CAA29068 (PubMed:3039294).Curated1
Sequence conflicti313 – 314GA → VQ in CAA29068 (PubMed:3039294).Curated2
Sequence conflicti372 – 373GI → RF in CAA29068 (PubMed:3039294).Curated2
Sequence conflicti394 – 402RDTEFLFDV → EIQNSCLT in CAA29068 (PubMed:3039294).Curated9
Sequence conflicti431 – 433KAH → QGT in CAA29068 (PubMed:3039294).Curated3
Sequence conflicti482I → T in CAA29068 (PubMed:3039294).Curated1
Sequence conflicti485I → N in CAA29068 (PubMed:3039294).Curated1
Sequence conflicti492A → G in CAA29068 (PubMed:3039294).Curated1
Sequence conflicti501 – 510TAEFVRKVIL → NAAKQRDVDR in CAA29068 (PubMed:3039294).Curated10
Sequence conflicti1411 – 1412EV → S in AAA35198 (PubMed:2498313).Curated2
Sequence conflicti1582I → M in AAA35198 (PubMed:2498313).Curated1
Sequence conflicti1588N → K in AAA35198 (PubMed:2498313).Curated1
Sequence conflicti1592V → G in AAA35198 (PubMed:2498313).Curated1
Sequence conflicti1595S → A in AAA35198 (PubMed:2498313).Curated1
Sequence conflicti1872Missing AA sequence (PubMed:1977585).Curated1
Sequence conflicti1937A → R in AAA68280 (PubMed:2570735).Curated1
Sequence conflicti1937A → R in AAA35198 (PubMed:2498313).Curated1
Sequence conflicti1997T → I in AAA35198 (PubMed:2498313).Curated1
Sequence conflicti2039H → L in AAA35198 (PubMed:2498313).Curated1
Sequence conflicti2158 – 2165KILAHAKE → VRSWHTQQK in AAA35198 (PubMed:2498313).Curated8

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27174 Genomic DNA Translation: AAA68280.1
Z49405 Genomic DNA Translation: CAA89425.1
X05553 Genomic DNA Translation: CAA29068.1
DQ881452 mRNA Translation: ABI95879.1 Different initiation.
EF123133 mRNA Translation: ABM97477.1
X87371 Genomic DNA Translation: CAA60825.1
D28139 Genomic DNA Translation: BAA05680.1
J04711 Genomic DNA Translation: AAA35198.1
BK006943 Genomic DNA Translation: DAA08671.2
PIRiS56911 QZBYU2
RefSeqiNP_012405.2, NM_001181563.2

Genome annotation databases

EnsemblFungiiYJL130C; YJL130C; YJL130C
GeneIDi853311
KEGGisce:YJL130C

Similar proteinsi

Entry informationi

Entry nameiPYR1_YEAST
AccessioniPrimary (citable) accession number: P07259
Secondary accession number(s): A2TBN0, D6VW55, Q06HN1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: September 21, 2011
Last modified: May 23, 2018
This is version 212 of the entry and version 5 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

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