Reviewed, UniProtKB/Swiss-Prot P07259 (PYR1_YEAST)

Names and origin

Protein names

Recommended name:
    Protein URA1
Including the following 2 domains:
    1- Recommended name:
            Glutamine-dependent carbamoyl-phosphate synthase
              EC=6.3.5.5
    2- Recommended name:
            Aspartate carbamoyltransferase
              EC=2.1.3.2

Gene names

Name:	URA2
Ordered Locus Names:	YJL130C
ORF Names:	J0686

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	2214 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	This protein is a "fusion" protein encoding three enzymatic activities of the pyrimidine pathway (GATase, CPSase, and ATCase).
Catalytic activity	2 ATP + L-glutamine + HCO3- + H2O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate. Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate.
Pathway	Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3.
Domain	The DHOase domain is defective.
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. Ref.11
Sequence similarities	In the central section; belongs to the DHOase family. Contains 2 ATP-grasp domains. Contains 1 glutamine amidotransferase type-1 domain.

Ontologies

Keywords
Biological process	Pyrimidine biosynthesis
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Multifunctional enzyme
Gene Ontology (GO)
Biological process	'de novo' pyrimidine base biosynthetic process Inferred from direct assay. Source: SGD glutamine metabolic process Inferred from direct assay. Source: SGD negative regulation of pyrimidine base metabolic process Inferred from direct assay. Source: SGD pyrimidine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	integral to membrane Inferred from direct assay. Source: SGD mitochondrion Inferred from direct assay. Source: SGD
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW amino acid binding Inferred from electronic annotation. Source: InterPro aspartate carbamoyltransferase activity Inferred from direct assay. Source: SGD carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Inferred from direct assay. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PDS5	Q04264	1	EBI-14372,EBI-13077
STI1	P15705	1	EBI-14372,EBI-18418

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2214	2214	Protein URA1		PRO_0000199511
Regions
	Domain	228 – 413	186	Glutamine amidotransferase type-1
	Domain	562 – 754	193	ATP-grasp 1
	Domain	1099 – 1290	192	ATP-grasp 2
	Region	1 – 400	400	GATase (Glutamine amidotransferase)
	Region	401 – 440	40	Linker
	Region	441 – 1482	1042	CPSase (Carbamoyl-phosphate synthase)
	Region	1483 – 1492	10	Linker
	Region	1493 – 1821	329	Defective DHOase domain
	Region	1822 – 1909	88	Linker
	Region	1910 – 2214	305	ATCase (Aspartate transcarbamylase)
Sites
	Active site	302	1	For GATase activity By similarity
	Active site	386	1	For GATase activity By similarity
	Active site	388	1	For GATase activity By similarity
Amino acid modifications
	Modified residue	1452	1	Phosphoserine Ref.16
	Modified residue	1453	1	Phosphotyrosine Ref.16
	Modified residue	1553	1	Phosphoserine Ref.16
	Modified residue	1857	1	Phosphoserine; by PKA Ref.16 Ref.10 Ref.12 Ref.13 Ref.14
	Modified residue	1859	1	Phosphothreonine Ref.16 Ref.15
	Modified residue	1986	1	Phosphoserine Ref.16
	Modified residue	2142	1	Phosphoserine Ref.16
Experimental info
	Sequence conflict	86	1	H → D in CAA29068. Ref.3
	Sequence conflict	123	1	R → A in AAA68280. Ref.1
	Sequence conflict	123	1	R → A in CAA29068. Ref.3
	Sequence conflict	250 – 257	8	ELKVVPWN → RIESCSMD in CAA29068. Ref.3
	Sequence conflict	270	1	I → Y in CAA29068. Ref.3
	Sequence conflict	313 – 314	2	GA → VQ in CAA29068. Ref.3
	Sequence conflict	372 – 373	2	GI → RF in CAA29068. Ref.3
	Sequence conflict	394 – 402	9	RDTEFLFDV → EIQNSCLT in CAA29068. Ref.3
	Sequence conflict	431 – 433	3	KAH → QGT in CAA29068. Ref.3
	Sequence conflict	482	1	I → T in CAA29068. Ref.3
	Sequence conflict	485	1	I → N in CAA29068. Ref.3
	Sequence conflict	492	1	A → G in CAA29068. Ref.3
	Sequence conflict	501 – 510	10	TAEFVRKVIL → NAAKQRDVDR in CAA29068. Ref.3
	Sequence conflict	1411 – 1412	2	EV → S in AAA35198. Ref.9
	Sequence conflict	1582	1	I → M in AAA35198. Ref.9
	Sequence conflict	1588	1	N → K in AAA35198. Ref.9
	Sequence conflict	1592	1	V → G in AAA35198. Ref.9
	Sequence conflict	1595	1	S → A in AAA35198. Ref.9
	Sequence conflict	1872	1	Missing AA sequence Ref.10
	Sequence conflict	1937	1	A → R in AAA68280. Ref.1
	Sequence conflict	1937	1	A → R in AAA35198. Ref.9
	Sequence conflict	1997	1	T → I in AAA35198. Ref.9
	Sequence conflict	2039	1	H → L in AAA35198. Ref.9
	Sequence conflict	2158 – 2165	8	KILAHAKE → VRSWHTQQK in AAA35198. Ref.9

Sequences

	Sequence		Length	Mass (Da)
	P07259-1 [UniParc]. Last modified November 1, 1995. Version 4. Checksum: 4CA58304DAECAD21	FASTA	2,214	245,126
	10 20 30 40 50 60 MATIAPTAPI TPPMESTGDR LVTLELKDGT VLQGYSFGAE KSVAGELVFQ TGMVGYPESV 70 80 90 100 110 120 TDPSYEGQIL VITYPLVGNY GVPDMHLRDE LVEELPRYFE SNRIHIAGLV ISHYTDEYSH 130 140 150 160 170 180 YLRKSSLGKW LQNEGIPAVY GVDTRSLTKH LRDAGSMLGR LSLEKSGSDR TISRSSSWRS 190 200 210 220 230 240 AFDVPEWVDP NVQNLVSKVS INEPKLYVPP ADNKHIELQT GPDGKVLRIL AIDVGMKYNQ 250 260 270 280 290 300 IRCFIKRGVE LKVVPWNYDF TKEDYDGLFI SNGPGDPSVL DDLSQRLSNV LEAKKTPVFG 310 320 330 340 350 360 ICLGHQLIAR AAGASTLKLK FGNRGHNIPC TSTISGRCYI TSQNHGFAVD VDTLTSGWKP 370 380 390 400 410 420 LFVNANDDSN EGIYHSELPY FSVQFHPEST PGPRDTEFLF DVFIQAVKEF KYTQVLKPIA 430 440 450 460 470 480 FPGGLLEDNV KAHPRIEAKK VLVLGSGGLS IGQAGEFDYS GSQAIKALKE EGIYTILINP 490 500 510 520 530 540 NIATIQTSKG LADKVYFVPV TAEFVRKVIL HERPDAIYVT FGGQTALSVG IAMKDEFEAL 550 560 570 580 590 600 GVKVLGTPID TIITTEDREL FSNAIDEINE KCAKSQAANS VDEALAAVKE IGFPVIVRAA 610 620 630 640 650 660 YALGGLGSGF ANNEKELVDL CNVAFSSSPQ VLVEKSMKGW KEVEYEVVRD AFDNCITVCN 670 680 690 700 710 720 MENFDPLGIH TGDSIVVAPS QTLSDEDYNM LRTTAVNVIR HLGVVGECNI QYALNPVSKD 730 740 750 760 770 780 YCIIEVNARL SRSSALASKA TGYPLAYTAA KLGLNIPLNE VKNSVTKSTC ACFEPSLDYC 790 800 810 820 830 840 VVKMPRWDLK KFTRVSTELS SSMKSVGEVM SIGRTFEEAI QKAIRSTEYA NLGFNETDLD 850 860 870 880 890 900 IDIDYELNNP TDMRVFAIAN AFAKKGYSVD KVWEMTRIDK WFLNKLHDLV QFAEKISSFG 910 920 930 940 950 960 TKEELPSLVL RQAKQLGFDD RQIARFLDSN EVAIRRLRKE YGITPFVKQI DTVAAEFPAY 970 980 990 1000 1010 1020 TNYLYMTYNA DSHDLSFDDH GVMVLGSGVY RIGSSVEFDW CAVTAVRTLR ANNIKTIMVN 1030 1040 1050 1060 1070 1080 YNPETVSTDY DEADRLYFET INLERVLDIY EIENSSGVVV SMGGQTSNNI AMTLHRENVK 1090 1100 1110 1120 1130 1140 ILGTSPDMID SAENRYKFSR MLDQIGVDQP AWKELTSMDE AESFAEKVGY PVLVRPSYVL 1150 1160 1170 1180 1190 1200 SGAAMNTVYS KNDLESYLNQ AVEVSRDYPV VITKYIENAK EIEMDAVARN GELVMHVVSE 1210 1220 1230 1240 1250 1260 HVENAGVHSG DATLIVPPQD LAPETVDRIV VATAKIGKAL KITGPYNIQF IAKDNEIKVI 1270 1280 1290 1300 1310 1320 ECNVRASRSF PFISKVVGVN LIELATKAIM GLPLTPYPVE KLPDDYVAVK VPQFSFPRLA 1330 1340 1350 1360 1370 1380 GADPVLGVEM ASTGEVATFG HSKYEAYLKS LLATGFKLPK KNILLSIGSY KEKQELLSSV 1390 1400 1410 1420 1430 1440 QKLYNMGYKL FATSGTADFL SEHGIAVQYL EVLNKDDDDQ KSEYSLTQHL ANNEIDLYIN 1450 1460 1470 1480 1490 1500 LPSANRFRRP ASYVSKGYKT RRLAVDYSVP LVTNVKCAKL LIEAISRNIT LDVSERDAQT 1510 1520 1530 1540 1550 1560 SHRTITLPGL INIATYVPNA SHVIKGPAEL KETTRLFLES GFTYCQLMPR SISGPVITDV 1570 1580 1590 1600 1610 1620 ASLKAANSVS QDSSYTDFSF TIAGTAHNAH SVTQSASKVT ALFLPLRELK NKITAVAELL 1630 1640 1650 1660 1670 1680 NQWPTEKQVI AEAKTADLAS VLLLTSLQNR SIHITGVSNK EDLALIMTVK AKDPRVTCDV 1690 1700 1710 1720 1730 1740 NIYSLFIAQD DYPEAVFLPT KEDQEFFWNN LDSIDAFSVG ALPVALANVT GNKVDVGMGI 1750 1760 1770 1780 1790 1800 KDSLPLLLAA VEEGKLTIDD IVLRLHDNPA KIFNIPTQDS VVEIDLDYSF RRNKRWSPFN 1810 1820 1830 1840 1850 1860 KDMNGGIERV VYNGETLVLS GELVSPGAKG KCIVNPSPAS ITASAELQST SAKRRFSITE 1870 1880 1890 1900 1910 1920 EAIADNLDAA EDAIPEQPLE QKLMSSRPPR ELVAPGAIQN LIRSNNPFRG RHILSIKQFK 1930 1940 1950 1960 1970 1980 RSDFHVLFAV AQELRAAVAR EGVLDLMKGH VITTIFFEPS TRTCSSFIAA MERLGGRIVN 1990 2000 2010 2020 2030 2040 VNPLVSSVKK GETLQDTIRT LACYSDAIVM RHSEEMSVHI AAKYSPVPII NGGNGSREHP 2050 2060 2070 2080 2090 2100 TQAFLDLFTI REEIGTVNGI TVTFMGDLKH GRTVHSLCRL LMHYQVRINL VSPPELRLPE 2110 2120 2130 2140 2150 2160 GLREELRKAG LLGVESIELT PHIISKTDVL YCTRVQEERF NSPEEYARLK DTYIVDNKIL 2170 2180 2190 2200 2210 AHAKENMAIM HPLPRVNEIK EEVDYDHRAA YFRQMKYGLF VRMALLAMVM GVDM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Organization of the yeast URA2 gene: identification of a defective dihydroorotase-like domain in the multifunctional carbamoylphosphate synthetase-aspartate transcarbamylase complex." Souciet J.-L., Nagy M., le Gouar M., Lacroute F., Potier S. Gene 79:59-70(1989) [PubMed: 2570735] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 28383 / FL100 / VTT C-80102.
[2]	"Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X." Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C., Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D., Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J., Heumann K. , Hilger F., Hollenberg C.P., Huang M.-E., Jacq C., Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E., Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T., Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R., Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N., To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H., von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L. EMBO J. 15:2031-2049(1996) [PubMed: 8641269] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[3]	"Nucleotide sequence of the pyrimidine specific carbamoyl phosphate synthetase, a part of the yeast multifunctional protein encoded by the URA2 gene." Souciet J.-L., Potier S., Hubert J.-C., Lacroute F. Mol. Gen. Genet. 207:314-319(1987) [PubMed: 3039294] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-510. Strain: ATCC 28383 / FL100 / VTT C-80102.
[4]	"Sequencing analysis of a 40.2 kb fragment of yeast chromosome X reveals 19 open reading frames including URA2 (5' end), TRK1, PBS2, SPT10, GCD14, RPE1, PHO86, NCA3, ASF1, CCT7, GZF3, two tRNA genes, three remnant delta elements and a Ty4 transposon." Cziepluch C., Kordes E., Pujol A., Jauniaux J.-C. Yeast 12:1471-1474(1996) [PubMed: 8948101] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-276. Strain: ATCC 96604 / S288c / FY1679.
[5]	"High-density yeast-tiling array reveals previously undiscovered introns and extensive regulation of meiotic splicing." Juneau K., Palm C., Miranda M., Davis R.W. Proc. Natl. Acad. Sci. U.S.A. 104:1522-1527(2007) [PubMed: 17244705] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-117. Strain: ATCC 201390 / BY4743.
[6]	"Genome-wide identification of spliced introns using a tiling microarray." Zhang Z., Hesselberth J.R., Fields S. Genome Res. 17:503-509(2007) [PubMed: 17351133] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-119. Strain: ATCC 201390 / BY4743.
[7]	"Sequence analysis of a 40.7 kb segment from the left arm of yeast chromosome X reveals 14 known genes and 13 new open reading frames including homologues of genes clustered on the right arm of chromosome XI." Katsoulou C., Tzermia M., Tavernarakis N., Alexandraki D. Yeast 12:787-797(1996) [PubMed: 8813765] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 175-2214. Strain: ATCC 96604 / S288c / FY1679.
[8]	"Screening and identification of yeast sequences that cause growth inhibition when overexpressed." Akada R., Yamamoto J., Yamashita I. Mol. Gen. Genet. 254:267-274(1997) [PubMed: 9150260] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 838-877.
[9]	"The primary structure of the aspartate transcarbamylase region of the URA2 gene product in Saccharomyces cerevisiae. Features involved in activity and nuclear localization." Nagy M., le Gouar M., Potier S., Souciet J.-L., Herve G. J. Biol. Chem. 264:8366-8374(1989) [PubMed: 2498313] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1268-2214.
[10]	"Yeast carbamoyl-phosphate-synthetase--aspartate-transcarbamylase multidomain protein is phosphorylated in vitro by cAMP-dependent protein kinase." Denis-Duphil M., Lecaer J.-P., Hardie D.G., Carrey E.A. Eur. J. Biochem. 193:581-587(1990) [PubMed: 1977585] [Abstract] Cited for: PROTEIN SEQUENCE OF 1855-1874, PHOSPHORYLATION AT SER-1857.
[11]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[12]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1857, MASS SPECTROMETRY.
[13]	"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae." Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P. J. Proteome Res. 6:1190-1197(2007) [PubMed: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1857, MASS SPECTROMETRY.
[14]	"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F. Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed: 17287358] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1857, MASS SPECTROMETRY.
[15]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1859, MASS SPECTROMETRY.
[16]	"A multidimensional chromatography technology for in-depth phosphoproteome analysis." Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H. Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1452; TYR-1453; SER-1553; SER-1857; THR-1859; SER-1986 AND SER-2142, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M27174 Genomic DNA. Translation: AAA68280.1. Z49405 Genomic DNA. Translation: CAA89425.1. X05553 Genomic DNA. Translation: CAA29068.1. EF123133 mRNA. Translation: ABM97477.1. DQ881452 mRNA. Translation: ABI95879.1. X87371 Genomic DNA. Translation: CAA60825.1. D28139 Genomic DNA. Translation: BAA05680.1. J04711 Genomic DNA. Translation: AAA35198.1.
PIR	QZBYU2. S56911.
RefSeq	NP_012405.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P07259. 417 interactions.
STRING	P07259.
Proteomic databases
PeptideAtlas	P07259.
PRIDE	P07259.
Genome annotation databases
Ensembl	YJL130C; YJL130C; YJL130C; Saccharomyces cerevisiae. [Genome view]
GeneID	853311.
KEGG	sce:YJL130C.
NMPDR	fig|4932.3.peg.3372.
Organism-specific databases
CYGD	YJL130c.
SGD	S000003666. URA2.
Phylogenomic databases
HOGENOM	P07259.
OMA	TIQTSKG
OrthoDB	EOG9X9907
Enzyme and pathway databases
BRENDA	2.1.3.2. 250. 6.3.5.5. 250.
Gene expression databases
ArrayExpress	P07259.
Genevestigator	P07259.
GermOnline	YJL130C. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR006132. Asp/Orn_carbamoyltranf_P_bd. IPR006130. Asp/Orn_carbamoylTrfase. IPR006131. Asp_carbamoyltransf_Asp/Orn_bd. IPR002082. Asp_carbamoyltransf_euk. IPR011761. ATP-grasp. IPR013816. ATP_grasp_subdomain_2. IPR001317. CarbamoylP_synth_GATase. IPR005483. CarbamoylP_synth_lsu. IPR005479. CarbamoylP_synth_lsu_ATP-bd. IPR006275. CarbamoylP_synth_lsu_Gln-dep. IPR005481. CarbamoylP_synth_lsu_N. IPR005480. CarbamoylP_synth_lsu_oligo. IPR006274. CarbamoylP_synth_ssu. IPR002474. CarbamoylP_synth_ssu_N. IPR011702. GATASE. IPR017926. GATASE_1. IPR000991. GATase_class1_C. IPR011607. MGS. IPR013817. Pre-ATP_grasp. IPR016185. PreATP-grasp-like. [Graphical view]
Gene3D	G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 2 hits. G3DSA:3.40.50.20. Pre-ATP_grasp. 2 hits.
Pfam	PF00289. CPSase_L_chain. 2 hits. 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. [Graphical view]
PRINTS	PR00100. AOTCASE. PR00101. ATCASE. PR00098. CPSASE. PR00099. CPSGATASE. PR00096. GATASE.
SMART	SM00851. MGS. 1 hit. [Graphical view]
TIGRFAMs	TIGR00670. asp_carb_tr. 1 hit. TIGR01369. CPSaseII_lrg. 1 hit. TIGR01368. CPSaseIIsmall. 1 hit.
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. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	973648.

Entry information

Entry name

PYR1_YEAST

Accession

Primary (citable) accession number: P07259
Secondary accession number(s): A2TBN0, Q06HN1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	November 1, 1995
Last modified:	November 24, 2009
This is version 130 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)