Reviewed, UniProtKB/Swiss-Prot Q09794 (PYR1_SCHPO)

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:	ura1
ORF Names:	SPAC22G7.06c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	2244 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) By similarity.
Catalytic activity	2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 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; UMP from HCO(3)(-): step 1/6. Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 2/6.
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.
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
Molecular function	Ligase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	'de novo' pyrimidine base biosynthetic process Inferred from electronic annotation. Source: InterPro aspartate metabolic process Inferred by curator. Source: GeneDB_SPombe glutamine metabolic process Inferred from electronic annotation. Source: InterPro pyrimidine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro amino acid binding Inferred from electronic annotation. Source: InterPro aspartate carbamoyltransferase activity Ref.1 Inferred from electronic annotation. Source: InterPro carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Ref.1 Inferred from electronic annotation. Source: EC dihydroorotase activity Ref.1 Inferred from genetic interaction. Source: GeneDB_SPombe
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 2244	2244	Protein ura1		PRO_0000199510
Regions
	Domain	264 – 449	186	Glutamine amidotransferase type-1
	Domain	598 – 790	193	ATP-grasp 1
	Domain	1133 – 1324	192	ATP-grasp 2
	Region	1 – 437	437	GATase (Glutamine amidotransferase) By similarity
	Region	438 – 477	40	Linker By similarity
	Region	478 – 1514	1037	CPSase (Carbamoyl-phosphate synthase) By similarity
	Region	1515 – 1524	10	Linker By similarity
	Region	1525 – 1853	329	Defective DHOase domain By similarity
	Region	1854 – 1935	82	Linker By similarity
	Region	1936 – 2244	309	ATCase (Aspartate transcarbamylase) By similarity
Sites
	Active site	338	1	For GATase activity By similarity
	Active site	422	1	For GATase activity By similarity
	Active site	424	1	For GATase activity By similarity
Amino acid modifications
	Modified residue	1119	1	Phosphoserine
	Modified residue	1881	1	Phosphoserine
	Modified residue	1885	1	Phosphoserine
Experimental info
	Sequence conflict	336 – 338	3	GIC → RYF in CAA57433. Ref.1
	Sequence conflict	1035 – 1039	5	CAVRA → LQFAQ in CAA57433. Ref.1
	Sequence conflict	1409 – 1410	2	EL → DV in CAA57433. Ref.1
	Sequence conflict	1975	1	G → E in CAA57433. Ref.1
	Sequence conflict	2002	1	G → E in CAA57433. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q09794-1 [UniParc]. Last modified November 1, 1995. Version 1. Checksum: 5700D153B50CD3E9	FASTA	2,244	248,309
	10 20 30 40 50 60 MSGLLPSLSS SFPLVQSEAL GMPRTHGPKP SENDPKEPTC SPSPAFYSVN GEMKDYKLMA 70 80 90 100 110 120 LELEDKSVLQ GYSFGADHSV SGELVFQTGM VGYPESLTDP SYRGQILVFT FPTVGNYGVP 130 140 150 160 170 180 DRRILDEISG LPKYFESNQI HVAAIIISSY SQNYSHFLAH SSLGEWLKEQ GIPGIFGIDT 190 200 210 220 230 240 RALTKKIRDQ GSMLGRLLIQ KDESPINPSS ITGLGKDWST AFEDIPWKNP NTENLTSQVS 250 260 270 280 290 300 IKEPKLYEPH PTTAIKKADG KIIRILVIDV GMKYNQIRCF LNRGVELLVV PWDYDFTKET 310 320 330 340 350 360 YDGLFISNGP GDPSLMDLVV DRVKRVLESK TVPVFGICFG HQIMARAAGA STTKMKFGNR 370 380 390 400 410 420 GHNIPCTCMI SGRCYITSQN HGYAVDASSL SNGWKELFVN ANDGSNEGIY NTEYPFFSVQ 430 440 450 460 470 480 FHPESTPGPR DTEFLFDVFI DVVKRSADAK SLQPFKLPGG TIEENRSRHP LVDAKRVLIL 490 500 510 520 530 540 GSGGLSIGQA GEFDYSGSQA IKALREEGIY TILINPNIAT IQTSKGLADK VYFLPVNADF 550 560 570 580 590 600 VRKVIKQERP DSIYVTFGGQ TALNVGIELK DEFEQLGVKV LGTPIDTIIT TEDRELFARA 610 620 630 640 650 660 MDEINEKCAK SASASSIEEA IKVSKDISFP VIVRAAYALG GLGSGFADNE AELIDLCTLA 670 680 690 700 710 720 FATSPQVLIE RSMKGWKEIE YEVVRDAFDN CITVCNMENF DPLGIHTGDS IVVAPSQTLT 730 740 750 760 770 780 DEDYNMLRTT AVNVIRHLGV VGECNIQYAL NPFTKEYCII EVNARLSRSS ALASKATGYP 790 800 810 820 830 840 LAFTAAKLGL NIPLNEVKNS VTKVTCACFE PSLDYVVVKI PRWDLKKFTR VSTQLSSAMK 850 860 870 880 890 900 SVGEVMSIGR TFEEAIQKAI RAIDYSNTGF NVKDALMSID TELQTPSDQR LFAIANAMAS 910 920 930 940 950 960 GYSVDRIWEL TRIDKWFLEK LMGLIRTSQL ISKHDISSLP ISLLKTAKQL GFADVQIAAF 970 980 990 1000 1010 1020 MNSTELAVRR IRTEAGIRPF VKQIDTVAAE FPAFTNYLYT TYNAVEHDIH FNDKGVMVLG 1030 1040 1050 1060 1070 1080 SGVYRIGSSV EFDWCAVRAV RTLRDRGVKT IMVNYNPETV STDYDEADRL YFENIGLETV 1090 1100 1110 1120 1130 1140 LDIYEQESSS GIIIAMGGQT ANNIALPLHR ENVKILGTSP EMIDGAENRF KFSRMLDDIG 1150 1160 1170 1180 1190 1200 VDQPKWKELT SFDEADKFCD TVGYPVLVRP SYVLSGAAMN TVYSQSDLHS YLQQAVAINK 1210 1220 1230 1240 1250 1260 DHPVVISKYI ENAKEIELDA VAREGKMVMH VISEHVENAG VHSGDATLVL PPQDLAPTTI 1270 1280 1290 1300 1310 1320 ERIVDAAAKI GEALNITGPY NIQFIAKDNE IKVIECNVRA SRSFPFVSKV IGVDMISMAT 1330 1340 1350 1360 1370 1380 DVIMGNPIQP YPDVDLPRDY VAVKVPQFSF SRLSGADPVL GVEMASTGEV ACFGHNKFEA 1390 1400 1410 1420 1430 1440 YLKAMISTGF RLPKKNILIS IGSYKEKAEL LPYVKKLYEN NYNIFATAGT SDYFMESGVP 1450 1460 1470 1480 1490 1500 CKYLADLPAE EANNEYSLSA HLANNMIDMY INLPSNNRYR RPANYISSGY KSRRLAIDYS 1510 1520 1530 1540 1550 1560 VPLVTNVKCA KLMIEAICRN LDFSLSTVDF QSSFQTANLP GLINISAFLP EFTSEAVSDY 1570 1580 1590 1600 1610 1620 TKECIASGFT MARFLPFSTS STLADKDSLS AVKKLALDHA HCDYNFSVIA SSTNEVTISE 1630 1640 1650 1660 1670 1680 LTSESGCLFF HFEKDDSGID HVTAVASHFN VWPDTQTVMT DAKSTTLASL LLLASLHNRR 1690 1700 1710 1720 1730 1740 IHITNVSSKD DLNLIVLAKQ RSLPVTFDVS VYSLFLNQND YPGATFLPTA DDQVEIWNKL 1750 1760 1770 1780 1790 1800 SYIDCFSIGS IPSRLAKFVG NTAFTGFGVR EAIPLLLTAV NEGRLTLKDV VDRFYSNPKA 1810 1820 1830 1840 1850 1860 IFRLHDQDDS GVQLEVDRSV SWSSKDWTPF NGKKLYGSIQ SVQFDGHDVF FDGELNFEHT 1870 1880 1890 1900 1910 1920 YGRDYSSASL ADKSKATRKV SALMSPGLPH AAPSLAEAFG QAPENKAHPD ISLNMTPNFK 1930 1940 1950 1960 1970 1980 PSHELVQLIN SSPFYRKHII SVHQVTRSDL HVLFAIAHQM RIIVERQGVI DLCYGKLLCT 1990 2000 2010 2020 2030 2040 MFFEPSTRTS SSFDAAMQRL GGKVVAVTAS ASSVNKGESL ADTIRTLGCY GDAIVLRHPS 2050 2060 2070 2080 2090 2100 IESARIAANF SPVPIINGGN GSKEHPTQAF LDLYTIREEL GSVNGLTITF IGDLKYGRTV 2110 2120 2130 2140 2150 2160 HSLARLLAFW HVELHLVSPE QLALPDDVKD DIRANGLNFI EHRELTKEVV AQSDVLYCTR 2170 2180 2190 2200 2210 2220 VQKERFASVD EYEKLKDSFI VDNSVLASAK SHCIVMHPLP RNREISEEVD FDQRRAAYFR 2230 2240 QMRYGLYIRM ALLACVMGAT EVAN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"As in Saccharomyces cerevisiae, aspartate transcarbamoylase is assembled on a multifunctional protein including a dihydroorotase-like cryptic domain in Schizosaccharomyces pombe." Lollier M., Jaquet L., Nedeva T., Lacroute F., Potier S., Souciet J.-L. Curr. Genet. 28:138-149(1995) [PubMed: 8590465] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-2244. Strain: ATCC 38366 / 972.
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[3]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1119; SER-1881 AND SER-1885, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X81841 mRNA. Translation: CAA57433.1. CU329670 Genomic DNA. Translation: CAA91130.1.
PIR	S65074. T11616.
RefSeq	NP_593055.1.
3D structure databases
HSSP	HSSP built from PDB template 1GQ3 based on UniProtKB P00479.
ModBase	Search...
Genome annotation databases
GeneID	2541544.
KEGG	spo:SPAC22G7.06c.
NMPDR	fig|4896.1.peg.3025.
Organism-specific databases
GeneDB_Spombe	SPAC22G7.06c.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-000771-MON.
Gene expression databases
ArrayExpress	Q09794.
Family and domain databases
InterPro	IPR006220. Anth_synthII. IPR006130. Asp/Orn_carbamoyltranf. IPR006132. Asp/Orn_carbamoyltranf_P_bd. IPR006131. Asp_carbamoyltransf_Asp/Orn_bd. IPR002082. Aspartate_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. IPR012998. GATase_1_AS. IPR000991. GATase_class1_C. IPR011607. MGS. IPR013817. Pre-ATP_grasp. [Graphical view]
Gene3D	G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 2 hits. G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit.
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	PR00097. ANTSNTHASEII. PR00100. AOTCASE. PR00101. ATCASE. PR00098. CPSASE. PR00099. CPSGATASE. PR00096. GATASE.
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...

Entry information

Entry name

PYR1_SCHPO

Accession

Primary (citable) accession number: Q09794

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	November 1, 1995
Last modified:	November 25, 2008
This is version 80 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)