[1]	NUCLEOTIDE SEQUENCE [MRNA] OF 22-2244. STRAIN=ATCC 38366 / 972; DOI=10.1007/BF00315780; PubMed=8590465 [NCBI, ExPASy, EBI, Israel, Japan] Lollier M., Jaquet L., Nedeva T., Lacroute F., Potier S., Souciet J.-L.; "As in Saccharomyces cerevisiae, aspartate transcarbamoylase is assembled on a multifunctional protein including a dihydroorotase-like cryptic domain in Schizosaccharomyces pombe."; Curr. Genet. 28:138-149(1995).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC 38366 / 972; DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "The genome sequence of Schizosaccharomyces pombe."; Nature 415:871-880(2002).
[3]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1119; SER-1881 AND SER-1885, AND MASS SPECTROMETRY. DOI=10.1021/pr7006335; PubMed=18257517 [NCBI, ExPASy, EBI, Israel, Japan] Wilson-Grady J.T., Villen J., Gygi S.P.; "Phosphoproteome analysis of fission yeast."; J. Proteome Res. 7:1088-1097(2008).

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 + HCO₃^- + H₂O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate.
CATALYTIC ACTIVITY: 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 .
PATHWAY: 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).
MISCELLANEOUS: In eukaryotes EC 6.3.5.5 is synthesized by two pathway-specific (arginine and pyrimidine) genes under separate control.
SIMILARITY: In the central section; belongs to the DHOase family.
SIMILARITY: Contains 2 ATP-grasp domains.
SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X81841; CAA57433.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CU329670; CAA91130.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S65074; S65074.
T11616; T11616.

RefSeq

NP_593055.1; -.

3D structure databases

HSSP

P00479; 1GQ3. [HSSP ENTRY / SWISS-3DIMAGE / PDB]

ModBase

Q09794.

Enzyme and pathway databases

BioCyc

SPOM-XXX-01:SPOM-XXX-01-000771-MON; -.

Organism-specific databases

GeneDB_Spombe

SPAC22G7.06c; -.

Gene expression databases

ArrayExpress

Q09794; -.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from direct assay from GeneDB_SPombe).
GO:0004070;	Molecular function: aspartate carbamoyltransferase activity (inferred from genetic interaction from GeneDB_SPombe).
GO:0004088;	Molecular function: carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity (inferred from genetic interaction from GeneDB_SPombe).
GO:0004151;	Molecular function: dihydroorotase activity (inferred from genetic interaction from GeneDB_SPombe).
GO:0006207;	Biological process: 'de novo' pyrimidine base biosynthetic process (inferred from genetic interaction from GeneDB_SPombe).
GO:0006531;	Biological process: aspartate metabolic process (inferred by curator from GeneDB_SPombe).
QuickGo view.

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 of domain structure.

Gene3D

G3DSA:3.30.470.20; ATP_grasp_subdomain_2; 2.
G3DSA:3.40.50.20; Pre-ATP_grasp; 1.

Pfam

PF00289; CPSase_L_chain; 2.
PF02786; CPSase_L_D2; 2.
PF02787; CPSase_L_D3; 1.
PF00988; CPSase_sm_chain; 1.
PF00117; GATase; 1.
PF02142; MGS; 1.
PF00185; OTCace; 1.
PF02729; OTCace_N; 1.
Pfam graphical view of domain structure.

PRINTS

PR00097; ANTSNTHASEII.
PR00100; AOTCASE.
PR00101; ATCASE.
PR00098; CPSASE.
PR00099; CPSGATASE.
PR00096; GATASE.

TIGRFAMs

TIGR00670; asp_carb_tr; 1.
TIGR01369; CPSaseII_lrg; 1.
TIGR01368; CPSaseIIsmall; 1.

PROSITE

PS50975; ATP_GRASP; 2.
PS00097; CARBAMOYLTRANSFERASE; 1.
PS00866; CPSASE_1; 2.
PS00867; CPSASE_2; 2.
PS51273; GATASE_TYPE_1; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

Q09794.

Genome annotation databases

2541544; -.

fig|4896.1.peg.3025; -.

Other

ProtoNet

Q09794.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Ligase; Multifunctional enzyme; Phosphoprotein; Pyrimidine biosynthesis; Repeat; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 2244`	`2244`	`Protein ura1.`	`PRO_0000199510`
`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).`
`ACT_SITE`	`338 338`		`For GATase activity (By similarity).`
`ACT_SITE`	`422 422`		`For GATase activity (By similarity).`
`ACT_SITE`	`424 424`		`For GATase activity (By similarity).`
`MOD_RES`	`1119 1119`		`Phosphoserine.`
`MOD_RES`	`1881 1881`		`Phosphoserine.`
`MOD_RES`	`1885 1885`		`Phosphoserine.`
`CONFLICT`	`336 338`		`GIC -> RYF (in Ref. 1; CAA57433).`
`CONFLICT`	`1035 1039`		`CAVRA -> LQFAQ (in Ref. 1; CAA57433).`
`CONFLICT`	`1409 1410`		`EL -> DV (in Ref. 1; CAA57433).`
`CONFLICT`	`1975 1975`		`G -> E (in Ref. 1; CAA57433).`
`CONFLICT`	`2002 2002`		`G -> E (in Ref. 1; CAA57433).`

Sequence information

Length: 2244 AA [This is the length of the unprocessed precursor]

Molecular weight: 248309 Da [This is the MW of the unprocessed precursor]

CRC64: 5700D153B50CD3E9 [This is a checksum on the sequence]

        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

Q09794 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools