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Protein

Protein ura1

Gene

ura1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

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 ura1 (ura1)
  2. Protein ura1 (ura1)
  3. Probable dihydroorotase (ura2)
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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei338 – 3381For GATase activityBy similarity
Active sitei422 – 4221For GATase activityBy similarity
Active sitei424 – 4241For GATase activityBy similarity

GO - Molecular functioni

  • amino acid binding Source: InterPro
  • aspartate carbamoyltransferase activity Source: PomBase
  • ATP binding Source: UniProtKB-KW
  • carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity Source: PomBase
  • dihydroorotase activity Source: PomBase
  • GMP synthase (glutamine-hydrolyzing) activity Source: PomBase
  • metal ion binding Source: InterPro

GO - Biological processi

  • 'de novo' pyrimidine nucleobase biosynthetic process Source: PomBase
  • 'de novo' UMP biosynthetic process Source: UniProtKB-UniPathway
  • glutamine metabolic process Source: PomBase

Keywords - Molecular functioni

Ligase, Transferase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SPO-500753. Pyrimidine biosynthesis.
UniPathwayiUPA00070; UER00115.
UPA00070; UER00116.

Protein family/group databases

MEROPSiC26.956.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein ura1
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:ura1
ORF Names:SPAC22G7.06c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC22G7.06c.
PomBaseiSPAC22G7.06c. ura1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 22442244Protein ura1PRO_0000199510Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1119 – 11191Phosphoserine1 Publication
Modified residuei1881 – 18811Phosphoserine1 Publication
Modified residuei1885 – 18851Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ09794.

PTM databases

iPTMnetiQ09794.

Interactioni

Protein-protein interaction databases

BioGridi278044. 22 interactions.
DIPiDIP-59121N.
MINTiMINT-4695156.

Structurei

3D structure databases

ProteinModelPortaliQ09794.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini264 – 449186Glutamine amidotransferase type-1Add
BLAST
Domaini598 – 790193ATP-grasp 1Add
BLAST
Domaini1133 – 1324192ATP-grasp 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 437437GATase (Glutamine amidotransferase)By similarityAdd
BLAST
Regioni438 – 47740LinkerBy similarityAdd
BLAST
Regioni478 – 15141037CPSase (Carbamoyl-phosphate synthase)By similarityAdd
BLAST
Regioni1515 – 152410LinkerBy similarity
Regioni1525 – 1853329Defective DHOase domainBy similarityAdd
BLAST
Regioni1854 – 193582LinkerBy similarityAdd
BLAST
Regioni1936 – 2244309ATCase (Aspartate transcarbamylase)By similarityAdd
BLAST

Domaini

The DHOase domain is defective.

Sequence similaritiesi

In the central section; belongs to the DHOase family.Curated
Contains 2 ATP-grasp domains.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

HOGENOMiHOG000234584.
InParanoidiQ09794.
KOiK11541.
OMAiLYSVRLN.
OrthoDBiEOG7XPZDV.
PhylomeDBiQ09794.

Family and domain databases

Gene3Di1.10.1030.10. 1 hit.
3.30.1490.20. 1 hit.
3.30.470.20. 2 hits.
3.40.50.1370. 2 hits.
3.40.50.1380. 1 hit.
3.40.50.20. 2 hits.
3.40.50.880. 1 hit.
3.50.30.20. 1 hit.
HAMAPiMF_00001. Asp_carb_tr.
MF_01209. CPSase_S_chain.
InterProiIPR006132. Asp/Orn_carbamoyltranf_P-bd.
IPR006130. Asp/Orn_carbamoylTrfase.
IPR002082. Asp_carbamoyltransf.
IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006275. CarbamoylP_synth_lsu.
IPR005480. CarbamoylP_synth_lsu_oligo.
IPR006274. CarbamoylP_synth_ssu.
IPR002474. CarbamoylP_synth_ssu_N.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR005483. CbamoylP_synth_lsu_CPSase_dom.
IPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
IPR011607. MGS-like_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamiPF02786. 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]
PRINTSiPR00100. AOTCASE.
PR00101. ATCASE.
PR00098. CPSASE.
SMARTiSM01096. CPSase_L_D3. 1 hit.
SM01097. CPSase_sm_chain. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMiSSF48108. SSF48108. 1 hit.
SSF51338. SSF51338. 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.
PROSITEiPS50975. 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]

Sequencei

Sequence statusi: Complete.

Q09794-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGLLPSLSS SFPLVQSEAL GMPRTHGPKP SENDPKEPTC SPSPAFYSVN
60 70 80 90 100
GEMKDYKLMA LELEDKSVLQ GYSFGADHSV SGELVFQTGM VGYPESLTDP
110 120 130 140 150
SYRGQILVFT FPTVGNYGVP DRRILDEISG LPKYFESNQI HVAAIIISSY
160 170 180 190 200
SQNYSHFLAH SSLGEWLKEQ GIPGIFGIDT RALTKKIRDQ GSMLGRLLIQ
210 220 230 240 250
KDESPINPSS ITGLGKDWST AFEDIPWKNP NTENLTSQVS IKEPKLYEPH
260 270 280 290 300
PTTAIKKADG KIIRILVIDV GMKYNQIRCF LNRGVELLVV PWDYDFTKET
310 320 330 340 350
YDGLFISNGP GDPSLMDLVV DRVKRVLESK TVPVFGICFG HQIMARAAGA
360 370 380 390 400
STTKMKFGNR GHNIPCTCMI SGRCYITSQN HGYAVDASSL SNGWKELFVN
410 420 430 440 450
ANDGSNEGIY NTEYPFFSVQ FHPESTPGPR DTEFLFDVFI DVVKRSADAK
460 470 480 490 500
SLQPFKLPGG TIEENRSRHP LVDAKRVLIL GSGGLSIGQA GEFDYSGSQA
510 520 530 540 550
IKALREEGIY TILINPNIAT IQTSKGLADK VYFLPVNADF VRKVIKQERP
560 570 580 590 600
DSIYVTFGGQ TALNVGIELK DEFEQLGVKV LGTPIDTIIT TEDRELFARA
610 620 630 640 650
MDEINEKCAK SASASSIEEA IKVSKDISFP VIVRAAYALG GLGSGFADNE
660 670 680 690 700
AELIDLCTLA FATSPQVLIE RSMKGWKEIE YEVVRDAFDN CITVCNMENF
710 720 730 740 750
DPLGIHTGDS IVVAPSQTLT DEDYNMLRTT AVNVIRHLGV VGECNIQYAL
760 770 780 790 800
NPFTKEYCII EVNARLSRSS ALASKATGYP LAFTAAKLGL NIPLNEVKNS
810 820 830 840 850
VTKVTCACFE PSLDYVVVKI PRWDLKKFTR VSTQLSSAMK SVGEVMSIGR
860 870 880 890 900
TFEEAIQKAI RAIDYSNTGF NVKDALMSID TELQTPSDQR LFAIANAMAS
910 920 930 940 950
GYSVDRIWEL TRIDKWFLEK LMGLIRTSQL ISKHDISSLP ISLLKTAKQL
960 970 980 990 1000
GFADVQIAAF MNSTELAVRR IRTEAGIRPF VKQIDTVAAE FPAFTNYLYT
1010 1020 1030 1040 1050
TYNAVEHDIH FNDKGVMVLG SGVYRIGSSV EFDWCAVRAV RTLRDRGVKT
1060 1070 1080 1090 1100
IMVNYNPETV STDYDEADRL YFENIGLETV LDIYEQESSS GIIIAMGGQT
1110 1120 1130 1140 1150
ANNIALPLHR ENVKILGTSP EMIDGAENRF KFSRMLDDIG VDQPKWKELT
1160 1170 1180 1190 1200
SFDEADKFCD TVGYPVLVRP SYVLSGAAMN TVYSQSDLHS YLQQAVAINK
1210 1220 1230 1240 1250
DHPVVISKYI ENAKEIELDA VAREGKMVMH VISEHVENAG VHSGDATLVL
1260 1270 1280 1290 1300
PPQDLAPTTI ERIVDAAAKI GEALNITGPY NIQFIAKDNE IKVIECNVRA
1310 1320 1330 1340 1350
SRSFPFVSKV IGVDMISMAT DVIMGNPIQP YPDVDLPRDY VAVKVPQFSF
1360 1370 1380 1390 1400
SRLSGADPVL GVEMASTGEV ACFGHNKFEA YLKAMISTGF RLPKKNILIS
1410 1420 1430 1440 1450
IGSYKEKAEL LPYVKKLYEN NYNIFATAGT SDYFMESGVP CKYLADLPAE
1460 1470 1480 1490 1500
EANNEYSLSA HLANNMIDMY INLPSNNRYR RPANYISSGY KSRRLAIDYS
1510 1520 1530 1540 1550
VPLVTNVKCA KLMIEAICRN LDFSLSTVDF QSSFQTANLP GLINISAFLP
1560 1570 1580 1590 1600
EFTSEAVSDY TKECIASGFT MARFLPFSTS STLADKDSLS AVKKLALDHA
1610 1620 1630 1640 1650
HCDYNFSVIA SSTNEVTISE LTSESGCLFF HFEKDDSGID HVTAVASHFN
1660 1670 1680 1690 1700
VWPDTQTVMT DAKSTTLASL LLLASLHNRR IHITNVSSKD DLNLIVLAKQ
1710 1720 1730 1740 1750
RSLPVTFDVS VYSLFLNQND YPGATFLPTA DDQVEIWNKL SYIDCFSIGS
1760 1770 1780 1790 1800
IPSRLAKFVG NTAFTGFGVR EAIPLLLTAV NEGRLTLKDV VDRFYSNPKA
1810 1820 1830 1840 1850
IFRLHDQDDS GVQLEVDRSV SWSSKDWTPF NGKKLYGSIQ SVQFDGHDVF
1860 1870 1880 1890 1900
FDGELNFEHT YGRDYSSASL ADKSKATRKV SALMSPGLPH AAPSLAEAFG
1910 1920 1930 1940 1950
QAPENKAHPD ISLNMTPNFK PSHELVQLIN SSPFYRKHII SVHQVTRSDL
1960 1970 1980 1990 2000
HVLFAIAHQM RIIVERQGVI DLCYGKLLCT MFFEPSTRTS SSFDAAMQRL
2010 2020 2030 2040 2050
GGKVVAVTAS ASSVNKGESL ADTIRTLGCY GDAIVLRHPS IESARIAANF
2060 2070 2080 2090 2100
SPVPIINGGN GSKEHPTQAF LDLYTIREEL GSVNGLTITF IGDLKYGRTV
2110 2120 2130 2140 2150
HSLARLLAFW HVELHLVSPE QLALPDDVKD DIRANGLNFI EHRELTKEVV
2160 2170 2180 2190 2200
AQSDVLYCTR VQKERFASVD EYEKLKDSFI VDNSVLASAK SHCIVMHPLP
2210 2220 2230 2240
RNREISEEVD FDQRRAAYFR QMRYGLYIRM ALLACVMGAT EVAN
Length:2,244
Mass (Da):248,309
Last modified:November 1, 1995 - v1
Checksum:i5700D153B50CD3E9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti336 – 3383GIC → RYF in CAA57433 (PubMed:8590465).Curated
Sequence conflicti1035 – 10395CAVRA → LQFAQ in CAA57433 (PubMed:8590465).Curated
Sequence conflicti1409 – 14102EL → DV in CAA57433 (PubMed:8590465).Curated
Sequence conflicti1975 – 19751G → E in CAA57433 (PubMed:8590465).Curated
Sequence conflicti2002 – 20021G → E in CAA57433 (PubMed:8590465).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81841 mRNA. Translation: CAA57433.1.
CU329670 Genomic DNA. Translation: CAA91130.1.
PIRiS65074.
T11616.
RefSeqiNP_593055.1. NM_001018453.2.

Genome annotation databases

EnsemblFungiiSPAC22G7.06c.1; SPAC22G7.06c.1:pep; SPAC22G7.06c.
GeneIDi2541544.
KEGGispo:SPAC22G7.06c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81841 mRNA. Translation: CAA57433.1.
CU329670 Genomic DNA. Translation: CAA91130.1.
PIRiS65074.
T11616.
RefSeqiNP_593055.1. NM_001018453.2.

3D structure databases

ProteinModelPortaliQ09794.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278044. 22 interactions.
DIPiDIP-59121N.
MINTiMINT-4695156.

Protein family/group databases

MEROPSiC26.956.

PTM databases

iPTMnetiQ09794.

Proteomic databases

MaxQBiQ09794.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC22G7.06c.1; SPAC22G7.06c.1:pep; SPAC22G7.06c.
GeneIDi2541544.
KEGGispo:SPAC22G7.06c.

Organism-specific databases

EuPathDBiFungiDB:SPAC22G7.06c.
PomBaseiSPAC22G7.06c. ura1.

Phylogenomic databases

HOGENOMiHOG000234584.
InParanoidiQ09794.
KOiK11541.
OMAiLYSVRLN.
OrthoDBiEOG7XPZDV.
PhylomeDBiQ09794.

Enzyme and pathway databases

UniPathwayiUPA00070; UER00115.
UPA00070; UER00116.
ReactomeiR-SPO-500753. Pyrimidine biosynthesis.

Miscellaneous databases

NextBioi20802641.
PROiQ09794.

Family and domain databases

Gene3Di1.10.1030.10. 1 hit.
3.30.1490.20. 1 hit.
3.30.470.20. 2 hits.
3.40.50.1370. 2 hits.
3.40.50.1380. 1 hit.
3.40.50.20. 2 hits.
3.40.50.880. 1 hit.
3.50.30.20. 1 hit.
HAMAPiMF_00001. Asp_carb_tr.
MF_01209. CPSase_S_chain.
InterProiIPR006132. Asp/Orn_carbamoyltranf_P-bd.
IPR006130. Asp/Orn_carbamoylTrfase.
IPR002082. Asp_carbamoyltransf.
IPR006131. Asp_carbamoyltransf_Asp/Orn-bd.
IPR011761. ATP-grasp.
IPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR006275. CarbamoylP_synth_lsu.
IPR005480. CarbamoylP_synth_lsu_oligo.
IPR006274. CarbamoylP_synth_ssu.
IPR002474. CarbamoylP_synth_ssu_N.
IPR005479. CbamoylP_synth_lsu-like_ATP-bd.
IPR005483. CbamoylP_synth_lsu_CPSase_dom.
IPR029062. Class_I_gatase-like.
IPR017926. GATASE.
IPR011059. Metal-dep_hydrolase_composite.
IPR032466. Metal_Hydrolase.
IPR011607. MGS-like_dom.
IPR016185. PreATP-grasp_dom.
[Graphical view]
PfamiPF02786. 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]
PRINTSiPR00100. AOTCASE.
PR00101. ATCASE.
PR00098. CPSASE.
SMARTiSM01096. CPSase_L_D3. 1 hit.
SM01097. CPSase_sm_chain. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMiSSF48108. SSF48108. 1 hit.
SSF51338. SSF51338. 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.
PROSITEiPS50975. 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]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-2244.
    Strain: 972 / ATCC 24843.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1119; SER-1881 AND SER-1885, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiPYR1_SCHPO
AccessioniPrimary (citable) accession number: Q09794
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: May 11, 2016
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.