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Protein

Pentafunctional AROM polypeptide

Gene

ARO1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis.

Catalytic activityi

3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate = 3-dehydroquinate + phosphate.UniRule annotation
3-dehydroquinate = 3-dehydroshikimate + H2O.UniRule annotation
Shikimate + NADP+ = 3-dehydroshikimate + NADPH.UniRule annotation
ATP + shikimate = ADP + shikimate 3-phosphate.UniRule annotation
Phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate.UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 2 Zn2+ ions per subunit.UniRule annotation

Pathwayi: chorismate biosynthesis

This protein is involved in step 2, 3, 4, 5 and 6 of the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate.UniRule annotation
Proteins known to be involved in the 7 steps of the subpathway in this organism are:
  1. Phospho-2-dehydro-3-deoxyheptonate aldolase, tyrosine-inhibited (ARO4), Phospho-2-dehydro-3-deoxyheptonate aldolase, phenylalanine-inhibited (ARO3)
  2. Pentafunctional AROM polypeptide (ARO1)
  3. Pentafunctional AROM polypeptide (ARO1)
  4. Pentafunctional AROM polypeptide (ARO1)
  5. Pentafunctional AROM polypeptide (ARO1)
  6. Pentafunctional AROM polypeptide (ARO1)
  7. Chorismate synthase (ARO2)
This subpathway is part of the pathway chorismate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate, the pathway chorismate biosynthesis and in Metabolic intermediate biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei114 – 1141NADUniRule annotation
Binding sitei125 – 1251Substrate 1UniRule annotation
Binding sitei141 – 1411Substrate 2UniRule annotation
Binding sitei147 – 1471Substrate 2UniRule annotation
Binding sitei156 – 1561NADUniRule annotation
Binding sitei157 – 1571Substrate 2UniRule annotation
Binding sitei185 – 1851NADUniRule annotation
Metal bindingi189 – 1891Zinc; catalyticUniRule annotation
Binding sitei258 – 2581Substrate 2UniRule annotation
Active sitei268 – 2681Proton acceptor; for 3-dehydroquinate synthase activityUniRule annotation
Metal bindingi279 – 2791Zinc; catalyticUniRule annotation
Binding sitei279 – 2791Substrate 2UniRule annotation
Active sitei283 – 2831Proton acceptor; for 3-dehydroquinate synthase activityUniRule annotation
Metal bindingi295 – 2951Zinc; catalyticUniRule annotation
Binding sitei295 – 2951Substrate 2UniRule annotation
Binding sitei364 – 3641Substrate 2UniRule annotation
Active sitei853 – 8531For EPSP synthase activityUniRule annotation
Active sitei1198 – 11981Proton acceptor; for 3-dehydroquinate dehydratase activityUniRule annotation
Active sitei1227 – 12271Schiff-base intermediate with substrate; for 3-dehydroquinate dehydratase activityUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi43 – 453NADUniRule annotation
Nucleotide bindingi78 – 814NADUniRule annotation
Nucleotide bindingi109 – 1113NADUniRule annotation
Nucleotide bindingi134 – 1352NADUniRule annotation
Nucleotide bindingi174 – 1774NADUniRule annotation
Nucleotide bindingi895 – 9028ATPUniRule annotation

GO - Molecular functioni

  • 3-dehydroquinate dehydratase activity Source: SGD
  • 3-dehydroquinate synthase activity Source: SGD
  • 3-phosphoshikimate 1-carboxyvinyltransferase activity Source: SGD
  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • shikimate 3-dehydrogenase (NADP+) activity Source: SGD
  • shikimate kinase activity Source: SGD

GO - Biological processi

  • aromatic amino acid family biosynthetic process Source: UniProtKB-KW
  • chorismate biosynthetic process Source: SGD

Keywords - Molecular functioni

Kinase, Lyase, Oxidoreductase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, NADP, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyciMetaCyc:YDR127W-MONOMER.
YEAST:YDR127W-MONOMER.
UniPathwayiUPA00053; UER00085.
UPA00053; UER00086.
UPA00053; UER00087.
UPA00053; UER00088.
UPA00053; UER00089.

Names & Taxonomyi

Protein namesi
Recommended name:
Pentafunctional AROM polypeptideUniRule annotation
Including the following 5 domains:
3-dehydroquinate synthaseUniRule annotation (EC:4.2.3.4UniRule annotation)
Short name:
DHQSUniRule annotation
3-phosphoshikimate 1-carboxyvinyltransferaseUniRule annotation (EC:2.5.1.19UniRule annotation)
Alternative name(s):
5-enolpyruvylshikimate-3-phosphate synthaseUniRule annotation
Short name:
EPSP synthaseUniRule annotation
Short name:
EPSPSUniRule annotation
Shikimate kinaseUniRule annotation (EC:2.7.1.71UniRule annotation)
Short name:
SKUniRule annotation
3-dehydroquinate dehydrataseUniRule annotation (EC:4.2.1.10UniRule annotation)
Short name:
3-dehydroquinaseUniRule annotation
Shikimate dehydrogenaseUniRule annotation (EC:1.1.1.25UniRule annotation)
Gene namesi
Name:ARO1UniRule annotation
Synonyms:AROM
Ordered Locus Names:YDR127W
ORF Names:YD9302.02
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR127W.
SGDiS000002534. ARO1.

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15881588Pentafunctional AROM polypeptidePRO_0000140862Add
BLAST

Proteomic databases

MaxQBiP08566.

PTM databases

iPTMnetiP08566.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
HSC82P151083EBI-2883,EBI-8666

Protein-protein interaction databases

BioGridi32183. 351 interactions.
DIPiDIP-2611N.
IntActiP08566. 49 interactions.
MINTiMINT-426824.

Structurei

3D structure databases

ProteinModelPortaliP08566.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 3923923-dehydroquinate synthaseAdd
BLAST
Regioni189 – 1924Substrate binding 2UniRule annotation
Regioni272 – 2765Substrate binding 2UniRule annotation
Regioni405 – 871467EPSP synthaseAdd
BLAST
Regioni890 – 1080191Shikimate kinaseAdd
BLAST
Regioni1081 – 12932133-dehydroquinaseAdd
BLAST
Regioni1306 – 1588283Shikimate dehydrogenaseAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the dehydroquinate synthase family.UniRule annotation
In the 2nd section; belongs to the EPSP synthase family.UniRule annotation
In the 3rd section; belongs to the shikimate kinase family.UniRule annotation
In the 4th section; belongs to the type-I 3-dehydroquinase family.UniRule annotation
In the C-terminal section; belongs to the shikimate dehydrogenase family.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000011238.
HOGENOMiHOG000205493.
InParanoidiP08566.
KOiK13830.
OMAiEGQCKIK.
OrthoDBiEOG7KQ28X.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
3.40.50.300. 1 hit.
3.40.50.720. 1 hit.
3.65.10.10. 2 hits.
HAMAPiMF_00109. Shikimate_kinase.
MF_00110. DHQ_synthase.
MF_00210. EPSP_synth.
MF_03143. Pentafunct_AroM.
InterProiIPR018508. 3-dehydroquinate_DH_AS.
IPR013785. Aldolase_TIM.
IPR016037. DHQ_synth_AroB.
IPR030960. DHQS/DOIS.
IPR001381. DHquinase_I.
IPR001986. Enolpyruvate_Tfrase_dom.
IPR006264. EPSP_synthase.
IPR023193. EPSP_synthase_CS.
IPR016040. NAD(P)-bd_dom.
IPR027417. P-loop_NTPase.
IPR008289. Pentafunct_AroM.
IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
IPR031322. Shikimate/glucono_kinase.
IPR013708. Shikimate_DH-bd_N.
IPR010110. Shikimate_DH_AroM-type.
IPR000623. Shikimate_kinase/TSH1.
IPR023000. Shikimate_kinase_CS.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamiPF01761. DHQ_synthase. 1 hit.
PF01487. DHquinase_I. 1 hit.
PF00275. EPSP_synthase. 1 hit.
PF01488. Shikimate_DH. 1 hit.
PF08501. Shikimate_dh_N. 1 hit.
PF01202. SKI. 1 hit.
[Graphical view]
PIRSFiPIRSF000514. Pentafunct_AroM. 1 hit.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF55205. SSF55205. 1 hit.
TIGRFAMsiTIGR01356. aroA. 1 hit.
TIGR01357. aroB. 1 hit.
TIGR01093. aroD. 1 hit.
TIGR01809. Shik-DH-AROM. 1 hit.
PROSITEiPS01028. DEHYDROQUINASE_I. 1 hit.
PS00104. EPSP_SYNTHASE_1. 1 hit.
PS00885. EPSP_SYNTHASE_2. 1 hit.
PS01128. SHIKIMATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P08566-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVQLAKVPIL GNDIIHVGYN IHDHLVETII KHCPSSTYVI CNDTNLSKVP
60 70 80 90 100
YYQQLVLEFK ASLPEGSRLL TYVVKPGETS KSRETKAQLE DYLLVEGCTR
110 120 130 140 150
DTVMVAIGGG VIGDMIGFVA STFMRGVRVV QVPTSLLAMV DSSIGGKTAI
160 170 180 190 200
DTPLGKNFIG AFWQPKFVLV DIKWLETLAK REFINGMAEV IKTACIWNAD
210 220 230 240 250
EFTRLESNAS LFLNVVNGAK NVKVTNQLTN EIDEISNTDI EAMLDHTYKL
260 270 280 290 300
VLESIKVKAE VVSSDERESS LRNLLNFGHS IGHAYEAILT PQALHGECVS
310 320 330 340 350
IGMVKEAELS RYFGILSPTQ VARLSKILVA YGLPVSPDEK WFKELTLHKK
360 370 380 390 400
TPLDILLKKM SIDKKNEGSK KKVVILESIG KCYGDSAQFV SDEDLRFILT
410 420 430 440 450
DETLVYPFKD IPADQQKVVI PPGSKSISNR ALILAALGEG QCKIKNLLHS
460 470 480 490 500
DDTKHMLTAV HELKGATISW EDNGETVVVE GHGGSTLSAC ADPLYLGNAG
510 520 530 540 550
TASRFLTSLA ALVNSTSSQK YIVLTGNARM QQRPIAPLVD SLRANGTKIE
560 570 580 590 600
YLNNEGSLPI KVYTDSVFKG GRIELAATVS SQYVSSILMC APYAEEPVTL
610 620 630 640 650
ALVGGKPISK LYVDMTIKMM EKFGINVETS TTEPYTYYIP KGHYINPSEY
660 670 680 690 700
VIESDASSAT YPLAFAAMTG TTVTVPNIGF ESLQGDARFA RDVLKPMGCK
710 720 730 740 750
ITQTATSTTV SGPPVGTLKP LKHVDMEPMT DAFLTACVVA AISHDSDPNS
760 770 780 790 800
ANTTTIEGIA NQRVKECNRI LAMATELAKF GVKTTELPDG IQVHGLNSIK
810 820 830 840 850
DLKVPSDSSG PVGVCTYDDH RVAMSFSLLA GMVNSQNERD EVANPVRILE
860 870 880 890 900
RHCTGKTWPG WWDVLHSELG AKLDGAEPLE CTSKKNSKKS VVIIGMRAAG
910 920 930 940 950
KTTISKWCAS ALGYKLVDLD ELFEQQHNNQ SVKQFVVENG WEKFREEETR
960 970 980 990 1000
IFKEVIQNYG DDGYVFSTGG GIVESAESRK ALKDFASSGG YVLHLHRDIE
1010 1020 1030 1040 1050
ETIVFLQSDP SRPAYVEEIR EVWNRREGWY KECSNFSFFA PHCSAEAEFQ
1060 1070 1080 1090 1100
ALRRSFSKYI ATITGVREIE IPSGRSAFVC LTFDDLTEQT ENLTPICYGC
1110 1120 1130 1140 1150
EAVEVRVDHL ANYSADFVSK QLSILRKATD SIPIIFTVRT MKQGGNFPDE
1160 1170 1180 1190 1200
EFKTLRELYD IALKNGVEFL DLELTLPTDI QYEVINKRGN TKIIGSHHDF
1210 1220 1230 1240 1250
QGLYSWDDAE WENRFNQALT LDVDVVKFVG TAVNFEDNLR LEHFRDTHKN
1260 1270 1280 1290 1300
KPLIAVNMTS KGSISRVLNN VLTPVTSDLL PNSAAPGQLT VAQINKMYTS
1310 1320 1330 1340 1350
MGGIEPKELF VVGKPIGHSR SPILHNTGYE ILGLPHKFDK FETESAQLVK
1360 1370 1380 1390 1400
EKLLDGNKNF GGAAVTIPLK LDIMQYMDEL TDAAKVIGAV NTVIPLGNKK
1410 1420 1430 1440 1450
FKGDNTDWLG IRNALINNGV PEYVGHTAGL VIGAGGTSRA ALYALHSLGC
1460 1470 1480 1490 1500
KKIFIINRTT SKLKPLIESL PSEFNIIGIE STKSIEEIKE HVGVAVSCVP
1510 1520 1530 1540 1550
ADKPLDDELL SKLERFLVKG AHAAFVPTLL EAAYKPSVTP VMTISQDKYQ
1560 1570 1580
WHVVPGSQML VHQGVAQFEK WTGFKGPFKA IFDAVTKE
Length:1,588
Mass (Da):174,755
Last modified:August 1, 1988 - v1
Checksum:i9880EE2423CDE410
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06077 Genomic DNA. Translation: CAA29458.1.
Z48179 Genomic DNA. Translation: CAA88208.1.
X13802 Genomic DNA. Translation: CAA32036.1.
X13803 Genomic DNA. Translation: CAA32037.1.
BK006938 Genomic DNA. Translation: DAA11973.1.
PIRiA32519. BVBYA1.
RefSeqiNP_010412.1. NM_001180435.1.

Genome annotation databases

EnsemblFungiiYDR127W; YDR127W; YDR127W.
GeneIDi851705.
KEGGisce:YDR127W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X06077 Genomic DNA. Translation: CAA29458.1.
Z48179 Genomic DNA. Translation: CAA88208.1.
X13802 Genomic DNA. Translation: CAA32036.1.
X13803 Genomic DNA. Translation: CAA32037.1.
BK006938 Genomic DNA. Translation: DAA11973.1.
PIRiA32519. BVBYA1.
RefSeqiNP_010412.1. NM_001180435.1.

3D structure databases

ProteinModelPortaliP08566.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32183. 351 interactions.
DIPiDIP-2611N.
IntActiP08566. 49 interactions.
MINTiMINT-426824.

PTM databases

iPTMnetiP08566.

Proteomic databases

MaxQBiP08566.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR127W; YDR127W; YDR127W.
GeneIDi851705.
KEGGisce:YDR127W.

Organism-specific databases

EuPathDBiFungiDB:YDR127W.
SGDiS000002534. ARO1.

Phylogenomic databases

GeneTreeiENSGT00390000011238.
HOGENOMiHOG000205493.
InParanoidiP08566.
KOiK13830.
OMAiEGQCKIK.
OrthoDBiEOG7KQ28X.

Enzyme and pathway databases

UniPathwayiUPA00053; UER00085.
UPA00053; UER00086.
UPA00053; UER00087.
UPA00053; UER00088.
UPA00053; UER00089.
BioCyciMetaCyc:YDR127W-MONOMER.
YEAST:YDR127W-MONOMER.

Miscellaneous databases

PROiP08566.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
3.40.50.300. 1 hit.
3.40.50.720. 1 hit.
3.65.10.10. 2 hits.
HAMAPiMF_00109. Shikimate_kinase.
MF_00110. DHQ_synthase.
MF_00210. EPSP_synth.
MF_03143. Pentafunct_AroM.
InterProiIPR018508. 3-dehydroquinate_DH_AS.
IPR013785. Aldolase_TIM.
IPR016037. DHQ_synth_AroB.
IPR030960. DHQS/DOIS.
IPR001381. DHquinase_I.
IPR001986. Enolpyruvate_Tfrase_dom.
IPR006264. EPSP_synthase.
IPR023193. EPSP_synthase_CS.
IPR016040. NAD(P)-bd_dom.
IPR027417. P-loop_NTPase.
IPR008289. Pentafunct_AroM.
IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
IPR031322. Shikimate/glucono_kinase.
IPR013708. Shikimate_DH-bd_N.
IPR010110. Shikimate_DH_AroM-type.
IPR000623. Shikimate_kinase/TSH1.
IPR023000. Shikimate_kinase_CS.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
PfamiPF01761. DHQ_synthase. 1 hit.
PF01487. DHquinase_I. 1 hit.
PF00275. EPSP_synthase. 1 hit.
PF01488. Shikimate_DH. 1 hit.
PF08501. Shikimate_dh_N. 1 hit.
PF01202. SKI. 1 hit.
[Graphical view]
PIRSFiPIRSF000514. Pentafunct_AroM. 1 hit.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF55205. SSF55205. 1 hit.
TIGRFAMsiTIGR01356. aroA. 1 hit.
TIGR01357. aroB. 1 hit.
TIGR01093. aroD. 1 hit.
TIGR01809. Shik-DH-AROM. 1 hit.
PROSITEiPS01028. DEHYDROQUINASE_I. 1 hit.
PS00104. EPSP_SYNTHASE_1. 1 hit.
PS00885. EPSP_SYNTHASE_2. 1 hit.
PS01128. SHIKIMATE_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The pentafunctional arom enzyme of Saccharomyces cerevisiae is a mosaic of monofunctional domains."
    Duncan K., Edwards R.M., Coggins J.R.
    Biochem. J. 246:375-386(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
    Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T.
    , del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.
    Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "The Saccharomyces cerevisiae ARO1 gene. An example of the co-ordinate regulation of five enzymes on a single biosynthetic pathway."
    Duncan K., Edwards R.M., Coggins J.R.
    FEBS Lett. 241:83-88(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44 AND 1557-1588.
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiARO1_YEAST
AccessioniPrimary (citable) accession number: P08566
Secondary accession number(s): D6VSB3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: July 6, 2016
This is version 172 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 6420 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

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.