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P08566 (ARO1_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pentafunctional AROM polypeptide

Including the following 5 domains:

  1. 3-dehydroquinate synthase
    Short name=DHQS
    EC=4.2.3.4
  2. 3-phosphoshikimate 1-carboxyvinyltransferase
    EC=2.5.1.19
    Alternative name(s):
    5-enolpyruvylshikimate-3-phosphate synthase
    Short name=EPSP synthase
    Short name=EPSPS
  3. Shikimate kinase
    Short name=SK
    EC=2.7.1.71
  4. 3-dehydroquinate dehydratase
    Short name=3-dehydroquinase
    EC=4.2.1.10
  5. Shikimate dehydrogenase
    EC=1.1.1.25
Gene names
Name:ARO1
Synonyms:AROM
Ordered Locus Names:YDR127W
ORF Names:YD9302.02
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length1588 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate = 3-dehydroquinate + phosphate.

3-dehydroquinate = 3-dehydroshikimate + H2O.

Shikimate + NADP+ = 3-dehydroshikimate + NADPH.

ATP + shikimate = ADP + shikimate 3-phosphate.

Phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Pathway

Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.

Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.

Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.

Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.

Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm.

Miscellaneous

Present with 6420 molecules/cell in log phase SD medium. Ref.5

Sequence similarities

In the N-terminal section; belongs to the dehydroquinate synthase family.

In the 2nd section; belongs to the EPSP synthase family.

In the 3rd section; belongs to the shikimate kinase family.

In the 4th section; belongs to the type-I 3-dehydroquinase family.

In the C-terminal section; belongs to the shikimate dehydrogenase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

HSC82P151083EBI-2883,EBI-8666

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 15881588Pentafunctional AROM polypeptide
PRO_0000140862

Regions

Nucleotide binding43 – 453NAD By similarity
Nucleotide binding78 – 814NAD By similarity
Nucleotide binding109 – 1113NAD By similarity
Nucleotide binding134 – 1352NAD By similarity
Nucleotide binding174 – 1774NAD By similarity
Nucleotide binding895 – 9028ATP By similarity
Region1 – 3923923-dehydroquinate synthase
Region189 – 1924Substrate binding 2 By similarity
Region272 – 2765Substrate binding 2 By similarity
Region405 – 871467EPSP synthase
Region888 – 1080193Shikimate kinase
Region1081 – 12932133-dehydroquinase
Region1306 – 1588283Shikimate dehydrogenase

Sites

Active site2681Proton acceptor; for 3-dehydroquinate synthase activity By similarity
Active site2831Proton acceptor; for 3-dehydroquinate synthase activity By similarity
Active site8531For EPSP synthase activity Potential
Active site11981Proton acceptor; for 3-dehydroquinate dehydratase activity By similarity
Active site12271Schiff-base intermediate with substrate; for 3-dehydroquinate dehydratase activity By similarity
Metal binding1891Zinc; catalytic By similarity
Metal binding2791Zinc; catalytic By similarity
Metal binding2951Zinc; catalytic By similarity
Binding site1141NAD By similarity
Binding site1251Substrate 1 By similarity
Binding site1411Substrate 2 By similarity
Binding site1471Substrate 2 By similarity
Binding site1561NAD By similarity
Binding site1571Substrate 2 By similarity
Binding site1851NAD By similarity
Binding site2581Substrate 2 By similarity
Binding site2791Substrate 2 By similarity
Binding site2951Substrate 2 By similarity
Binding site3641Substrate 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
P08566 [UniParc].

Last modified August 1, 1988. Version 1.
Checksum: 9880EE2423CDE410

FASTA1,588174,755
        10         20         30         40         50         60 
MVQLAKVPIL GNDIIHVGYN IHDHLVETII KHCPSSTYVI CNDTNLSKVP YYQQLVLEFK 

        70         80         90        100        110        120 
ASLPEGSRLL TYVVKPGETS KSRETKAQLE DYLLVEGCTR DTVMVAIGGG VIGDMIGFVA 

       130        140        150        160        170        180 
STFMRGVRVV QVPTSLLAMV DSSIGGKTAI DTPLGKNFIG AFWQPKFVLV DIKWLETLAK 

       190        200        210        220        230        240 
REFINGMAEV IKTACIWNAD EFTRLESNAS LFLNVVNGAK NVKVTNQLTN EIDEISNTDI 

       250        260        270        280        290        300 
EAMLDHTYKL VLESIKVKAE VVSSDERESS LRNLLNFGHS IGHAYEAILT PQALHGECVS 

       310        320        330        340        350        360 
IGMVKEAELS RYFGILSPTQ VARLSKILVA YGLPVSPDEK WFKELTLHKK TPLDILLKKM 

       370        380        390        400        410        420 
SIDKKNEGSK KKVVILESIG KCYGDSAQFV SDEDLRFILT DETLVYPFKD IPADQQKVVI 

       430        440        450        460        470        480 
PPGSKSISNR ALILAALGEG QCKIKNLLHS DDTKHMLTAV HELKGATISW EDNGETVVVE 

       490        500        510        520        530        540 
GHGGSTLSAC ADPLYLGNAG TASRFLTSLA ALVNSTSSQK YIVLTGNARM QQRPIAPLVD 

       550        560        570        580        590        600 
SLRANGTKIE YLNNEGSLPI KVYTDSVFKG GRIELAATVS SQYVSSILMC APYAEEPVTL 

       610        620        630        640        650        660 
ALVGGKPISK LYVDMTIKMM EKFGINVETS TTEPYTYYIP KGHYINPSEY VIESDASSAT 

       670        680        690        700        710        720 
YPLAFAAMTG TTVTVPNIGF ESLQGDARFA RDVLKPMGCK ITQTATSTTV SGPPVGTLKP 

       730        740        750        760        770        780 
LKHVDMEPMT DAFLTACVVA AISHDSDPNS ANTTTIEGIA NQRVKECNRI LAMATELAKF 

       790        800        810        820        830        840 
GVKTTELPDG IQVHGLNSIK DLKVPSDSSG PVGVCTYDDH RVAMSFSLLA GMVNSQNERD 

       850        860        870        880        890        900 
EVANPVRILE RHCTGKTWPG WWDVLHSELG AKLDGAEPLE CTSKKNSKKS VVIIGMRAAG 

       910        920        930        940        950        960 
KTTISKWCAS ALGYKLVDLD ELFEQQHNNQ SVKQFVVENG WEKFREEETR IFKEVIQNYG 

       970        980        990       1000       1010       1020 
DDGYVFSTGG GIVESAESRK ALKDFASSGG YVLHLHRDIE ETIVFLQSDP SRPAYVEEIR 

      1030       1040       1050       1060       1070       1080 
EVWNRREGWY KECSNFSFFA PHCSAEAEFQ ALRRSFSKYI ATITGVREIE IPSGRSAFVC 

      1090       1100       1110       1120       1130       1140 
LTFDDLTEQT ENLTPICYGC EAVEVRVDHL ANYSADFVSK QLSILRKATD SIPIIFTVRT 

      1150       1160       1170       1180       1190       1200 
MKQGGNFPDE EFKTLRELYD IALKNGVEFL DLELTLPTDI QYEVINKRGN TKIIGSHHDF 

      1210       1220       1230       1240       1250       1260 
QGLYSWDDAE WENRFNQALT LDVDVVKFVG TAVNFEDNLR LEHFRDTHKN KPLIAVNMTS 

      1270       1280       1290       1300       1310       1320 
KGSISRVLNN VLTPVTSDLL PNSAAPGQLT VAQINKMYTS MGGIEPKELF VVGKPIGHSR 

      1330       1340       1350       1360       1370       1380 
SPILHNTGYE ILGLPHKFDK FETESAQLVK EKLLDGNKNF GGAAVTIPLK LDIMQYMDEL 

      1390       1400       1410       1420       1430       1440 
TDAAKVIGAV NTVIPLGNKK FKGDNTDWLG IRNALINNGV PEYVGHTAGL VIGAGGTSRA 

      1450       1460       1470       1480       1490       1500 
ALYALHSLGC KKIFIINRTT SKLKPLIESL PSEFNIIGIE STKSIEEIKE HVGVAVSCVP 

      1510       1520       1530       1540       1550       1560 
ADKPLDDELL SKLERFLVKG AHAAFVPTLL EAAYKPSVTP VMTISQDKYQ WHVVPGSQML 

      1570       1580 
VHQGVAQFEK WTGFKGPFKA IFDAVTKE

« Hide

References

« Hide 'large scale' references
[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: 2825635] [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. expand/collapse author list , 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: 9169867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204511 / S288c / AB972.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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: 2848727] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44 AND 1557-1588.
[5]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		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.
PIRBVBYA1. A32519.
RefSeqNP_010412.1. NM_001180435.1.

3D structure databases

ProteinModelPortalP08566.
SMRP08566. Positions 3-401, 404-870, 887-1037, 1077-1302, 1304-1587.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-2611N.
IntActP08566. 55 interactions.
MINTMINT-426824.
STRINGP08566.

Proteomic databases

PeptideAtlasP08566.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDR127W; YDR127W; YDR127W.
GeneID851705.
KEGGsce:YDR127W.
NMPDRfig|4932.3.peg.1161.

Organism-specific databases

CYGDYDR127w.
SGDS000002534. ARO1.

Phylogenomic databases

eggNOGfuNOG05766.
GeneTreeEFGT00050000002265.
HOGENOMHBG398536.
OMASSQYVSS.
OrthoDBEOG4PRWZT.

Enzyme and pathway databases

BioCycMetaCyc:YDR127W-MONOMER.

Gene expression databases

ArrayExpressP08566.
GenevestigatorP08566.
GermOnlineYDR127W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR018508. 3-dehydroquinate_DH_AS.
IPR013785. Aldolase_TIM.
IPR016037. DHQ_synth_AroB.
IPR001381. DHquinase_I.
IPR001986. Enolpyruvate_Tfrase_dom.
IPR006264. EPSP_synthase.
IPR023193. EPSP_synthase_CS.
IPR016040. NAD(P)-bd_dom.
IPR008289. Pentafunct_AroM.
IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
IPR013708. Shikimate_DH-bd_N.
IPR010110. Shikimate_DH_AroM-type.
IPR000623. Shikimate_kinase.
IPR023000. Shikimate_kinase_CS.
IPR006151. Shikm_DH/Glu-tRNA_Rdtase.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
G3DSA:3.65.10.10. EPSP_synthase. 2 hits.
G3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
KOK13830.
PANTHERPTHR21090:SF1. DHQ_synth_AroB. 1 hit.
PfamPF01487. 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]
PIRSFPIRSF000514. Pentafunct_AroM. 1 hit.
PRINTSPR01100. SHIKIMTKNASE.
SUPFAMSSF55205. RNA3'_cycl/enolpyr_transf_A/B. 1 hit.
TIGRFAMsTIGR01356. AroA. 1 hit.
TIGR01357. AroB. 1 hit.
TIGR01093. AroD. 1 hit.
TIGR01809. Shik-DH-AROM. 1 hit.
PROSITEPS01028. DEHYDROQUINASE_I. 1 hit.
PS00104. EPSP_SYNTHASE_1. 1 hit.
PS00885. EPSP_SYNTHASE_2. 1 hit.
PS01128. SHIKIMATE_KINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio969386.

Entry information

Entry nameARO1_YEAST
AccessionPrimary (citable) accession number: P08566
Secondary accession number(s): D6VSB3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: August 1, 1988
Last modified: December 14, 2011
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents