Reviewed, UniProtKB/Swiss-Prot Q9P7R0 (ARO1_SCHPO)

Names and origin

Protein names

Recommended name:
    Pentafunctional AROM polypeptide
Including the following 5 domains:
    1- Recommended name:
            3-dehydroquinate synthase
              EC=4.2.3.4
    2- Recommended name:
            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- Recommended name:
            Shikimate kinase
              EC=2.7.1.71
    4- Recommended name:
            3-dehydroquinate dehydratase
                Short name=3-dehydroquinase
              EC=4.2.1.10
    5- Recommended name:
            Shikimate dehydrogenase
              EC=1.1.1.25

Gene names

Name:	aro1
ORF Names:	SPAC1834.02

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	1573 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis By similarity.
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.
Pathway	Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and PEP: step 2/7. Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and PEP: step 3/7. Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and PEP: step 4/7. Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and PEP: step 5/7. Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and PEP: step 6/7.
Subcellular location	Cytoplasm By similarity.
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 C-terminal section; belongs to the shikimate dehydrogenase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding NADP Nucleotide-binding
Molecular function	Kinase Lyase Oxidoreductase Transferase
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	aromatic amino acid family biosynthetic process Non-traceable author statement. Source: GeneDB_SPombe oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	3-dehydroquinate dehydratase activity Inferred from electronic annotation. Source: EC 3-dehydroquinate synthase activity Inferred from electronic annotation. Source: EC 3-phosphoshikimate 1-carboxyvinyltransferase activity Inferred from electronic annotation. Source: EC ATP binding Inferred from electronic annotation. Source: UniProtKB-KW shikimate 5-dehydrogenase activity Inferred from electronic annotation. Source: EC shikimate kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1573	1573	Pentafunctional AROM polypeptide		PRO_0000140861
Regions
	Nucleotide binding	870 – 877	8	ATP Potential
	Region	1 – 384	384	3-dehydroquinate synthase Potential
	Region	397 – 843	447	EPSP synthase Potential
	Region	858 – 1058	201	Shikimate kinase Potential
	Region	1059 – 1280	222	3-dehydroquinase Potential
	Region	1293 – 1573	281	Shikimate dehydrogenase Potential
Sites
	Active site	825	1	Potential
	Active site	1182	1	Proton acceptor By similarity
	Active site	1211	1	Schiff-base intermediate with substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9P7R0-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 418968DA6330280D	FASTA	1,573	173,782
	10 20 30 40 50 60 MSNESNIITV PILGKDTVRV GFGIHQYICT EILENFKSST YVVITDSNIA PLYLEKIEST 70 80 90 100 110 120 FNKSIKDAKA EARLLTYVIP PGESSKCRAM KAEIEDWLLT QSCTRDTILI AMGGGVIGDL 130 140 150 160 170 180 VGYVAASFMR GIRFIQMPTT LLAMVDSSIG GKTGIDTPLG KNLVGAFWQP LRVYVDMVFL 190 200 210 220 230 240 HTLPPRQVIN GLSEIIKTAA MWNENDFQLL ENNSAVLLDA LNKPSVPGEY KFDSIKPLLQ 250 260 270 280 290 300 KIILSSIRTK CEVVTLDEHE GGLRNLLNFG HSIGHAYEAI LYPQILHGEC VAIGMVKEAE 310 320 330 340 350 360 LARYLGILKP NAVGRLTKCL VSYNLPISVN DPKVKKYASF KHCPVEKLIE YMAVDKKNQG 370 380 390 400 410 420 SKKRIVILKA IGETYEKHAT VVSDDDIRFI LSRDVKVDEF TKSSWDVVVT PPGSKSISNR 430 440 450 460 470 480 ALVLAAMGNG TCRLTNMLHS DDTQFMMSAL ESLGAATFSW EDGGETLVVK GNGGKLAVPK 490 500 510 520 530 540 EELYLGNAGT AARFLTGIAA LVSSKDGAKV VLTGNHRMKV RPIGPLVDAL RANGCEINYL 550 560 570 580 590 600 EKQGSLPLDL SSKNGLKGGI IELAATVSSQ YVSSILMCAP YASQPVTLKL VGGKPISQLY 610 620 630 640 650 660 IDMTIAMMAS FGVNVTKSTT EENTYNIPCG KYQNPPHYEI ESDASSATYP LAIAAITGTK 670 680 690 700 710 720 CTVPNIGSAS LQGDARFACD VLRPMGCTVE QTATSTTVQG PPKGTLKPLE SIDMETMTDA 730 740 750 760 770 780 FLTASVVAAV ACNVSEGDPV TRITGIANQR VKECNRIAAM VHELAKFGVR TGELEDGIYI 790 800 810 820 830 840 FGKNYKELKK PEEGIYTYDD HRIAMSFSVL SLICPSRTLI IDKACVEKTW PYWWDVLHQS 850 860 870 880 890 900 FGVKLTGATS VASDPLKGSI SKNASIILIG MRGAGKTTIG KIIAKQLNFK FLDLDELLED 910 920 930 940 950 960 YLEMPIAEVI FRMGWDAFRL EEHKVLRKFI TEHPEGYVAA SGGGVIEMDE SRNLLSNFVK 970 980 990 1000 1010 1020 EGGIVLHVHR NLEHIKSYLS EDQTRPTYKD QESIDDVYKR RHVWYRECRS HYFISPVLSN 1030 1040 1050 1060 1070 1080 QVIDEKIQYS MSRFLDVVTG SSQVLQKFKT KKRSTFLTLN YPRIEDALPT LRDVTVGCDA 1090 1100 1110 1120 1130 1140 IEVRVDYLKD PKSSNGISSL DFVAEQISLL RCSTTLPIIF TIRTISQGGL FPNDKEEEAK 1150 1160 1170 1180 1190 1200 ELMLSAMRYG CDFVDVELGW SSETINILYQ HKGYTKLIMS WHDLSGTWSW ARPHEWMQKV 1210 1220 1230 1240 1250 1260 ELASSYADVI KLVGMANNLN DNLELEEFRT RITNSMDIPL ILFNMGRFGQ LSRILNKFMT 1270 1280 1290 1300 1310 1320 PVTHPLLPSK AAPGQLTVKQ LNEARVLIGE ILPEKFFLFG KPIKHSRSPI LHSTAYELLG 1330 1340 1350 1360 1370 1380 LPHTYEAFET DTVDEVQKVL NLPDFGGANV TIPYKLSVMK FMDELSDEAR FFGAVNTIIP 1390 1400 1410 1420 1430 1440 IRIGDKLVLR GDNTDWRGIY DTFANALDGV SLRDTNGLVI GAGGTSRAAI YSLHRLGVSR 1450 1460 1470 1480 1490 1500 IYLLNRTLAN SYRVQDVFPP DYNIHIIDSD NIPSEELSSV TLSAVVSTIP ADIELPEKVA 1510 1520 1530 1540 1550 1560 SVIKALLANK ADGGVFLDMA YKPLHTPLMA VASDLEWKCC NGLEALVRQG LASFHLWTGM 1570 TAPFDAVYQK VIE

References

[1]

"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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329670 Genomic DNA. Translation: CAB75770.1.
PIR	T50113.
RefSeq	NP_594681.1.
3D structure databases
HSSP	HSSP built from PDB template 1NVE based on UniProtKB P07547.
ModBase	Search...
Genome annotation databases
GeneID	2542115.
KEGG	spo:SPAC1834.02.
NMPDR	fig|4896.1.peg.4651.
Organism-specific databases
GeneDB_Spombe	SPAC1834.02.
Phylogenomic databases
OMA	Q9P7R0. SSQYVSS.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-002767-MON.
BRENDA	1.1.1.25. 653. 2.5.1.19. 653. 2.7.1.71. 653. 4.2.1.10. 653. 4.2.3.4. 653.
Gene expression databases
ArrayExpress	Q9P7R0.
Family and domain databases
InterPro	IPR018508. 3-dehydroquinate_DH_AS. IPR013785. Aldolase_TIM. IPR002658. DHQ_synth_AroB. IPR016037. DHQ_synth_AroB_sub. IPR001381. DHquinase_I. IPR001986. EPSP_synthase_core. IPR006264. EPSP_synthase_subgroup. IPR008289. Pentafunct_AroM. IPR010110. Shik_DH_AROM. IPR000623. Shik_kinase. IPR013708. Shikimate_DH-bd_N. IPR006151. Shikm_DH/Glu-tRNA_Rdtase. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit. G3DSA:3.65.10.10. EPSP_synthase. 1 hit.
PANTHER	PTHR21090:SF1. DHQ_synth_AroB. 1 hit.
Pfam	PF01761. 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]
PIRSF	PIRSF000514. Pentafunct_AroM. 1 hit.
PRINTS	PR01100. SHIKIMTKNASE.
ProDom	PD005337. DHquinase_I. 1 hit. PD001867. EPSP_synth. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR01356. aroA. 1 hit. TIGR01357. aroB. 1 hit. TIGR01093. aroD. 1 hit. TIGR01809. Shik-DH-AROM. 1 hit.
PROSITE	PS01028. DEHYDROQUINASE_I. False negative. PS00104. EPSP_SYNTHASE_1. 1 hit. PS00885. EPSP_SYNTHASE_2. 1 hit. PS01128. SHIKIMATE_KINASE. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARO1_SCHPO

Accession

Primary (citable) accession number: Q9P7R0

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 14, 2001
Last sequence update:	October 1, 2000
Last modified:	June 16, 2009
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)