Reviewed, UniProtKB/Swiss-Prot P07547 (ARO1_EMENI)

Names and origin

Protein names

Recommended name:
    Pentafunctional AROM polypeptide
Including the following 5 domains:
    1- Recommended name:
            3-dehydroquinate synthase
                Short name=DHQS
              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:	aroMA
Synonyms:	aroM
ORF Names:	AN0708

Organism

Emericella nidulans (Aspergillus nidulans)

Taxonomic identifier

162425 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella

Protein attributes

Sequence length	1583 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.
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.
Subunit structure	Homodimer.
Subcellular location	Cytoplasm.
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.
Sequence caution	The sequence CAA28836.1 differs from that shown. Reason: Erroneous gene model prediction. The sequence CAA28836.1 differs from that shown. Reason: Frameshift at positions 534, 545, 708, 733 and 743. The sequence EAA65484.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Metal-binding NADP Nucleotide-binding Zinc
Molecular function	Kinase Lyase Oxidoreductase Transferase
Technical term	3D-structure Multifunctional enzyme
Gene Ontology (GO)
Biological process	aromatic amino acid family biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 1583

1583

Pentafunctional AROM polypeptide

PRO_0000140859

Regions

Nucleotide binding

44 – 46

3

NAD

Nucleotide binding

81 – 84

4

NAD

Nucleotide binding

114 – 116

3

NAD

Nucleotide binding

139 – 140

2

NAD

Nucleotide binding

179 – 182

4

NAD

Nucleotide binding

870 – 877

8

ATP By similarity

Region

1 – 384

384

3-dehydroquinate synthase

Region

194 – 197

4

Substrate binding 2

Region

264 – 268

5

Substrate binding 2

Region

397 – 842

446

EPSP synthase

Region

862 – 1055

194

Shikimate kinase

Region

1056 – 1276

221

3-dehydroquinase

Region

1289 – 1583

295

Shikimate dehydrogenase

Sites

Active site

260

1

Proton acceptor

Active site

275

1

Proton acceptor

Active site

824

1

Potential

Active site

1179

1

Proton acceptor By similarity

Active site

1207

1

Schiff-base intermediate with substrate By similarity

Metal binding

194

1

Zinc; catalytic

Metal binding

271

1

Zinc; catalytic

Metal binding

287

1

Zinc; catalytic

Binding site

119

1

NAD

Binding site

130

1

Substrate 1

Binding site

146

1

Substrate 2

Binding site

152

1

Substrate 2

Binding site

161

1

NAD

Binding site

162

1

Substrate 2

Binding site

190

1

NAD

Binding site

250

1

Substrate 2

Binding site

271

1

Substrate 2

Binding site

287

1

Substrate 2

Binding site

356

1

Substrate 2

Experimental info

Sequence conflict

62

1

A → R in CAA28836. Ref.1

Sequence conflict

77

1

A → R in CAA28836. Ref.1

Sequence conflict

226

1

R → T in CAA28836. Ref.1

Sequence conflict

235

1

I → T in CAA28836. Ref.1

Sequence conflict

403

1

Q → H in CAA28836. Ref.1

Sequence conflict

535

1

A → P in CAA28836. Ref.1

Sequence conflict

646

1

S → C in CAA28836. Ref.1

Sequence conflict

862

1

A → G in CAA28836. Ref.1

Sequence conflict

862

1

A → G Ref.3

Sequence conflict

984

1

T → S in CAA28836. Ref.1

Sequence conflict

984

1

T → S Ref.3

Sequence conflict

1048

1

K → G Ref.3

Sequence conflict

1093

1

D → N Ref.3

Sequence conflict

1154

1

E → D in CAA28836. Ref.1

Sequence conflict

1154

1

E → D Ref.3

Sequence conflict

1345 – 1349

5

SVTIP → FRNNS in CAA28836. Ref.1

Secondary structure

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1583

Helix Strand Turn

Details...

Beta strand

5 – 9

5

Beta strand

12 – 17

6

Helix

21 – 24

4

Helix

26 – 33

8

Beta strand

37 – 44

8

Turn

45 – 47

3

Helix

48 – 62

15

Turn

63 – 65

3

Beta strand

71 – 77

7

Helix

81 – 83

3

Helix

86 – 97

12

Beta strand

99 – 101

3

Beta strand

108 – 114

7

Helix

115 – 127

13

Beta strand

133 – 138

6

Helix

141 – 145

5

Turn

146 – 148

3

Beta strand

152 – 157

6

Beta strand

160 – 167

8

Beta strand

171 – 175

5

Helix

177 – 182

6

Helix

185 – 200

16

Helix

204 – 222

19

Helix

233 – 235

3

Helix

236 – 256

21

Helix

263 – 268

6

Helix

271 – 281

11

Turn

282 – 284

3

Helix

287 – 304

18

Helix

310 – 322

13

Helix

332 – 337

6

Helix

345 – 352

8

Beta strand

368 – 370

3

Beta strand

373 – 378

6

Helix

384 – 390

7

Sequences

	Sequence		Length	Mass (Da)
	P07547-1 [UniParc]. Last modified May 26, 2009. Version 3. Checksum: FBC8610B961840D8	FASTA	1,583	172,664
	10 20 30 40 50 60 MSNPTKISIL GRESIIADFG LWRNYVAKDL ISDCSSTTYV LVTDTNIGSI YTPSFEEAFR 70 80 90 100 110 120 KAAAEITPSP RLLIYNAPPG EVSKSRQTKA DIEDWMLSQN PPCGRDTVVI ALGGGVIGDL 130 140 150 160 170 180 TGFVASTYMR GVRYVQVPTT LLAMVDSSIG GKTAIDTPLG KNLIGAIWQP TKIYIDLEFL 190 200 210 220 230 240 ETLPVREFIN GMAEVIKTAA ISSEEEFTAL EENAETILKA VRREVRPGEH RFEGIEEILK 250 260 270 280 290 300 ARILASARHK AYVVSADERE GGLRNLLNWG HSIGHAIEAI LTPQILHGEC VAIGMVKEAE 310 320 330 340 350 360 LARHLGILKG VAVSRIVKCL AAYGLPTSLK DARIRKLTAG KHCSVDQLMF NMALDKKNDG 370 380 390 400 410 420 PKKKIVLLSA IGTPYETRAS VVANEDIRVV LAPSIEVHPG VAQSSNVICA PPGSKSISNR 430 440 450 460 470 480 ALVLAALGSG TCRIKNLLHS DDTEVMLNAL ERLGAATFSW EEEGEVLVVN GKGGNLQASS 490 500 510 520 530 540 SPLYLGNAGT ASRFLTTVAT LANSSTVDSS VLTGNNRMKQ RPIGDLVDAL TANGASIEYV 550 560 570 580 590 600 ERTGSLPLKI AASGGFAGGN INLAAKVSSQ YVSSLLMCAP YAKEPVTLRL VGGKPISQPY 610 620 630 640 650 660 IDMTTAMMRS FGIDVQKSTT EEHTYHIPQG RYVNPAEYVI ESDASSATYP LAVAAVTGTT 670 680 690 700 710 720 CTVPNIGSAS LQGDARFAVE VLRPMGCTVE QTETSTTVTG PSDGILRPLP NVDMEPMTDA 730 740 750 760 770 780 FLGASVLAAI ARGKESNHTT RIYGIANQRV KECNRIKAMK DELAKFGVIC REHDDGLEID 790 800 810 820 830 840 GIDRSNLRQP VGGVFCYDDH RVAFSFSVLS LVTPQPTLIL EKECVGKTWP GWWDTLRQLF 850 860 870 880 890 900 KVKLEGKELE EEPVAASGPD RANASIYIIG MRGAGKSTAG NWVSKALNRP FVDLDTELET 910 920 930 940 950 960 VEGMTIPDII KTRGWQGFRN AELEILKRTL KERSRGYVFA CGGGVVEMPE ARKLLTDYHK 970 980 990 1000 1010 1020 TKGNVLLLMR DIKKIMDFLS IDKTRPAYVE DMMGVWLRRK PWFQECSNIQ YYSRDASPSG 1030 1040 1050 1060 1070 1080 LARASEDFNR FLQVATGQID SLSIIKEKEH SFFASLTLPD LREAGDILEE VCVGSDAVEL 1090 1100 1110 1120 1130 1140 RVDLLKDPAS NNDIPSVDYV VEQLSFLRSR VTLPIIFTIR TQSQGGRFPD NAHDAALELY 1150 1160 1170 1180 1190 1200 RLAFRSGCEF VDLEIAFPED MLRAVTEMKG FSKIIASHHD PKGELSWANM SWIKFYNKAL 1210 1220 1230 1240 1250 1260 EYGDIIKLVG VARNIDDNTA LRKFKNWAAE AHDVPLIAIN MGDQGQLSRI LNGFMTPVSH 1270 1280 1290 1300 1310 1320 PSLPFKAAPG QLSATEIRKG LSLMGEIKPK KFAIFGSPIS QSRSPALHNT LFAQVGLPHN 1330 1340 1350 1360 1370 1380 YTRLETTNAQ DVQEFIRSPD FGGASVTIPL KLDIMPLLDE VAAEAEIIGA VNTIIPVSTG 1390 1400 1410 1420 1430 1440 KNTPSRLVGR NTDWQGMILS LRKAGVYGPK RKDQEQSALV VGGGGTARAA IYALHNMGYS 1450 1460 1470 1480 1490 1500 PIYIVGRTPS KLENMVSTFP SSYNIRIVES PSSFESVPHV AIGTIPADQP IDPTMRETLC 1510 1520 1530 1540 1550 1560 HMFERAQEAD AEAVKAIEHA PRILLEMAYK PQVTALMRLA SDSGWKTIPG LEVLVGQGWY 1570 1580 QFKYWTGISP LYESARACSS PLI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The isolation and nucleotide sequence of the complex AROM locus of Aspergillus nidulans." Charles I.G., Keyte J.W., Brammar W.J., Smith M., Hawkins A.R. Nucleic Acids Res. 14:2201-2213(1986) [PubMed: 3515316] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: R153.
[2]	"Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H. , Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L., Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W. Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC 4.
[3]	"Nucleotide sequence encoding the biosynthetic dehydroquinase function of the penta-functional arom locus of Aspergillus nidulans." Charles I.G., Keyte J.W., Brammar W.J., Hawkins A.R. Nucleic Acids Res. 13:8119-8128(1985) [PubMed: 3906567] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 843-1473. Strain: R153.
[4]	Hawkins A.R. Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO C-TERMINUS.
[5]	"Comparative analysis of the QUTR transcription repressor protein and the three C-terminal domains of the pentafunctional AROM enzyme." Lamb H.K., Moore J.D., Lakey J.H., Levett L.J., Wheeler K.A., Lago H., Coggins J.R., Hawkins A.R. Biochem. J. 313:941-950(1996) [PubMed: 8611179] [Abstract] Cited for: IDENTIFICATION OF INTRON.
[6]	"Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis." Carpenter E.P., Hawkins A.R., Frost J.W., Brown K.A. Nature 394:299-302(1998) [PubMed: 9685163] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-393 IN COMPLEX WITH NAD; ZINC AND SUBSTRATE ANALOG, SUBUNIT.
[7]	"Ligand-induced conformational changes and a mechanism for domain closure in Aspergillus nidulans dehydroquinate synthase." Nichols C.E., Ren J., Lamb H.K., Hawkins A.R., Stammers D.K. J. Mol. Biol. 327:129-144(2003) [PubMed: 12614613] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-393 IN COMPLEX WITH ADP; NAD; ZINC AND SUBSTRATE ANALOG.
[8]	"Structure of the 'open' form of Aspergillus nidulans 3-dehydroquinate synthase at 1.7 A resolution from crystals grown following enzyme turnover." Nichols C.E., Hawkins A.R., Stammers D.K. Acta Crystallogr. D 60:971-973(2004) [PubMed: 15103156] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-393.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X05204 Genomic DNA. Translation: CAA28836.1. Sequence problems.
AACD01000010 Genomic DNA. Translation: EAA65484.1. Sequence problems.
AACD01000011 Genomic DNA. No translation available.

PIR

BVASA1. A24962.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DQS	X-ray	1.80	A/B	1-393	[»]
1NR5	X-ray	2.10	A/B	1-393	[»]
1NRX	X-ray	2.90	A/B	1-393	[»]
1NUA	X-ray	2.85	A/B	1-393	[»]
1NVA	X-ray	2.62	A/B	1-393	[»]
1NVB	X-ray	2.70	A/B	1-393	[»]
1NVD	X-ray	2.51	A/B	1-393	[»]
1NVE	X-ray	2.58	A/B/C/D	1-393	[»]
1NVF	X-ray	2.80	A/B/C	1-393	[»]
1SG6	X-ray	1.70	A/B	1-393	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

1.1.1.25. 3859.
2.5.1.19. 3859.
2.7.1.71. 3859.
4.2.1.10. 3859.
4.2.3.4. 3859.

Family and domain databases

ProDom

PD005337. DHquinase_I. 1 hit.
PD001867. EPSP_synth. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS01028. DEHYDROQUINASE_I. 1 hit.
PS00104. EPSP_SYNTHASE_1. 1 hit.
PS00885. EPSP_SYNTHASE_2. 1 hit.
PS01128. SHIKIMATE_KINASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

ARO1_EMENI

Accession

Primary (citable) accession number: P07547
Secondary accession number(s): Q5BFH2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	May 26, 2009
Last modified:	June 16, 2009
This is version 97 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)