3-dehydroquinate synthase
     (EC 4.2.3.4)
3-phosphoshikimate 1-carboxyvinyltransferase
     (EC 2.5.1.19)
     (5-enolpyruvylshikimate-3-phosphate synthase)
     (EPSP synthase)
     (EPSPS)
Shikimate kinase
     (EC 2.7.1.71)
3-dehydroquinate dehydratase
     (3-dehydroquinase)
     (EC 4.2.1.10)
Shikimate dehydrogenase
     (EC 1.1.1.25)

Gene name

	Name:	aroMA
	Synonyms:	aroM

From

Emericella nidulans (Aspergillus nidulans)

[TaxID: 162425]

Taxonomy

Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; Eurotiomycetidae; Eurotiales; Trichocomaceae; Emericella.

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=R153; DOI=10.1093/nar/14.5.2201; PubMed=3515316 [NCBI, ExPASy, EBI, Israel, Japan] Charles I.G., Keyte J.W., Brammar W.J., Smith M., Hawkins A.R.; "The isolation and nucleotide sequence of the complex AROM locus of Aspergillus nidulans."; Nucleic Acids Res. 14:2201-2213(1986).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 844-1474. STRAIN=R153; DOI=10.1093/nar/13.22.8119; PubMed=3906567 [NCBI, ExPASy, EBI, Israel, Japan] Charles I.G., Keyte J.W., Brammar W.J., Hawkins A.R.; "Nucleotide sequence encoding the biosynthetic dehydroquinase function of the penta-functional arom locus of Aspergillus nidulans."; Nucleic Acids Res. 13:8119-8128(1985).
[3]	SEQUENCE REVISION TO C-TERMINUS. Hawkins A.R.; Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
[4]	X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-393. DOI=10.1038/28431; PubMed=9685163 [NCBI, ExPASy, EBI, Israel, Japan] Carpenter E.P., Hawkins A.R., Frost J.W., Brown K.A.; "Structure of dehydroquinate synthase reveals an active site capable of multistep catalysis."; Nature 394:299-302(1998).

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.
CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H₂O.
CATALYTIC ACTIVITY: Shikimate + NADP⁺ = 3-dehydroshikimate + NADPH.
CATALYTIC ACTIVITY: ATP + shikimate = ADP + shikimate 3-phosphate.
CATALYTIC ACTIVITY: 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 .
PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and PEP: step 3/7 .
PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and PEP: step 4/7 .
PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and PEP: step 5/7 .
PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and PEP: step 6/7 .
PATHWAY: Context: Aromatic amino acids biosynthesis .
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: In the N-terminal section; belongs to the dehydroquinate synthase family.
SIMILARITY: In the 2nd section; belongs to the EPSP synthase family.
SIMILARITY: In the 3rd section; belongs to the shikimate kinase family.
SIMILARITY: In the C-terminal section; belongs to the shikimate dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X05204; CAA28836.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A24962; BVASA1.

3D structure databases

PDB

1DQS; X-ray; 1.80 A; A/B=1-393.	[ExPASy / RCSB / EBI]
1NR5; X-ray; 2.10 A; A/B=1-393.	[ExPASy / RCSB / EBI]
1NRX; X-ray; 2.90 A; A/B=1-393.	[ExPASy / RCSB / EBI]
1NUA; X-ray; 2.85 A; A/B=1-393.	[ExPASy / RCSB / EBI]
1NVA; X-ray; 2.62 A; A/B=1-393.	[ExPASy / RCSB / EBI]
1NVB; X-ray; 2.70 A; A/B=1-393.	[ExPASy / RCSB / EBI]
1NVD; X-ray; 2.51 A; A/B=1-393.	[ExPASy / RCSB / EBI]
1NVE; X-ray; 2.58 A; A/B/C/D=1-393.	[ExPASy / RCSB / EBI]
1NVF; X-ray; 2.80 A; A/B/C=1-393.	[ExPASy / RCSB / EBI]
1SG6; X-ray; 1.70 A; A/B=1-393.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1DQS; -.
1NR5; -.
1NRX; -.
1NUA; -.
1NVA; -.
1NVB; -.
1NVD; -.
1NVE; -.
1NVF; -.
1SG6; -.

ModBase

P07547.

Family and domain databases

InterPro

IPR013785; Aldolase_TIM.
IPR002658; DHQ_synth_AroB.
IPR016037; DHQ_synth_AroB_sub.
IPR001381; DHquinase_I.
IPR001986; EPSP_synthase_core.
IPR006264; EPSP_synthase_subgroup.
IPR016040; NAD(P)-bd.
IPR008289; Pentafunct_AroM.
IPR010110; Shik_DHase_AROM.
IPR000623; Shik_kinase.
IPR013708; Shikimate_DHase-bd_N.
IPR006151; Shikm_DHase/Glu-tRNA_Rdtase.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.70; Aldolase_TIM; 1.
G3DSA:3.65.10.10; EPSP_synthase; 1.
G3DSA:3.40.50.720; NAD(P)-bd; 1.

PANTHER

PTHR21090:SF1; DHQ_synth_AroB; 1.

Pfam

PF01761; DHQ_synthase; 1.
PF01487; DHquinase_I; 1.
PF00275; EPSP_synthase; 1.
PF01488; Shikimate_DH; 1.
PF08501; Shikimate_dh_N; 1.
PF01202; SKI; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000514; Pentafunct_AroM; 1.

PRINTS

PR01100; SHIKIMTKNASE.

ProDom

PD005337; DHquinase_I; 1.
PD001867; EPSP_synth; 1.
[Domain structure / List of seq. sharing at least 1 domain]

TIGRFAMs

TIGR01356; aroA; 1.
TIGR01357; aroB; 1.
TIGR01093; aroD; 1.
TIGR01809; Shik-DH-AROM; 1.

PROSITE

PS01028; DEHYDROQUINASE_I; 1.
PS00104; EPSP_SYNTHASE_1; 1.
PS00885; EPSP_SYNTHASE_2; 1.
PS01128; SHIKIMATE_KINASE; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Amino-acid biosynthesis; Aromatic amino acid biosynthesis; ATP-binding; Cytoplasm; Kinase; Lyase; Multifunctional enzyme; NADP; Nucleotide-binding; Oxidoreductase; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 1586`	`1586`	`Pentafunctional AROM polypeptide.`	`PRO_0000140859`
`NP_BIND`	`871 878`	`8`	`ATP (By similarity).`
`REGION`	`1 384`	`384`	`3-dehydroquinate synthase.`
`REGION`	`397 843`	`447`	`EPSP synthase.`
`REGION`	`863 1056`	`194`	`Shikimate kinase.`
`REGION`	`1057 1277`	`221`	`3-dehydroquinase.`
`REGION`	`1290 1586`	`297`	`Shikimate dehydrogenase.`
`ACT_SITE`	`825 825`		`Potential.`
`ACT_SITE`	`1180 1180`		`Proton acceptor (By similarity).`
`ACT_SITE`	`1208 1208`		`Schiff-base intermediate with substrate (By similarity).`
`STRAND`	`5 9`	`5`
`STRAND`	`12 17`	`6`
`HELIX`	`21 24`	`4`
`HELIX`	`26 33`	`8`
`STRAND`	`37 44`	`8`
`TURN`	`45 47`	`3`
`HELIX`	`48 62`	`15`
`TURN`	`63 65`	`3`
`STRAND`	`71 77`	`7`
`HELIX`	`81 83`	`3`
`HELIX`	`86 97`	`12`
`STRAND`	`99 101`	`3`
`STRAND`	`108 114`	`7`
`HELIX`	`115 127`	`13`
`STRAND`	`133 138`	`6`
`HELIX`	`141 145`	`5`
`TURN`	`146 148`	`3`
`STRAND`	`152 157`	`6`
`STRAND`	`160 167`	`8`
`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`
`STRAND`	`368 370`	`3`
`STRAND`	`373 378`	`6`
`HELIX`	`384 390`	`7`

Sequence information

Length: 1586 AA [This is the length of the unprocessed precursor]

Molecular weight: 173187 Da [This is the MW of the unprocessed precursor]

CRC64: B4AD51605585043C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSNPTKISIL GRESIIADFG LWRNYVAKDL ISDCSSTTYV LVTDTNIGSI YTPSFEEAFR 

        70         80         90        100        110        120 
KRAAEITPSP RLLIYNRPPG 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 VRREVTPGEH RFEGTEEILK 

       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 VAHSSNVICA PPGSKSISNR 

       430        440        450        460        470        480 
ALVLAALGSG TCRIKNLLHS DDTEVMLNAL ERLGAATFSW EEEGEVLVVN GKGGNLQASS 

       490        500        510        520        530        540 
SPLYLGNAGT ASRFLTTVAT LANSSTVDSS VLTGNNRMKQ RPIGDLVDAL TANVLPLNTS 

       550        560        570        580        590        600 
KGRASLPLKI AASGGFAGGN INLAAKVSSQ YVSSLLMCAP YAKEPVTLRL VGGKPISQPY 

       610        620        630        640        650        660 
IDMTTAMMRS FGIDVQKSTT EEHTYHIPQG RYVNPAEYVI ESDASCATYP LAVAAVTGTT 

       670        680        690        700        710        720 
CTVPNIGSAS LQGDARFAVE VLRPMGCTVE QTETSTTVTG PSDGILRATS KRGYGTNDRC 

       730        740        750        760        770        780 
VPRCFRTGSH RPMEKSQTTP PVSSGIANQR VKECNRIKAM KDELAKFGVI CREHDDGLEI 

       790        800        810        820        830        840 
DGIDRSNLRQ PVGGVFCYDD HRVAFSFSVL SLVTPQPTLI LEKECVGKTW PGWWDTLRQL 

       850        860        870        880        890        900 
FKVKLEGKEL EEEPVAASGP DRGNASIYII GMRGAGKSTA GNWVSKALNR PFVDLDTELE 

       910        920        930        940        950        960 
TVEGMTIPDI IKTRGWQGFR NAELEILKRT LKERSRGYVF ACGGGVVEMP EARKLLTDYH 

       970        980        990       1000       1010       1020 
KTKGNVLLLM RDIKKIMDFL SIDKSRPAYV EDMMGVWLRR KPWFQECSNI QYYSRDASPS 

      1030       1040       1050       1060       1070       1080 
GLARASEDFN RFLQVATGQI DSLSIIKEKE HSFFASLTLP DLREAGDILE EVCVGSDAVE 

      1090       1100       1110       1120       1130       1140 
LRVDLLKDPA SNNDIPSVDY VVEQLSFLRS RVTLPIIFTI RTQSQGGRFP DNAHDAALEL 

      1150       1160       1170       1180       1190       1200 
YRLAFRSGCE FVDLDIAFPE DMLRAVTEMK GFSKIIASHH DPKGELSWAN MSWIKFYNKA 

      1210       1220       1230       1240       1250       1260 
LEYGDIIKLV GVARNIDDNT ALRKFKNWAA EAHDVPLIAI NMGDQGQLSR ILNGFMTPVS 

      1270       1280       1290       1300       1310       1320 
HPSLPFKAAP GQLSATEIRK GLSLMGEIKP KKFAIFGSPI SQSRSPALHN TLFAQVGLPH 

      1330       1340       1350       1360       1370       1380 
NYTRLETTNA QDVQEFIRSP DFGGAFRNNS LKLDIMPLLD EVAAEAEIIG AVNTIIPVST 

      1390       1400       1410       1420       1430       1440 
GKNTPSRLVG RNTDWQGMIL SLRKAGVYGP KRKDQEQSAL VVGGGGTARA AIYALHNMGY 

      1450       1460       1470       1480       1490       1500 
SPIYIVGRTP SKLENMVSTF PSSYNIRIVE SPSSFESVPH VAIGTIPADQ PIDPTMRETL 

      1510       1520       1530       1540       1550       1560 
CHMFERAQEA DAEAVKAIEH APRILLEMAY KPQVTALMRL ASDSGWKTIP GLEVLVGQGW 

      1570       1580 
YHSLNTGLGS RRYMRVPGHV APPSFN

P07547 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools