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:	aro1
	ORFNames:	SPAC1834.02

From

Schizosaccharomyces pombe (Fission yeast)

[TaxID: 4896]

Taxonomy

Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.

Protein existence

2: Evidence at transcript level;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).

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.
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 (By similarity).
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

CU329670; CAB75770.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

T50113; T50113.

RefSeq

NP_594681.1; -.

3D structure databases

HSSP

P07547; 1NVE. [HSSP ENTRY / PDB]

ModBase

Q9P7R0.

Enzyme and pathway databases

BioCyc

SPOM-XXX-01:SPOM-XXX-01-002767-MON; -.

Organism-specific databases

GeneDB_Spombe

SPAC1834.02; -.

Gene expression databases

ArrayExpress

Q9P7R0; -.

Ontologies

GO:0005829;	Cellular component: cytosol (inferred from direct assay from GeneDB_SPombe).
GO:0009073;	Biological process: aromatic amino acid family biosynthetic process (non-traceable author statement from GeneDB_SPombe).
QuickGo view.

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.
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.

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; FALSE_NEG.
PS00104; EPSP_SYNTHASE_1; 1.
PS00885; EPSP_SYNTHASE_2; 1.
PS01128; SHIKIMATE_KINASE; FALSE_NEG.

BLOCKS

Q9P7R0.

Genome annotation databases

GeneID

2542115; -.

KEGG

spo:SPAC1834.02; -.

NMPDR

fig|4896.1.peg.4651; -.

Other

ProtoNet

Q9P7R0.

UniRef

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

Keywords

Amino-acid biosynthesis; Aromatic amino acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm; Kinase; Lyase; Multifunctional enzyme; NADP; Nucleotide-binding; Oxidoreductase; Transferase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 1573`	`1573`	`Pentafunctional AROM polypeptide.`	`PRO_0000140861`
`NP_BIND`	`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).`
`ACT_SITE`	`825 825`		`Potential.`
`ACT_SITE`	`1182 1182`		`Proton acceptor (By similarity).`
`ACT_SITE`	`1211 1211`		`Schiff-base intermediate with substrate (By similarity).`

Sequence information

Length: 1573 AA [This is the length of the unprocessed precursor]

Molecular weight: 173782 Da [This is the MW of the unprocessed precursor]

CRC64: 418968DA6330280D [This is a checksum on the sequence]

        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

Q9P7R0 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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