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Protein

Pentafunctional AROM polypeptide

Gene

aromA

Organism
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

3-deoxy-D-arabino-hept-2-ulosonate 7-phosphate = 3-dehydroquinate + phosphate.UniRule annotation
3-dehydroquinate = 3-dehydroshikimate + H2O.UniRule annotation
Shikimate + NADP+ = 3-dehydroshikimate + NADPH.UniRule annotation
ATP + shikimate = ADP + shikimate 3-phosphate.UniRule annotation
Phosphoenolpyruvate + 3-phosphoshikimate = phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate.UniRule annotation

Cofactori

Zn2+Note: Binds 2 Zn2+ ions per subunit.

Pathwayi: chorismate biosynthesis

This protein is involved in step 2, 3, 4, 5 and 6 of the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate.UniRule annotation
Proteins known to be involved in the 7 steps of the subpathway in this organism are:
  1. Phospho-2-dehydro-3-deoxyheptonate aldolase (AN0354.2), Phospho-2-dehydro-3-deoxyheptonate aldolase (ANIA_00354), Phospho-2-dehydro-3-deoxyheptonate aldolase (AN1673.2), Phospho-2-dehydro-3-deoxyheptonate aldolase (AN5701.2)
  2. Pentafunctional AROM polypeptide (aromA)
  3. Pentafunctional AROM polypeptide (aromA)
  4. Pentafunctional AROM polypeptide (aromA)
  5. Pentafunctional AROM polypeptide (aromA)
  6. Pentafunctional AROM polypeptide (aromA)
  7. Chorismate synthase (AN5731.2)
This subpathway is part of the pathway chorismate biosynthesis, which is itself part of Metabolic intermediate biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate, the pathway chorismate biosynthesis and in Metabolic intermediate biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei119 – 1191NADUniRule annotation2 Publications
Binding sitei130 – 1301Substrate 1
Binding sitei146 – 1461Substrate 2
Binding sitei152 – 1521Substrate 2
Binding sitei161 – 1611NADUniRule annotation2 Publications
Binding sitei162 – 1621Substrate 2
Binding sitei190 – 1901NADUniRule annotation2 Publications
Metal bindingi194 – 1941Zinc; catalyticUniRule annotation2 Publications
Binding sitei250 – 2501Substrate 2
Active sitei260 – 2601Proton acceptor; for 3-dehydroquinate synthase activity
Metal bindingi271 – 2711Zinc; catalyticUniRule annotation2 Publications
Binding sitei271 – 2711Substrate 2
Active sitei275 – 2751Proton acceptor; for 3-dehydroquinate synthase activity
Metal bindingi287 – 2871Zinc; catalyticUniRule annotation2 Publications
Binding sitei287 – 2871Substrate 2
Binding sitei356 – 3561Substrate 2
Active sitei824 – 8241For EPSP synthase activityUniRule annotation
Active sitei1179 – 11791Proton acceptor; for 3-dehydroquinate dehydratase activityUniRule annotation
Active sitei1207 – 12071Schiff-base intermediate with substrate; for 3-dehydroquinate dehydratase activityUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi44 – 463NADUniRule annotation2 Publications
Nucleotide bindingi81 – 844NADUniRule annotation2 Publications
Nucleotide bindingi114 – 1163NADUniRule annotation2 Publications
Nucleotide bindingi139 – 1402NADUniRule annotation2 Publications
Nucleotide bindingi179 – 1824NADUniRule annotation2 Publications
Nucleotide bindingi870 – 8778ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Keywords - Molecular functioni

Kinase, Lyase, Oxidoreductase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Aromatic amino acid biosynthesis

Keywords - Ligandi

ATP-binding, Metal-binding, NADP, Nucleotide-binding, Zinc

Enzyme and pathway databases

BRENDAi4.2.3.4. 517.
SABIO-RKP07547.
UniPathwayiUPA00053; UER00085.
UPA00053; UER00086.
UPA00053; UER00087.
UPA00053; UER00088.
UPA00053; UER00089.

Names & Taxonomyi

Protein namesi
Recommended name:
Pentafunctional AROM polypeptideUniRule annotation
Including the following 5 domains:
3-dehydroquinate synthaseUniRule annotation (EC:4.2.3.4UniRule annotation)
Short name:
DHQSUniRule annotation
3-phosphoshikimate 1-carboxyvinyltransferaseUniRule annotation (EC:2.5.1.19UniRule annotation)
Alternative name(s):
5-enolpyruvylshikimate-3-phosphate synthaseUniRule annotation
Short name:
EPSP synthaseUniRule annotation
Short name:
EPSPSUniRule annotation
Shikimate kinaseUniRule annotation (EC:2.7.1.71UniRule annotation)
Short name:
SKUniRule annotation
3-dehydroquinate dehydrataseUniRule annotation (EC:4.2.1.10UniRule annotation)
Short name:
3-dehydroquinaseUniRule annotation
Shikimate dehydrogenaseUniRule annotation (EC:1.1.1.25UniRule annotation)
Gene namesi
Name:aromA
Synonyms:aroA, aroM
ORF Names:AN0708
OrganismiEmericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Taxonomic identifieri227321 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
Proteomesi
  • UP000000560 Componenti: Chromosome VIII
  • UP000005890 Componenti: Partially assembled WGS sequence

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 15831583Pentafunctional AROM polypeptidePRO_0000140859Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation2 Publications

Structurei

Secondary structure

1
1583
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 95Combined sources
Beta strandi12 – 187Combined sources
Helixi21 – 244Combined sources
Helixi26 – 338Combined sources
Beta strandi37 – 448Combined sources
Helixi45 – 6521Combined sources
Beta strandi66 – 683Combined sources
Beta strandi71 – 777Combined sources
Helixi81 – 833Combined sources
Helixi86 – 9712Combined sources
Beta strandi99 – 1013Combined sources
Beta strandi108 – 1147Combined sources
Helixi115 – 12713Combined sources
Helixi128 – 1303Combined sources
Beta strandi133 – 1386Combined sources
Helixi141 – 1455Combined sources
Turni146 – 1483Combined sources
Beta strandi152 – 1576Combined sources
Beta strandi160 – 1678Combined sources
Beta strandi171 – 1766Combined sources
Helixi177 – 1815Combined sources
Helixi185 – 20016Combined sources
Helixi204 – 22219Combined sources
Beta strandi227 – 2293Combined sources
Helixi233 – 2353Combined sources
Helixi236 – 25520Combined sources
Turni257 – 2593Combined sources
Helixi263 – 2686Combined sources
Helixi271 – 28111Combined sources
Turni282 – 2843Combined sources
Helixi287 – 30418Combined sources
Helixi310 – 32213Combined sources
Helixi332 – 3376Combined sources
Turni338 – 3403Combined sources
Helixi345 – 3539Combined sources
Beta strandi362 – 3654Combined sources
Beta strandi368 – 3703Combined sources
Beta strandi373 – 3786Combined sources
Beta strandi380 – 3834Combined sources
Helixi384 – 3907Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DQSX-ray1.80A/B1-393[»]
1NR5X-ray2.10A/B1-393[»]
1NRXX-ray2.90A/B1-393[»]
1NUAX-ray2.85A/B1-393[»]
1NVAX-ray2.62A/B1-393[»]
1NVBX-ray2.70A/B1-393[»]
1NVDX-ray2.51A/B1-393[»]
1NVEX-ray2.58A/B/C/D1-393[»]
1NVFX-ray2.80A/B/C1-393[»]
1SG6X-ray1.70A/B1-393[»]
ProteinModelPortaliP07547.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07547.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 3843843-dehydroquinate synthaseAdd
BLAST
Regioni194 – 1974Substrate binding 2
Regioni264 – 2685Substrate binding 2
Regioni397 – 842446EPSP synthaseAdd
BLAST
Regioni863 – 1055193Shikimate kinaseAdd
BLAST
Regioni1056 – 12762213-dehydroquinaseAdd
BLAST
Regioni1289 – 1583295Shikimate dehydrogenaseAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the dehydroquinate synthase family.UniRule annotation
In the 2nd section; belongs to the EPSP synthase family.UniRule annotation
In the 3rd section; belongs to the shikimate kinase family.UniRule annotation
In the 4th section; belongs to the type-I 3-dehydroquinase family.UniRule annotation
In the C-terminal section; belongs to the shikimate dehydrogenase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000007970.
InParanoidiP07547.
KOiK13830.
OrthoDBiEOG7KQ28X.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
3.40.50.300. 1 hit.
3.40.50.720. 1 hit.
3.65.10.10. 2 hits.
HAMAPiMF_00109. Shikimate_kinase.
MF_00110. DHQ_synthase.
MF_00210. EPSP_synth.
MF_03143. Pentafunct_AroM.
InterProiIPR018508. 3-dehydroquinate_DH_AS.
IPR013785. Aldolase_TIM.
IPR016037. DHQ_synth_AroB.
IPR030960. DHQS/DOIS.
IPR001381. DHquinase_I.
IPR001986. Enolpyruvate_Tfrase_dom.
IPR006264. EPSP_synthase.
IPR023193. EPSP_synthase_CS.
IPR016040. NAD(P)-bd_dom.
IPR027417. P-loop_NTPase.
IPR008289. Pentafunct_AroM.
IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
IPR031322. Shikimate/glucono_kinase.
IPR013708. Shikimate_DH-bd_N.
IPR010110. Shikimate_DH_AroM-type.
IPR000623. Shikimate_kinase/TSH1.
IPR023000. Shikimate_kinase_CS.
[Graphical view]
PfamiPF01761. DHQ_synthase. 1 hit.
PF01487. DHquinase_I. 1 hit.
PF00275. EPSP_synthase. 1 hit.
PF08501. Shikimate_dh_N. 1 hit.
PF01202. SKI. 1 hit.
[Graphical view]
PIRSFiPIRSF000514. Pentafunct_AroM. 1 hit.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF55205. SSF55205. 1 hit.
TIGRFAMsiTIGR01356. aroA. 1 hit.
TIGR01357. aroB. 1 hit.
TIGR01093. aroD. 1 hit.
TIGR01809. Shik-DH-AROM. 1 hit.
PROSITEiPS01028. DEHYDROQUINASE_I. 1 hit.
PS00104. EPSP_SYNTHASE_1. 1 hit.
PS00885. EPSP_SYNTHASE_2. 1 hit.
PS01128. SHIKIMATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P07547-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNPTKISIL GRESIIADFG LWRNYVAKDL ISDCSSTTYV LVTDTNIGSI
60 70 80 90 100
YTPSFEEAFR KAAAEITPSP RLLIYNAPPG EVSKSRQTKA DIEDWMLSQN
110 120 130 140 150
PPCGRDTVVI ALGGGVIGDL TGFVASTYMR GVRYVQVPTT LLAMVDSSIG
160 170 180 190 200
GKTAIDTPLG KNLIGAIWQP TKIYIDLEFL ETLPVREFIN GMAEVIKTAA
210 220 230 240 250
ISSEEEFTAL EENAETILKA VRREVRPGEH RFEGIEEILK ARILASARHK
260 270 280 290 300
AYVVSADERE GGLRNLLNWG HSIGHAIEAI LTPQILHGEC VAIGMVKEAE
310 320 330 340 350
LARHLGILKG VAVSRIVKCL AAYGLPTSLK DARIRKLTAG KHCSVDQLMF
360 370 380 390 400
NMALDKKNDG PKKKIVLLSA IGTPYETRAS VVANEDIRVV LAPSIEVHPG
410 420 430 440 450
VAQSSNVICA PPGSKSISNR ALVLAALGSG TCRIKNLLHS DDTEVMLNAL
460 470 480 490 500
ERLGAATFSW EEEGEVLVVN GKGGNLQASS SPLYLGNAGT ASRFLTTVAT
510 520 530 540 550
LANSSTVDSS VLTGNNRMKQ RPIGDLVDAL TANGASIEYV ERTGSLPLKI
560 570 580 590 600
AASGGFAGGN INLAAKVSSQ YVSSLLMCAP YAKEPVTLRL VGGKPISQPY
610 620 630 640 650
IDMTTAMMRS FGIDVQKSTT EEHTYHIPQG RYVNPAEYVI ESDASSATYP
660 670 680 690 700
LAVAAVTGTT CTVPNIGSAS LQGDARFAVE VLRPMGCTVE QTETSTTVTG
710 720 730 740 750
PSDGILRPLP NVDMEPMTDA FLGASVLAAI ARGKESNHTT RIYGIANQRV
760 770 780 790 800
KECNRIKAMK DELAKFGVIC REHDDGLEID GIDRSNLRQP VGGVFCYDDH
810 820 830 840 850
RVAFSFSVLS LVTPQPTLIL EKECVGKTWP GWWDTLRQLF KVKLEGKELE
860 870 880 890 900
EEPVAASGPD RANASIYIIG MRGAGKSTAG NWVSKALNRP FVDLDTELET
910 920 930 940 950
VEGMTIPDII KTRGWQGFRN AELEILKRTL KERSRGYVFA CGGGVVEMPE
960 970 980 990 1000
ARKLLTDYHK TKGNVLLLMR DIKKIMDFLS IDKTRPAYVE DMMGVWLRRK
1010 1020 1030 1040 1050
PWFQECSNIQ YYSRDASPSG LARASEDFNR FLQVATGQID SLSIIKEKEH
1060 1070 1080 1090 1100
SFFASLTLPD LREAGDILEE VCVGSDAVEL RVDLLKDPAS NNDIPSVDYV
1110 1120 1130 1140 1150
VEQLSFLRSR VTLPIIFTIR TQSQGGRFPD NAHDAALELY RLAFRSGCEF
1160 1170 1180 1190 1200
VDLEIAFPED MLRAVTEMKG FSKIIASHHD PKGELSWANM SWIKFYNKAL
1210 1220 1230 1240 1250
EYGDIIKLVG VARNIDDNTA LRKFKNWAAE AHDVPLIAIN MGDQGQLSRI
1260 1270 1280 1290 1300
LNGFMTPVSH PSLPFKAAPG QLSATEIRKG LSLMGEIKPK KFAIFGSPIS
1310 1320 1330 1340 1350
QSRSPALHNT LFAQVGLPHN YTRLETTNAQ DVQEFIRSPD FGGASVTIPL
1360 1370 1380 1390 1400
KLDIMPLLDE VAAEAEIIGA VNTIIPVSTG KNTPSRLVGR NTDWQGMILS
1410 1420 1430 1440 1450
LRKAGVYGPK RKDQEQSALV VGGGGTARAA IYALHNMGYS PIYIVGRTPS
1460 1470 1480 1490 1500
KLENMVSTFP SSYNIRIVES PSSFESVPHV AIGTIPADQP IDPTMRETLC
1510 1520 1530 1540 1550
HMFERAQEAD AEAVKAIEHA PRILLEMAYK PQVTALMRLA SDSGWKTIPG
1560 1570 1580
LEVLVGQGWY QFKYWTGISP LYESARACSS PLI
Length:1,583
Mass (Da):172,664
Last modified:May 26, 2009 - v3
Checksum:iFBC8610B961840D8
GO

Sequence cautioni

The sequence CAA28836.1 differs from that shown. Reason: Frameshift at positions 534, 545, 708, 733 and 743. Curated
The sequence CAA28836.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence EAA65484.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti62 – 621A → R in CAA28836 (PubMed:3515316).Curated
Sequence conflicti77 – 771A → R in CAA28836 (PubMed:3515316).Curated
Sequence conflicti226 – 2261R → T in CAA28836 (PubMed:3515316).Curated
Sequence conflicti235 – 2351I → T in CAA28836 (PubMed:3515316).Curated
Sequence conflicti403 – 4031Q → H in CAA28836 (PubMed:3515316).Curated
Sequence conflicti535 – 5351A → P in CAA28836 (PubMed:3515316).Curated
Sequence conflicti646 – 6461S → C in CAA28836 (PubMed:3515316).Curated
Sequence conflicti862 – 8621A → G in CAA28836 (PubMed:3515316).Curated
Sequence conflicti862 – 8621A → G no nucleotide entry (PubMed:3906567).Curated
Sequence conflicti984 – 9841T → S in CAA28836 (PubMed:3515316).Curated
Sequence conflicti984 – 9841T → S no nucleotide entry (PubMed:3906567).Curated
Sequence conflicti1048 – 10481K → G no nucleotide entry (PubMed:3906567).Curated
Sequence conflicti1093 – 10931D → N no nucleotide entry (PubMed:3906567).Curated
Sequence conflicti1154 – 11541E → D in CAA28836 (PubMed:3515316).Curated
Sequence conflicti1154 – 11541E → D no nucleotide entry (PubMed:3906567).Curated
Sequence conflicti1345 – 13495SVTIP → FRNNS in CAA28836 (PubMed:3515316).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05204 Genomic DNA. Translation: CAA28836.1. Sequence problems.
AACD01000010 Genomic DNA. Translation: EAA65484.1. Sequence problems.
AACD01000011 Genomic DNA. No translation available.
BN001308 Genomic DNA. Translation: CBF88944.1.
PIRiA24962. BVASA1.
RefSeqiXP_658312.1. XM_653220.1.

Genome annotation databases

EnsemblFungiiCADANIAT00001961; CADANIAP00001961; CADANIAG00001961.
EAA65484; EAA65484; AN0708.2.
GeneIDi2876485.
KEGGiani:AN0708.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05204 Genomic DNA. Translation: CAA28836.1. Sequence problems.
AACD01000010 Genomic DNA. Translation: EAA65484.1. Sequence problems.
AACD01000011 Genomic DNA. No translation available.
BN001308 Genomic DNA. Translation: CBF88944.1.
PIRiA24962. BVASA1.
RefSeqiXP_658312.1. XM_653220.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DQSX-ray1.80A/B1-393[»]
1NR5X-ray2.10A/B1-393[»]
1NRXX-ray2.90A/B1-393[»]
1NUAX-ray2.85A/B1-393[»]
1NVAX-ray2.62A/B1-393[»]
1NVBX-ray2.70A/B1-393[»]
1NVDX-ray2.51A/B1-393[»]
1NVEX-ray2.58A/B/C/D1-393[»]
1NVFX-ray2.80A/B/C1-393[»]
1SG6X-ray1.70A/B1-393[»]
ProteinModelPortaliP07547.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiCADANIAT00001961; CADANIAP00001961; CADANIAG00001961.
EAA65484; EAA65484; AN0708.2.
GeneIDi2876485.
KEGGiani:AN0708.2.

Phylogenomic databases

HOGENOMiHOG000007970.
InParanoidiP07547.
KOiK13830.
OrthoDBiEOG7KQ28X.

Enzyme and pathway databases

UniPathwayiUPA00053; UER00085.
UPA00053; UER00086.
UPA00053; UER00087.
UPA00053; UER00088.
UPA00053; UER00089.
BRENDAi4.2.3.4. 517.
SABIO-RKP07547.

Miscellaneous databases

EvolutionaryTraceiP07547.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
3.40.50.300. 1 hit.
3.40.50.720. 1 hit.
3.65.10.10. 2 hits.
HAMAPiMF_00109. Shikimate_kinase.
MF_00110. DHQ_synthase.
MF_00210. EPSP_synth.
MF_03143. Pentafunct_AroM.
InterProiIPR018508. 3-dehydroquinate_DH_AS.
IPR013785. Aldolase_TIM.
IPR016037. DHQ_synth_AroB.
IPR030960. DHQS/DOIS.
IPR001381. DHquinase_I.
IPR001986. Enolpyruvate_Tfrase_dom.
IPR006264. EPSP_synthase.
IPR023193. EPSP_synthase_CS.
IPR016040. NAD(P)-bd_dom.
IPR027417. P-loop_NTPase.
IPR008289. Pentafunct_AroM.
IPR013792. RNA3'P_cycl/enolpyr_Trfase_a/b.
IPR031322. Shikimate/glucono_kinase.
IPR013708. Shikimate_DH-bd_N.
IPR010110. Shikimate_DH_AroM-type.
IPR000623. Shikimate_kinase/TSH1.
IPR023000. Shikimate_kinase_CS.
[Graphical view]
PfamiPF01761. DHQ_synthase. 1 hit.
PF01487. DHquinase_I. 1 hit.
PF00275. EPSP_synthase. 1 hit.
PF08501. Shikimate_dh_N. 1 hit.
PF01202. SKI. 1 hit.
[Graphical view]
PIRSFiPIRSF000514. Pentafunct_AroM. 1 hit.
SUPFAMiSSF51735. SSF51735. 1 hit.
SSF52540. SSF52540. 1 hit.
SSF55205. SSF55205. 1 hit.
TIGRFAMsiTIGR01356. aroA. 1 hit.
TIGR01357. aroB. 1 hit.
TIGR01093. aroD. 1 hit.
TIGR01809. Shik-DH-AROM. 1 hit.
PROSITEiPS01028. DEHYDROQUINASE_I. 1 hit.
PS00104. EPSP_SYNTHASE_1. 1 hit.
PS00885. EPSP_SYNTHASE_2. 1 hit.
PS01128. SHIKIMATE_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: R153.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  3. "The 2008 update of the Aspergillus nidulans genome annotation: a community effort."
    Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J., Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M., Estrada C.G.
    , Geysens S., Goldman G., de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B., van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.
    Fungal Genet. Biol. 46:S2-13(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GENOME REANNOTATION.
    Strain: FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139.
  4. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 843-1473.
    Strain: R153.
  5. Hawkins A.R.
    Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION TO C-TERMINUS.
  6. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION OF INTRON.
  7. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-393 IN COMPLEX WITH NAD; ZINC AND SUBSTRATE ANALOG, SUBUNIT.
  8. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-393 IN COMPLEX WITH ADP; NAD; ZINC AND SUBSTRATE ANALOG.
  9. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 1-393.

Entry informationi

Entry nameiARO1_EMENI
AccessioniPrimary (citable) accession number: P07547
Secondary accession number(s): C8VRD2, Q5BFH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: May 26, 2009
Last modified: February 17, 2016
This is version 151 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.