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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)DescriptionActionsGraphical viewLength
Binding sitei119NADUniRule annotation2 Publications1
Binding sitei130Substrate 11
Binding sitei146Substrate 21
Binding sitei152Substrate 21
Binding sitei161NADUniRule annotation2 Publications1
Binding sitei162Substrate 21
Binding sitei190NADUniRule annotation2 Publications1
Metal bindingi194Zinc; catalyticUniRule annotation2 Publications1
Binding sitei250Substrate 21
Active sitei260Proton acceptor; for 3-dehydroquinate synthase activity1
Metal bindingi271Zinc; catalyticUniRule annotation2 Publications1
Binding sitei271Substrate 21
Active sitei275Proton acceptor; for 3-dehydroquinate synthase activity1
Metal bindingi287Zinc; catalyticUniRule annotation2 Publications1
Binding sitei287Substrate 21
Binding sitei356Substrate 21
Active sitei824For EPSP synthase activityUniRule annotation1
Active sitei1179Proton acceptor; for 3-dehydroquinate dehydratase activityUniRule annotation1
Active sitei1207Schiff-base intermediate with substrate; for 3-dehydroquinate dehydratase activityUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi44 – 46NADUniRule annotation2 Publications3
Nucleotide bindingi81 – 84NADUniRule annotation2 Publications4
Nucleotide bindingi114 – 116NADUniRule annotation2 Publications3
Nucleotide bindingi139 – 140NADUniRule annotation2 Publications2
Nucleotide bindingi179 – 182NADUniRule annotation2 Publications4
Nucleotide bindingi870 – 877ATPUniRule annotation8

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)DescriptionActionsGraphical viewLength
ChainiPRO_00001408591 – 1583Pentafunctional AROM polypeptideAdd BLAST1583

Interactioni

Subunit structurei

Homodimer.UniRule annotation2 Publications

Structurei

Secondary structure

11583
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 9Combined sources5
Beta strandi12 – 18Combined sources7
Helixi21 – 24Combined sources4
Helixi26 – 33Combined sources8
Beta strandi37 – 44Combined sources8
Helixi45 – 65Combined sources21
Beta strandi66 – 68Combined sources3
Beta strandi71 – 77Combined sources7
Helixi81 – 83Combined sources3
Helixi86 – 97Combined sources12
Beta strandi99 – 101Combined sources3
Beta strandi108 – 114Combined sources7
Helixi115 – 127Combined sources13
Helixi128 – 130Combined sources3
Beta strandi133 – 138Combined sources6
Helixi141 – 145Combined sources5
Turni146 – 148Combined sources3
Beta strandi152 – 157Combined sources6
Beta strandi160 – 167Combined sources8
Beta strandi171 – 176Combined sources6
Helixi177 – 181Combined sources5
Helixi185 – 200Combined sources16
Helixi204 – 222Combined sources19
Beta strandi227 – 229Combined sources3
Helixi233 – 235Combined sources3
Helixi236 – 255Combined sources20
Turni257 – 259Combined sources3
Helixi263 – 268Combined sources6
Helixi271 – 281Combined sources11
Turni282 – 284Combined sources3
Helixi287 – 304Combined sources18
Helixi310 – 322Combined sources13
Helixi332 – 337Combined sources6
Turni338 – 340Combined sources3
Helixi345 – 353Combined sources9
Beta strandi362 – 365Combined sources4
Beta strandi368 – 370Combined sources3
Beta strandi373 – 378Combined sources6
Beta strandi380 – 383Combined sources4
Helixi384 – 390Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
SMRiP07547.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07547.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 3843-dehydroquinate synthaseAdd BLAST384
Regioni194 – 197Substrate binding 24
Regioni264 – 268Substrate binding 25
Regioni397 – 842EPSP synthaseAdd BLAST446
Regioni863 – 1055Shikimate kinaseAdd BLAST193
Regioni1056 – 12763-dehydroquinaseAdd BLAST221
Regioni1289 – 1583Shikimate dehydrogenaseAdd BLAST295

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.
OrthoDBiEOG092C02JU.

Family and domain databases

CDDicd00502. DHQase_I. 1 hit.
cd01556. EPSP_synthase. 1 hit.
cd00464. SK. 1 hit.
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_00110. DHQ_synthase. 1 hit.
MF_00210. EPSP_synth. 1 hit.
MF_03143. Pentafunct_AroM. 1 hit.
MF_00109. Shikimate_kinase. 1 hit.
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 differs from that shown. Reason: Frameshift at positions 534, 545, 708, 733 and 743.Curated
The sequence CAA28836 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence EAA65484 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti62A → R in CAA28836 (PubMed:3515316).Curated1
Sequence conflicti77A → R in CAA28836 (PubMed:3515316).Curated1
Sequence conflicti226R → T in CAA28836 (PubMed:3515316).Curated1
Sequence conflicti235I → T in CAA28836 (PubMed:3515316).Curated1
Sequence conflicti403Q → H in CAA28836 (PubMed:3515316).Curated1
Sequence conflicti535A → P in CAA28836 (PubMed:3515316).Curated1
Sequence conflicti646S → C in CAA28836 (PubMed:3515316).Curated1
Sequence conflicti862A → G in CAA28836 (PubMed:3515316).Curated1
Sequence conflicti862A → G no nucleotide entry (PubMed:3906567).Curated1
Sequence conflicti984T → S in CAA28836 (PubMed:3515316).Curated1
Sequence conflicti984T → S no nucleotide entry (PubMed:3906567).Curated1
Sequence conflicti1048K → G no nucleotide entry (PubMed:3906567).Curated1
Sequence conflicti1093D → N no nucleotide entry (PubMed:3906567).Curated1
Sequence conflicti1154E → D in CAA28836 (PubMed:3515316).Curated1
Sequence conflicti1154E → D no nucleotide entry (PubMed:3906567).Curated1
Sequence conflicti1345 – 1349SVTIP → FRNNS in CAA28836 (PubMed:3515316).Curated5

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
PDB 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.
SMRiP07547.
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.
OrthoDBiEOG092C02JU.

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

CDDicd00502. DHQase_I. 1 hit.
cd01556. EPSP_synthase. 1 hit.
cd00464. SK. 1 hit.
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_00110. DHQ_synthase. 1 hit.
MF_00210. EPSP_synth. 1 hit.
MF_03143. Pentafunct_AroM. 1 hit.
MF_00109. Shikimate_kinase. 1 hit.
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...

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: November 30, 2016
This is version 155 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.