C5G8R4 · ARO1_AJEDR
- ProteinPentafunctional AROM polypeptide
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1597 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis.
Catalytic activity
- 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate
Cofactor
Note: Binds 2 Zn2+ ions per subunit.
Pathway
Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7.
Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7.
Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7.
Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7.
Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 44-46 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: DTN | ||||||
Binding site | 81-84 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: ESSK | ||||||
Binding site | 114-116 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: GGV | ||||||
Binding site | 119 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 130 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 139-140 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: TT | ||||||
Binding site | 146 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 152 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 161 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 162 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 179-182 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: FLNT | ||||||
Binding site | 190 | NAD+ (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 194 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 194-197 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: EVIK | ||||||
Binding site | 250 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 260 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: E | ||||||
Binding site | 264-268 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: RNLLN | ||||||
Binding site | 271 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 271 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Active site | 275 | Proton acceptor; for 3-dehydroquinate synthase activity | ||||
Sequence: H | ||||||
Binding site | 287 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 287 | Zn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: H | ||||||
Binding site | 356 | 7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Active site | 824 | For EPSP synthase activity | ||||
Sequence: C | ||||||
Binding site | 872-879 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GMRGAGKT | ||||||
Active site | 1181 | Proton acceptor; for 3-dehydroquinate dehydratase activity | ||||
Sequence: H | ||||||
Active site | 1209 | Schiff-base intermediate with substrate; for 3-dehydroquinate dehydratase activity | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | 3-dehydroquinate dehydratase activity | |
Molecular Function | 3-dehydroquinate synthase activity | |
Molecular Function | 3-phosphoshikimate 1-carboxyvinyltransferase activity | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | shikimate 3-dehydrogenase (NADP+) activity | |
Molecular Function | shikimate kinase activity | |
Biological Process | amino acid biosynthetic process | |
Biological Process | aromatic amino acid family biosynthetic process | |
Biological Process | chorismate biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePentafunctional AROM polypeptide
Including 5 domains:
- Recommended name3-dehydroquinate synthase
- EC number
- Short namesDHQS
- Recommended name3-phosphoshikimate 1-carboxyvinyltransferase
- EC number
- Alternative names
- Recommended nameShikimate kinase
- EC number
- Short namesSK
- Recommended name3-dehydroquinate dehydratase
- EC number
- Short names3-dehydroquinase
- Recommended nameShikimate dehydrogenase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Onygenales > Ajellomycetaceae > Blastomyces
Accessions
- Primary accessionC5G8R4
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000406700 | 1-1597 | Pentafunctional AROM polypeptide | |||
Sequence: MGVPTKISILGRESIVADFGIWRNYVAKDLLNSCSSSTYILISDTNITPLYLDGFQKSFDDAAANLSPKPRLLTYEIPPGESSKSRETKAGIEDWMLTRQPPCGRDTVIIALGGGVIGDLIGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPNGKNLIGAIWQPQRIYLDMEFLNTLPEREFINGMAEVIKTAAISSEEKFAALEDDAEIILAAVKSKNTPERPRFSGIEETLKRTILSSAEFKAQVVSADEREGGLRNLLNFGHSIGHAIEAILAPQVLHGECVAIGMVKEAELARHLGILNNVSVSRISKCLASYGLPTSLKDERIRKLTADKHCSVEQLITYMGVDKKNDGPKKKVVLLSAIGRTHEPRASTVSNEEIQIVLAPSIEVSPGVPKNLNVTCTPPGSKSISNRALVLAALGSGTCRLKNLLHSDDTEVMLNALERLGAATFSWENEGEVLVVNGKGGKMKASPDELYLGNAGTASRFLTTVATLAQKSSVDSSVLTGNARMKQRPIGDLVDALAANGAGVEYLENSGSLPLKIAASGGFAGGEINLAAKVSSQYVSSLLMCAPYAKKPVTLRLVGGKPISQTYIDMTTTMMRSFGIDVKKSETEEHTYHIPLGFYISPAEYIVESDASSSTYPLAVAAITGTSCTVPNIGSKSLQGDARFAVEVLRPMGCTVDQKDFSTTVTGPANGILRPLPNVDMEPMTDAFLTASVLAAVARGGGSNHTTRIFGIANQRVKECNRIKAMKDELAKFGVTCREHDDGLEIDGIDRSTLRHPSDGVYCYDDHRVAMSFSVLSLVAPQPTLILEKECVGKTWPGWWDSLAQTFKVKLDGKEVEKKTGRGGIVHLDKPAASIFIIGMRGAGKTTSGVWVSKALQRPFIDLDDELERTEGMTIPEIIKQRGWEGFREAELSLLRRVMTEKPTRYIFACGGGIVETPEARKLLIQYHKTKGNVILVMRDIKEIMDFLKIDKTRPAYVEDMMSVWLRRKPWYQECSNVQYFSRLTGLDGMAQVLGGFNRFLKVITGQVDSLAQMRSKENTFFVSLTLPDLAPAAPILKEVTLGSDAVELRVDLLKDPQSDSEIPSVDYVAEQISVLRSRTSVPLVFTIRTKAQGGRFPDDAYDAALQLYRLAIRMGSEFVDLEISFPEQLLRTVTEMKGFSKIIASHHDPKGELSWANGSWIQFYNKALQYGDVIKLVGVARSLDDNASLKKFKTWAEEKHDVPIIAINMGDKGQLSRMLNGFMTPVSHPSLPFKAAPGQLSAREIRKGLSLIGEIKSKKFAVIGNPVSASRSPAMHNALFRQMGLPHIYGTLETEDPEIVKKFIRSPDFGGASITIPLKLDIMPLLDEIAPEAVSIGAVNTIVCAPPAPDDQSQAPRLIGRNTDWQGMVRCLSDAGAYPAATPTTTSAGLVIGGGGTARAAIFALQSMGYSPIYVVGRSPDKLSSMTSTFAPDHDIRILEDVKALESLPTVAIGTIPGDKPIEPHMREILCELFDLCEKANSDAEQARGISTKRILLEMAYKPSVTSLMQLASDSGWTVLPGLEALVAQGVYQCEYWTDITPVYEDARNAVMGVQPKDDDIST |
Interaction
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-384 | 3-dehydroquinate synthase | ||||
Sequence: MGVPTKISILGRESIVADFGIWRNYVAKDLLNSCSSSTYILISDTNITPLYLDGFQKSFDDAAANLSPKPRLLTYEIPPGESSKSRETKAGIEDWMLTRQPPCGRDTVIIALGGGVIGDLIGFVAATYMRGVRFVQVPTTLLAMVDSSIGGKTAIDTPNGKNLIGAIWQPQRIYLDMEFLNTLPEREFINGMAEVIKTAAISSEEKFAALEDDAEIILAAVKSKNTPERPRFSGIEETLKRTILSSAEFKAQVVSADEREGGLRNLLNFGHSIGHAIEAILAPQVLHGECVAIGMVKEAELARHLGILNNVSVSRISKCLASYGLPTSLKDERIRKLTADKHCSVEQLITYMGVDKKNDGPKKKVVLLSAIGRTHEPRASTVSN | ||||||
Region | 397-842 | EPSP synthase | ||||
Sequence: VSPGVPKNLNVTCTPPGSKSISNRALVLAALGSGTCRLKNLLHSDDTEVMLNALERLGAATFSWENEGEVLVVNGKGGKMKASPDELYLGNAGTASRFLTTVATLAQKSSVDSSVLTGNARMKQRPIGDLVDALAANGAGVEYLENSGSLPLKIAASGGFAGGEINLAAKVSSQYVSSLLMCAPYAKKPVTLRLVGGKPISQTYIDMTTTMMRSFGIDVKKSETEEHTYHIPLGFYISPAEYIVESDASSSTYPLAVAAITGTSCTVPNIGSKSLQGDARFAVEVLRPMGCTVDQKDFSTTVTGPANGILRPLPNVDMEPMTDAFLTASVLAAVARGGGSNHTTRIFGIANQRVKECNRIKAMKDELAKFGVTCREHDDGLEIDGIDRSTLRHPSDGVYCYDDHRVAMSFSVLSLVAPQPTLILEKECVGKTWPGWWDSLAQTFKV | ||||||
Region | 866-1057 | Shikimate kinase | ||||
Sequence: ASIFIIGMRGAGKTTSGVWVSKALQRPFIDLDDELERTEGMTIPEIIKQRGWEGFREAELSLLRRVMTEKPTRYIFACGGGIVETPEARKLLIQYHKTKGNVILVMRDIKEIMDFLKIDKTRPAYVEDMMSVWLRRKPWYQECSNVQYFSRLTGLDGMAQVLGGFNRFLKVITGQVDSLAQMRSKENTFFVS | ||||||
Region | 1058-1278 | 3-dehydroquinase | ||||
Sequence: LTLPDLAPAAPILKEVTLGSDAVELRVDLLKDPQSDSEIPSVDYVAEQISVLRSRTSVPLVFTIRTKAQGGRFPDDAYDAALQLYRLAIRMGSEFVDLEISFPEQLLRTVTEMKGFSKIIASHHDPKGELSWANGSWIQFYNKALQYGDVIKLVGVARSLDDNASLKKFKTWAEEKHDVPIIAINMGDKGQLSRMLNGFMTPVSHPSLPFKAAPGQLSARE | ||||||
Region | 1291-1597 | Shikimate dehydrogenase | ||||
Sequence: SKKFAVIGNPVSASRSPAMHNALFRQMGLPHIYGTLETEDPEIVKKFIRSPDFGGASITIPLKLDIMPLLDEIAPEAVSIGAVNTIVCAPPAPDDQSQAPRLIGRNTDWQGMVRCLSDAGAYPAATPTTTSAGLVIGGGGTARAAIFALQSMGYSPIYVVGRSPDKLSSMTSTFAPDHDIRILEDVKALESLPTVAIGTIPGDKPIEPHMREILCELFDLCEKANSDAEQARGISTKRILLEMAYKPSVTSLMQLASDSGWTVLPGLEALVAQGVYQCEYWTDITPVYEDARNAVMGVQPKDDDIST |
Sequence similarities
In the N-terminal section; belongs to the sugar phosphate cyclases superfamily. 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 4th section; belongs to the type-I 3-dehydroquinase family.
In the C-terminal section; belongs to the shikimate dehydrogenase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,597
- Mass (Da)173,569
- Last updated2009-07-28 v1
- ChecksumB55147E1AE07F6E6