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protein coding gene - aro1 (SPAC1834.02) - pentafunctional aromatic polypeptide Aro1

Gene summary

Standard name
aro1
Systematic ID
SPAC1834.02
Product
pentafunctional aromatic polypeptide Aro1
Organism
Schizosaccharomyces pombe (fission yeast)
UniProt ID
Q9P7R0
ORFeome ID
31/31A02
Characterisation status
biological role inferred
Feature type
mRNA gene
Genomic location
chromosome I: 4693723..4698606 forward strand

Annotation

GO biological process

GO:0009073 - aromatic amino acid biosynthetic process

References:

GO:0009423 - chorismate biosynthetic process

References:

GO cellular component

GO:0005829 - cytosol

References:

GO molecular function

GO:0003855 - 3-dehydroquinate dehydratase activity

References:

GO:0003856 - 3-dehydroquinate synthase activity

References:

GO:0003866 - 3-phosphoshikimate 1-carboxyvinyltransferase activity

References:

GO:0005524 - ATP binding

References:

GO:0046872 - metal ion binding

References:

GO:0004764 - shikimate 3-dehydrogenase (NADP+) activity

References:

GO:0004765 - shikimate kinase activity

References:

Modification

MOD:00046 - O-phospho-L-serine

References:

MOD:00047 - O-phospho-L-threonine

References:

MOD:00048 - O4'-phospho-L-tyrosine

References:

MOD:00696 - phosphorylated residue

References:

MOD:01148 - ubiquitinylated lysine

References:

Protein sequence feature

SO:0001812 - transmembrane_helix

References:

Qualitative gene expression

PomGeneEx:0000019 - protein level decreased

References:

Quantitative gene expression

PBO:0006310 - protein level

References:

PBO:0011963 - RNA level

References:

Single locus phenotype

FYPO:0003412 - decreased chromatin silencing at centromere outer repeat

References:

Genotypes:

FYPO:0000311 - inviable after spore germination with normal, unseptated germ tube morphology

References:

Genotypes:

FYPO:0002151 - inviable spore

References:

Genotypes:

FYPO:0002061 - inviable vegetative cell population

References:

Genotypes:

Taxonomic conservation

PBO:0011067 - conserved in bacteria

PBO:0011065 - conserved in eukaryotes

PBO:0011064 - conserved in fungi

Protein features

IDNameInterPro nameDB name
PF18317SDH_CSDH_CPFAM
PF01761DHQ_synthaseDHQS/DOIS_NPFAM
PF00275EPSP_synthaseEnolpyruvate_Tfrase_domPFAM
PF01202SKIShikimate/glucono_kinasePFAM
PF01487DHquinase_IDHquinase_IPFAM
PF24621DHQS_CDHQS_CPFAM
PF08501Shikimate_dh_NShikimate_DH-bd_NPFAM
cd08195DHQSCDD
cd00502DHQase_IDHquinase_ICDD
cd01065NAD_bind_Shikimate_DHCDD
cd00464SKShikimate_kinase/TSH1CDD
cd01556EPSP_synthaseEPSP_synthaseCDD
PS00104EPSP_SYNTHASE_1EPSP_synthase_CSPROSITE_PATTERNS
PS00885EPSP_SYNTHASE_2EPSP_synthase_CSPROSITE_PATTERNS
PR01100SHIKIMTKNASEPRINTS
G3DSA:3.65.10.10:FF:000008FUNFAM
G3DSA:3.40.50.1970:FF:000007FUNFAM
G3DSA:3.65.10.10:FF:000007FUNFAM
G3DSA:1.20.1090.10:FF:000007FUNFAM
G3DSA:3.40.50.10860:FF:000015FUNFAM
G3DSA:3.40.50.300:FF:001256FUNFAM
G3DSA:3.20.20.70:FF:000135FUNFAM
G3DSA:3.40.50.720:FF:001275FUNFAM
SSF52540P-loop containing nucleoside triphosphate hydrolasesP-loop_NTPaseSUPERFAMILY
SSF51569AldolaseSUPERFAMILY
SSF55205EPT/RTPC-likeRNA3'P_cycl/enolpyr_Trfase_a/bSUPERFAMILY
SSF56796Dehydroquinate synthase-likeSUPERFAMILY
SSF53223Aminoacid dehydrogenase-like, N-terminal domainAminoacid_DH-like_N_sfSUPERFAMILY
SSF51735NAD(P)-binding Rossmann-fold domainsNAD(P)-bd_dom_sfSUPERFAMILY
G3DSA:3.40.50.300P-loop_NTPaseGENE3D
G3DSA:3.40.50.10860Leucine Dehydrogenase, chain A, domain 1GENE3D
G3DSA:3.65.10.10Enolpyruvate transferase domainEnolpyruvate_Tfrase_sfGENE3D
G3DSA:3.20.20.70Aldolase class IAldolase_TIMGENE3D
G3DSA:3.40.50.720GENE3D
G3DSA:1.20.1090.10GENE3D
G3DSA:3.40.50.1970GENE3D
PTHR21090AROM/DEHYDROQUINATE SYNTHASEPANTHER
PIRSF000514Pentafunct_AroMPentafunct_AroMPIRSF
MF_00210EPSP_synthEPSP_synthaseHAMAP
MF_00109Shikimate_kinaseShikimate_kinase/TSH1HAMAP
MF_03143Pentafunct_AroMPentafunct_AroMHAMAP
TIGR01356aroAEPSP_synthaseNCBIFAM
TIGR01093aroDDHquinase_INCBIFAM
TIGR01357aroBDHQ_synth_AroBNCBIFAM
TIGR01809Shik-DH-AROMShikimate_DH_AroM-typeNCBIFAM

Orthologs

References / Literature

PMID:39705284 - Proteomic and phosphoproteomic analyses reveal that TORC1 is reactivated by pheromone signaling during sexual reproduction in fission yeast.
Bérard M et al. PLoS Biol 2024 Dec 20;22(12):e3002963
PMID:30355493 - Expanded Interactome of the Intrinsically Disordered Protein Dss1.
Schenstrøm SM et al. Cell Rep 2018 Oct 23;25(4):862-870
PMID:37970674 - SUMOylation regulates Lem2 function in centromere clustering and silencing.
Strachan J et al. J Cell Sci 2023 Dec 01;136(23)
PMID:19547744 - Evolution of phosphoregulation: comparison of phosphorylation patterns across yeast species.
Beltrao P et al. PLoS Biol 2009 Jun 16;7(6):e1000134
PMID:24763107 - Absolute proteome and phosphoproteome dynamics during the cell cycle of Schizosaccharomyces pombe (Fission Yeast).
Carpy A et al. Mol Cell Proteomics 2014 Aug;13(8):1925-36
PMID:16823372 - ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe.
Matsuyama A et al. Nat Biotechnol 2006 Jul;24(7):841-7
PMID:23697806 - A genome-wide resource of cell cycle and cell shape genes of fission yeast.
Hayles J et al. Open Biol 2013 May 22;3(5):130053
PMID:11152613 - Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes.
Krogh A et al. J Mol Biol 2001 Jan 19;305(3):567-80
GO_REF:0000033 - Annotation inferences using phylogenetic trees
PMID:20473289 - Analysis of a genome-wide set of gene deletions in the fission yeast Schizosaccharomyces pombe.
Kim DU et al. Nat Biotechnol 2010 Jun;28(6):617-623
PMID:23101633 - Quantitative analysis of fission yeast transcriptomes and proteomes in proliferating and quiescent cells.
Marguerat S et al. Cell 2012 Oct 26;151(3):671-83
PMID:25720772 - Quantitative phosphoproteomics reveals pathways for coordination of cell growth and division by the conserved fission yeast kinase pom1.
Kettenbach AN et al. Mol Cell Proteomics 2015 May;14(5):1275-87
PMID:29996109 - Quantitative Phosphoproteomics Reveals the Signaling Dynamics of Cell-Cycle Kinases in the Fission Yeast Schizosaccharomyces pombe.
Swaffer MP et al. Cell Rep 2018 Jul 10;24(2):503-514
GO_REF:0000024 - Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity.
PMID:29899453 - A Cdk9-PP1 switch regulates the elongation-termination transition of RNA polymerase II.
Parua PK et al. Nature 2018 Jun;558(7710):460-464
PMID:22119525 - SIN-inhibitory phosphatase complex promotes Cdc11p dephosphorylation and propagates SIN asymmetry in fission yeast.
Singh NS et al. Curr Biol 2011 Dec 06;21(23):1968-78
PMID:30726745 - Fission Yeast NDR/LATS Kinase Orb6 Regulates Exocytosis via Phosphorylation of the Exocyst Complex.
Tay YD et al. Cell Rep 2019 Feb 05;26(6):1654-1667.e7
PMID:34496258 - Transcription and chromatin-based surveillance mechanism controls suppression of cryptic antisense transcription.
Heo DH et al. Cell Rep 2021 Sep 07;36(10):109671
PMID:40015273 - A comprehensive Schizosaccharomyces pombe atlas of physical transcription factor interactions with proteins and chromatin.
Skribbe M et al. Mol Cell 2025 Feb 19;
GO_REF:0000002 - Comments
PMID:26152728 - A Two-step Protein Quality Control Pathway for a Misfolded DJ-1 Variant in Fission Yeast.
Mathiassen SG et al. J Biol Chem 2015 Aug 21;290(34):21141-21153
PMID:32101745 - Dense Transposon Integration Reveals Essential Cleavage and Polyadenylation Factors Promote Heterochromatin Formation.
Lee SY et al. Cell Rep 2020 Feb 25;30(8):2686-2698.e8
PMID:33823663 - A TOR (target of rapamycin) and nutritional phosphoproteome of fission yeast reveals novel targets in networks conserved in humans.
Halova L et al. Open Biol 2021 Apr;11(4):200405
PMID:21511999 - Comparative functional genomics of the fission yeasts.
Rhind N et al. Science 2011 May 20;332(6032):930-6
GO_REF:0000104 - Electronic Gene Ontology annotations created by transferring manual GO annotations between related proteins based on shared sequence features.
PMID:28218250 - Chromatin remodeller Fun30 Fft3 induces nucleosome disassembly to facilitate RNA polymerase II elongation.
Lee J et al. Nat Commun 2017 Feb 20;8:14527