QUTG_EMENI
ID QUTG_EMENI Reviewed; 330 AA.
AC P25416; C8VTB1; Q5BE94;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Protein qutG;
GN Name=qutG; ORFNames=AN1136;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2976880; DOI=10.1007/bf00337715;
RA Hawkins A.R., Lamb H.K., Smith M., Keyte J.W., Roberts C.F.;
RT "Molecular organisation of the quinic acid utilization (QUT) gene cluster
RT in Aspergillus nidulans.";
RL Mol. Gen. Genet. 214:224-231(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
RN [4]
RP SIMILARITY TO INOSITOL MONOPHOSPHATASE.
RX PubMed=2175387; DOI=10.1007/bf00315792;
RA Lamb H.K., Hawkins A.R., Smith M., Harvey I.J., Brown J., Turner G.,
RA Roberts C.F.;
RT "Spatial and biological characterisation of the complete quinic acid
RT utilisation gene cluster in Aspergillus nidulans.";
RL Mol. Gen. Genet. 223:17-23(1990).
CC -!- FUNCTION: Not known. Probably involved in quinate metabolism.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA66254.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; X13525; CAA31878.1; -; Genomic_DNA.
DR EMBL; AACD01000016; EAA66254.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001308; CBF88072.1; -; Genomic_DNA.
DR PIR; S08500; S08500.
DR RefSeq; XP_658740.1; XM_653648.1.
DR AlphaFoldDB; P25416; -.
DR SMR; P25416; -.
DR STRING; 162425.CADANIAP00001493; -.
DR EnsemblFungi; CBF88072; CBF88072; ANIA_01136.
DR EnsemblFungi; EAA66254; EAA66254; AN1136.2.
DR GeneID; 2876910; -.
DR KEGG; ani:AN1136.2; -.
DR VEuPathDB; FungiDB:AN1136; -.
DR eggNOG; KOG2951; Eukaryota.
DR HOGENOM; CLU_044118_1_2_1; -.
DR InParanoid; P25416; -.
DR OMA; HAWDCLA; -.
DR OrthoDB; 915621at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006020; P:inositol metabolic process; IBA:GO_Central.
DR GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0019630; P:quinate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR CDD; cd01639; IMPase; 1.
DR InterPro; IPR033942; IMPase.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR InterPro; IPR020550; Inositol_monophosphatase_CS.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR PROSITE; PS00629; IMP_1; 1.
DR PROSITE; PS00630; IMP_2; 1.
PE 3: Inferred from homology;
KW Magnesium; Metal-binding; Quinate metabolism; Reference proteome.
FT CHAIN 1..330
FT /note="Protein qutG"
FT /id="PRO_0000142540"
FT BINDING 78
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 102..105
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 85
FT /note="Q -> E (in Ref. 1; CAA31878)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="T -> A (in Ref. 1; CAA31878)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 330 AA; 36792 MW; B1C440DA2E01D792 CRC64;
MDCPIPQTEL DEIYAFATDL ARKAGQLLLE RVNDRNSEQV YAEKENAVDL VTQTDEDVES
LIKTAIQTKY PAHKFLGEES YAKGQSREYL IDEQPTWCVD PLDGTVNFTH AFPMFCVSIG
FIVNHYPVIG VIYAPMLNQL FSSCLNRGAW LNEMQQLPLI RKPSIPPLPA TAPSKCIFAC
EWGKDRRDIP DGTLQRKIES FVNMAAERGS RGGKGGMVHG VRSLGSATMD LAYTAMGSVD
IWWEGGCWEW DVAAGIAILL EAGGLVTAAN PPEDIEGPIE PVKLGSRLYL AIRPAGPSET
ETGRETQERT VREVWRRVRQ LDYERPTRQS
