QAX_NEUCR
ID QAX_NEUCR Reviewed; 340 AA.
AC P11634; Q7RVA4;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Protein QA-X;
GN Name=qa-x; ORFNames=NCU06022;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=2525625; DOI=10.1016/0022-2836(89)90438-5;
RA Geever R.F., Huiet L., Baum J.A., Tyler B.M., Patel V.B., Rutledge B.J.,
RA Case M.E., Giles N.H.;
RT "DNA sequence, organization and regulation of the qa gene cluster of
RT Neurospora crassa.";
RL J. Mol. Biol. 207:15-34(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
CC -!- FUNCTION: Not known. Probably involved in quinate metabolism.
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000305}.
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DR EMBL; X14603; CAA32748.1; -; Genomic_DNA.
DR EMBL; CM002242; EAA30376.1; -; Genomic_DNA.
DR PIR; S04250; B31277.
DR RefSeq; XP_959612.1; XM_954519.1.
DR AlphaFoldDB; P11634; -.
DR SMR; P11634; -.
DR STRING; 5141.EFNCRP00000005413; -.
DR PRIDE; P11634; -.
DR EnsemblFungi; EAA30376; EAA30376; NCU06022.
DR GeneID; 3875771; -.
DR KEGG; ncr:NCU06022; -.
DR VEuPathDB; FungiDB:NCU06022; -.
DR HOGENOM; CLU_044118_1_2_1; -.
DR InParanoid; P11634; -.
DR OMA; HAWDCLA; -.
DR Proteomes; UP000001805; Chromosome 7, Linkage Group VII.
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..340
FT /note="Protein QA-X"
FT /id="PRO_0000142539"
FT BINDING 90
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 117..120
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 117
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 262
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 340 AA; 37323 MW; C185E29E0C05B8FF CRC64;
MTSRTTTATE LDEIYTFAVQ LGKDAGNLLM EAARLRFSNN NANHDKESTT QEFTEKDSAV
DIVTQTDEDV EAFIKSAINT RYPSHDFIGE ETYAKSSQST RPYLVTHTTP TWVVDPLDGT
VNYTHLFPMF CVSIAFLVDG TPVIGVICAP MLGQLFTACK GRGAWLNETQ RLPLVRQPMP
KSAPGGCVFS CEWGKDRKDR PEGNLYRKVE SFVNMAAEVG GRGGKGGMVH GVRSLGSATL
DLAYTAMGSF DIWWEGGCWE WDVAAGIAIL QEAGGLITSA NPPEDWATAE IPDVKLGSRL
YLVVRPAGPS EGETAREGQE RTIREVWRRV RALDYTRPGA
