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Database: UniProt
Entry: A0A1V6QF66_9EURO
LinkDB: A0A1V6QF66_9EURO
Original site: A0A1V6QF66_9EURO 
ID   A0A1V6QF66_9EURO        Unreviewed;       351 AA.
AC   A0A1V6QF66;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=fructose-bisphosphatase {ECO:0000256|ARBA:ARBA00013093};
DE            EC=3.1.3.11 {ECO:0000256|ARBA:ARBA00013093};
DE   AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase {ECO:0000256|ARBA:ARBA00032973};
GN   ORFNames=PENANT_c005G00662 {ECO:0000313|EMBL:OQD87662.1};
OS   Penicillium antarcticum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=416450 {ECO:0000313|EMBL:OQD87662.1, ECO:0000313|Proteomes:UP000191672};
RN   [1] {ECO:0000313|Proteomes:UP000191672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 31811 {ECO:0000313|Proteomes:UP000191672};
RX   PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA   Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA   Frisvad J.C., Workman M., Nielsen J.;
RT   "Global analysis of biosynthetic gene clusters reveals vast potential of
RT   secondary metabolite production in Penicillium species.";
RL   Nat. Microbiol. 2:17044-17044(2017).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-
CC         phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11;
CC         Evidence={ECO:0000256|ARBA:ARBA00001273};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Carbohydrate biosynthesis. {ECO:0000256|ARBA:ARBA00024331}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the FBPase class 1 family.
CC       {ECO:0000256|ARBA:ARBA00010941, ECO:0000256|RuleBase:RU000508}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OQD87662.1}.
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DR   EMBL; MDYN01000005; OQD87662.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V6QF66; -.
DR   STRING; 416450.A0A1V6QF66; -.
DR   OrthoDB; 292at2759; -.
DR   Proteomes; UP000191672; Unassembled WGS sequence.
DR   GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd00354; FBPase; 1.
DR   Gene3D; 3.40.190.80; -; 1.
DR   Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
DR   HAMAP; MF_01855; FBPase_class1; 1.
DR   InterPro; IPR044015; FBPase_C_dom.
DR   InterPro; IPR000146; FBPase_class-1.
DR   InterPro; IPR033391; FBPase_N.
DR   InterPro; IPR028343; FBPtase.
DR   InterPro; IPR020548; Fructose_bisphosphatase_AS.
DR   PANTHER; PTHR11556; FRUCTOSE-1,6-BISPHOSPHATASE-RELATED; 1.
DR   PANTHER; PTHR11556:SF1; FRUCTOSE-BISPHOSPHATASE; 1.
DR   Pfam; PF00316; FBPase; 1.
DR   Pfam; PF18913; FBPase_C; 1.
DR   PIRSF; PIRSF500210; FBPtase; 1.
DR   PIRSF; PIRSF000904; FBPtase_SBPase; 1.
DR   PRINTS; PR00115; F16BPHPHTASE.
DR   SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR   PROSITE; PS00124; FBPASE; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW   ECO:0000256|RuleBase:RU000508};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000508};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191672}.
FT   DOMAIN          19..212
FT                   /note="Fructose-1-6-bisphosphatase class I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00316"
FT   DOMAIN          216..346
FT                   /note="Fructose-1-6-bisphosphatase class 1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18913"
SQ   SEQUENCE   351 AA;  38511 MW;  7EB85B4FA3AB46A4 CRC64;
     MASGAPPVGQ ENINTDIVTL SRFFTEEQIK YPEASGDFTL LCHALQFSFK SIAYYIRRAS
     LINLTGLAGS SNTTGDDQKK LDVIGNDIFI SAMRGSGKCR IVVSEEEEEV IKFDEHPDAR
     YAVVCDPIDG SSNLDAGVSV GTIFGIFQLP DEVLGPNKSV GPEDLLHPGT SLVASGFTMY
     GASAQLVITM RGGGVNGFTL ENSLGEFILT HPNMQMPPSR SIYSVNEGNS MYWDEWCNAY
     FHSLKYPGEG KKPYSARYIG SMVADAYRTL LYGGMFAYPA DSKSPKGKLR ILYECAPMAM
     LFENAGGLAV NSRMERLMEV VPENIHDKSG VFLGSKDEVQ KVIDMYNKYH K
//
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