ID A0A168Q3X7_ABSGL Unreviewed; 1362 AA.
AC A0A168Q3X7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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 Name=ABSGL_09313.1 scaffold 11175 {ECO:0000313|EMBL:SAM03472.1};
OS Absidia glauca (Pin mould).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=4829 {ECO:0000313|EMBL:SAM03472.1};
RN [1] {ECO:0000313|EMBL:SAM03472.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAM03472.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; LT554202; SAM03472.1; -; Genomic_DNA.
DR STRING; 4829.A0A168Q3X7; -.
DR InParanoid; A0A168Q3X7; -.
DR OrthoDB; 292at2759; -.
DR Proteomes; UP000078561; Unassembled WGS sequence.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IEA:UniProtKB-EC.
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; 3.90.70.10; Cysteine proteinases; 2.
DR Gene3D; 3.30.2230.10; DUSP-like; 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; IPR035927; DUSP-like_sf.
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 InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR006615; Pept_C19_DUSP.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR PANTHER; PTHR11556; FRUCTOSE-1,6-BISPHOSPHATASE-RELATED; 1.
DR PANTHER; PTHR11556:SF1; FRUCTOSE-BISPHOSPHATASE; 1.
DR Pfam; PF06337; DUSP; 1.
DR Pfam; PF00316; FBPase; 1.
DR Pfam; PF18913; FBPase_C; 1.
DR Pfam; PF00443; UCH; 1.
DR PIRSF; PIRSF500210; FBPtase; 1.
DR PIRSF; PIRSF000904; FBPtase_SBPase; 1.
DR PRINTS; PR00115; F16BPHPHTASE.
DR SMART; SM00695; DUSP; 1.
DR SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR SUPFAM; SSF143791; DUSP-like; 1.
DR PROSITE; PS51283; DUSP; 1.
DR PROSITE; PS00124; FBPASE; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 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:UP000078561}.
FT DOMAIN 406..516
FT /note="DUSP"
FT /evidence="ECO:0000259|PROSITE:PS51283"
FT DOMAIN 707..1362
FT /note="USP"
FT /evidence="ECO:0000259|PROSITE:PS50235"
FT REGION 310..389
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..353
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..389
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1362 AA; 152102 MW; 17A932FFD69A35FB CRC64;
MSFEEVKIGK GEDLVTLTRW VLSQQQEVPE ATGDLTILLT AIQFGCKFVA SKVKQAGLIN
LLGLTGTANV QGEDVKKLDV LANDIFRNSL IASGKACILV SEEDENAMII KNPNERGKYV
VTFDPLDGSS NIDCGVSIGT IFGIFKVNDE ENPTMADCIR SGREILASGY CMYGSYCEMI
LSVGNGVQGF TLDPAIGEFI MTHPNITMPP RGKIYSVNEG NYKYFDEPCK KYVDQVKQKY
SARYVGSMVS DIHRTLLYGG IFGYPADSKS KKGKLRILYE VFPMAFLIEQ AGGKATTGTQ
NALDIIPEHI HDRSAKVNQP VDKSKRHSES PRKGQQSTDM AHHQPNQCTP LPTTSASPSP
PPVSKRARSY SSQDDTNNSA SQRQKLPDLT GNDQGCFTWG CYTSSDDPKE QLHCVSMIME
TPLEVGDAWY LVSITWVSKW KQYCRFASSS GAMNQQRCLD LYPGAVNNKS LLHTETQQLL
PNLVEDTDFI SIPEIAWHSL EKWYGKSDTP LKRYVIDNGS YTKMNVLEIY PAIFDVYVTL
ATGHGLRLDS GNSKPVINLS MDTPLEDARY QLLAAHHLAQ DTPIKTFWVA KSTAAALDSS
VVSSLVLHQA PKMDTGNPVA TIGDHCFDNS ALMMDLSPYL DDWIDSSPQS SLTLPSTPSS
PLCAFGTGFK NHSSASGVLL SPILLDGPLN SAASDDLDPV YQHQGICGLV NLGNTCFMNS
ALQCLSNTPQ LSRWFLANNH TQDLNRDNPL GMHGALAESY GDLIQQMWDT DTSLANPKQL
KLIINQFSPL FTGYQQHDSQ ELLAFLLDGL HEDTNRILDK PYKELSNFGD MPDREIAKAS
WDYHKARNDS VIVDLFQGQF KSRLVCNVCQ KVSVTFDPFM YLSLPLPTDM KCHIEIIFVP
YDTIFFPQHM ILTLDNDATI VDLKAATANL TDLTEIDDLS TLLVLEIYND NIYKVFLDFD
LVTSIQPNDG IYIYQLPGSF SPDTAHRTHL GAPSSSNDGN NHAEHPGCEW IVFPVYCSTF
LDYEEHGPGY QQFGGPLILA IQVKYAHCVE NVYRLIAKHL ERYTRVRLFR DVYFPDATKD
PPTPISPSSP LVDSTLPAQQ QPKCIHHLEP ISNLFSMNIF SPAPDERVSK SNIPHTDGDW
RYMYFQDMEN RLEDLLGDTT TDVPEATNSQ HPSPFLSPLR TAPPHTLIRQ GEGILLDWDL
RSAQDCFGIN LGSPEISPLG TTTTTLSTID DSKWTTVSSL MDPPIISLTD CLDEFTKMEH
LSEEDQWYCP QCKRHQPATK KFDLWRLPDI LVIHLKRFDD RLHEKIHINI EFPLEALDMA
DRVLGGEQVP PVYDLYAVDN HMGSMDSGHY TAFAQNWLDN KW
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