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Database: UniProt
Entry: A0A016RS90_9BILA
LinkDB: A0A016RS90_9BILA
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ID   A0A016RS90_9BILA        Unreviewed;       410 AA.
AC   A0A016RS90;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=Acey_s0388.g498 {ECO:0000313|EMBL:EYB81260.1};
GN   ORFNames=Y032_0388g498 {ECO:0000313|EMBL:EYB81260.1};
OS   Ancylostoma ceylanicum.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC   Ancylostomatinae; Ancylostoma.
OX   NCBI_TaxID=53326 {ECO:0000313|EMBL:EYB81260.1, ECO:0000313|Proteomes:UP000024635};
RN   [1] {ECO:0000313|Proteomes:UP000024635}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HY135 {ECO:0000313|Proteomes:UP000024635};
RX   PubMed=25730766; DOI=10.1038/ng.3237;
RA   Schwarz E.M., Hu Y., Antoshechkin I., Miller M.M., Sternberg P.W.,
RA   Aroian R.V.;
RT   "The genome and transcriptome of the zoonotic hookworm Ancylostoma
RT   ceylanicum identify infection-specific gene families.";
RL   Nat. Genet. 47:416-422(2015).
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:EYB81260.1}.
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DR   EMBL; JARK01001724; EYB81260.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A016RS90; -.
DR   STRING; 53326.A0A016RS90; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000024635; 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:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
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   Gluconeogenesis {ECO:0000256|ARBA:ARBA00022432};
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:UP000024635}.
FT   DOMAIN          83..271
FT                   /note="Fructose-1-6-bisphosphatase class I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00316"
FT   DOMAIN          275..403
FT                   /note="Fructose-1-6-bisphosphatase class 1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18913"
SQ   SEQUENCE   410 AA;  45091 MW;  A14FE66CE56A42A3 CRC64;
     MELCSFSSRT TRSSMTVVQR RHGLRTTIAH ICACSVAEGS DPCHIGGLTK ECLLSLIANL
     RQNIPGYNMS QSSNTYGIET NAMTLQRFVL HEQRKHPSAT GDLTHLLTSL LTAFKAISSS
     VRKAGLAHLY GIAGNTNVQG EEVKKLDVLS NELMINMVRS SYTSCAMVSE ENENVIEVDE
     GKQGKYIVTF DPLDGSSNID CLVSIGTIFG IWRKQTDGPV TQADLLQSGR AMVAAGYCLY
     GSATMVVLST GRGVNGFMLD PSIGEFILTH PKMRIPEKGK YYSINEGYAK QWPKSLAEYV
     HTRKFPEPGK KGMALRYVGS MVADVHRTML NGGIFLYPAT QDAPKGKLRY LYECAPMAFL
     VEQAGGIATT GERAVLDHVP TDIHERGLIY LGSKLDVEEM LSFFEKYKEQ
//
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