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Database: UniProt
Entry: L1IGJ0_GUITC
LinkDB: L1IGJ0_GUITC
Original site: L1IGJ0_GUITC 
ID   L1IGJ0_GUITC            Unreviewed;       443 AA.
AC   L1IGJ0;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=fructose-bisphosphatase {ECO:0000256|ARBA:ARBA00013093};
DE            EC=3.1.3.11 {ECO:0000256|ARBA:ARBA00013093};
GN   ORFNames=GUITHDRAFT_97957 {ECO:0000313|EMBL:EKX34950.1};
OS   Guillardia theta (strain CCMP2712) (Cryptophyte).
OC   Eukaryota; Cryptophyceae; Pyrenomonadales; Geminigeraceae; Guillardia.
OX   NCBI_TaxID=905079 {ECO:0000313|EMBL:EKX34950.1};
RN   [1] {ECO:0000313|EMBL:EKX34950.1, ECO:0000313|Proteomes:UP000011087}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP2712 {ECO:0000313|EMBL:EKX34950.1,
RC   ECO:0000313|Proteomes:UP000011087};
RX   PubMed=23201678; DOI=10.1038/nature11681;
RG   DOE Joint Genome Institute;
RA   Curtis B.A., Tanifuji G., Burki F., Gruber A., Irimia M., Maruyama S.,
RA   Arias M.C., Ball S.G., Gile G.H., Hirakawa Y., Hopkins J.F., Kuo A.,
RA   Rensing S.A., Schmutz J., Symeonidi A., Elias M., Eveleigh R.J.,
RA   Herman E.K., Klute M.J., Nakayama T., Obornik M., Reyes-Prieto A.,
RA   Armbrust E.V., Aves S.J., Beiko R.G., Coutinho P., Dacks J.B.,
RA   Durnford D.G., Fast N.M., Green B.R., Grisdale C.J., Hempel F.,
RA   Henrissat B., Hoppner M.P., Ishida K., Kim E., Koreny L., Kroth P.G.,
RA   Liu Y., Malik S.B., Maier U.G., McRose D., Mock T., Neilson J.A.,
RA   Onodera N.T., Poole A.M., Pritham E.J., Richards T.A., Rocap G., Roy S.W.,
RA   Sarai C., Schaack S., Shirato S., Slamovits C.H., Spencer D.F., Suzuki S.,
RA   Worden A.Z., Zauner S., Barry K., Bell C., Bharti A.K., Crow J.A.,
RA   Grimwood J., Kramer R., Lindquist E., Lucas S., Salamov A., McFadden G.I.,
RA   Lane C.E., Keeling P.J., Gray M.W., Grigoriev I.V., Archibald J.M.;
RT   "Algal genomes reveal evolutionary mosaicism and the fate of
RT   nucleomorphs.";
RL   Nature 492:59-65(2012).
RN   [2] {ECO:0000313|Proteomes:UP000011087}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CCMP2712 {ECO:0000313|Proteomes:UP000011087};
RA   Kuo A., Curtis B.A., Tanifuji G., Burki F., Gruber A., Irimia M.,
RA   Maruyama S., Arias M.C., Ball S.G., Gile G.H., Hirakawa Y., Hopkins J.F.,
RA   Rensing S.A., Schmutz J., Symeonidi A., Elias M., Eveleigh R.J.,
RA   Herman E.K., Klute M.J., Nakayama T., Obornik M., Reyes-Prieto A.,
RA   Armbrust E.V., Aves S.J., Beiko R.G., Coutinho P., Dacks J.B.,
RA   Durnford D.G., Fast N.M., Green B.R., Grisdale C., Hempe F., Henrissat B.,
RA   Hoppner M.P., Ishida K.-I., Kim E., Koreny L., Kroth P.G., Liu Y.,
RA   Malik S.-B., Maier U.G., McRose D., Mock T., Neilson J.A., Onodera N.T.,
RA   Poole A.M., Pritham E.J., Richards T.A., Rocap G., Roy S.W., Sarai C.,
RA   Schaack S., Shirato S., Slamovits C.H., Spencer D.F., Suzuki S.,
RA   Worden A.Z., Zauner S., Barry K., Bell C., Bharti A.K., Crow J.A.,
RA   Grimwood J., Kramer R., Lindquist E., Lucas S., Salamov A., McFadden G.I.,
RA   Lane C.E., Keeling P.J., Gray M.W., Grigoriev I.V., Archibald J.M.;
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EnsemblProtists:EKX34950}
RP   IDENTIFICATION.
RG   EnsemblProtists;
RL   Submitted (MAR-2016) to UniProtKB.
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; Calvin cycle.
CC       {ECO:0000256|ARBA:ARBA00005215}.
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; JH993100; EKX34950.1; -; Genomic_DNA.
DR   RefSeq; XP_005821930.1; XM_005821873.1.
DR   AlphaFoldDB; L1IGJ0; -.
DR   STRING; 905079.L1IGJ0; -.
DR   PaxDb; 55529-EKX34950; -.
DR   EnsemblProtists; EKX34950; EKX34950; GUITHDRAFT_97957.
DR   GeneID; 17291668; -.
DR   KEGG; gtt:GUITHDRAFT_97957; -.
DR   eggNOG; KOG1458; Eukaryota.
DR   HOGENOM; CLU_039977_2_0_1; -.
DR   OMA; VAYYASE; -.
DR   OrthoDB; 292at2759; -.
DR   Proteomes; UP000011087; 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:SF1; FRUCTOSE-1,6-BISPHOSPHATASE 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR11556; FRUCTOSE-1,6-BISPHOSPHATASE-RELATED; 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   Chloroplast {ECO:0000256|ARBA:ARBA00022528};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000508};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Plastid {ECO:0000256|ARBA:ARBA00022640};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011087};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..443
FT                   /note="fructose-bisphosphatase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011944434"
FT   DOMAIN          71..288
FT                   /note="Fructose-1-6-bisphosphatase class I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00316"
FT   DOMAIN          292..422
FT                   /note="Fructose-1-6-bisphosphatase class 1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18913"
SQ   SEQUENCE   443 AA;  48455 MW;  5734A640D78E51B0 CRC64;
     MRAVLLAVAA TCASAFMAPS PVSLSRRPLR LSQSRSAAVR VPRASPVMMA NIKERTVRAP
     VFDEVCEQTG ITLTRYMMEV SRANPELRDL ESLISGIQQA CKTISSLVDR ATITGMVGYA
     NGGGSINVQG EEQKKLDVVT NDVLKRALRF TGKVGIIASE EEDVPVFNKD AYKVPGGEGK
     YQDVTVDIGS KYVTVFDPLD GSSNVDANIP TGTIFGVYEE AESMENCMVN DDSVEGSCLL
     NTLQPGDALV ASGYCLYSSS CMFVFTIGAG VNGFTYDRSI GEFVLTHPNI QLPKRGKIYS
     MNEANRWDWD KPLQDYVTAI QTGQGQTKAK YSSRYIGSMV GDVHRTLLYG GIFGYPADKK
     NKDGKLRLLY EAAPMSFLME QAGGLSLTGK TRIMDLVPQK VHQRVPFLAG SYDDVMEMRS
     YYDACDDPEI IKRCLARLEG SAK
//
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