ID Q5UWP9_HALMA Unreviewed; 265 AA.
AC Q5UWP9;
DT 07-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 07-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=fructose-bisphosphatase {ECO:0000256|ARBA:ARBA00013093};
DE EC=3.1.3.11 {ECO:0000256|ARBA:ARBA00013093};
GN Name=suhB2 {ECO:0000313|EMBL:AAV48304.1};
GN OrderedLocusNames=rrnB0102 {ECO:0000313|EMBL:AAV48304.1};
GN ORFNames=E6P14_02890 {ECO:0000313|EMBL:QCP89843.1};
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OG Plasmid pHMA288 {ECO:0000313|EMBL:QCP89843.1}, and
OG Plasmid phma288 {ECO:0000313|Proteomes:UP000298722}.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569 {ECO:0000313|EMBL:AAV48304.1, ECO:0000313|Proteomes:UP000001169};
RN [1] {ECO:0000313|EMBL:AAV48304.1, ECO:0000313|Proteomes:UP000001169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 {ECO:0000313|EMBL:AAV48304.1}, and ATCC 43049 / DSM
RC 3752 / JCM 8966 / VKM B-1809 {ECO:0000313|Proteomes:UP000001169};
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
RN [2] {ECO:0000313|EMBL:QCP89843.1, ECO:0000313|Proteomes:UP000298722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 {ECO:0000313|EMBL:QCP89843.1,
RC ECO:0000313|Proteomes:UP000298722};
RC PLASMID=pHMA288 {ECO:0000313|EMBL:QCP89843.1}, and phma288
RC {ECO:0000313|Proteomes:UP000298722};
RA DasSarma S., DasSarma P., DasSarma S., Fomenkov A., Vincze T., Anton B.P.,
RA Roberts R.J.;
RT "Methylomes of two halophilic Archaea, Haloarcula marismortui and Haloferax
RT mediterranei.";
RL Submitted (APR-2019) 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 -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily. FBPase
CC class 4 family. {ECO:0000256|ARBA:ARBA00038103}.
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DR EMBL; AY596298; AAV48304.1; -; Genomic_DNA.
DR EMBL; CP039136; QCP89843.1; -; Genomic_DNA.
DR RefSeq; WP_011225022.1; NZ_CP039136.1.
DR AlphaFoldDB; Q5UWP9; -.
DR STRING; 272569.rrnB0102; -.
DR PaxDb; 272569-rrnB0102; -.
DR EnsemblBacteria; AAV48304; AAV48304; rrnB0102.
DR GeneID; 40151067; -.
DR KEGG; hma:rrnB0102; -.
DR PATRIC; fig|272569.17.peg.4132; -.
DR eggNOG; arCOG01349; Archaea.
DR HOGENOM; CLU_044118_0_0_2; -.
DR Proteomes; UP000001169; Chromosome II.
DR Proteomes; UP000298722; Plasmid phma288.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd01639; IMPase; 1.
DR Gene3D; 3.40.190.80; -; 1.
DR Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
DR InterPro; IPR033942; IMPase.
DR InterPro; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR PANTHER; PTHR20854; INOSITOL MONOPHOSPHATASE; 1.
DR PANTHER; PTHR20854:SF4; INOSITOL-1-MONOPHOSPHATASE-RELATED; 1.
DR Pfam; PF00459; Inositol_P; 1.
DR PRINTS; PR00377; IMPHPHTASES.
DR SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR PROSITE; PS00629; IMP_1; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Hydrolase {ECO:0000313|EMBL:AAV48304.1};
KW Lithium {ECO:0000256|ARBA:ARBA00022671};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Plasmid {ECO:0000313|EMBL:QCP89843.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001169}.
SQ SEQUENCE 265 AA; 28418 MW; 7FBA0287F47525B3 CRC64;
MRDATYPQLW AAVRAARKAG RTLESVKPAA DQFQVKHNGD IVTEADRTVE ETILAELSGQ
FPVHTVVSEE SAPEFTTKPR WIIDPIDGTT NFLNGIPHYS ISIAFEGAGE PDVGIVYHVP
SETMYTAIEG GGAYANGQPL SLSATTELSE ALIVTGFDTA SMQAQEYDHF RTILNVTQGV
RRFGSAAGEL AMVAAGQFDA FFERQLSVWD TAAGVKIVEE AGGEVTRIKA LDGKNSEMVL
ASNEAIHQDL VALVSAGTVP KMDGQ
//
