ID D4GPQ1_HALVD Unreviewed; 267 AA.
AC D4GPQ1; L9VID2;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=fructose-bisphosphatase {ECO:0000256|ARBA:ARBA00013093};
DE EC=3.1.3.11 {ECO:0000256|ARBA:ARBA00013093};
GN Name=suhB3 {ECO:0000313|EMBL:ADE01280.1};
GN OrderedLocusNames=HVO_B0253 {ECO:0000313|EMBL:ADE01280.1};
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OG Plasmid pHV3 {ECO:0000313|EMBL:ADE01280.1,
OG ECO:0000313|Proteomes:UP000008243}.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800 {ECO:0000313|EMBL:ADE01280.1, ECO:0000313|Proteomes:UP000008243};
RN [1] {ECO:0000313|EMBL:ADE01280.1, ECO:0000313|Proteomes:UP000008243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 /
RC VKM B-1768 / DS2 {ECO:0000313|Proteomes:UP000008243};
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
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; CP001953; ADE01280.1; -; Genomic_DNA.
DR RefSeq; WP_004041284.1; NZ_AOHU01000021.1.
DR AlphaFoldDB; D4GPQ1; -.
DR PaxDb; 309800-C498_02375; -.
DR EnsemblBacteria; ADE01280; ADE01280; HVO_B0253.
DR GeneID; 8919101; -.
DR KEGG; hvo:HVO_B0253; -.
DR PATRIC; fig|309800.29.peg.463; -.
DR eggNOG; arCOG01349; Archaea.
DR HOGENOM; CLU_044118_0_2_2; -.
DR OrthoDB; 58111at2157; -.
DR Proteomes; UP000008243; Plasmid pHV3.
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 CDD; cd01637; IMPase_like; 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; 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:ADE01280.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Plasmid {ECO:0000313|EMBL:ADE01280.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008243}.
SQ SEQUENCE 267 AA; 28768 MW; CC004601F4AD26E8 CRC64;
MDADPREAVA IDAAEVGADH ASARFRTELD IEQKGDAIDL VTEVDRETQR RVIAAIRERF
PDDAVVGEED DELKTVPESG YAWIIDPIDG TQNYTRGARE WVTSVAVVEN QTPIAAVNVS
PETGDTYVAT AARVERNGRP MTVSDESNTS AFLVSSTLRY QVGDRPGIER LSGDIFGTFG
EMRKLGTTQL TLSRLADGSI DAVIGFDEHP NAWDTVAGVY LVERAGGTVT DIHGNAWGPG
QPGLVASNGH AHDEVLEAAQ AAFEETR
//
