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Entry: A0A327QT70_9BACT
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ID   A0A327QT70_9BACT        Unreviewed;       335 AA.
AC   A0A327QT70;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=Fructose-1,6-bisphosphatase class 1 {ECO:0000256|HAMAP-Rule:MF_01855};
DE            Short=FBPase class 1 {ECO:0000256|HAMAP-Rule:MF_01855};
DE            EC=3.1.3.11 {ECO:0000256|HAMAP-Rule:MF_01855};
DE   AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase class 1 {ECO:0000256|HAMAP-Rule:MF_01855};
GN   Name=fbp {ECO:0000256|HAMAP-Rule:MF_01855};
GN   ORFNames=LX64_02020 {ECO:0000313|EMBL:RAJ06892.1};
OS   Chitinophaga skermanii.
OC   Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC   Chitinophaga.
OX   NCBI_TaxID=331697 {ECO:0000313|EMBL:RAJ06892.1, ECO:0000313|Proteomes:UP000249547};
RN   [1] {ECO:0000313|EMBL:RAJ06892.1, ECO:0000313|Proteomes:UP000249547}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23857 {ECO:0000313|EMBL:RAJ06892.1,
RC   ECO:0000313|Proteomes:UP000249547};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (JUN-2018) 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, ECO:0000256|HAMAP-
CC         Rule:MF_01855};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01855};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01855};
CC   -!- PATHWAY: Carbohydrate biosynthesis. {ECO:0000256|ARBA:ARBA00024331}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_01855}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01855}.
CC   -!- SIMILARITY: Belongs to the FBPase class 1 family.
CC       {ECO:0000256|ARBA:ARBA00010941, ECO:0000256|HAMAP-Rule:MF_01855,
CC       ECO:0000256|RuleBase:RU000508}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01855}.
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:RAJ06892.1}.
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DR   EMBL; QLLL01000003; RAJ06892.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A327QT70; -.
DR   OrthoDB; 9806756at2; -.
DR   Proteomes; UP000249547; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:UniProtKB-UniRule.
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   PANTHER; PTHR11556; FRUCTOSE-1,6-BISPHOSPHATASE-RELATED; 1.
DR   PANTHER; PTHR11556:SF35; SEDOHEPTULOSE-1,7-BISPHOSPHATASE, CHLOROPLASTIC; 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.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW   Rule:MF_01855};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01855};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01855};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01855};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01855};
KW   Reference proteome {ECO:0000313|Proteomes:UP000249547}.
FT   DOMAIN          8..200
FT                   /note="Fructose-1-6-bisphosphatase class I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00316"
FT   DOMAIN          204..333
FT                   /note="Fructose-1-6-bisphosphatase class 1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18913"
FT   BINDING         95
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01855"
FT   BINDING         118
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01855"
FT   BINDING         118
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01855"
FT   BINDING         120
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01855"
FT   BINDING         121..124
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01855"
FT   BINDING         121
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01855"
FT   BINDING         214
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01855"
FT   BINDING         282
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01855"
SQ   SEQUENCE   335 AA;  37366 MW;  809DF2B41A2224AE CRC64;
     MNSKQKVMTL DEFTIQELRN FPEATGQLSG LLRDIGLAAK RVNVEVNKAG IADILGEAGK
     TNVQGESVKK LDEFANDQFI NSLRHSIYCA GMASEENEDF IAFNDEKSLQ SKYVVLIDPL
     DGSSNIDVNV SIGTIFSVYR RLSANGSPCD LNDFLQEGAK QIAAGYIIYG SSTMLVYATR
     RSVQGFTLDP SIGEFCLSHP NIQVPNNSDI FSVNAGYYHL YEENVREAID LYMAKDMNDR
     IYRHRFVGCM VAEIHRTLIQ GGIFMYPAFG KYKNGRLRLC YECNPMSFLI EKAGGASIVD
     GHTRLLDVKP TELHQRIPIF IGSKDMVDVV KVVLQ
//
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