ID A0A3M2I5Y5_9GAMM Unreviewed; 342 AA.
AC A0A3M2I5Y5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=EBB59_04295 {ECO:0000313|EMBL:RMH93867.1};
OS Lysobacter pythonis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=2483112 {ECO:0000313|EMBL:RMH93867.1, ECO:0000313|Proteomes:UP000275012};
RN [1] {ECO:0000313|EMBL:RMH93867.1, ECO:0000313|Proteomes:UP000275012}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4284/11 {ECO:0000313|EMBL:RMH93867.1,
RC ECO:0000313|Proteomes:UP000275012};
RA Hans-Juergen B., Huptas C., Sandra B., Igor L., Joachim S., Siegfried S.,
RA Mareike W., Peter K.;
RT "Proposal of Lysobacter pythonis sp. nov. isolated from royal pythons
RT (Python regius).";
RL Submitted (OCT-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:RMH93867.1}.
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DR EMBL; RFLY01000004; RMH93867.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M2I5Y5; -.
DR OrthoDB; 9806756at2; -.
DR Proteomes; UP000275012; 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:UP000275012}.
FT DOMAIN 9..196
FT /note="Fructose-1-6-bisphosphatase class I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00316"
FT DOMAIN 201..334
FT /note="Fructose-1-6-bisphosphatase class 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18913"
FT BINDING 94
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01855"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01855"
FT BINDING 116
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 119..122
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01855"
FT BINDING 119
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01855"
FT BINDING 211
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01855"
FT BINDING 277
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01855"
FT BINDING 283
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01855"
SQ SEQUENCE 342 AA; 37656 MW; AED06A4D60A8061C CRC64;
MPHKRKSVSL TRFLIEEERA GHVNAELRLL IEVVARACKT ISVAVGKGAL GGVLGDAGTG
NVQGEAQKKL DVIANDVLLE ANAWGGHLAA CASEEMDEPH PIPDAFPRGN FLLLFDPLDG
SSNIDVNVSV GTIFSVLKCP GDTACVDTAA FLQPGREQVA AGYCVYGPST TLILTVGHGV
HQFTLDREQG SFVLTQRGMR VPEETREFAI NMSNKRHWET PMQQYVDDLL IGKEGPRGKD
FNMRWIASMV ADVHRILTRG GIFIYPWDRK DPNKPGKLRL MYEANPMSFL IEQAGGAATD
GRGRIMDIQP GQLHQRVPVF LGSKREVEEA TRYHRHHDAL PE
//
