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Database: UniProt
Entry: H8KZ44_FRAAD
LinkDB: H8KZ44_FRAAD
Original site: H8KZ44_FRAAD 
ID   H8KZ44_FRAAD            Unreviewed;       337 AA.
AC   H8KZ44;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   24-JAN-2024, entry version 61.
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   OrderedLocusNames=Fraau_0024 {ECO:0000313|EMBL:AFC84535.1};
OS   Frateuria aurantia (strain ATCC 33424 / DSM 6220 / KCTC 2777 / LMG 1558 /
OS   NBRC 3245 / NCIMB 13370) (Acetobacter aurantius).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Frateuria.
OX   NCBI_TaxID=767434 {ECO:0000313|EMBL:AFC84535.1, ECO:0000313|Proteomes:UP000005234};
RN   [1] {ECO:0000313|Proteomes:UP000005234}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33424 / DSM 6220 / KCTC 2777 / LMG 1558 / NBRC 3245 /
RC   NCIMB 13370 {ECO:0000313|Proteomes:UP000005234};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Ovchinnikova G., Teshima H.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Frateuria aurantia DSM 6220.";
RL   Submitted (FEB-2012) 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; Calvin cycle.
CC       {ECO:0000256|ARBA:ARBA00005215}.
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01855}.
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}.
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DR   EMBL; CP003350; AFC84535.1; -; Genomic_DNA.
DR   RefSeq; WP_014401541.1; NC_017033.1.
DR   AlphaFoldDB; H8KZ44; -.
DR   STRING; 767434.Fraau_0024; -.
DR   KEGG; fau:Fraau_0024; -.
DR   eggNOG; COG0158; Bacteria.
DR   HOGENOM; CLU_039977_0_0_6; -.
DR   OMA; YIPENCP; -.
DR   OrthoDB; 9806756at2; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000005234; Chromosome.
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:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
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; 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.
DR   PROSITE; PS00124; FBPASE; 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|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01855};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_01855}; Reference proteome {ECO:0000313|Proteomes:UP000005234}.
FT   DOMAIN          6..192
FT                   /note="Fructose-1-6-bisphosphatase class I N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00316"
FT   DOMAIN          197..330
FT                   /note="Fructose-1-6-bisphosphatase class 1 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF18913"
FT   BINDING         90
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01855"
FT   BINDING         112
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01855"
FT   BINDING         112
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01855"
FT   BINDING         114
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01855"
FT   BINDING         115..118
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01855"
FT   BINDING         115
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01855"
FT   BINDING         207
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01855"
FT   BINDING         273
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01855"
FT   BINDING         279
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01855"
SQ   SEQUENCE   337 AA;  37292 MW;  2A4EDF8C22DC0147 CRC64;
     MKSISLIQFL IEARRKGQLN AELSLLIEVV ARACKRIAVA TGKGALGDVL GGAGTDNVQG
     EHQKKLDVIS NEILLEANAW GGHLAACASE EMEDPQPIPD AYPKGHHLLL FDPLDGSSNI
     DINVSVGTIF SVLRCPDGIS QVDAEHFLQP GVEQLAAGYV LYGPRTLLVL TFGHGTHEFT
     LDREIGSFIL TRRDIRIPEE TAEFAINMSN QRHWQPPMKR YIHELLEGSE GPRGKDFNMR
     WVAAMVADVH RILTRGGVFY YPLDTKNQAQ GGKLRLLYEA NPMAFLVEQA GGAATDGHQR
     IMELQPTGLH QRIPVFLGSR EEIELVTRYH QQDQTSS
//
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