(data stored in SCRATCH zone)

SWISSPROT: D3UYW8_XENBS

ID   D3UYW8_XENBS            Unreviewed;       334 AA.
AC   D3UYW8;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 63.
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   ECO:0000313|EMBL:CBJ79496.1};
GN   OrderedLocusNames=XBJ1_0346 {ECO:0000313|EMBL:CBJ79496.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79496.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|EMBL:CBJ79496.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79496.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose
CC         6-phosphate + phosphate; Xref=Rhea:RHEA:11064,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:32966, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57634; EC=3.1.3.11; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01855, ECO:0000256|SAAS:SAAS01116638};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01855};
CC       Note=Binds 2 magnesium ions per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_01855};
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|HAMAP-Rule:MF_01855, ECO:0000256|RuleBase:RU000508,
CC       ECO:0000256|SAAS:SAAS00819920}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01855}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; FN667741; CBJ79496.1; -; Genomic_DNA.
DR   RefSeq; WP_012986956.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0346; -.
DR   EnsemblBacteria; CBJ79496; CBJ79496; XBJ1_0346.
DR   GeneID; 8829971; -.
DR   KEGG; xbo:XBJ1_0346; -.
DR   PATRIC; fig|406818.4.peg.317; -.
DR   eggNOG; ENOG4105CZI; Bacteria.
DR   eggNOG; COG0158; LUCA.
DR   HOGENOM; HOG000191265; -.
DR   KO; K03841; -.
DR   OMA; QSGLVCR; -.
DR   BioCyc; XBOV406818:XBJ1_RS01505-MONOMER; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000002045; 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   HAMAP; MF_01855; FBPase_class1; 1.
DR   InterPro; IPR000146; FBPase_class-1.
DR   InterPro; IPR033391; FBPase_N.
DR   InterPro; IPR028343; FBPtase.
DR   InterPro; IPR020548; Fructose_bisphosphatase_AS.
DR   PANTHER; PTHR11556; PTHR11556; 1.
DR   Pfam; PF00316; FBPase; 1.
DR   PIRSF; PIRSF500210; FBPtase; 1.
DR   PIRSF; PIRSF000904; FBPtase_SBPase; 1.
DR   PRINTS; PR00115; F16BPHPHTASE.
DR   PROSITE; PS00124; FBPASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3UYW8.
DR   SWISS-2DPAGE; D3UYW8.
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01855,
KW   ECO:0000256|RuleBase:RU000508, ECO:0000256|SAAS:SAAS00142634};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01855};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01855,
KW   ECO:0000256|RuleBase:RU000508, ECO:0000256|SAAS:SAAS00142646,
KW   ECO:0000313|EMBL:CBJ79496.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01855};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01855};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045}.
FT   DOMAIN        3    194       FBPase. {ECO:0000259|Pfam:PF00316}.
FT   REGION      115    118       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01855}.
FT   METAL        89     89       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01855}.
FT   METAL       112    112       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01855}.
FT   METAL       112    112       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01855}.
FT   METAL       114    114       Magnesium 1; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01855}.
FT   METAL       115    115       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01855}.
FT   METAL       277    277       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01855}.
FT   BINDING     208    208       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01855}.
FT   BINDING     241    241       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01855}.
FT   BINDING     271    271       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01855}.
SQ   SEQUENCE   334 AA;  36747 MW;  BAE181E1EC2770B4 CRC64;
     MKTLGEFIVE KQQDFPHATG ELTALLSAIK LGAKIIHRDI NKAGLVDILG TSGVSNVQGE
     VQMKLDLYAN EKLKAALKAR GEVAGIASEE EDEIVVFDGD RAENAKYVVL MDPLDGSSNI
     DVNVSVGTIF SIYHRITPIG QPVTEDDFLQ PGNRQVAAGY VVYGSSTMLV YTTGYGVHTF
     TYDPSLGVFC LTHEKVQFPA KGNMYSINEG NYIKFPMGVK KYIKYCQEQD EATQRPYTTR
     YIGSLVADFH RNLLKGGIYI YPSTASNPTG KLRLLYECNP IAFLAEQAGG KASDGKNRIL
     DITPTQLHQR VPFFVGTKSM VEKAESFMAE FPGE
//

If you have problems or comments...

PBIL Back to PBIL home page