(data stored in ACNUC7421 zone)

SWISSPROT: C3MIA3_SINFN

ID   C3MIA3_SINFN            Unreviewed;       340 AA.
AC   C3MIA3;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 64.
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=cbbF {ECO:0000313|EMBL:ACP24451.1};
GN   Synonyms=fbp {ECO:0000256|HAMAP-Rule:MF_01855};
GN   OrderedLocusNames=NGR_c06580 {ECO:0000313|EMBL:ACP24451.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24451.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24451.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate + H(2)O = D-
CC       fructose 6-phosphate + phosphate. {ECO:0000256|HAMAP-
CC       Rule:MF_01855, ECO:0000256|SAAS:SAAS00003077}.
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}.
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DR   EMBL; CP001389; ACP24451.1; -; Genomic_DNA.
DR   RefSeq; WP_012707236.1; NC_012587.1.
DR   RefSeq; YP_002825204.1; NC_012587.1.
DR   ProteinModelPortal; C3MIA3; -.
DR   STRING; 394.NGR_c06580; -.
DR   EnsemblBacteria; ACP24451; ACP24451; NGR_c06580.
DR   GeneID; 7791884; -.
DR   KEGG; rhi:NGR_c06580; -.
DR   PATRIC; fig|394.7.peg.3471; -.
DR   eggNOG; ENOG4105CZI; Bacteria.
DR   eggNOG; COG0158; LUCA.
DR   HOGENOM; HOG000191264; -.
DR   KO; K03841; -.
DR   OMA; QSGLVCR; -.
DR   OrthoDB; POG091H05DB; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP.
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; C3MIA3.
DR   SWISS-2DPAGE; C3MIA3.
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01855,
KW   ECO:0000256|RuleBase:RU000508, ECO:0000256|SAAS:SAAS00142634};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
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:ACP24451.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_01855};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01855};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054}.
FT   DOMAIN       31    194       FBPase. {ECO:0000259|Pfam:PF00316}.
FT   METAL       102    102       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01855}.
FT   METAL       120    120       Magnesium 1. {ECO:0000256|HAMAP-Rule:
FT                                MF_01855}.
FT   METAL       120    120       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01855}.
FT   METAL       122    122       Magnesium 1; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01855}.
FT   METAL       123    123       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01855}.
FT   METAL       282    282       Magnesium 2. {ECO:0000256|HAMAP-Rule:
FT                                MF_01855}.
FT   BINDING     210    210       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01855}.
SQ   SEQUENCE   340 AA;  36190 MW;  BC193825FB9A72AC CRC64;
     MSTPATLASD EASFQHESVD EYLSTWAGED RSRQRVTALI NGVLDAACLL SERIATGSLE
     GDPARLVGSN SDGDAQKAID VASHALFVEI LERAGAGRIL SEEADEPVVF KGSGFGVAID
     PIDGSGNVGL GAPVGTLFSI IPFTETEDPF LTSGRRQVAA GYVSFGNTID LGFSVGDGML
     LATMHPQTGE FLIVRRQVRI PPDTSELAFN ASVHRHLQSG LSLYVQDCLA GSAGSRGRDF
     NMRWLGSAVG ELHRILLRGG VFFYAADKRP GYQNGRLRLV YEANPIAFLM EQAGGRATDG
     TSAILDKVPT SHHCRTPLVF GSATEVDLIA SYLNSNPTSE
//

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