(data stored in ACNUC1104 zone)

SWISSPROT: Q9FBN2_STRCO

ID   Q9FBN2_STRCO            Unreviewed;       343 AA.
AC   Q9FBN2;
DT   01-MAR-2001, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2001, sequence version 1.
DT   11-DEC-2019, entry version 89.
DE   RecName: Full=Fructose-1,6-bisphosphatase {ECO:0000256|PIRNR:PIRNR004532};
GN   OrderedLocusNames=SCO5047 {ECO:0000313|EMBL:CAC05892.1};
GN   ORFNames=FHV98_108255 {ECO:0000313|EMBL:TYP12669.1};
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226 {ECO:0000313|Proteomes:UP000001973};
RN   [1] {ECO:0000313|EMBL:CAC05892.1, ECO:0000313|Proteomes:UP000001973}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A3 {ECO:0000313|EMBL:CAC05892.1}, and ATCC BAA-471 / A3(2) /
RC   M145 {ECO:0000313|Proteomes:UP000001973};
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.H.,
RA   Kieser T., Larke L., Murphy L., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
RN   [2] {ECO:0000313|EMBL:TYP12669.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ICSSB 1010 {ECO:0000313|EMBL:TYP12669.1};
RA   Yuzawa S.;
RT   "Genome sequencing of Streptomyces strains engineered using actinophage
RT   integration system.";
RL   Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|PIRSR:PIRSR004532-1};
CC   -!- SIMILARITY: Belongs to the FBPase class 2 family.
CC       {ECO:0000256|PIRNR:PIRNR004532}.
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DR   EMBL; AL939122; CAC05892.1; -; Genomic_DNA.
DR   EMBL; VNID01000008; TYP12669.1; -; Genomic_DNA.
DR   RefSeq; NP_629199.1; NC_003888.3.
DR   RefSeq; WP_003973930.1; NC_003888.3.
DR   STRING; 100226.SCO5047; -.
DR   PRIDE; Q9FBN2; -.
DR   EnsemblBacteria; CAC05892; CAC05892; CAC05892.
DR   GeneID; 1100488; -.
DR   KEGG; sco:SCO5047; -.
DR   PATRIC; fig|100226.15.peg.5127; -.
DR   eggNOG; ENOG4105CBT; Bacteria.
DR   eggNOG; COG1494; LUCA.
DR   HOGENOM; HOG000241252; -.
DR   InParanoid; Q9FBN2; -.
DR   KO; K02446; -.
DR   OMA; AVFYMDK; -.
DR   PhylomeDB; Q9FBN2; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR   GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR   GO; GO:0006071; P:glycerol metabolic process; IEA:InterPro.
DR   CDD; cd01516; FBPase_glpX; 1.
DR   InterPro; IPR004464; FBPase_class-2/SBPase.
DR   PANTHER; PTHR30447; PTHR30447; 1.
DR   Pfam; PF03320; FBPase_glpX; 1.
DR   PIRSF; PIRSF004532; GlpX; 1.
DR   TIGRFAMs; TIGR00330; glpX; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q9FBN2.
DR   SWISS-2DPAGE; Q9FBN2.
KW   Carbohydrate metabolism {ECO:0000256|PIRNR:PIRNR004532};
KW   Manganese {ECO:0000256|PIRSR:PIRSR004532-1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR004532-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001973}.
FT   REGION          104..106
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004532-2"
FT   REGION          181..183
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004532-2"
FT   REGION          203..205
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004532-2"
FT   METAL           49
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004532-1"
FT   METAL           73
FT                   /note="Manganese 1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004532-1"
FT   METAL           101
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004532-1"
FT   METAL           104
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004532-1"
FT   METAL           230
FT                   /note="Manganese 2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004532-1"
FT   BINDING         136
FT                   /note="Substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004532-2"
FT   BINDING         227
FT                   /note="Substrate; via amide nitrogen"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004532-2"
SQ   SEQUENCE   343 AA;  36552 MW;  DC147AD62CF15AAA CRC64;
     MTEHHLPSEL DVPSEAPDRN LAMELVRVTE AAAMAAGRWV GRGDKNGADG AAVRAMRTLV
     HTVSMNGVVV IGEGEKDEAP MLFNGERVGD GTGAEVDIAV DPIDGTTLTA NGMTNAIAVL
     AAAERGSMFD PSAVFYMDKL VTGPEAADFV DINAPVAVNI RRIAKAKRRT PEDVTVVILD
     RPRHQGLIKE VRETGARIKL ISDGDVAGSI LALREGTGID LLLGIGGTPE GIISACAVKC
     LGGTIQGKLW PKDAEERQRA VDAGHDLDRV LTTDDLVSGD NVFFVATGIT DGELLRGVRY
     RSETATTDSI VMRSKSGTVR RIDSEHRLSK LRAYSAVDFD RAK
//

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