(data stored in SCRATCH 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   08-MAY-2019, entry version 86.
DE   RecName: Full=Fructose-1,6-bisphosphatase {ECO:0000256|PIRNR:PIRNR004532};
GN   OrderedLocusNames=SCO5047 {ECO:0000313|EMBL:CAC05892.1};
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=ATCC BAA-471 / A3(2) / M145
RC   {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.,
RA   Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M.,
RA   Cronin A., Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S.,
RA   Huang C.H., Kieser T., Larke L., Murphy L., Oliver K., O'Neil S.,
RA   Rabbinowitsch E., Rajandream M.A., Rutherford K., Rutter S.,
RA   Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K.,
RA   Warren T., Wietzorrek A., Woodward J., Barrell B.G., Parkhill J.,
RA   Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces
RT   coelicolor A3(2).";
RL   Nature 417:141-147(2002).
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   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:0005829; C:cytosol; IBA:GO_Central.
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   Complete proteome {ECO:0000313|Proteomes:UP000001973};
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       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR004532-2}.
FT   REGION      181    183       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR004532-2}.
FT   REGION      203    205       Substrate binding. {ECO:0000256|PIRSR:
FT                                PIRSR004532-2}.
FT   METAL        49     49       Manganese 1. {ECO:0000256|PIRSR:
FT                                PIRSR004532-1}.
FT   METAL        73     73       Manganese 1. {ECO:0000256|PIRSR:
FT                                PIRSR004532-1}.
FT   METAL       101    101       Manganese 2. {ECO:0000256|PIRSR:
FT                                PIRSR004532-1}.
FT   METAL       104    104       Manganese 2. {ECO:0000256|PIRSR:
FT                                PIRSR004532-1}.
FT   METAL       230    230       Manganese 2. {ECO:0000256|PIRSR:
FT                                PIRSR004532-1}.
FT   BINDING     136    136       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR004532-2}.
FT   BINDING     227    227       Substrate; via amide nitrogen.
FT                                {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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