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UniProtKB/Swiss-Prot entry P00637

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name F16P1_RABIT
Primary accession number P00637
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on December 15, 1998 (Sequence version 3)
Annotations were last modified on    November 4, 2008 (Entry version 72)
Name and origin of the protein
Protein name Fructose-1,6-bisphosphatase 1
Synonyms FBPase 1
EC 3.1.3.11
D-fructose-1,6-bisphosphate 1-phosphohydrolase 1
Gene name
Name: FBP1
Synonyms: FBP
From
Oryctolagus cuniculus (Rabbit) [TaxID: 9986] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
Protein existence 1: Evidence at protein level;
References
[1]
 PROTEIN SEQUENCE.
TISSUE=Liver;
DOI=10.1016/0014-5793(96)00594-7; PubMed=8766709 [NCBI, ExPASy, EBI, Israel, Japan]
Kaiser R., Olsson H., Erman M., Weeks C.M., Hjelmqvist L., Ghosh D., Joernvall H.;
"Fructose-1,6-bisphosphatase. Primary structure of the rabbit liver enzyme. 'Intermediate' variability of an oligomeric protein.";
FEBS Lett. 389:249-252(1996).
[2]
 PROTEIN SEQUENCE OF 1-18.
STRAIN=New Zealand white;
TISSUE=Liver;
DOI=10.1016/0003-9861(77)90185-0; PubMed=189691 [NCBI, ExPASy, EBI, Israel, Japan]
El-Dorry H.A., Chu D.K., Dzugaj A., Tsolas O., Pontremoli S., Horecker B.L.;
"Rabbit liver fructose 1,6-bisphosphatase: the sequence of the amino-terminal region.";
Arch. Biochem. Biophys. 178:200-207(1977).
[3]
 PROTEIN SEQUENCE OF 16-60.
STRAIN=New Zealand white;
TISSUE=Liver;
DOI=10.1016/0003-9861(77)90558-6; PubMed=197893 [NCBI, ExPASy, EBI, Israel, Japan]
El-Dorry H.A., Chu D.K., Dzugaj A., Botelho L.H., Pontremoli S., Horecker B.L.;
"Primary structure of the S-peptide formed by digestion of rabbit liver fructose 1,6-biphosphatase with subtilisin.";
Arch. Biochem. Biophys. 182:763-773(1977).
[4]
 PROTEIN SEQUENCE OF 19-77.
STRAIN=New Zealand white;
TISSUE=Liver;
DOI=10.1016/0003-9861(77)90463-5; PubMed=202200 [NCBI, ExPASy, EBI, Israel, Japan]
Botelho L.H., El-Dorry H.A., Crivellaro O., Chu D.K., Pontremoli S., Horecker B.L.;
"Digestion of rabbit liver fructose 1,6-bisphosphatase with subtilisin: sites of cleavage and activity of the modified enzyme.";
Arch. Biochem. Biophys. 184:535-545(1977).
[5]
 PRELIMINARY PROTEIN SEQUENCE OF 83-122 AND 135-154, AND ALLOSTERIC REGULATION.
TISSUE=Liver;
DOI=10.1016/0003-9861(82)90473-8; PubMed=6289748 [NCBI, ExPASy, EBI, Israel, Japan]
Suda H., Xu G.-J., Kutny R.M., Natalini P., Pontremoli S., Horecker B.L.;
"Location of lysyl residues at the allosteric site of fructose 1,6-bisphosphatase.";
Arch. Biochem. Biophys. 217:10-14(1982).
[6]
 PROTEIN SEQUENCE OF 248-288 AND 295-337, AND ACTIVE SITE.
TISSUE=Liver;
DOI=10.1016/0003-9861(82)90075-3; PubMed=6284034 [NCBI, ExPASy, EBI, Israel, Japan]
Xu G.J., Natalini P., Suda H., Tsolas O., Dzugaj A., Sun S.C., Pontremoli S., Horecker B.L.;
"Rabbit liver fructose-1,6-bisphosphatase: location of an active site lysyl residue in the COOH-terminal fragment generated by a lysosomal proteinase.";
Arch. Biochem. Biophys. 214:688-694(1982).
[7]
 X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
DOI=10.1107/S0907444998008750; PubMed=10089399 [NCBI, ExPASy, EBI, Israel, Japan]
Weeks C.M., Roszak A.W., Erman M., Kaiser R., Joernvall H., Ghosh D.;
"Structure of rabbit liver fructose 1,6-bisphosphatase at 2.3 A resolution.";
Acta Crystallogr. D 55:93-102(1999).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
PIR S70469; S70469.
3D structure databases
PDB
1BK4; X-ray; 2.30 A; A=1-337.[ExPASy / RCSB / EBI]
PDBsum 1BK4; -.
ModBase P00637.
Ontologies
GO
GO:0042132; Molecular function: fructose 1,6-bisphosphate 1-phosphatase activity (inferred from electronic annotation from EC).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006094; Biological process: gluconeogenesis (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000146; In_FB_phphtase.
Graphical view of domain structure.
PANTHER PTHR11556; In_FB_phphtase; 1.
Pfam PF00316; FBPase; 1.
Pfam graphical view of domain structure.
PRINTS PR00115; FBPHPHTASE.
PR00377; INFBPHPHTASE.
ProDom PD001491; In_FB_phphtase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00124; FBPASE; 1.
BLOCKS P00637.
ProtoNet P00637.
Phylogenomic databases
HOVERGEN P00637; -.
Other
LinkHub P00637; -.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; Allosteric enzyme; Carbohydrate metabolism; Direct protein sequencing; Gluconeogenesis; Hydrolase; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   337  337     Fructose-1,6-bisphosphatase 1. PRO_0000200501
ACT_SITE   274   274         
BINDING   141   141        Allosteric inhibitor (By similarity). 
MOD_RES   1     1        N-acetylalanine. 
CONFLICT   83    83        N -> D (in Ref. 5; AA sequence). 
CONFLICT   88    88        S -> A (in Ref. 5; AA sequence). 
CONFLICT   92    92        C -> S (in Ref. 5; AA sequence). 
CONFLICT   115   116        VC -> SN (in Ref. 5; AA sequence). 
CONFLICT   121   122        DG -> VP (in Ref. 5; AA sequence). 
CONFLICT   267   267        N -> D (in Ref. 6; AA sequence). 
CONFLICT   280   280        E -> Q (in Ref. 6; AA sequence). 
CONFLICT   283   283        Missing (in Ref. 6; AA sequence). 
CONFLICT   300   300        E -> Q (in Ref. 6; AA sequence). 
CONFLICT   307   312        PTDIHQ -> QTPDH (in Ref. 6; AA sequence). 
CONFLICT   326   326        E -> Q (in Ref. 6; AA sequence). 
CONFLICT   329   330        Missing (in Ref. 6; AA sequence). 
HELIX   13    24  12      
HELIX   29    48  20      
TURN   49    52  4      
HELIX   73    87  15      
STRAND   91    96  6      
HELIX   107   109  3      
STRAND   110   121  12      
HELIX   125   128  4      
STRAND   132   140  9      
HELIX   149   152  4      
HELIX   156   158  3      
STRAND   160   177  18      
STRAND   180   187  8      
TURN   188   191  4      
STRAND   192   197  6      
STRAND   207   210  4      
HELIX   213   218  6      
HELIX   221   231  11      
HELIX   248   258  11      
STRAND   261   264  4      
STRAND   274   276  3      
TURN   277   280  4      
HELIX   281   291  11      
STRAND   294   296  3      
STRAND   298   301  4      
HELIX   302   304  3      
STRAND   316   319  4      
HELIX   321   332  12      
TURN   333   335  3      
Sequence information
Length: 337 AA [This is the length of the unprocessed precursor] Molecular weight: 36447 Da [This is the MW of the unprocessed precursor] CRC64: 72FC502C43B75151 [This is a checksum on the sequence] 
        10         20         30         40         50         60 
ADKAPFDTDI STMTRFVMEE GRKAGGTGEM TQLLNSLCTA VKAISTAVRK AGIAHLYGIA 

        70         80         90        100        110        120 
GSTNVTGDQV KKLDVLSNDL VMNMLKSSFA TCVLVSEEDK NAIIVEPEKR GKYVVCFDPL 

       130        140        150        160        170        180 
DGSSNIDCLV SIGTIFGIYR KKSTDEPSTK DALQPGRNLV AAGYALYGSA TMLVLAGGSG 

       190        200        210        220        230        240 
VNSFMLDPAI GEFILVDKNV KIKKKGNIYS LNEGYAKDFD PAVTEYIQKK KFPPDNSSPY 

       250        260        270        280        290        300 
GARYVGSMVA DVHRTLVYGG IFLYPANKKS PDGKLRLLYE CNPMAFIMEK AGGMATTGKE 

       310        320        330 
AILDIVPTDI HQRAPVILGS PDDVQEFLEI YKKHAVK
P00637 in FASTA format

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