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Reviewed, UniProtKB/Swiss-Prot Q91348 (F26L_CHICK)

Last modified September 22, 2009. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    6PF-2-K/Fru-2,6-P2ASE liver isozyme
Including the following 2 domains:
    1- Recommended name:
            6-phosphofructo-2-kinase
              EC=2.7.1.105
    2- Recommended name:
            Fructose-2,6-bisphosphatase
              EC=3.1.3.46
OrganismGallus gallus (Chicken)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

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Protein attributes

Sequence length470 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Synthesis and degradation of fructose 2,6-bisphosphate.

Catalytic activity

Beta-D-fructose 2,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.

ATP + D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate.

Enzyme regulation

Phosphorylation results in inhibition of the kinase activity By similarity.

Subunit structure

Homodimer By similarity.

Tissue specificity

Liver.

Sequence similarities

In the C-terminal section; belongs to the phosphoglycerate mutase family.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 4704706PF-2-K/Fru-2,6-P2ASE liver isozyme
PRO_0000179972

Regions

Nucleotide binding47 – 548ATP Potential
Region1 – 2492496-phosphofructo-2-kinase
Region250 – 469220Fructose-2,6-bisphosphatase

Sites

Active site1301 Potential
Active site1601 Potential
Active site2581Tele-phosphohistidine intermediate
Active site3271 Potential
Active site3921Proton donor By similarity
Binding site1041Fructose-6-phosphate By similarity
Binding site1951Fructose-6-phosphate By similarity

Amino acid modifications

Modified residue311Phosphoserine; by PKA By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q91348-1 [UniParc].

Last modified January 16, 2004. Version 2.
Checksum: DCDBFB5D392033F8

FASTA47054,404
        10         20         30         40         50         60 
MAAVASGQLT QNPLQKVWVP LSLHRLRRRG STVPQFTNCP TMVILVGLRR PGKTYISRKL 

        70         80         90        100        110        120 
TRYLNWIGMP TRVFNVGQYR REAVQSYKNY EFFRHDNEEA MQIRRQCALA ALQDVRTYLS 

       130        140        150        160        170        180 
SEEGQVAVFD ATNTTRERRA LIMQFARENG YKVLFVESIC DDPAIIEENI KQVKLSSPDY 

       190        200        210        220        230        240 
KGCTPEEAVA DFLQRIECYK ATYEPLDEQL DSGLSYIKIF DVGVRYLANR VQGHVQSRTV 

       250        260        270        280        290        300 
YYLMNTHVTP RAIYLSRHGE SQLNLKGRIG GDAGLSTRGR QYAQALAEFI RSQSIRELKV 

       310        320        330        340        350        360 
WTSHMKRTIE TAEALGVPYE QWKALNEIDA GVCEEMTYEE IQERYPEEFA LRDQDKYRYR 

       370        380        390        400        410        420 
YPKGESYEDL VQRLEPVIME LERQENVLVI CHQAVMRCLL AYFLDKSSEE LPYLRCPLHT 

       430        440        450        460        470 
VLKLTPVAYG CEVESIFLNV EAVNTHRERP QNVDISRPPA EALVTVPEHY

« Hide

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References

[1]"Isolation of a cDNA for chicken liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase."
Li L., Lange A.J., Pilkis S.J.
Biochem. Biophys. Res. Commun. 190:397-405(1993) [PubMed: 7916593] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]Yang Q.H., Dong M.Q., Li L.
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 184-186 AND 365-366.

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Cross-references

Sequence databases

AF146428 mRNA. Translation: AAD37721.1.
IPIIPI00601795.
PIRJC1470.
RefSeqNP_001025755.1.
UniGeneGga.17198

3D structure databases

HSSPHSSP built from PDB template 1C80 based on UniProtKB P07953.
SMRQ91348. Positions 39-469.
ModBaseSearch...

Genome annotation databases

GeneID415906.
KEGGgga:415906.

Organism-specific databases

CTD415906.

Phylogenomic databases

HOVERGENQ91348.

Enzyme and pathway databases

BRENDA2.7.1.105. 4.
3.1.3.46. 4.

Family and domain databases

InterProIPR003094. 6Pfruct_kin.
IPR013079. 6Phosfructo_kin.
IPR016260. Bifunct_6PFK/fruc_bisP_Ptase.
IPR001345. PG/BPGM_mutase_AC.
IPR013078. PG_mutase.
[Graphical view]
PANTHERPTHR10606. 6Pfruct_kin. 1 hit.
PfamPF01591. 6PF2K. 1 hit.
PF00300. PGAM. 1 hit.
[Graphical view]
PIRSFPIRSF000709. 6PFK_2-Ptase. 1 hit.
PRINTSPR00991. 6PFRUCTKNASE.
PROSITEPS00175. PG_MUTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameF26L_CHICK
AccessionPrimary (citable) accession number: Q91348
Secondary accession number(s): Q9PWA7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 16, 2004
Last modified: September 22, 2009
This is version 69 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents