SMART: Pfam domain FBPase

The domain within your query sequence starts at position 12 and ends at position 334; the E-value for the FBPase domain shown below is 7.3e-145.

STLTRFVMEQGRKAQGTGELTQLLNSLCTAIKAISSAVRQAGIAQLYGIAGSTNVTGDQV
KKLDILSNDLVINMLKSSYATCVLVSEENTNAIIIEPEKRGKYVVCFDPLDGSSNIDCLV
SIGTIFGIYRKKSTDEPSEKDALQPGRDLVAAGYALYGSATMLVLAMDCGVNCFMLDPSI
GEFIMVDRDVKMKKKGNIYSLNEGYAKDFDPAINEYLQRKKFPPDGSAPYGARYVGSMVA
DIHRTLVYGGIFLYPANKKSPSGKLRLLYECNPIAYVMEKAGGLATTGDKDILDIVPTEI
HQKAPVVMGSSEDVQEFLEIYRK

FBPase

PFAM accession number:	PF00316
Interpro abstract (IPR033391):	Fructose-1,6-bisphosphatase (FBPase) is a critical regulatory enzyme in gluconeogenesis that catalyses the removal of 1-phosphate from fructose 1,6-bis-phosphate to form fructose 6-phosphate [ (PUBMED:2159755) (PUBMED:3008716) ]. Five different classes (or types) of FBPases have been identified based on their amino acid sequences, with class I most widely distributed among living organisms [ (PUBMED:16670087) ]. This entry represents the N terminus of the FBPase class 1 family.

PFAM accession number:

PF00316

Interpro abstract (IPR033391):

Fructose-1,6-bisphosphatase (FBPase) is a critical regulatory enzyme in gluconeogenesis that catalyses the removal of 1-phosphate from fructose 1,6-bis-phosphate to form fructose 6-phosphate [ (PUBMED:2159755) (PUBMED:3008716) ]. Five different classes (or types) of FBPases have been identified based on their amino acid sequences, with class I most widely distributed among living organisms [ (PUBMED:16670087) ].

This entry represents the N terminus of the FBPase class 1 family.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry FBPase