ACL_RS05400

Uniprot: A9NH72
Description: 6-phosphofructokinase
EC number: 2.7.1.90
Annotation score: 4 out of 5
Miscellaneous [CC]:
Protein existence: Inferred from homology
Catalytic activity: CATALYTIC ACTIVITY: Diphosphate + D-fructose 6-phosphate = phosphate + D-fructose 1,6-bisphosphate. {ECO:0000256|HAMAP-Rule:MF_01978}.
Cofactor: COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-Rule:MF_01978};
Enzyme regulation: ENZYME REGULATION: Non-allosteric. {ECO:0000256|HAMAP-Rule:MF_01978}.
Function [CC]: FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions. {ECO:0000256|HAMAP-Rule:MF_01978}.
Pathway: PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. {ECO:0000256|HAMAP-Rule:MF_01978}.
Active site: ACT_SITE 145 145 Proton acceptor. {ECO:0000256|HAMAP-Rule:MF_01978}.
Binding site: BINDING 15 15 Diphosphate; via amide nitrogen. {ECO:0000256|HAMAP-Rule:MF_01978}.; BINDING 245 245 Substrate. {ECO:0000256|HAMAP-Rule:MF_01978}.
Calcium binding:
DNA binding:
Metal binding: METAL 115 115 Magnesium; catalytic. {ECO:0000256|HAMAP-Rule:MF_01978}.
Nucleotide binding:
Site: SITE 116 116 Important for catalytic activity and substrate specificity; stabilizes the transition state when the phosphoryl donor is PPi; prevents ATP from binding by mimicking the alpha-phosphate group of ATP. {ECO:0000256|HAMAP-Rule:MF_01978}.; SITE 142 142 Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi. {ECO:0000256|HAMAP-Rule:MF_01978}.
Gene names (primary): pfk2
Gene names (synonym): pfp
Mass: 45,627
Subunit structure [CC]: SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01978}.
Gene ontology (GO): cytoplasm [GO:0005737]; 6-phosphofructokinase activity [GO:0003872]; diphosphate-fructose-6-phosphate 1-phosphotransferase activity [GO:0047334]; metal ion binding [GO:0046872]; fructose 6-phosphate metabolic process [GO:0006002]
Gene ontology IDs: GO:0003872; GO:0005737; GO:0006002; GO:0046872; GO:0047334
Chain:
Signal peptide:
Domain [CC]:
Sequence similarities: SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. PPi-dependent PFK group II subfamily. Clade "B2" sub-subfamily. {ECO:0000256|HAMAP-Rule:MF_01978}.
Protein families: Phosphofructokinase type A (PFKA) family, PPi-dependent PFK group II subfamily, Clade "B2" sub-subfamily
Coiled coil:
Domain [FT]: DOMAIN 12 291 PFK. {ECO:0000259|Pfam:PF00365}.
Motif:
Region: REGION 143 145 Substrate binding. {ECO:0000256|HAMAP-Rule:MF_01978}.; REGION 189 191 Substrate binding. {ECO:0000256|HAMAP-Rule:MF_01978}.
EMBL: CP000896
ProteinModelPortal: A9NH72
MEROPS:
EnsemblBacteria KO: ABX81702
UniPathway: K00850
CDD:
Gene3D:
HAMAP:
InterPro: MF_01978
PANTHER: IPR022953;IPR000023;IPR011404
PIRSF:
PRINTS: PIRSF036483
PROSITE: PR00476
Pfam:
ProDom: PF00365
SMART:
SUPFAM:
TIGRFAMs: SSF53784

1128969-1130214(+)

>nucleotide sequence
ATGAAAAAATTAGTTGGTGCTGCACTCTTAGGACAATCTGGAGGTCCAACCTCAGTGATT
AACGCCTCAGCAGCAGGTGTATTTTTAGAGAGTTTAAAGCATGATGAGATTACAGAAATC
TATGGTGCTCAACACGGTATCAAAGGTATCTTAGATGAAAACTTCTATGATATTAGAAAA
GAAGATGTTGAAGAATTAGAAAGATTAAAGTATACTCCATCATCTGCAATTGGTTCAGTA
AGATACAAATTAAAAGATTACAAAAAAGATCCAACAGACTATAATAAATTATTAGAAATC
TTTAAAAAATATAACATTCGTTATTTCTTCTACAATGGTGGAAATGACTCAATGGATACA
TGTTTAAAAATTTCTAAATTTATGAAAACAGCTGGTTGGGAAATGCGCGTTGTTGGGGTA
CCTAAAACAATCGATAACGACTTAGCAGGTATCGACCATTCACCTGGATATGGTTCAGCA
GCTAAATACGTTGCAACTTCTATCATGGAATTATACTTAGATGCTACAGTTTATAACACA
CAACAATTCATTATTGTTGAAGTAATGGGTAGAAATGCTGGTTGGTTAACTGCTGCTGCT
GCACTTGCTTCAGTTGGTGGTGTTAAACCAGACTTAATGTATTTACCAGAAACTCCATTT
GATATGGACAAATTCTACAACCAAGTAGGTGAATTACTAAAAACTGGTAAATCAGTATTT
GTAGTTGTATCAGAAGGTATTAAAACTGCTGAAGGTAAATACATCCCTGAATATGAAACA
GAAATCGCTCGTGATGCATTCGGACATGCGAACTTAGGTGGTACTGCAAGTGTACTTGCA
AACCACGTAGGTGAAAAATTCGGTGTTAAGACTCGTGCTATCGAATTCTCATTATTACAA
AGATCAGCTGCTCACATTGCATCTCAAACAGATATCAATGAAGCATTCAAAGTTGGACAA
ATTGCTGTTAAAAAAGCAATCAATGGTACAACAAACAAATTTGTAGGTATCCAAAGAGTT
CCTGGGGATAAATACAAAGTGAAGTATCCTCTACTTCCATTAAAGATTGTTGCTAACGCA
GAACGTAAAGTACCATTAGAGTGGATCTTACCTGATGGACAAGGTTTAACTCAAGACTTT
ATTGATTATGCATTACCATTAATCCAAGGTGAAACTAAATTAGAAAAAGTAAACGGGTTA
CCTCGTTTTGCTAAATTAAATAAAGTTTTAGCACCTAAAAAATAA

>protein sequence
MKKLVGAALLGQSGGPTSVINASAAGVFLESLKHDEITEIYGAQHGIKGILDENFYDIRK
EDVEELERLKYTPSSAIGSVRYKLKDYKKDPTDYNKLLEIFKKYNIRYFFYNGGNDSMDT
CLKISKFMKTAGWEMRVVGVPKTIDNDLAGIDHSPGYGSAAKYVATSIMELYLDATVYNT
QQFIIVEVMGRNAGWLTAAAALASVGGVKPDLMYLPETPFDMDKFYNQVGELLKTGKSVF
VVVSEGIKTAEGKYIPEYETEIARDAFGHANLGGTASVLANHVGEKFGVKTRAIEFSLLQ
RSAAHIASQTDINEAFKVGQIAVKKAINGTTNKFVGIQRVPGDKYKVKYPLLPLKIVANA
ERKVPLEWILPDGQGLTQDFIDYALPLIQGETKLEKVNGLPRFAKLNKVLAPKK