ACL_RS05395

Uniprot: A9NH71
Description: 6-phosphofructokinase
EC number: 2.7.1.11
Annotation score: 4 out of 5
Miscellaneous [CC]:
Protein existence: Inferred from homology
Catalytic activity: CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. {ECO:0000256|HAMAP-Rule:MF_00339, ECO:0000256|SAAS:SAAS00197186}.
Cofactor: COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-Rule:MF_00339, ECO:0000256|SAAS:SAAS00610220};
Enzyme regulation: ENZYME REGULATION: Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate. {ECO:0000256|HAMAP-Rule:MF_00339}.
Function [CC]: FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis. {ECO:0000256|HAMAP-Rule:MF_00339, ECO:0000256|SAAS:SAAS00197172}.
Pathway: PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. {ECO:0000256|HAMAP-Rule:MF_00339, ECO:0000256|SAAS:SAAS00054603}.
Active site: ACT_SITE 126 126 Proton acceptor. {ECO:0000256|HAMAP-Rule:MF_00339}.
Binding site: BINDING 10 10 ATP; via amide nitrogen. {ECO:0000256|HAMAP-Rule:MF_00339}.; BINDING 153 153 Allosteric activator ADP. {ECO:0000256|HAMAP-Rule:MF_00339}.; BINDING 161 161 Substrate; shared with dimeric partner. {ECO:0000256|HAMAP-Rule:MF_00339}.; BINDING 221 221 Substrate. {ECO:0000256|HAMAP-Rule:MF_00339}.; BINDING 242 242 Substrate; shared with dimeric partner. {ECO:0000256|HAMAP-Rule:MF_00339}.
Calcium binding:
DNA binding:
Metal binding: METAL 102 102 Magnesium; catalytic. {ECO:0000256|HAMAP-Rule:MF_00339}.
Nucleotide binding: NP_BIND 71 72 ATP. {ECO:0000256|HAMAP-Rule:MF_00339}.; NP_BIND 101 104 ATP. {ECO:0000256|HAMAP-Rule:MF_00339}.
Site:
Gene names (primary): pfk1
Gene names (synonym): pfkA
Mass: 34,104
Subunit structure [CC]: SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00339, ECO:0000256|SAAS:SAAS00557934}.
Gene ontology (GO): cytoplasm [GO:0005737]; 6-phosphofructokinase activity [GO:0003872]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; fructose 6-phosphate metabolic process [GO:0006002]
Gene ontology IDs: GO:0003872; GO:0005524; GO:0005737; GO:0006002; GO:0046872
Chain:
Signal peptide:
Domain [CC]:
Sequence similarities: SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade "B1" sub-subfamily. {ECO:0000256|HAMAP-Rule:MF_00339, ECO:0000256|SAAS:SAAS00541548}.
Protein families: Phosphofructokinase type A (PFKA) family, ATP-dependent PFK group I subfamily, Prokaryotic clade "B1" sub-subfamily
Coiled coil:
Domain [FT]: DOMAIN 2 274 PFK. {ECO:0000259|Pfam:PF00365}.
Motif:
Region: REGION 20 24 Allosteric activator ADP binding; shared with dimeric partner. {ECO:0000256|HAMAP-Rule:MF_00339}.; REGION 124 126 Substrate binding. {ECO:0000256|HAMAP-Rule:MF_00339}.; REGION 168 170 Substrate binding. {ECO:0000256|HAMAP-Rule:MF_00339}.; REGION 184 186 Allosteric activator ADP binding. {ECO:0000256|HAMAP-Rule:MF_00339}.; REGION 248 251 Substrate binding. {ECO:0000256|HAMAP-Rule:MF_00339}.
EMBL: CP000896
ProteinModelPortal: A9NH71
MEROPS:
EnsemblBacteria KO: ABX81701
UniPathway: K00850
CDD:
Gene3D:
HAMAP:
InterPro: MF_00339
PANTHER: IPR022953;IPR012003;IPR012828;IPR000023
PIRSF:
PRINTS: PIRSF000532
PROSITE: PR00476
Pfam:
ProDom: PF00365
SMART:
SUPFAM:
TIGRFAMs: SSF53784

1127745-1128696(-)

>nucleotide sequence
TTATCTTAATTTCTTAATGAGATCATATAGCTCAACGCGTTCTTTTGGATGGTTGATGAT
ATCAGATAATGGTGATGTTACTAGTTTATCATCTTTTATACCAACACATTGTCCACTCAC
ACCTTTGGCAAGCATTTCGACTGCAAATGCACCCATACGTGATGCTAAGATACGGTCTTC
AGCAATTGGTGTTCCACCTCTTTGGATATAACCAAGTACTGTTGCTCGTGAACTAAATCC
AGATTTGATTGAGATTTCAGCAGCAAGTTTATGCACATCAAATTGTTGTTCAGTGACAAC
AATGATGGCATGGCGTCTGCCTTCTTCATTATGTTTTTTTAATGTTGAAATTAACTTATC
TTTATTAATTGGGTTTTCTGGTGTAATAATGAACTCAGCACCACCACAGATACCTGCATA
TAATGCTAAATCACCTGATGTTCTACCCATAACTTCAATAATACTACAACGTCTATGTGA
CGATGATGTATCTCTTAGTTTATCTATTGCTTCTACAATTGTATTTAATGCAGTATGGAA
TCCGATTGTATAATCTGTTCCATAAACGTCATTATCAATTGTTCCAGGAATAGCTATGGT
TTGGAATTCTAGTTCATGGAGTGCTTGAGCACCTCTGTAACTACCATCACCACCAATAAC
GATTAAAGCATCAATACCACGATTACGTAGATTATCGATTGCTACCATTTGAACTGGTAC
TTCTTTAAACTCAGATACTCTTGCAGTACCCAGTTTTGTACCACCAATGCTTAACATACC
TGAAACATCTTTGGCAGCTAGCGGTATAAAACGATCTTCTAAAAGACCTCTATAACCATC
CATAATACCAAACATCTCATGACCTTCTGCAATACCTGTACGCACAATTGCACGAATTGC
TGCGTTCATTCCAGGTGCATCGCCGCCAGAAGTTAAAACTGCTATTTTCAT

>protein sequence
MKIAVLTSGGDAPGMNAAIRAIVRTGIAEGHEMFGIMDGYRGLLEDRFIPLAAKDVSGML
SIGGTKLGTARVSEFKEVPVQMVAIDNLRNRGIDALIVIGGDGSYRGAQALHELEFQTIA
IPGTIDNDVYGTDYTIGFHTALNTIVEAIDKLRDTSSSHRRCSIIEVMGRTSGDLALYAG
ICGGAEFIITPENPINKDKLISTLKKHNEEGRRHAIIVVTEQQFDVHKLAAEISIKSGFS
SRATVLGYIQRGGTPIAEDRILASRMGAFAVEMLAKGVSGQCVGIKDDKLVTSPLSDIIN
HPKERVELYDLIKKLR