SPM_000070

Uniprot: A0A037UPK1
Description: 6-phosphofructokinase
EC number: 2.7.1.11
Annotation score: 3 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:SAAS00609123};
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:SAAS00041065}.
Active site: ACT_SITE 128 128 Proton acceptor. {ECO:0000256|HAMAP-Rule:MF_00339}.
Binding site: BINDING 12 12 ATP; via amide nitrogen. {ECO:0000256|HAMAP-Rule:MF_00339}.; BINDING 155 155 Allosteric activator ADP. {ECO:0000256|HAMAP-Rule:MF_00339}.; BINDING 163 163 Substrate; shared with dimeric partner. {ECO:0000256|HAMAP-Rule:MF_00339}.; BINDING 223 223 Substrate. {ECO:0000256|HAMAP-Rule:MF_00339}.; BINDING 245 245 Substrate; shared with dimeric partner. {ECO:0000256|HAMAP-Rule:MF_00339}.
Calcium binding:
DNA binding:
Metal binding: METAL 104 104 Magnesium; catalytic. {ECO:0000256|HAMAP-Rule:MF_00339}.
Nucleotide binding: NP_BIND 73 74 ATP. {ECO:0000256|HAMAP-Rule:MF_00339}.; NP_BIND 103 106 ATP. {ECO:0000256|HAMAP-Rule:MF_00339}.
Site:
Gene names (primary): pfkA
Gene names (synonym):
Mass: 35,258
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 4 276 PFK. {ECO:0000259|Pfam:PF00365}.
Motif:
Region: REGION 126 128 Substrate binding. {ECO:0000256|HAMAP-Rule:MF_00339}.; REGION 170 172 Substrate binding. {ECO:0000256|HAMAP-Rule:MF_00339}.; REGION 186 188 Allosteric activator ADP binding. {ECO:0000256|HAMAP-Rule:MF_00339}.; REGION 214 216 Allosteric activator ADP binding. {ECO:0000256|HAMAP-Rule:MF_00339}.; REGION 251 254 Substrate binding. {ECO:0000256|HAMAP-Rule:MF_00339}.
EMBL: AGBZ02000001
ProteinModelPortal:
MEROPS:
EnsemblBacteria KO: KAI92516
UniPathway:
CDD:
Gene3D:
HAMAP:
InterPro: MF_00339
PANTHER: IPR022953;IPR012003;IPR012828;IPR015912;IPR000023
PIRSF:
PRINTS: PIRSF000532
PROSITE: PR00476
Pfam: PS00433
ProDom: PF00365
SMART:
SUPFAM:
TIGRFAMs: SSF53784

11979-12963(-)

>nucleotide sequence
TTATGATTTTTGATAAATATTCTGATTTAATTGATCAAATTTAGCTCAAATTTCTTTCCG
TGATGAACGCGGAATACTTAATGCTTCCATAATTGGACGAGCAATAATTTGATCACCTTG
ATTGCCAATTGCTAAACCACCTACGCCTGCAATAATTTGTTCAACAGCAAATTGTGCCAT
TTGAAAAGCACGATAACGGTCCATGGCCGTTGGATTACCACCCCGTTGAGTGTGTCCTAA
AACTGTTGCACGAGTAATGTAACCACTTTTACTTTCAACTAATTTTGCTAATTTATGCAC
ATCGGGATAAATCATTTCACTAACAACAACAATGACACTTCGCTTTTGTGCTTGATGTAA
CATCGCAACCCGATTAGCAATTTCTGTTTCAGATAAAGCAGCTTCATTAATTGAAATAAT
ATCTGCTCCACCAGCAATCCCAGCGTATAAAGCAATATCACCGCAAGCATGACCCATTAC
TTCAACAATTGAACAACGATTATGTGATTGCATTGTATCACGCAAGCGGTCAATTGCTTC
AACAACAATATTAATTGCAGTATCAAACCCAATCGTATAATCTGATGAAGTGATATCATT
ATCAATTGTTCCCGGTAAAGCAATACAATTAATTCCCAACTCTGTTAACCGTTGAGCACC
TTGATAACTACCATCACCACCAATAACTACTAATGCCGCAATTTCTTGCTTTTTTAAAAT
ATCAACAGCTTTTTTTTGTACTTCTGGGTCTTTAAATTCCGGTAAGCGTGCACTTCCAAT
CACAGTTCCCCCTAAACGCATAATACTATCCGCAAAATTATTATCAACAACTTCCATTCA
ATTATTAATTAATCCTAAATAACCATCACGAATAATATATGTTTCTAGTCCTTTTGCATG
TGCTGTTTTAATAACTCCCGCAATTGCAGCATTCATTCCTTGTGAATCACCACCAGATGT
TAAAATTCCAATTTTTTTAAGCAT

>protein sequence
MLKKIGILTSGGDSQGMNAAIAGVIKTAHAKGLETYIIRDGYLGLINNWMEVVDNNFADS
IMRLGGTVIGSARLPEFKDPEVQKKAVDILKKQEIAALVVIGGDGSYQGAQRLTELGINC
IALPGTIDNDITSSDYTIGFDTAINIVVEAIDRLRDTMQSHNRCSIVEVMGHACGDIALY
AGIAGGADIISINEAALSETEIANRVAMLHQAQKRSVIVVVSEMIYPDVHKLAKLVESKS
GYITRATVLGHTQRGGNPTAMDRYRAFQMAQFAVEQIIAGVGGLAIGNQGDQIIARPIME
ALSIPRSSRKEIWAKFDQLNQNIYQKS