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ATP-dependent 6-phosphofructokinase (ATP-PFK) (Phosphofructokinase) (EC 2.7.1.11) (Phosphohexokinase)

 V7CAY4_PHAVU            Unreviewed;       460 AA.
V7CAY4;
19-FEB-2014, integrated into UniProtKB/TrEMBL.
19-FEB-2014, sequence version 1.
25-OCT-2017, entry version 22.
RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_03186};
Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_03186};
Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_03186};
EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_03186};
AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_03186};
Name=PFK {ECO:0000256|HAMAP-Rule:MF_03186};
ORFNames=PHAVU_003G088700g {ECO:0000313|EMBL:ESW26066.1};
Phaseolus vulgaris (Kidney bean) (French bean).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae;
Phaseoleae; Phaseolus.
NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW26066.1, ECO:0000313|Proteomes:UP000000226};
[1] {ECO:0000313|EMBL:ESW26066.1, ECO:0000313|Proteomes:UP000000226}
NUCLEOTIDE SEQUENCE.
Schmutz J., McClean P., Shu S., Cregan P., Rokhsar D., Jackson S.;
Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
-!- 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_03186}.
-!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D-
fructose 1,6-bisphosphate. {ECO:0000256|HAMAP-Rule:MF_03186}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000256|HAMAP-Rule:MF_03186};
-!- ENZYME REGULATION: Allosterically activated by AMP.
{ECO:0000256|HAMAP-Rule:MF_03186}.
-!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
phosphate and glycerone phosphate from D-glucose: step 3/4.
{ECO:0000256|HAMAP-Rule:MF_03186}.
-!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_03186}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03186}.
-!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
family. PPi-dependent PFK group II subfamily. Atypical ATP-
dependent clade "X" sub-subfamily. {ECO:0000256|HAMAP-
Rule:MF_03186}.
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EMBL; CM002290; ESW26066.1; -; Genomic_DNA.
RefSeq; XP_007154072.1; XM_007154010.1.
GeneID; 18634335; -.
KEGG; pvu:PHAVU_003G088700g; -.
KO; K00850; -.
PhylomeDB; V7CAY4; -.
UniPathway; UPA00109; UER00182.
Proteomes; UP000000226; Chromosome 3.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
HAMAP; MF_01981; Phosphofructokinase_II_X; 1.
InterPro; IPR022953; ATP_PFK.
InterPro; IPR000023; Phosphofructokinase_dom.
InterPro; IPR035966; PKF_sf.
InterPro; IPR012004; PyroP-dep_PFK_TP0108.
Pfam; PF00365; PFK; 1.
PIRSF; PIRSF000534; PPi_PFK_TP0108; 1.
PRINTS; PR00476; PHFRCTKINASE.
SUPFAM; SSF53784; SSF53784; 1.
3: Inferred from homology;
Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_03186};
ATP-binding {ECO:0000256|HAMAP-Rule:MF_03186};
Complete proteome {ECO:0000313|Proteomes:UP000000226};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03186};
Glycolysis {ECO:0000256|HAMAP-Rule:MF_03186};
Kinase {ECO:0000256|HAMAP-Rule:MF_03186};
Magnesium {ECO:0000256|HAMAP-Rule:MF_03186};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_03186};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03186};
Reference proteome {ECO:0000313|Proteomes:UP000000226};
Transferase {ECO:0000256|HAMAP-Rule:MF_03186}.
DOMAIN 97 405 PFK. {ECO:0000259|Pfam:PF00365}.
NP_BIND 168 169 ATP. {ECO:0000256|HAMAP-Rule:MF_03186}.
NP_BIND 193 196 ATP. {ECO:0000256|HAMAP-Rule:MF_03186}.
REGION 222 224 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_03186}.
REGION 267 269 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_03186}.
REGION 381 384 Substrate binding. {ECO:0000256|HAMAP-
Rule:MF_03186}.
ACT_SITE 224 224 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_03186}.
METAL 194 194 Magnesium; catalytic. {ECO:0000256|HAMAP-
Rule:MF_03186}.
BINDING 105 105 ATP; via amide nitrogen.
{ECO:0000256|HAMAP-Rule:MF_03186}.
BINDING 323 323 Substrate. {ECO:0000256|HAMAP-
Rule:MF_03186}.
SITE 195 195 Important for substrate specificity;
cannot use PPi as phosphoryl donor.
{ECO:0000256|HAMAP-Rule:MF_03186}.
SEQUENCE 460 AA; 51359 MW; 90A8AA732CAC894D CRC64;
MAECSNSESD ISKLFKPIYL KEVPCLSHYV PNLQTRPNPL DHNPYFHTRQ LQQHGFYLTQ
SDLVLRQIEN DPSPLPRFAY HRAGPRKNIR FDPSHVRVAI VTCGGLCPGL NTVVRELVMG
LWHLYGVRHI LGITAGYRGF YSSEPLPLNP KLVHHWHNVG GTLLQTSRGG FDLKDIVDAI
QNHAFNQVYI IGGDGTMRGA VKIFDEIRRR KLEVAVVGIP KTVDNDVGII DKSFGFQTAV
EMAQEAISAA HVEAESAVNG IGLVKLMGRS TGHIALHATL SSRDVDCCLI PEIDFYLEGK
GGLFEFLGQR LKENGHAVLV VAEGAGQDII PRTDSQKEER DESGNLVFLD VGVWLKSELK
NWWARDHPHE LFTVKYIDPT YMIRAVHANA TDNLYCTLLA HSAIHGVMAG YTGFVTGPIN
GNYAYIPLED VAQANNPVDT KDHKWSWVRS VTNQPDFVRR


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