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Database: UniProt/TrEMBL
Entry: A0A142EQH9_9BACT
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ID   A0A142EQH9_9BACT        Unreviewed;       335 AA.
AC   A0A142EQH9;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_00339};
DE            Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_00339};
DE            Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_00339};
DE            EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_00339};
DE   AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_00339};
GN   Name=pfkA {ECO:0000256|HAMAP-Rule:MF_00339};
GN   ORFNames=AO498_13130 {ECO:0000313|EMBL:AMQ57384.1};
OS   Algoriphagus sanaruensis.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Algoriphagus.
OX   NCBI_TaxID=1727163 {ECO:0000313|EMBL:AMQ57384.1, ECO:0000313|Proteomes:UP000073816};
RN   [1] {ECO:0000313|Proteomes:UP000073816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M8-2 {ECO:0000313|Proteomes:UP000073816};
RA   Shintani M.;
RT   "Complete sequence of Algoriphagus sp. M8-2.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AMQ57384.1, ECO:0000313|Proteomes:UP000073816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M8-2 {ECO:0000313|EMBL:AMQ57384.1,
RC   ECO:0000313|Proteomes:UP000073816};
RX   PubMed=27174266;
RA   Muraguchi Y., Kushimoto K., Ohtsubo Y., Suzuki T., Dohra H., Kimbara K.,
RA   Shintani M.;
RT   "Complete Genome Sequence of Algoriphagus sp. Strain M8-2, Isolated from a
RT   Brackish Lake.";
RL   Genome Announc. 4:0-0(2016).
CC   -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to
CC       fructose 1,6-bisphosphate by ATP, the first committing step of
CC       glycolysis. {ECO:0000256|HAMAP-Rule:MF_00339}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-
CC         bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634,
CC         ChEBI:CHEBI:456216; EC=2.7.1.11;
CC         Evidence={ECO:0000256|ARBA:ARBA00000432, ECO:0000256|HAMAP-
CC         Rule:MF_00339};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|HAMAP-Rule:MF_00339};
CC   -!- ACTIVITY REGULATION: Allosterically activated by ADP and other
CC       diphosphonucleosides, and allosterically inhibited by
CC       phosphoenolpyruvate. {ECO:0000256|HAMAP-Rule:MF_00339}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 3/4.
CC       {ECO:0000256|ARBA:ARBA00004679, ECO:0000256|HAMAP-Rule:MF_00339}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00339}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00339}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC       ATP-dependent PFK group I subfamily. Prokaryotic clade 'B1' sub-
CC       subfamily. {ECO:0000256|HAMAP-Rule:MF_00339}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00339}.
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DR   EMBL; CP012836; AMQ57384.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A142EQH9; -.
DR   STRING; 1727163.AO498_13130; -.
DR   KEGG; alm:AO498_13130; -.
DR   PATRIC; fig|1727163.4.peg.2741; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000073816; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.450; -; 1.
DR   Gene3D; 3.40.50.460; Phosphofructokinase domain; 1.
DR   HAMAP; MF_00339; Phosphofructokinase_I_B1; 1.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR012003; ATP_PFK_prok-type.
DR   InterPro; IPR012828; PFKA_ATP_prok.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR035966; PKF_sf.
DR   NCBIfam; TIGR02482; PFKA_ATP; 1.
DR   PANTHER; PTHR13697:SF4; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE, MUSCLE TYPE; 1.
DR   PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1.
DR   Pfam; PF00365; PFK; 1.
DR   PIRSF; PIRSF000532; ATP_PFK_prok; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; Phosphofructokinase; 1.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
PE   3: Inferred from homology;
KW   Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533, ECO:0000256|HAMAP-
KW   Rule:MF_00339};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00339};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00339};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW   Rule:MF_00339};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00339};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00339};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00339};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00339}; Reference proteome {ECO:0000313|Proteomes:UP000073816};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00339}.
FT   DOMAIN          14..290
FT                   /note="Phosphofructokinase"
FT                   /evidence="ECO:0000259|Pfam:PF00365"
FT   ACT_SITE        139
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   BINDING         22
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   BINDING         32..36
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   BINDING         83..84
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   BINDING         113..116
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   BINDING         114
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   BINDING         137..139
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   BINDING         166
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   BINDING         174
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   BINDING         181..183
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   BINDING         197..199
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   BINDING         222
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   BINDING         224..226
FT                   /ligand="ADP"
FT                   /ligand_id="ChEBI:CHEBI:456216"
FT                   /ligand_note="allosteric activator; ligand shared between
FT                   dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   BINDING         233
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   BINDING         259
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
FT   BINDING         265..268
FT                   /ligand="substrate"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /note="in other chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00339"
SQ   SEQUENCE   335 AA;  35723 MW;  A42FEDAB8D902A3E CRC64;
     MAIFGALKPK PMKKIAVFTS GGDSPGMNAC IRAAVRTGIY KGLDVFGIYR GYEGMIEGDI
     KRLHSHSVSN IIQRGGTVLK SARSMEFKTP EGRKKAFENL SAHGIEGLVA IGGDGTFTGA
     KVFYEEFGIP TVGCPGTIDN DIYGTDYTIG FDTAVNTALE AIDKIRDTAA AHDRIFFIEV
     MGRDAGFIAV ESGIGGGAEF VMVPETQTDL DAVVKSLKKL RKTKTSSIIV VAEGDDLGSA
     DVIMKLVKEK IQDPSKEFKV TTLGHIQRGG NPTARDRVLG SRCGMAAVEG LLSGKTNCMA
     GIMNEQVVYT PFADCIGLPK PLNPDHLALI DILSI
//
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