PFKA_SPICI
ID PFKA_SPICI Reviewed; 327 AA.
AC P20275;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_00339};
DE Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_00339};
DE Short=Phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_00339};
DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_00339};
DE AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_00339};
GN Name=pfkA {ECO:0000255|HAMAP-Rule:MF_00339};
OS Spiroplasma citri.
OC Bacteria; Tenericutes; Mollicutes; Entomoplasmatales; Spiroplasmataceae;
OC Spiroplasma.
OX NCBI_TaxID=2133;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27556 / NCPPB 2647 / R8A2;
RX PubMed=2139649; DOI=10.1128/jb.172.5.2693-2703.1990;
RA Chevalier C., Saillard C., Bove J.M.;
RT "Organization and nucleotide sequences of the Spiroplasma citri genes for
RT ribosomal protein S2, elongation factor Ts, spiralin, phosphofructokinase,
RT pyruvate kinase, and an unidentified protein.";
RL J. Bacteriol. 172:2693-2703(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27556 / NCPPB 2647 / R8A2;
RX PubMed=9732535; DOI=10.1007/s002849900377;
RA Le Dantec L., Bove J.M., Saillard C.;
RT "Gene organization and transcriptional analysis of the Spiroplasma citri
RT rpsB/tsf/x operon.";
RL Curr. Microbiol. 37:269-273(1998).
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:0000255|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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_00339};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00339};
CC -!- ACTIVITY REGULATION: Allosterically activated by ADP and other
CC diphosphonucleosides, and allosterically inhibited by
CC phosphoenolpyruvate. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00339}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00339}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00339}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF012877; AAB69998.1; -; Genomic_DNA.
DR PIR; E35270; E35270.
DR RefSeq; WP_071937534.1; NZ_CP053304.1.
DR AlphaFoldDB; P20275; -.
DR SMR; P20275; -.
DR STRING; 2133.SCITRI_001128; -.
DR UniPathway; UPA00109; UER00182.
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 CDD; cd00763; Bacterial_PFK; 1.
DR Gene3D; 3.40.50.460; -; 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 Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF000532; ATP_PFK_prok; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 1.
DR TIGRFAMs; TIGR02482; PFKA_ATP; 1.
DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; ATP-binding; Cytoplasm; Glycolysis; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Transferase.
FT CHAIN 1..327
FT /note="ATP-dependent 6-phosphofructokinase"
FT /id="PRO_0000111975"
FT ACT_SITE 128
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT BINDING 12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT BINDING 73..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT BINDING 103..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT BINDING 104
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT BINDING 126..128
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT BINDING 155
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT BINDING 163
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT BINDING 170..172
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT BINDING 186..188
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT BINDING 214..216
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT BINDING 223
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT BINDING 245
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
FT BINDING 251..254
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00339"
SQ SEQUENCE 327 AA; 35197 MW; 19D9D47E176FE2F6 CRC64;
MLKKIGILTS GGDSQGMNAA IAGVIKTAHA KGLETYIIRD GYLGLINNWI EVVDNNFADS
IMLLGGTVIG SARLPEFKDP EVQKKAVDIL KKQEIAALVV IGGDGSYQGA QRLTELGINC
IALPGTIDND ITSSDYTIGF DTAINIVVEA IDRLRDTMQS HNRCSIVEVM GHACGDIALY
AGIAGGADII SINEAALSET EIADRVAMLH QAQKRSVIVV VSEMIYPDVH KLAKLVESKS
GYITRATVLG HTQRGGNPTA MDRYRAFQMA QFAVEQIIAG VGGLAIGNQG DQIIARPIME
ALSIPRSSRK EIWAKFDQLN QNIYQKS
