PFKA_COREF
ID PFKA_COREF Reviewed; 346 AA.
AC Q8RQN5;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01976};
DE Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_01976};
DE Short=Phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_01976};
DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_01976};
DE AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_01976};
GN Name=pfkA {ECO:0000255|HAMAP-Rule:MF_01976}; Synonyms=pfk;
GN OrderedLocusNames=CE1348;
OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS / NBRC 100395).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196164;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RA Hirano S., Kimura E., Kawahara Y., Sugimoto S.;
RT "pfk of Corynebacterium efficiens.";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX PubMed=12840036; DOI=10.1101/gr.1285603;
RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT "Comparative complete genome sequence analysis of the amino acid
RT replacements responsible for the thermostability of Corynebacterium
RT efficiens.";
RL Genome Res. 13:1572-1579(2003).
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_01976}.
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_01976};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01976};
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_01976}.
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-Rule:MF_01976}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01976}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC Mixed-substrate PFK group III subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_01976}.
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DR EMBL; AB083051; BAB88667.1; -; Genomic_DNA.
DR EMBL; BA000035; BAC18158.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8RQN5; -.
DR SMR; Q8RQN5; -.
DR STRING; 196164.23493187; -.
DR EnsemblBacteria; BAC18158; BAC18158; BAC18158.
DR KEGG; cef:CE1348; -.
DR eggNOG; COG0205; Bacteria.
DR HOGENOM; CLU_020655_0_0_11; -.
DR OMA; KFAVICV; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000001409; 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:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:InterPro.
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; 3.40.50.460; -; 1.
DR HAMAP; MF_01976; Phosphofructokinase_III; 1.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR012003; ATP_PFK_prok-type.
DR InterPro; IPR015912; Phosphofructokinase_CS.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR012829; Phosphofructokinase_III.
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; TIGR02483; PFK_mixed; 1.
DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..346
FT /note="ATP-dependent 6-phosphofructokinase"
FT /id="PRO_0000111947"
FT ACT_SITE 131
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 13
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 76..77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 106..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 107
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 129..131
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 166
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 173..175
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 226
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 270
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT BINDING 276..279
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
FT SITE 108
FT /note="Important for substrate specificity; cannot use PPi
FT as phosphoryl donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01976"
SQ SEQUENCE 346 AA; 37476 MW; 0F233545F77922A7 CRC64;
MGAMRIATLT SGGDCPGLNA VIRGIVRTAS NEFGSTVVGY QDGWEGLLAD RRVQLYDDED
IDRILLRGGT ILGTGRLHPD KFRAGIDQVK ANLADAGIDA LIPIGGEGTL KGAKWLADNG
IPVVGVPKTI DNDVNGTDFT FGFDSAVSVA TDAIDRLHTT AESHNRVMIV EVMGRHVGWI
ALHAGMAGGA HYTVIPEVPF DISEICKRME RRFQMGEKYG IIVVAEGALP KEGTMELREG
EVDQFGHKTF TGIGQQIADE VHRRLGHDVR TTVLGHIQRG GTPTAFDRVL ATRYGVRAAR
ACHEGQFNTV VALKGERIRM ISFDEAVGTL KKVPMERWVT AQAMFG
