PFKA2_KOMPG
ID PFKA2_KOMPG Reviewed; 941 AA.
AC C4QXA5;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 2.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=ATP-dependent 6-phosphofructokinase subunit beta {ECO:0000255|HAMAP-Rule:MF_03184};
DE EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03184};
DE AltName: Full=ATP-dependent 6-phosphofructokinase 2 {ECO:0000255|HAMAP-Rule:MF_03184};
DE Short=ATP-PFK 2 {ECO:0000255|HAMAP-Rule:MF_03184};
DE Short=Phosphofructokinase 2 {ECO:0000255|HAMAP-Rule:MF_03184};
DE AltName: Full=Phosphohexokinase 2 {ECO:0000255|HAMAP-Rule:MF_03184};
GN Name=PFK2; OrderedLocusNames=PAS_chr1-4_0047;
OS Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=644223;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GS115 / ATCC 20864;
RX PubMed=19465926; DOI=10.1038/nbt.1544;
RA De Schutter K., Lin Y.-C., Tiels P., Van Hecke A., Glinka S.,
RA Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT "Genome sequence of the recombinant protein production host Pichia
RT pastoris.";
RL Nat. Biotechnol. 27:561-566(2009).
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_03184}.
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_03184};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03184};
CC -!- ACTIVITY REGULATION: Allosterically activated by ADP, AMP, or fructose
CC 2,6-bisphosphate, and allosterically inhibited by ATP or citrate.
CC {ECO:0000255|HAMAP-Rule:MF_03184}.
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_03184}.
CC -!- SUBUNIT: Heterododecamer of 4 alpha, 4 beta and 4 gamma chains. The
CC gamma chain bridges the N-terminal halves of the alpha and beta
CC subunits (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E'
CC sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03184}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAY67878.1; Type=Frameshift; Evidence={ECO:0000305};
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; FN392319; CAY67878.1; ALT_FRAME; Genomic_DNA.
DR RefSeq; XP_002490159.1; XM_002490114.1.
DR AlphaFoldDB; C4QXA5; -.
DR SMR; C4QXA5; -.
DR STRING; 644223.C4QXA5; -.
DR PRIDE; C4QXA5; -.
DR EnsemblFungi; CAY67878; CAY67878; PAS_chr1-4_0047.
DR GeneID; 8196884; -.
DR KEGG; ppa:PAS_chr1-4_0047; -.
DR eggNOG; KOG2440; Eukaryota.
DR HOGENOM; CLU_011053_0_0_1; -.
DR InParanoid; C4QXA5; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000000314; Chromosome 1.
DR GO; GO:0005945; C:6-phosphofructokinase complex; IEA:EnsemblFungi.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0070095; F:fructose-6-phosphate binding; IEA:EnsemblFungi.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IEA:EnsemblFungi.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:EnsemblFungi.
DR Gene3D; 3.10.180.10; -; 1.
DR Gene3D; 3.40.50.460; -; 2.
DR HAMAP; MF_03184; Phosphofructokinase_I_E; 1.
DR InterPro; IPR009161; 6-Pfructokinase_euk.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
DR InterPro; IPR015912; Phosphofructokinase_CS.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR Pfam; PF00365; PFK; 2.
DR PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 2.
DR SUPFAM; SSF54593; SSF54593; 1.
DR TIGRFAMs; TIGR02478; 6PF1K_euk; 1.
DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
PE 3: Inferred from homology;
KW Allosteric enzyme; ATP-binding; Cytoplasm; Glycolysis; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..941
FT /note="ATP-dependent 6-phosphofructokinase subunit beta"
FT /id="PRO_0000429717"
FT REGION 2..558
FT /note="N-terminal catalytic PFK domain 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT REGION 559..572
FT /note="Interdomain linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT REGION 573..941
FT /note="C-terminal regulatory PFK domain 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT ACT_SITE 333
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 191
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 255..256
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 285..288
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 286
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 331..333
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_label="2"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 368
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_label="1"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 375..377
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_label="2"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 432
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_label="2"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 460
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_label="1"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 466..469
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_label="2"
FT /ligand_note="ligand shared with subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 643
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_label="2"
FT /ligand_note="allosteric activator; ligand shared with
FT subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 701..705
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_label="2"
FT /ligand_note="allosteric activator; ligand shared with
FT subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 739
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_label="1"
FT /ligand_note="allosteric activator; ligand shared with
FT subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 746..748
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_label="2"
FT /ligand_note="allosteric activator; ligand shared with
FT subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 806
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_label="2"
FT /ligand_note="allosteric activator; ligand shared with
FT subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 832
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_label="1"
FT /ligand_note="allosteric activator; ligand shared with
FT subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 838..841
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_label="2"
FT /ligand_note="allosteric activator; ligand shared with
FT subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 918
FT /ligand="beta-D-fructose 2,6-bisphosphate"
FT /ligand_id="ChEBI:CHEBI:58579"
FT /ligand_label="2"
FT /ligand_note="allosteric activator; ligand shared with
FT subunit alpha"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
SQ SEQUENCE 941 AA; 103753 MW; 4AF148B3EF83096D CRC64;
MPDASLFNGT SFITLFAPNI SLFQASIDFY TDRLGFAIKE TSNQKLVWLQ LEEDSNNVSI
QLLLDPEHAA SVSQIDQNIR NLTRSLYRKD WRSIQSNIAF KSSSLSKLVK LLKDGGHPVQ
QSPNEISPFE VYTLDPLGSL IGFSGFKNPF AVNERSLLPK VSEEKAYRTE DDSEKLFTPI
RKTIGVMTSG GDSPGMNPFV RAVVRAGIYK GCKVFCIHEG YEGLVRGGEK YIKETQWHDV
RGWLVEGGTN IGTARCKEFR ERSGRLKACK NMIDMGIDAL IVCGGDGSLT GADRFRSEWP
SLIEELLQTE RISQQQFETY QNLNICGAVG SIDNDMSSTD ATIGAFSSLD RICRAIDYID
ATANSHSRAF IVEVMGRHCG WLGLLAGLAT SADYILIPEK PASSREWQDQ MCDIVSKHRA
RGKRKTIVIV AEGAISNDLS PISCDQVKDV LVNRLGLDTR VTTLGHVQRG GTAVAFDRIY
ATLQGVEAVN AVLECNADTP SPMIAIKEDQ ITRVPLVDAV ELTQQVAKSI ESRNFKRAIS
LRDSEFVEHM KNFISTNSAD HVPPSLPLEK RKKVAIINVG APAGGMNSAV YSMATYCMSR
GHVPYAIHNG FSGLARHESV RSINWLDIEG WGSLGGSEIG TNRTLPNDAD IGMIAYFFEK
YGFDGLILVG GFEAFISLHQ LERARINYPS LRIPLVLIPA TISNNVPGTE YSLGSDTCLN
SFMEYCDVIK QSAAATRNRV FVVEVQGGNS GYIATHAQLA CGAQISYVPE EGISLAQLEM
DINSLKESFA NDQGKTKSGR LILKSENASK VLTTEVISTI IDDEASGRFD SKTAIPGHVQ
QGGIPSPMDR VRASRFAIRA VSFIEKHSDK CQAFKNSISF RQTDEITSTA VVLGIHKSQL
RFTPIRQLYD FESDVPRRMR KNIFWSNVRE ISDMLSGRTS L
