PFKA1_KOMPG
ID PFKA1_KOMPG Reviewed; 989 AA.
AC Q92448; C4R0J9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=ATP-dependent 6-phosphofructokinase subunit alpha {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 1 {ECO:0000255|HAMAP-Rule:MF_03184};
DE Short=ATP-PFK 1 {ECO:0000255|HAMAP-Rule:MF_03184};
DE Short=Phosphofructokinase 1 {ECO:0000255|HAMAP-Rule:MF_03184};
DE AltName: Full=Glucose-induced selective autophagy 1 protein;
DE AltName: Full=Phosphohexokinase 1 {ECO:0000255|HAMAP-Rule:MF_03184};
GN Name=PFK1; Synonyms=GSA1; OrderedLocusNames=PAS_chr2-1_0402;
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 [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF ASP-361.
RC STRAIN=GS115 / ATCC 20864;
RX PubMed=9296392; DOI=10.1242/jcs.110.16.1935;
RA Yuan W., Tuttle D.L., Shi Y.J., Ralph G.S., Dunn W.A. Jr.;
RT "Glucose-induced microautophagy in Pichia pastoris requires the alpha-
RT subunit of phosphofructokinase.";
RL J. Cell Sci. 110:1935-1945(1997).
RN [2]
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 (By similarity). Involved in the modulation of glucose-
CC induced microautophagy of peroxisomes independent of its ability to
CC metabolize glucose intermediates. {ECO:0000255|HAMAP-Rule:MF_03184,
CC ECO:0000269|PubMed:9296392}.
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}.
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DR EMBL; U73376; AAB97871.1; -; Genomic_DNA.
DR EMBL; FN392320; CAY69023.1; -; Genomic_DNA.
DR RefSeq; XP_002491303.1; XM_002491258.1.
DR AlphaFoldDB; Q92448; -.
DR SMR; Q92448; -.
DR STRING; 644223.Q92448; -.
DR MoonDB; Q92448; Curated.
DR MoonProt; Q92448; -.
DR EnsemblFungi; CAY69023; CAY69023; PAS_chr2-1_0402.
DR GeneID; 8198870; -.
DR KEGG; ppa:PAS_chr2-1_0402; -.
DR eggNOG; KOG2440; Eukaryota.
DR HOGENOM; CLU_011053_0_0_1; -.
DR OMA; SRYAVKC; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000000314; Chromosome 2.
DR GO; GO:0005945; C:6-phosphofructokinase complex; TAS:CAFA.
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:0071333; P:cellular response to glucose stimulus; IMP:CAFA.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR GO; GO:0061615; P:glycolytic process through fructose-6-phosphate; IMP:CAFA.
DR GO; GO:0000426; P:micropexophagy; IMP:CAFA.
DR GO; GO:0060151; P:peroxisome localization; IMP:CAFA.
DR GO; GO:1901098; P:positive regulation of autophagosome maturation; IMP:CAFA.
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; IPR040712; Pfk_N.
DR InterPro; IPR015912; Phosphofructokinase_CS.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR Pfam; PF00365; PFK; 2.
DR Pfam; PF18468; Pfk_N; 1.
DR PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; SSF53784; 2.
DR TIGRFAMs; TIGR02478; 6PF1K_euk; 1.
DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; ATP-binding; Cytoplasm; Glycolysis; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..989
FT /note="ATP-dependent 6-phosphofructokinase subunit alpha"
FT /id="PRO_0000112042"
FT REGION 1..585
FT /note="N-terminal catalytic PFK domain 1"
FT REGION 586..599
FT /note="Interdomain linker"
FT REGION 600..989
FT /note="C-terminal regulatory PFK domain 2"
FT ACT_SITE 361
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 220
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 283..284
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 313..316
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 314
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 359..361
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_label="1"
FT /ligand_note="ligand shared with subunit beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 396
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_label="2"
FT /ligand_note="ligand shared with subunit beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 403..405
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_label="1"
FT /ligand_note="ligand shared with subunit beta"
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 beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 487
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_label="2"
FT /ligand_note="ligand shared with subunit beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 493..496
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /ligand_label="1"
FT /ligand_note="ligand shared with subunit beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 670
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 beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 727..731
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 beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 765
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 beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 772..774
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 beta"
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 beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 858
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 beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 864..867
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 beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT BINDING 963
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 beta"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184"
FT MUTAGEN 361
FT /note="D->S: Abolishes catalytic activity, but not the
FT ability to modulate glucose-induced microautophagy of
FT peroxisomes."
FT /evidence="ECO:0000269|PubMed:9296392"
FT CONFLICT 178
FT /note="S -> SK (in Ref. 1; AAB97871)"
FT /evidence="ECO:0000305"
FT CONFLICT 570
FT /note="D -> E (in Ref. 1; AAB97871)"
FT /evidence="ECO:0000305"
FT CONFLICT 914
FT /note="Y -> C (in Ref. 1; AAB97871)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 989 AA; 108817 MW; 6708A34ED94C9DD4 CRC64;
MPEPSISALS FTSFVTNDDK LFEETFNFYT KLGFHATRSY VKDNRSDFEL TGISTDSIKE
IWLESFPLSE VVETSAGREL RKPLQESVGY QSEALLGYSP YQSDGVVIKL RLSNHDLQKN
KDLPGEVTFF TASIDKLRAK LIEIGAEIIP SEIDLVEFST KDPMGDVISF SSYPSLSSKK
ITSPDFFLHP KKEVRSQESI VEQVKSEEGK KKIAIITSGG DAPGMNAAVR AVTRAGIFYG
CKVYACYEGY TGLVKGGDML KELQWQDVRG LLSIGGTIIG TARSKEFRER WGRLQACYNM
VSNGIDALVV CGGDGSLTGA DLFRNEWPEL IKELLGEGKI TKEQYETHRN LTIVGLVGSI
DNDMCGTDST IGAYSSLERI IELVDYIDAT AASHSRAFVV EVMGRHCGWL GLMSGIATGA
DYIFIPERPP SETNWKDDLK KVCLRHREKG RRKTTVIVAE GAIDDQLNPI TSEEVKDVLV
EIGLDTRITR LGHVQRGGAP CAFDRFLATV QGVDAVRAVL ESTPAIPSPV ISILENKIVR
QPLVESVAQT KTVSDAIEAK DFDKALKLRD QEFATSYESF LSVSKYDDGS YLVPESSRLN
IAIIHVGAPT SALNPATRVA TLNSLAKGHR VFAIRNGFAG LIRHGAVREL NWIDVEDWHN
TGGSEIGTNR SLPSDDMGTV AYYFQQYKFD GLIIIGGFEA FTALYQLDAA RAQYPIFNIP
MCCLPATVSN NVPGTEYSLG SDTCLNTLSG YCDAVKQSAS ASRRRTFVVE VQGGYSGYLA
SYAGLITGAL AVYTPENPIN LQTVQEDIEL LTRTYEEDDG KNRSGKIFIH NEKASKVYTT
DLIAAIIGEA GKGRFESRTA VPGHVQQGKS PSSIDRVNAC RLAIKCCNFI EDANFQVKHN
ANLSADERHL RFFYDDGVKT SAVSGKSSVI DDNTSVVIGI QGSEVTFTPV KQLWEKETHH
KWRKGKNVHW EQLNIVSDLL SGRLSIRTT
