PFKA1_PICPA
ID PFKA1_PICPA Reviewed; 989 AA.
AC Q8NJU8;
DT 09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=Phosphohexokinase 1 {ECO:0000255|HAMAP-Rule:MF_03184};
GN Name=PFK1;
OS Komagataella pastoris (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=4922;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=MH458;
RX PubMed=17522059; DOI=10.1074/jbc.m611547200;
RA Tanneberger K., Kirchberger J., Baer J., Schellenberger W., Rothemund S.,
RA Kamprad M., Otto H., Schoeneberg T., Edelmann A.;
RT "A novel form of 6-phosphofructokinase. Identification and functional
RT relevance of a third type of subunit in Pichia pastoris.";
RL J. Biol. Chem. 282:23687-23697(2007).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
RP REGULATION, AND SUBUNIT.
RC STRAIN=ATCC 28485 / BCRC 21531 / CBS 704 / DSM 70382 / JCM 3650 / NBRC
RC 10777 / NRRLY-1603;
RX PubMed=12125050; DOI=10.1002/yea.885;
RA Kirchberger J., Baer J., Schellenberger W., Dihazi H., Kopperschlaeger G.;
RT "6-phosphofructokinase from Pichia pastoris: purification, kinetic and
RT molecular characterization of the enzyme.";
RL Yeast 19:933-947(2002).
RN [3]
RP STRUCTURE BY ELECTRON MICROSCOPY, AND SUBUNIT.
RX PubMed=19559794; DOI=10.1016/j.jsb.2009.06.014;
RA Benjamin S., Radermacher M., Kirchberger J., Schoeneberg T., Edelmann A.,
RA Ruiz T.;
RT "3D structure of phosphofructokinase from Pichia pastoris: Localization of
RT the novel gamma-subunits.";
RL J. Struct. Biol. 168:345-351(2009).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS).
RX PubMed=20833871; DOI=10.1096/fj.10-163865;
RA Straeter N., Marek S., Kuettner E.B., Kloos M., Keim A., Brueser A.,
RA Kirchberger J., Schoeneberg T.;
RT "Molecular architecture and structural basis of allosteric regulation of
RT eukaryotic phosphofructokinases.";
RL FASEB J. 25:89-98(2011).
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 ECO:0000269|PubMed:12125050}.
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, ECO:0000269|PubMed:12125050};
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, ECO:0000269|PubMed:12125050}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.971 mM for D-fructose 6-phosphate {ECO:0000269|PubMed:12125050};
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.
CC {ECO:0000269|PubMed:12125050, ECO:0000269|PubMed:17522059,
CC ECO:0000269|PubMed:19559794}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184,
CC ECO:0000269|PubMed:17522059}.
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; AF508861; AAM44819.1; -; Genomic_DNA.
DR PDB; 3OPY; X-ray; 3.05 A; A/C/E/G=1-989.
DR PDBsum; 3OPY; -.
DR AlphaFoldDB; Q8NJU8; -.
DR SMR; Q8NJU8; -.
DR SABIO-RK; Q8NJU8; -.
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 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 3D-structure; Allosteric enzyme; ATP-binding; Cytoplasm; Glycolysis;
KW Kinase; Magnesium; Metal-binding; Nucleotide-binding; Transferase.
FT CHAIN 1..989
FT /note="ATP-dependent 6-phosphofructokinase subunit alpha"
FT /id="PRO_0000429715"
FT REGION 1..585
FT /note="N-terminal catalytic PFK domain 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184,
FT ECO:0000305|PubMed:20833871"
FT REGION 586..599
FT /note="Interdomain linker"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184,
FT ECO:0000305|PubMed:20833871"
FT REGION 600..989
FT /note="C-terminal regulatory PFK domain 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03184,
FT ECO:0000305|PubMed:20833871"
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 STRAND 6..17
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 19..31
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 126..130
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 134..143
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 158..169
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 225..238
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 241..246
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 249..254
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:3OPY"
FT TURN 265..270
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 271..273
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 290..302
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 307..312
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 314..326
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 343..347
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 352..361
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 373..388
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 396..401
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 409..418
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 421..424
FT /evidence="ECO:0007829|PDB:3OPY"
FT TURN 432..434
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 435..448
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 453..458
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 472..480
FT /evidence="ECO:0007829|PDB:3OPY"
FT TURN 481..483
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 485..490
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 492..496
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 502..520
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 529..542
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 543..558
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 562..567
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 571..584
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 585..588
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 589..591
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 595..597
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 600..608
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 613..626
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 630..634
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 637..644
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 647..650
FT /evidence="ECO:0007829|PDB:3OPY"
FT TURN 652..660
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 673..676
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 677..687
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 690..697
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 698..710
FT /evidence="ECO:0007829|PDB:3OPY"
FT TURN 711..713
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 715..717
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 721..726
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 741..758
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 765..771
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 778..787
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 801..815
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 826..834
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 836..838
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 840..849
FT /evidence="ECO:0007829|PDB:3OPY"
FT TURN 850..854
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 857..860
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 863..867
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 873..890
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 893..895
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 899..901
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 905..910
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 912..915
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 918..921
FT /evidence="ECO:0007829|PDB:3OPY"
FT TURN 922..924
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 932..934
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 935..941
FT /evidence="ECO:0007829|PDB:3OPY"
FT STRAND 944..949
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 950..956
FT /evidence="ECO:0007829|PDB:3OPY"
FT TURN 959..961
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 971..980
FT /evidence="ECO:0007829|PDB:3OPY"
FT HELIX 983..986
FT /evidence="ECO:0007829|PDB:3OPY"
SQ SEQUENCE 989 AA; 108804 MW; 7ADD1A036B4B19C2 CRC64;
MPEPSISDLS FTSFVTNDDN LFEETFNFYT KLGFHATRSY VKDNRSDFEL TGISTDSIKE
IWLESFPLSE VVEASGGREL RKPLQESVGY ESEALLGYSP YQSGGVVIKL RLSNHDLEKN
NDLPGEVTFF TASIDKLKAK LIEIGAEIIP SKIDLVEFST RDPMGDVISF SSYPSLNSKK
ITSPDFFLHP KKEVRSEESI VEQVKSEEGK KKIAIITSGG DAPGMNAAVR AVTRAGIFYG
CKVYACYEGY TGLVKGGDML KELQWQDVRG LLSIGGTIIG TARCKEFRER WGRLQACYNM
VSNGIDALVV CGGDGSLTGA DLFRKEWPEL IKELLGEDKI TKEQYETHRN LTIVGLVGSI
DNDMCGTDST IGAYSSLERI IELVDYIDAT AASHSRAFVV EVMGRHCGWL GLMSGIATGA
DYIFIPERPP SESNWKDDLK KVCLRHREKG RRKTTVIVAE GAIDDQLNPI TSEEVKDVLV
EIGLDTRITR LGHVQRGGAP CAFDRFLATV QGVDAVRAVL ESTPAIPSPV ISILENKIVR
QPLVESVAQT KTVSAAIEAK DFDKALQLRD QEFATSYENF LSVSKYDDGS YLVPESSRLN
IAIIHVGAPT SALNPATRVA TLNSLAKGHR VFAIRNGFAG LIRHGAVREL NWIDVEDWHN
TGGSEIGTNR SLPSDDMGTV AYYFQQYKFD GLIIIGGFEA FTALYELDAA RAQYPIFNIP
MCCLPATVSN NVPGTEYSLG SDTCLNTLSG YCDAVKQSAS ASRRRTFVVE VQGGYSGYLA
SYAGLITGAL AVYTPENPIN LQTVQEDIEL LTRTYEEDDG KNRSGKIFIH NEKASKVYTT
DLIAAIIGEA GKGRFESRTA VPGHVQQGKS PSSIDRVNAC RLAIKCCNFI EDANFQVKHN
ANLSADERHL RFFYDDGVKT SAVSGKSSVI DDNTSVVIGI QGSEVTFTPV KQLWENETHH
KWRKGKNVHW EQLNIVSDLL SGRLSIRTT
