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ATP-dependent 6-phosphofructokinase subunit beta (EC 2.7.1.11) (ATP-dependent 6-phosphofructokinase 2) (ATP-PFK 2) (Phosphofructokinase 2) (Phosphohexokinase 2)

 PFKA2_PICPA             Reviewed;         941 AA.
Q8TGA0;
09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
05-DEC-2018, entry version 85.
RecName: Full=ATP-dependent 6-phosphofructokinase subunit beta {ECO:0000255|HAMAP-Rule:MF_03184};
EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03184};
AltName: Full=ATP-dependent 6-phosphofructokinase 2 {ECO:0000255|HAMAP-Rule:MF_03184};
Short=ATP-PFK 2 {ECO:0000255|HAMAP-Rule:MF_03184};
Short=Phosphofructokinase 2 {ECO:0000255|HAMAP-Rule:MF_03184};
AltName: Full=Phosphohexokinase 2 {ECO:0000255|HAMAP-Rule:MF_03184};
Name=PFK2;
Komagataella pastoris (Yeast) (Pichia pastoris).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Phaffomycetaceae; Komagataella.
NCBI_TaxID=4922;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-16.
STRAIN=MH458;
PubMed=12125051; DOI=10.1002/yea.889;
Edelmann A., Baer J.;
"Molecular genetics of 6-phosphofructokinase in Pichia pastoris.";
Yeast 19:949-956(2002).
[2]
FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY
REGULATION, AND SUBUNIT.
STRAIN=ATCC 28485 / BCRC 21531 / CBS 704 / DSM 70382 / JCM 3650 / NBRC
10777 / NRRLY-1603;
PubMed=12125050; DOI=10.1002/yea.885;
Kirchberger J., Baer J., Schellenberger W., Dihazi H.,
Kopperschlaeger G.;
"6-phosphofructokinase from Pichia pastoris: purification, kinetic and
molecular characterization of the enzyme.";
Yeast 19:933-947(2002).
[3]
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=17522059; DOI=10.1074/jbc.M611547200;
Tanneberger K., Kirchberger J., Baer J., Schellenberger W.,
Rothemund S., Kamprad M., Otto H., Schoeneberg T., Edelmann A.;
"A novel form of 6-phosphofructokinase. Identification and functional
relevance of a third type of subunit in Pichia pastoris.";
J. Biol. Chem. 282:23687-23697(2007).
[4]
STRUCTURE BY ELECTRON MICROSCOPY, AND SUBUNIT.
PubMed=19559794; DOI=10.1016/j.jsb.2009.06.014;
Benjamin S., Radermacher M., Kirchberger J., Schoeneberg T.,
Edelmann A., Ruiz T.;
"3D structure of phosphofructokinase from Pichia pastoris:
Localization of the novel gamma-subunits.";
J. Struct. Biol. 168:345-351(2009).
[5]
X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) IN COMPLEX WITH ALLOSTERIC
INHIBITOR ATP.
PubMed=20833871; DOI=10.1096/fj.10-163865;
Straeter N., Marek S., Kuettner E.B., Kloos M., Keim A., Brueser A.,
Kirchberger J., Schoeneberg T.;
"Molecular architecture and structural basis of allosteric regulation
of eukaryotic phosphofructokinases.";
FASEB J. 25:89-98(2011).
-!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate
to fructose 1,6-bisphosphate by ATP, the first committing step of
glycolysis. {ECO:0000255|HAMAP-Rule:MF_03184,
ECO:0000269|PubMed:12125050}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose
1,6-bisphosphate + H(+); Xref=Rhea:RHEA:16109,
ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:32966,
ChEBI:CHEBI:57634, ChEBI:CHEBI:456216; EC=2.7.1.11;
Evidence={ECO:0000255|HAMAP-Rule:MF_03184,
ECO:0000269|PubMed:12125050};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|HAMAP-Rule:MF_03184};
-!- ACTIVITY REGULATION: Allosterically activated by ADP, AMP, or
fructose 2,6-bisphosphate, and allosterically inhibited by ATP or
citrate. {ECO:0000255|HAMAP-Rule:MF_03184,
ECO:0000269|PubMed:12125050}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=6.971 mM for D-fructose 6-phosphate
{ECO:0000269|PubMed:12125050};
-!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
phosphate and glycerone phosphate from D-glucose: step 3/4.
{ECO:0000255|HAMAP-Rule:MF_03184}.
-!- SUBUNIT: Heterododecamer of 4 alpha, 4 beta and 4 gamma chains.
{ECO:0000269|PubMed:12125050, ECO:0000269|PubMed:17522059,
ECO:0000269|PubMed:19559794, ECO:0000269|PubMed:20833871}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184,
ECO:0000269|PubMed:17522059}.
-!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA)
family. ATP-dependent PFK group I subfamily. Eukaryotic two domain
clade "E" sub-subfamily. {ECO:0000255|HAMAP-Rule:MF_03184}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF395078; AAL82590.2; -; Genomic_DNA.
PDB; 3OPY; X-ray; 3.05 A; B/D/F/H=1-941.
PDBsum; 3OPY; -.
ProteinModelPortal; Q8TGA0; -.
SMR; Q8TGA0; -.
PRIDE; Q8TGA0; -.
UniPathway; UPA00109; UER00182.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
Gene3D; 3.10.180.10; -; 1.
HAMAP; MF_03184; Phosphofructokinase_I_E; 1.
InterPro; IPR009161; 6-Pfructokinase_euk.
InterPro; IPR022953; ATP_PFK.
InterPro; IPR029068; Glyas_Bleomycin-R_OHBP_Dase.
InterPro; IPR015912; Phosphofructokinase_CS.
InterPro; IPR000023; Phosphofructokinase_dom.
InterPro; IPR035966; PKF_sf.
Pfam; PF00365; PFK; 2.
PIRSF; PIRSF000533; ATP_PFK_euk; 1.
PRINTS; PR00476; PHFRCTKINASE.
SUPFAM; SSF53784; SSF53784; 2.
SUPFAM; SSF54593; SSF54593; 1.
TIGRFAMs; TIGR02478; 6PF1K_euk; 1.
PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
1: Evidence at protein level;
3D-structure; Allosteric enzyme; ATP-binding; Cytoplasm;
Direct protein sequencing; Glycolysis; Kinase; Magnesium;
Metal-binding; Nucleotide-binding; Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:12125051}.
CHAIN 2 941 ATP-dependent 6-phosphofructokinase
subunit beta.
/FTId=PRO_0000429716.
NP_BIND 255 256 ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
NP_BIND 285 288 ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
REGION 2 558 N-terminal catalytic PFK domain 1.
{ECO:0000255|HAMAP-Rule:MF_03184,
ECO:0000305|PubMed:20833871}.
REGION 331 333 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_03184}.
REGION 375 377 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_03184}.
REGION 394 395 Allosteric inhibitor ATP binding.
REGION 400 405 Allosteric inhibitor ATP binding.
REGION 466 469 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_03184}.
REGION 554 558 Allosteric inhibitor ATP binding.
REGION 559 572 Interdomain linker. {ECO:0000255|HAMAP-
Rule:MF_03184,
ECO:0000305|PubMed:20833871}.
REGION 573 941 C-terminal regulatory PFK domain 2.
{ECO:0000255|HAMAP-Rule:MF_03184,
ECO:0000305|PubMed:20833871}.
REGION 701 705 Allosteric activator fructose 2,6-
bisphosphate binding. {ECO:0000255|HAMAP-
Rule:MF_03184}.
REGION 746 748 Allosteric activator fructose 2,6-
bisphosphate binding. {ECO:0000255|HAMAP-
Rule:MF_03184}.
REGION 838 841 Allosteric activator fructose 2,6-
bisphosphate binding. {ECO:0000255|HAMAP-
Rule:MF_03184}.
ACT_SITE 333 333 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_03184}.
METAL 286 286 Magnesium; catalytic. {ECO:0000255|HAMAP-
Rule:MF_03184}.
BINDING 191 191 ATP; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_03184}.
BINDING 368 368 Substrate; shared with subunit alpha.
{ECO:0000255|HAMAP-Rule:MF_03184}.
BINDING 410 410 Allosteric inhibitor ATP.
{ECO:0000269|PubMed:20833871}.
BINDING 432 432 Substrate. {ECO:0000255|HAMAP-
Rule:MF_03184}.
BINDING 460 460 Substrate; shared with subunit alpha.
{ECO:0000255|HAMAP-Rule:MF_03184}.
BINDING 643 643 Allosteric activator fructose 2,6-
bisphosphate. {ECO:0000255|HAMAP-
Rule:MF_03184}.
BINDING 739 739 Allosteric activator fructose 2,6-
bisphosphate; shared with subunit alpha.
{ECO:0000255|HAMAP-Rule:MF_03184}.
BINDING 806 806 Allosteric activator fructose 2,6-
bisphosphate. {ECO:0000255|HAMAP-
Rule:MF_03184}.
BINDING 832 832 Allosteric activator fructose 2,6-
bisphosphate; shared with subunit alpha.
{ECO:0000255|HAMAP-Rule:MF_03184}.
BINDING 918 918 Allosteric activator fructose 2,6-
bisphosphate. {ECO:0000255|HAMAP-
Rule:MF_03184}.
STRAND 9 16 {ECO:0000244|PDB:3OPY}.
HELIX 24 32 {ECO:0000244|PDB:3OPY}.
STRAND 59 63 {ECO:0000244|PDB:3OPY}.
HELIX 70 80 {ECO:0000244|PDB:3OPY}.
STRAND 97 103 {ECO:0000244|PDB:3OPY}.
HELIX 105 113 {ECO:0000244|PDB:3OPY}.
TURN 114 116 {ECO:0000244|PDB:3OPY}.
STRAND 122 125 {ECO:0000244|PDB:3OPY}.
STRAND 129 131 {ECO:0000244|PDB:3OPY}.
STRAND 138 141 {ECO:0000244|PDB:3OPY}.
STRAND 147 149 {ECO:0000244|PDB:3OPY}.
STRAND 184 188 {ECO:0000244|PDB:3OPY}.
HELIX 196 209 {ECO:0000244|PDB:3OPY}.
STRAND 214 217 {ECO:0000244|PDB:3OPY}.
HELIX 220 226 {ECO:0000244|PDB:3OPY}.
TURN 229 231 {ECO:0000244|PDB:3OPY}.
STRAND 232 235 {ECO:0000244|PDB:3OPY}.
HELIX 237 240 {ECO:0000244|PDB:3OPY}.
TURN 241 245 {ECO:0000244|PDB:3OPY}.
HELIX 258 260 {ECO:0000244|PDB:3OPY}.
HELIX 262 275 {ECO:0000244|PDB:3OPY}.
STRAND 279 284 {ECO:0000244|PDB:3OPY}.
HELIX 286 297 {ECO:0000244|PDB:3OPY}.
HELIX 315 319 {ECO:0000244|PDB:3OPY}.
STRAND 324 333 {ECO:0000244|PDB:3OPY}.
HELIX 345 360 {ECO:0000244|PDB:3OPY}.
STRAND 367 373 {ECO:0000244|PDB:3OPY}.
HELIX 381 389 {ECO:0000244|PDB:3OPY}.
STRAND 393 396 {ECO:0000244|PDB:3OPY}.
HELIX 407 421 {ECO:0000244|PDB:3OPY}.
STRAND 426 430 {ECO:0000244|PDB:3OPY}.
HELIX 444 453 {ECO:0000244|PDB:3OPY}.
STRAND 458 463 {ECO:0000244|PDB:3OPY}.
HELIX 465 468 {ECO:0000244|PDB:3OPY}.
HELIX 475 494 {ECO:0000244|PDB:3OPY}.
STRAND 502 509 {ECO:0000244|PDB:3OPY}.
STRAND 511 515 {ECO:0000244|PDB:3OPY}.
HELIX 516 531 {ECO:0000244|PDB:3OPY}.
HELIX 535 541 {ECO:0000244|PDB:3OPY}.
HELIX 544 557 {ECO:0000244|PDB:3OPY}.
HELIX 568 570 {ECO:0000244|PDB:3OPY}.
STRAND 573 581 {ECO:0000244|PDB:3OPY}.
HELIX 586 600 {ECO:0000244|PDB:3OPY}.
STRAND 603 607 {ECO:0000244|PDB:3OPY}.
HELIX 610 617 {ECO:0000244|PDB:3OPY}.
STRAND 620 622 {ECO:0000244|PDB:3OPY}.
TURN 625 630 {ECO:0000244|PDB:3OPY}.
HELIX 631 633 {ECO:0000244|PDB:3OPY}.
TURN 646 648 {ECO:0000244|PDB:3OPY}.
HELIX 651 660 {ECO:0000244|PDB:3OPY}.
STRAND 664 671 {ECO:0000244|PDB:3OPY}.
HELIX 672 683 {ECO:0000244|PDB:3OPY}.
HELIX 684 686 {ECO:0000244|PDB:3OPY}.
HELIX 689 691 {ECO:0000244|PDB:3OPY}.
STRAND 695 700 {ECO:0000244|PDB:3OPY}.
HELIX 715 735 {ECO:0000244|PDB:3OPY}.
STRAND 739 745 {ECO:0000244|PDB:3OPY}.
HELIX 752 761 {ECO:0000244|PDB:3OPY}.
STRAND 764 767 {ECO:0000244|PDB:3OPY}.
TURN 769 771 {ECO:0000244|PDB:3OPY}.
HELIX 775 790 {ECO:0000244|PDB:3OPY}.
STRAND 800 805 {ECO:0000244|PDB:3OPY}.
HELIX 806 808 {ECO:0000244|PDB:3OPY}.
STRAND 810 812 {ECO:0000244|PDB:3OPY}.
HELIX 814 825 {ECO:0000244|PDB:3OPY}.
STRAND 828 834 {ECO:0000244|PDB:3OPY}.
TURN 838 841 {ECO:0000244|PDB:3OPY}.
HELIX 847 875 {ECO:0000244|PDB:3OPY}.
HELIX 884 887 {ECO:0000244|PDB:3OPY}.
STRAND 890 895 {ECO:0000244|PDB:3OPY}.
STRAND 900 904 {ECO:0000244|PDB:3OPY}.
HELIX 905 910 {ECO:0000244|PDB:3OPY}.
TURN 915 918 {ECO:0000244|PDB:3OPY}.
HELIX 926 936 {ECO:0000244|PDB:3OPY}.
SEQUENCE 941 AA; 103733 MW; BA5FCF3DE48C5899 CRC64;
MPDASLFNGT SFITLFAPNI SLLQASIDFY TNFLGFAIRK NSNQKLFWLQ LEEDQNNVSI
QLILDPEHAA SVSQIDQNIR NLTRSLYRKD WRSIQSNIAF KSSSLSKLVK LLKDGGHPVQ
QSPNEISPFE VYTVDPLGSL IGFSGFKNPF AVNERSLLPK VSEEKAYRAE DDSEKLLNPV
RKTIGVMTSG GDSPGMNPFV RAVVRAGIYK GCKVFCIHEG YEGLVRGGEK YIKETQWHDV
RGWLVEGGTN IGTARCKEFR ERSGRLKACK NMIDMGIDAL IVCGGDGSLT GADRFRSEWP
SLIEELLQTE QISQQQFNTH QNLNICGAVG SIDNDMSSTD ATIGAFSSLD RICRAIDYID
ATANSHSRAF IVEVMGRHCG WLGLLAGLAT SADYILIPEK PASSREWQDQ MCDIVGKHRA
RGKRKTIVIV AEGAISNDLS PISCDQVKDV LVNRLGLDTR VTTLGHVQRG GTAVAFDRIY
ATLQGVEAVN AVLECDADTP SPMIAIKEDQ ITRVPLVDAV ELTQQVAKSI ESRNFKKAIS
LRDSEFVEHM KNFISTNSAD HVPPSLPLEK RKKIAIINVG 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 VSFIERHSDR CQTFKNSISF RQTDEITSTA VVLGIHKSQL
RFTPIRQLYD FESDVPRRMR KNIFWSNVRE ISDMLSGRTS L


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