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ATP-dependent 6-phosphofructokinase, muscle type (ATP-PFK) (PFK-M) (EC 2.7.1.11) (6-phosphofructokinase type A) (Phosphofructo-1-kinase isozyme A) (PFK-A) (Phosphohexokinase)

 PFKAM_RABIT             Reviewed;         780 AA.
P00511;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
31-JAN-2018, entry version 136.
RecName: Full=ATP-dependent 6-phosphofructokinase, muscle type {ECO:0000255|HAMAP-Rule:MF_03184};
Short=ATP-PFK {ECO:0000255|HAMAP-Rule:MF_03184};
Short=PFK-M;
EC=2.7.1.11 {ECO:0000255|HAMAP-Rule:MF_03184};
AltName: Full=6-phosphofructokinase type A;
AltName: Full=Phosphofructo-1-kinase isozyme A;
Short=PFK-A;
AltName: Full=Phosphohexokinase {ECO:0000255|HAMAP-Rule:MF_03184};
Name=PFKM;
Oryctolagus cuniculus (Rabbit).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
Oryctolagus.
NCBI_TaxID=9986;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Muscle;
PubMed=2951385;
Lee C.P., Kao M.C., French B.A., Putney S.D., Chang S.H.;
"The rabbit muscle phosphofructokinase gene. Implications for protein
structure, function, and tissue specificity.";
J. Biol. Chem. 262:4195-4199(1987).
[2]
PROTEIN SEQUENCE OF 2-780, AND ACETYLATION AT THR-2.
PubMed=6233492; DOI=10.1038/309467a0;
Poorman R.A., Randolph A., Kemp R.G., Heinrikson R.L.;
"Evolution of phosphofructokinase -- gene duplication and creation of
new effector sites.";
Nature 309:467-469(1984).
[3]
PROTEIN SEQUENCE OF 768-780, AND PHOSPHORYLATION AT SER-775.
PubMed=2539199; DOI=10.1016/0167-4838(89)90079-4;
Valaitis A.P., Foe L.G., Kwiatkowska D., Latshaw S.P., Kemp R.G.;
"The sites of phosphorylation of rabbit brain phosphofructo-1-kinase
by cyclic AMP-dependent protein kinase.";
Biochim. Biophys. Acta 995:187-194(1989).
[4]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 194-959.
PubMed=21241708; DOI=10.1016/j.jmb.2011.01.019;
Banaszak K., Mechin I., Obmolova G., Oldham M., Chang S.H., Ruiz T.,
Radermacher M., Kopperschlager G., Rypniewski W.;
"The crystal structures of eukaryotic phosphofructokinases from
baker's yeast and rabbit skeletal muscle.";
J. Mol. Biol. 407:284-297(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}.
-!- CATALYTIC ACTIVITY: ATP + D-fructose 6-phosphate = ADP + D-
fructose 1,6-bisphosphate. {ECO:0000255|HAMAP-Rule:MF_03184}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
-!- ENZYME REGULATION: Allosterically activated by ADP, AMP, or
fructose 2,6-bisphosphate, and allosterically inhibited by ATP or
citrate. {ECO:0000255|HAMAP-Rule:MF_03184}.
-!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
phosphate and glycerone phosphate from D-glucose: step 3/4.
{ECO:0000255|HAMAP-Rule:MF_03184}.
-!- SUBUNIT: Homo- and heterotetramers (By similarity).
Phosphofructokinase (PFK) enzyme functions as a tetramer composed
of different combinations of 3 types of subunits, called PFKM (M),
PFKL (L) and PFKP (P). The composition of the PFK tetramer differs
according to the tissue type it is present in. The kinetic and
regulatory properties of the tetrameric enzyme are dependent on
the subunit composition, hence can vary across tissues (Probable).
Interacts (via C-terminus) with HK1 (via N-terminal spermatogenic
cell-specific region) (By similarity).
{ECO:0000250|UniProtKB:P47857, ECO:0000255|HAMAP-Rule:MF_03184,
ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.
-!- PTM: GlcNAcylation decreases enzyme activity. {ECO:0000250}.
-!- 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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EMBL; M14477; AAA31441.1; -; Genomic_DNA.
EMBL; M14456; AAA31441.1; JOINED; Genomic_DNA.
EMBL; M14457; AAA31441.1; JOINED; Genomic_DNA.
EMBL; M14458; AAA31441.1; JOINED; Genomic_DNA.
EMBL; M14459; AAA31441.1; JOINED; Genomic_DNA.
EMBL; M14460; AAA31441.1; JOINED; Genomic_DNA.
EMBL; M14461; AAA31441.1; JOINED; Genomic_DNA.
EMBL; M14462; AAA31441.1; JOINED; Genomic_DNA.
EMBL; M14463; AAA31441.1; JOINED; Genomic_DNA.
EMBL; M14464; AAA31441.1; JOINED; Genomic_DNA.
EMBL; M14465; AAA31441.1; JOINED; Genomic_DNA.
EMBL; M14466; AAA31441.1; JOINED; Genomic_DNA.
EMBL; M14467; AAA31441.1; JOINED; Genomic_DNA.
EMBL; M14468; AAA31441.1; JOINED; Genomic_DNA.
EMBL; M14469; AAA31441.1; JOINED; Genomic_DNA.
EMBL; M14470; AAA31441.1; JOINED; Genomic_DNA.
EMBL; M14471; AAA31441.1; JOINED; Genomic_DNA.
EMBL; M14472; AAA31441.1; JOINED; Genomic_DNA.
EMBL; M14473; AAA31441.1; JOINED; Genomic_DNA.
EMBL; M14474; AAA31441.1; JOINED; Genomic_DNA.
EMBL; M14475; AAA31441.1; JOINED; Genomic_DNA.
EMBL; M14476; AAA31441.1; JOINED; Genomic_DNA.
PIR; A26550; KIRBF.
PDB; 3O8L; X-ray; 3.20 A; A/B=1-762.
PDB; 3O8N; X-ray; 3.20 A; A/B=1-762.
PDBsum; 3O8L; -.
PDBsum; 3O8N; -.
ProteinModelPortal; P00511; -.
SMR; P00511; -.
STRING; 9986.ENSOCUP00000014991; -.
ChEMBL; CHEMBL1075312; -.
iPTMnet; P00511; -.
eggNOG; KOG2440; Eukaryota.
eggNOG; COG0205; LUCA.
HOGENOM; HOG000200154; -.
HOVERGEN; HBG000976; -.
InParanoid; P00511; -.
BRENDA; 2.7.1.11; 1749.
SABIO-RK; P00511; -.
UniPathway; UPA00109; UER00182.
EvolutionaryTrace; P00511; -.
Proteomes; UP000001811; Unplaced.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0003872; F:6-phosphofructokinase activity; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
HAMAP; MF_03184; Phosphofructokinase_I_E; 1.
InterPro; IPR009161; 6-Pfructokinase_euk.
InterPro; IPR022953; ATP_PFK.
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.
TIGRFAMs; TIGR02478; 6PF1K_euk; 1.
PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Allosteric enzyme; ATP-binding;
Complete proteome; Cytoplasm; Direct protein sequencing; Glycolysis;
Glycoprotein; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
Phosphoprotein; Reference proteome; Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:6233492}.
CHAIN 2 780 ATP-dependent 6-phosphofructokinase,
muscle type.
/FTId=PRO_0000112019.
NP_BIND 88 89 ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
NP_BIND 118 121 ATP. {ECO:0000255|HAMAP-Rule:MF_03184}.
REGION 2 390 N-terminal catalytic PFK domain 1.
{ECO:0000255|HAMAP-Rule:MF_03184,
ECO:0000305|PubMed:21241708}.
REGION 164 166 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_03184}.
REGION 208 210 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_03184}.
REGION 298 301 Substrate binding. {ECO:0000255|HAMAP-
Rule:MF_03184}.
REGION 391 401 Interdomain linker. {ECO:0000255|HAMAP-
Rule:MF_03184,
ECO:0000305|PubMed:21241708}.
REGION 402 780 C-terminal regulatory PFK domain 2.
{ECO:0000255|HAMAP-Rule:MF_03184,
ECO:0000305|PubMed:21241708}.
REGION 528 532 Allosteric activator fructose 2,6-
bisphosphate binding. {ECO:0000255|HAMAP-
Rule:MF_03184}.
REGION 573 575 Allosteric activator fructose 2,6-
bisphosphate binding. {ECO:0000255|HAMAP-
Rule:MF_03184}.
REGION 661 664 Allosteric activator fructose 2,6-
bisphosphate binding. {ECO:0000255|HAMAP-
Rule:MF_03184}.
ACT_SITE 166 166 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_03184}.
METAL 119 119 Magnesium; catalytic. {ECO:0000255|HAMAP-
Rule:MF_03184}.
BINDING 25 25 ATP; via amide nitrogen.
{ECO:0000255|HAMAP-Rule:MF_03184}.
BINDING 201 201 Substrate; shared with dimeric partner.
{ECO:0000255|HAMAP-Rule:MF_03184}.
BINDING 264 264 Substrate. {ECO:0000255|HAMAP-
Rule:MF_03184}.
BINDING 292 292 Substrate; shared with dimeric partner.
{ECO:0000255|HAMAP-Rule:MF_03184}.
BINDING 471 471 Allosteric activator fructose 2,6-
bisphosphate. {ECO:0000255|HAMAP-
Rule:MF_03184}.
BINDING 566 566 Allosteric activator fructose 2,6-
bisphosphate; shared with dimeric
partner. {ECO:0000255|HAMAP-
Rule:MF_03184}.
BINDING 629 629 Allosteric activator fructose 2,6-
bisphosphate. {ECO:0000255|HAMAP-
Rule:MF_03184}.
BINDING 655 655 Allosteric activator fructose 2,6-
bisphosphate; shared with dimeric
partner. {ECO:0000255|HAMAP-
Rule:MF_03184}.
BINDING 735 735 Allosteric activator fructose 2,6-
bisphosphate. {ECO:0000255|HAMAP-
Rule:MF_03184}.
MOD_RES 2 2 N-acetylthreonine.
{ECO:0000269|PubMed:6233492}.
MOD_RES 133 133 Phosphoserine.
{ECO:0000250|UniProtKB:P47858}.
MOD_RES 377 377 Phosphoserine.
{ECO:0000250|UniProtKB:P47857}.
MOD_RES 667 667 Phosphoserine.
{ECO:0000250|UniProtKB:P08237}.
MOD_RES 775 775 Phosphoserine; by PKA.
{ECO:0000269|PubMed:2539199}.
CARBOHYD 530 530 O-linked (GlcNAc) serine. {ECO:0000250}.
CONFLICT 269 269 R -> S (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 480 508 Missing (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 559 559 S -> I (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 566 566 Missing (in Ref. 2; AA sequence).
{ECO:0000305}.
TURN 10 13 {ECO:0000244|PDB:3O8L}.
STRAND 17 21 {ECO:0000244|PDB:3O8L}.
HELIX 30 43 {ECO:0000244|PDB:3O8L}.
STRAND 47 49 {ECO:0000244|PDB:3O8L}.
HELIX 54 59 {ECO:0000244|PDB:3O8L}.
HELIX 62 64 {ECO:0000244|PDB:3O8L}.
HELIX 71 73 {ECO:0000244|PDB:3O8L}.
HELIX 91 93 {ECO:0000244|PDB:3O8L}.
HELIX 95 108 {ECO:0000244|PDB:3O8L}.
STRAND 112 117 {ECO:0000244|PDB:3O8L}.
HELIX 119 130 {ECO:0000244|PDB:3O8L}.
HELIX 133 138 {ECO:0000244|PDB:3O8L}.
TURN 139 143 {ECO:0000244|PDB:3O8L}.
TURN 146 148 {ECO:0000244|PDB:3O8L}.
HELIX 149 151 {ECO:0000244|PDB:3O8L}.
STRAND 157 163 {ECO:0000244|PDB:3O8L}.
HELIX 178 193 {ECO:0000244|PDB:3O8L}.
STRAND 202 207 {ECO:0000244|PDB:3O8L}.
HELIX 214 223 {ECO:0000244|PDB:3O8L}.
HELIX 240 252 {ECO:0000244|PDB:3O8L}.
STRAND 256 260 {ECO:0000244|PDB:3O8N}.
STRAND 269 271 {ECO:0000244|PDB:3O8L}.
HELIX 276 286 {ECO:0000244|PDB:3O8L}.
STRAND 291 294 {ECO:0000244|PDB:3O8L}.
HELIX 307 325 {ECO:0000244|PDB:3O8L}.
STRAND 334 339 {ECO:0000244|PDB:3O8L}.
STRAND 342 347 {ECO:0000244|PDB:3O8L}.
HELIX 348 363 {ECO:0000244|PDB:3O8L}.
HELIX 367 374 {ECO:0000244|PDB:3O8L}.
HELIX 377 389 {ECO:0000244|PDB:3O8L}.
STRAND 402 410 {ECO:0000244|PDB:3O8L}.
HELIX 415 428 {ECO:0000244|PDB:3O8L}.
STRAND 432 438 {ECO:0000244|PDB:3O8L}.
HELIX 441 445 {ECO:0000244|PDB:3O8L}.
STRAND 448 450 {ECO:0000244|PDB:3O8L}.
TURN 453 456 {ECO:0000244|PDB:3O8L}.
HELIX 475 477 {ECO:0000244|PDB:3O8L}.
HELIX 478 487 {ECO:0000244|PDB:3O8L}.
STRAND 493 498 {ECO:0000244|PDB:3O8L}.
HELIX 499 514 {ECO:0000244|PDB:3O8L}.
STRAND 522 527 {ECO:0000244|PDB:3O8L}.
HELIX 542 556 {ECO:0000244|PDB:3O8L}.
TURN 557 560 {ECO:0000244|PDB:3O8L}.
STRAND 562 564 {ECO:0000244|PDB:3O8L}.
STRAND 566 572 {ECO:0000244|PDB:3O8L}.
HELIX 579 587 {ECO:0000244|PDB:3O8L}.
STRAND 591 594 {ECO:0000244|PDB:3O8L}.
STRAND 596 598 {ECO:0000244|PDB:3O8L}.
HELIX 602 616 {ECO:0000244|PDB:3O8L}.
STRAND 621 628 {ECO:0000244|PDB:3O8L}.
STRAND 633 635 {ECO:0000244|PDB:3O8L}.
HELIX 637 647 {ECO:0000244|PDB:3O8L}.
TURN 648 651 {ECO:0000244|PDB:3O8L}.
STRAND 653 658 {ECO:0000244|PDB:3O8L}.
HELIX 670 692 {ECO:0000244|PDB:3O8L}.
STRAND 697 700 {ECO:0000244|PDB:3O8L}.
STRAND 708 714 {ECO:0000244|PDB:3O8L}.
STRAND 717 722 {ECO:0000244|PDB:3O8L}.
HELIX 723 726 {ECO:0000244|PDB:3O8L}.
HELIX 727 729 {ECO:0000244|PDB:3O8L}.
TURN 732 735 {ECO:0000244|PDB:3O8L}.
STRAND 736 739 {ECO:0000244|PDB:3O8L}.
HELIX 741 744 {ECO:0000244|PDB:3O8L}.
HELIX 746 751 {ECO:0000244|PDB:3O8L}.
TURN 752 754 {ECO:0000244|PDB:3O8N}.
SEQUENCE 780 AA; 85203 MW; ACDDF38C36F48EDB CRC64;
MTHEEHHAAR TLGVGKAIAV LTSGGDAQGM NAAVRAVVRV GIFTGARVFF VHEGYQGLVD
GGDHIREATW ESVSMMLQLG GTVIGSARCK DFREREGRLR AAHNLVKRGI TNLCVIGGDG
SLTGADTFRS EWSDLLSDLQ KAGKITAEEA TRSSYLNIVG LVGSIDNDFC GTDMTIGTDS
ALHRITEIVD AITTTAQSHQ RTFVLEVMGR HCGYLALVTS LSCGADWVFI PECPPDDNWE
DHLCRRLSET RTRGSRLNII IVAEGAIDRN GKPITSEGVK DLVVRRLGYD TRVTVLGHVQ
RGGTPSAFDR ILGSRMGVEA VMALLEGTPD TPACVVSLSG NQAVRLPLME CVQVTKDVTK
AMDEKRFDEA MKLRGRSFMN NWEVYKLLAH IRPPAPKSGS YTVAVMNVGA PAAGMNAAVR
STVRIGLIQG NRVLVVHDGF EGPAKGQIEE AGWSYVGGWT GQGGSKLGSK RTLPKKSFEQ
ISANITKFNI QGLVIIGGFE AYTGGLELME GRKQFDELCI PFVVIPATVS NNVPGSDFSV
GADTALNTIC TTCDRIKQSA AGTKRRVFII ETMGGYCGYL ATMAGLAAGA DAAYIFEEPF
TIRDLQANVE HLVQKMKTTV KRGLVLRNEK CNENYTTDFI FNLYSEEGKG IFDSRKNVLG
HMQQGGSPTP FDRNFATKMG AKAMNWMAGK IKESYRNGRI FANTPDSGCV LGMRKRALVF
QPVTELQNQT DFEHRIPKEQ WWLKLRPILK ILAKYEIDLD TSEHAHLEHI SRKRSGEATV


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