ID A0A1Z5R3J0_SORBI Unreviewed; 1089 AA.
AC A0A1Z5R3J0;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_03186};
DE Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_03186};
DE Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_03186};
DE EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_03186};
DE AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_03186};
GN Name=PFK {ECO:0000256|HAMAP-Rule:MF_03186};
GN ORFNames=SORBI_3009G204601 {ECO:0000313|EMBL:OQU78332.1};
OS Sorghum bicolor (Sorghum) (Sorghum vulgare).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Andropogonodae; Andropogoneae; Sorghinae; Sorghum.
OX NCBI_TaxID=4558 {ECO:0000313|EMBL:OQU78332.1, ECO:0000313|Proteomes:UP000000768};
RN [1] {ECO:0000313|EMBL:OQU78332.1, ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=19189423; DOI=10.1038/nature07723;
RA Paterson A.H., Bowers J.E., Bruggmann R., Dubchak I., Grimwood J.,
RA Gundlach H., Haberer G., Hellsten U., Mitros T., Poliakov A., Schmutz J.,
RA Spannagl M., Tang H., Wang X., Wicker T., Bharti A.K., Chapman J.,
RA Feltus F.A., Gowik U., Grigoriev I.V., Lyons E., Maher C.A., Martis M.,
RA Narechania A., Otillar R.P., Penning B.W., Salamov A.A., Wang Y., Zhang L.,
RA Carpita N.C., Freeling M., Gingle A.R., Hash C.T., Keller B., Klein P.,
RA Kresovich S., McCann M.C., Ming R., Peterson D.G., Mehboob-ur-Rahman,
RA Ware D., Westhoff P., Mayer K.F., Messing J., Rokhsar D.S.;
RT "The Sorghum bicolor genome and the diversification of grasses.";
RL Nature 457:551-556(2009).
RN [2] {ECO:0000313|Proteomes:UP000000768}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. BTx623 {ECO:0000313|Proteomes:UP000000768};
RX PubMed=29161754; DOI=10.1111/tpj.13781;
RA McCormick R.F., Truong S.K., Sreedasyam A., Jenkins J., Shu S., Sims D.,
RA Kennedy M., Amirebrahimi M., Weers B.D., McKinley B., Mattison A.,
RA Morishige D.T., Grimwood J., Schmutz J., Mullet J.E.;
RT "The Sorghum bicolor reference genome: improved assembly, gene annotations,
RT a transcriptome atlas, and signatures of genome organization.";
RL Plant J. 93:338-354(2018).
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:0000256|HAMAP-Rule:MF_03186}.
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;
CC Evidence={ECO:0000256|ARBA:ARBA00000432, ECO:0000256|HAMAP-
CC Rule:MF_03186};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_03186};
CC -!- ACTIVITY REGULATION: Allosterically activated by AMP.
CC {ECO:0000256|HAMAP-Rule:MF_03186}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC {ECO:0000256|HAMAP-Rule:MF_03186}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_03186}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03186}.
CC -!- SIMILARITY: Belongs to the peptidase M16 family.
CC {ECO:0000256|RuleBase:RU004447}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC PPi-dependent PFK group II subfamily. Atypical ATP-dependent clade 'X'
CC sub-subfamily. {ECO:0000256|HAMAP-Rule:MF_03186}.
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DR EMBL; CM000768; OQU78332.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z5R3J0; -.
DR STRING; 4558.A0A1Z5R3J0; -.
DR EnsemblPlants; OQU78332; OQU78332; SORBI_3009G204601.
DR Gramene; OQU78332; OQU78332; SORBI_3009G204601.
DR eggNOG; KOG2440; Eukaryota.
DR InParanoid; A0A1Z5R3J0; -.
DR OMA; ASWGDES; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000000768; Chromosome 9.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.450; -; 1.
DR Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR HAMAP; MF_01981; Phosphofructokinase_II_X; 1.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR011249; Metalloenz_LuxS/M16.
DR InterPro; IPR011765; Pept_M16_N.
DR InterPro; IPR001431; Pept_M16_Zn_BS.
DR InterPro; IPR007863; Peptidase_M16_C.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR InterPro; IPR012004; PyroP-dep_PFK_TP0108.
DR PANTHER; PTHR45770:SF10; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE; 1.
DR PANTHER; PTHR45770; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 1; 1.
DR Pfam; PF00675; Peptidase_M16; 1.
DR Pfam; PF05193; Peptidase_M16_C; 1.
DR Pfam; PF00365; PFK; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR SUPFAM; SSF53784; Phosphofructokinase; 1.
DR PROSITE; PS00143; INSULINASE; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_03186};
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03186};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03186};
KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_03186};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_03186};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_03186};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_03186}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03186};
KW Reference proteome {ECO:0000313|Proteomes:UP000000768};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_03186}.
FT DOMAIN 81..224
FT /note="Peptidase M16 N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00675"
FT DOMAIN 237..416
FT /note="Peptidase M16 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05193"
FT DOMAIN 688..993
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT REGION 522..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1046..1089
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1072..1089
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 814
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 695
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 758..759
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 783..786
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 784
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 812..814
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 857..859
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 913
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT BINDING 969..972
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT SITE 785
FT /note="Important for substrate specificity; cannot use PPi
FT as phosphoryl donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
SQ SEQUENCE 1089 AA; 118646 MW; A590DF44EF7F10A8 CRC64;
MYRAAGSHLR SLKHHGASRF ASTNVVKQSS GGLFSWLLGG KSSQLPPLDV PLPGIAIPSP
LPDFVEPSKT KVTTLPNGVK IASETSSSPA ASVGLYIDCG SIYETPASSG VSHLLERMAF
KSTVNRTHLR LVREVEAIGG NVSASASREQ MSYTYDALKC YTPEMVEVLI DSVRNPAFLD
WEVKEQLQNI KSEIADVSAN PQGLLLEALH SAGYSGALAK PLMASESAVN QLDVSILEEF
VAEHYTAPRM VLAASGVEHD ALVSVVEPLL SDLPCVKRPE EPKSVYVGGD YRCQADSPST
HIALAFEVPG GWNQEKTAMV VTVLQMLMGG GGSFSAGGPG KGMHSRLYLR VLTNFQQIDS
FSAFNSVYNN SGLFGIYAVT SPDFSSKAVD LAAGELLEIA TPGKVTQEQL DRAKEATKSA
VLMNLESRSI ASEDIGRQVL TYGERKPIEY FLKTVEEITL NDILSTAKKM MSSPLTMASW
GDVIHVPSYE SVSRKFHSKL RPVPVPCPDR SAALPTMASH IILPPDDADE NHNHQAEEEE
REELGRDEDA DDEEHGHGHP PALPPKAALP FSATCVRISR DSYPNLRALR NASSVSLADA
AYVKISEGDY GYVLDDVPHF TDYLPDIPTY PNPLQDHPAY STVKQYFVNE DDTVPQKVVV
QKNSRRGVHF RRAGPRQRIY FGTDEVKACI VTCGGLCPGL NTVIRELVCG LSHMYNVSSI
FGIQNGYKGF YSSNYLPLTP KSVNDIHKRG GTVLGTSRGG HDTKKIVDNI QDRGINQVYI
IGGDGTQKGA YEIFKEIRKR GLKVSVAGVP KTIDNDIAII DKSFGFDTAV EEAQRAIDSA
HVEACSAENG IGLVKLMGRY SGFIAMYATL ASRDVDCCLI PESPFYLDGE GGLLQYVEKR
LKENKHMVIV VAEGAGQDLI AKSIATSDQQ DASGNKLLLD IGLWLTHKIK DYFKSKKMEM
TIKYIDPTYM IRAIPSNASD NVYCTLLAHS AIHGAMAGYS FTVGMVNGRH TYIPFYRVTS
TRNKVKVTDR MWARLLSSTN QPSFLSQKDI DEASEADRLA NRPPLPTGAS SRVARSFDQS
SSCSSNGEI
//