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Database: UniProt
Entry: A0A1Z5R3J0_SORBI
LinkDB: A0A1Z5R3J0_SORBI
Original site: A0A1Z5R3J0_SORBI 
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
//
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