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Database: UniProt
Entry: B9SGA6_RICCO
LinkDB: B9SGA6_RICCO
Original site: B9SGA6_RICCO 
ID   B9SGA6_RICCO            Unreviewed;       561 AA.
AC   B9SGA6;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 64.
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=RCOM_0880730 {ECO:0000313|EMBL:EEF37352.1};
OS   Ricinus communis (Castor bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Malpighiales; Euphorbiaceae; Acalyphoideae; Acalypheae;
OC   Ricinus.
OX   NCBI_TaxID=3988 {ECO:0000313|Proteomes:UP000008311};
RN   [1] {ECO:0000313|Proteomes:UP000008311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Hale {ECO:0000313|Proteomes:UP000008311};
RX   PubMed=20729833; DOI=10.1038/nbt.1674;
RA   Chan A.P., Crabtree J., Zhao Q., Lorenzi H., Orvis J., Puiu D.,
RA   Melake-Berhan A., Jones K.M., Redman J., Chen G., Cahoon E.B., Gedil M.,
RA   Stanke M., Haas B.J., Wortman J.R., Fraser-Liggett C.M., Ravel J.,
RA   Rabinowicz P.D.;
RT   "Draft genome sequence of the oilseed species Ricinus communis.";
RL   Nat. Biotechnol. 28:951-956(2010).
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 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; EQ973951; EEF37352.1; -; Genomic_DNA.
DR   AlphaFoldDB; B9SGA6; -.
DR   STRING; 3988.B9SGA6; -.
DR   eggNOG; KOG2440; Eukaryota.
DR   InParanoid; B9SGA6; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000008311; Unassembled WGS sequence.
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:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.450; -; 1.
DR   HAMAP; MF_01981; Phosphofructokinase_II_X; 1.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR035966; PKF_sf.
DR   InterPro; IPR012004; PyroP-dep_PFK_TP0108.
DR   PANTHER; PTHR45770; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 1; 1.
DR   PANTHER; PTHR45770:SF9; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 2; 1.
DR   Pfam; PF00365; PFK; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; Phosphofructokinase; 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:UP000008311};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_03186}.
FT   DOMAIN          106..412
FT                   /note="Phosphofructokinase"
FT                   /evidence="ECO:0000259|Pfam:PF00365"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        231
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT   BINDING         112
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT   BINDING         175..176
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT   BINDING         200..203
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT   BINDING         201
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT   BINDING         229..231
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT   BINDING         274..276
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT   BINDING         330
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT   BINDING         388..391
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
FT   SITE            202
FT                   /note="Important for substrate specificity; cannot use PPi
FT                   as phosphoryl donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03186"
SQ   SEQUENCE   561 AA;  62130 MW;  B3D62344D6BB0B7D CRC64;
     MASALPEDTD PALTSRNSEE PIPSHPFNLQ KPSHLTDYLK GLKSCTNPLD NNPFYRPIEG
     FYITQTDVIL RQTILDFSTI LSPRFAYHRA GPRKRIFFDP GTTCAAIVTC GGLCPGMNTV
     IRELVVGLWE LYGVRKIFGV VAGYRGFYSR EPIELNPKLV HNWHKKGGTV LETSRGGFDL
     HKIVDAIQSR GFNQVYIIGG DGTMRGAVKI FNEIRQRKLN IGVAGIPKTV DNDIGVIDKS
     FGFQTAVEMA QQAINAAHVE AESAVNGIGL VKLMGRSTGH IALHATLSSR DVDCCLIPEI
     DFYLEGKGGL FEFLEKRLQE NGHAVLVVAE GAGQDKIPRT EAQKEERDES GNPVFLDVGA
     WLKSELKNWW SRDHPTELFT VKHIDPTYMI RAVPANATDN LYCTLLAHSA IHGVMAGYTG
     FVCGPINGNF GYIPLEEVAE AKNEVNLKDH KWAWVRSVTN QPGFVRSVLK VHHVGLICKR
     LPSIVSLSYM TGTPRENNRV LKWKGILTSG IRERERKRGG LELQCNCEIR NPGWTLNCLV
     MCNALLGSIL LSAEETKLIG V
//
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