ID F4NXT6_BATDJ Unreviewed; 783 AA.
AC F4NXT6;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=6-phosphofructokinase {ECO:0000256|ARBA:ARBA00012055, ECO:0000256|PIRNR:PIRNR000533};
DE EC=2.7.1.11 {ECO:0000256|ARBA:ARBA00012055, ECO:0000256|PIRNR:PIRNR000533};
DE AltName: Full=Phosphohexokinase {ECO:0000256|PIRNR:PIRNR000533};
GN ORFNames=BATDEDRAFT_29700 {ECO:0000313|EMBL:EGF81904.1};
OS Batrachochytrium dendrobatidis (strain JAM81 / FGSC 10211) (Frog chytrid
OS fungus).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Chytridiomycetes; Rhizophydiales;
OC Rhizophydiales incertae sedis; Batrachochytrium.
OX NCBI_TaxID=684364 {ECO:0000313|EMBL:EGF81904.1, ECO:0000313|Proteomes:UP000007241};
RN [1] {ECO:0000313|EMBL:EGF81904.1, ECO:0000313|Proteomes:UP000007241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAM81 / FGSC 10211 {ECO:0000313|Proteomes:UP000007241};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Kuo A., Salamov A., Schmutz J., Lucas S., Pitluck S., Rosenblum E.,
RA Stajich J., Eisen M., Grigoriev I.V.;
RT "The draft genome of Batrachochytrium dendrobatidis.";
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
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,
CC ECO:0000256|PIRNR:PIRNR000533};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC {ECO:0000256|ARBA:ARBA00004679, ECO:0000256|PIRNR:PIRNR000533}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC ATP-dependent PFK group I subfamily. Eukaryotic two domain clade "E"
CC sub-subfamily. {ECO:0000256|PIRNR:PIRNR000533}.
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DR EMBL; GL882881; EGF81904.1; -; Genomic_DNA.
DR RefSeq; XP_006677372.1; XM_006677309.1.
DR AlphaFoldDB; F4NXT6; -.
DR STRING; 684364.F4NXT6; -.
DR GeneID; 18239907; -.
DR HOGENOM; CLU_011053_0_0_1; -.
DR InParanoid; F4NXT6; -.
DR OMA; EWQDQMC; -.
DR OrthoDB; 374214at2759; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000007241; Unassembled WGS sequence.
DR GO; GO:0005945; C:6-phosphofructokinase complex; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IBA:GO_Central.
DR GO; GO:0016208; F:AMP binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR GO; GO:0070095; F:fructose-6-phosphate binding; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0048029; F:monosaccharide binding; IBA:GO_Central.
DR GO; GO:0061621; P:canonical glycolysis; IBA:GO_Central.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR Gene3D; 3.40.50.450; -; 2.
DR Gene3D; 3.40.50.460; Phosphofructokinase domain; 2.
DR InterPro; IPR009161; 6-Pfructokinase_euk.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR015912; Phosphofructokinase_CS.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR NCBIfam; TIGR02478; 6PF1K_euk; 1.
DR PANTHER; PTHR13697:SF4; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE; 1.
DR PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1.
DR Pfam; PF00365; PFK; 2.
DR PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; Phosphofructokinase; 2.
DR PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
PE 3: Inferred from homology;
KW Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR000533};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|PIRNR:PIRNR000533};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|PIRNR:PIRNR000533};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR000533};
KW Reference proteome {ECO:0000313|Proteomes:UP000007241};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000533}.
FT DOMAIN 1..312
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT DOMAIN 394..686
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
SQ SEQUENCE 783 AA; 85082 MW; 7177F3D542B4691E CRC64;
MNAAVRAIVR VALQRNCLPF AIFEGYQGLV DGGDKIKAMS WENVRGFLAV GGTSIGTARC
SAFRTRQGRL DATYNLIKNG IDALVIIGGD GSLTGADILR AEWATLVDEL IKQGNAFYYT
FNVGRLTKEE SEHLRSDLTI VGLVGSIDND MSATDITIGA VTSLHRICEA VDSLTSTAQS
HKRAFVVEVM GRHCGWLGLM AGIAVGADWV CLPERPPPLD NKYGDDWAEE MVDIVKQYRS
MGNRKSIIIV CEGAIDRNLK PIKPEEVKQI LEERLGLDTR VTTLGHVQRG GSPCAFDRYL
ATVQGVEAVE AVLSSTPNTP AAMIGMSQNK VISVPLMDAV KLTQSVAQAI SHKDFKHAME
LRDPDFTSAF GAYMESTLIG CPGSLQVPVE KRLRIGIIHC GAPAGGMNAA TRVAASLSLN
RGHVPLAIRN GFTGLVNDEV HPFQWQEIVG WQVRGGSELG TNRIDNFVDM GLIAYHMQKH
DIQALMIIGG FEAYTAQLTL TEARKVYPAF AIPMIHLPAT VSNNVPGTDY SIGCDTALNV
IVESCDRLKL SANASRKRVF VVEVQGGTCG YLATLGGLTV GATTVYIPEQ EIGIKILQKD
IKHLCKRYTE DQRNGVNSEG RVILRTESTL PEVYSTEVIS GILRAEGKGL FDSRTAVLGH
LQQGGVPSPL DRIRATRLAV KCIDWLEAVA CHVRTEGGSG STNHLNMSSD DIAKRAGMSI
YTIEKNHSAV IGIRGALVVF SPIEDLVAEV DMKARRTKDA WWMGLGKLIR VLSKYEYDDV
KSN
//