ID C7P5E2_METFA Unreviewed; 458 AA.
AC C7P5E2;
DT 13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT 13-OCT-2009, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=ADP-specific phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_00561};
DE EC=2.7.1.146 {ECO:0000256|HAMAP-Rule:MF_00561};
DE AltName: Full=ADP-dependent phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_00561};
DE Short=ADP-Pfk {ECO:0000256|HAMAP-Rule:MF_00561};
GN Name=pfkC {ECO:0000256|HAMAP-Rule:MF_00561};
GN OrderedLocusNames=Mefer_1517 {ECO:0000313|EMBL:ACV25320.1};
OS Methanocaldococcus fervens (strain DSM 4213 / JCM 15782 / AG86)
OS (Methanococcus fervens).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=573064 {ECO:0000313|EMBL:ACV25320.1, ECO:0000313|Proteomes:UP000001495};
RN [1] {ECO:0000313|EMBL:ACV25320.1, ECO:0000313|Proteomes:UP000001495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4213 / JCM 15782 / AG86
RC {ECO:0000313|Proteomes:UP000001495};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA Lupa-Sieprawska M., Whitman W.B.;
RT "Complete sequence of chromosome of Methanocaldococcus fervens AG86.";
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation of fructose 6-phosphate to
CC fructose 1,6-bisphosphate using ADP as the phosphate donor.
CC {ECO:0000256|HAMAP-Rule:MF_00561}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP + beta-D-fructose 6-phosphate = AMP + beta-D-fructose 1,6-
CC bisphosphate + H(+); Xref=Rhea:RHEA:20105, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:57634, ChEBI:CHEBI:456215,
CC ChEBI:CHEBI:456216; EC=2.7.1.146; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00561};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00561};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00561};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis. {ECO:0000256|HAMAP-
CC Rule:MF_00561}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00561}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkC family.
CC {ECO:0000256|HAMAP-Rule:MF_00561}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001696; ACV25320.1; -; Genomic_DNA.
DR RefSeq; WP_015792053.1; NC_013156.1.
DR AlphaFoldDB; C7P5E2; -.
DR STRING; 573064.Mefer_1517; -.
DR GeneID; 8366223; -.
DR KEGG; mfe:Mefer_1517; -.
DR eggNOG; arCOG03370; Archaea.
DR HOGENOM; CLU_046643_0_0_2; -.
DR OrthoDB; 85200at2157; -.
DR UniPathway; UPA00109; -.
DR Proteomes; UP000001495; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0043844; F:ADP-specific phosphofructokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0008443; F:phosphofructokinase activity; IEA:InterPro.
DR GO; GO:0006000; P:fructose metabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.1110.20; -; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR HAMAP; MF_00561; ADP_PFKinase; 1.
DR InterPro; IPR007666; ADP_PFK/GK.
DR InterPro; IPR015990; ADP_PFK/GK_arc.
DR InterPro; IPR011790; ADP_PFK_arc.
DR InterPro; IPR029056; Ribokinase-like.
DR NCBIfam; TIGR02045; P_fruct_ADP; 1.
DR PANTHER; PTHR21208; ADP-DEPENDENT GLUCOKINASE; 1.
DR PANTHER; PTHR21208:SF1; ADP-DEPENDENT GLUCOKINASE; 1.
DR Pfam; PF04587; ADP_PFK_GK; 1.
DR PIRSF; PIRSF015883; ADP-Pfk_glckin; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
DR PROSITE; PS51255; ADPK; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00561};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW Rule:MF_00561};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00561};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00561};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00561};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00561}.
FT ACT_SITE 438
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00561"
FT BINDING 268
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00561"
FT BINDING 298
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00561"
FT BINDING 438
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00561"
SQ SEQUENCE 458 AA; 52630 MW; 802D67B4877553D2 CRC64;
MVVNKFIETI KETKLFTAYN TNVDAIKYLN DEDVQKLVDE FNHEDIIKRM EEYPRIIEEP
LDFVARLVYS IKTGKPAEVP LKDKKELQDW FNKIKYDEER MGGQAGIVSN LMATLQIDKI
IVYTPFLSKK QAEMFIDYDN LLYPSVENGN LVLKKVRESY RDDPLKINRI FEFKKGLKFK
LAGEEVTAKQ STRFIVASRP EALRIEIKDG VRSFLPEIGE MVDCAFLSGY QAIKEKYSDG
KTAEYYFKRA KEDIKLLKKN KDIKAHLEFA SISDIKIREM VVDYILSSVN SVGMDETEIA
NVLHILGYEN LSNKILKDSF VEDVIEGAKI LLDRFKNLEV VQVHTIYYIL FVCRADNPLS
KKELEECLEF STILASTRAK LGNIKSIDDL YEGLKVPHNK YGDLLKEIAE KLNGDNYKIA
LSPSRYVEKP KSTVGLGDTI SSGAFVYYVS LLKKKENE
//
