ID   A6VGN3_METM7            Unreviewed;       463 AA.
AC   A6VGN3;
DT   21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT   21-AUG-2007, sequence version 1.
DT   27-MAR-2024, entry version 80.
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=MmarC7_0541 {ECO:0000313|EMBL:ABR65609.1};
OS   Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=426368 {ECO:0000313|EMBL:ABR65609.1};
RN   [1] {ECO:0000313|EMBL:ABR65609.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C7 {ECO:0000313|EMBL:ABR65609.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C7.";
RL   Submitted (JUN-2007) 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; Evidence={ECO:0000256|HAMAP-
CC         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}.
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DR   EMBL; CP000745; ABR65609.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6VGN3; -.
DR   STRING; 426368.MmarC7_0541; -.
DR   KEGG; mmz:MmarC7_0541; -.
DR   eggNOG; arCOG03370; Archaea.
DR   HOGENOM; CLU_046643_0_0_2; -.
DR   OrthoDB; 85200at2157; -.
DR   UniPathway; UPA00109; -.
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        443
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00561"
FT   BINDING         270
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00561"
FT   BINDING         300
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00561"
FT   BINDING         443
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00561"
SQ   SEQUENCE   463 AA;  52795 MW;  93D70076E27F12C3 CRC64;
     MELLNQFKNF SNVSIFLAYN VNVDALKYLA DSSDIEKLKE NFSDSDIGLK IEEYPRTIEK
     PIDFVARLIH AMKSGKPAEV PLKNNLEIEP FFNGLNYNEE RIGGQVGIIS NLLSILNLKR
     IIFYSPILAK KQAEMFENNE NLVFPNLIDG KLVLKKPIES FKNDELKINR IFEYKEDIEF
     HLQNEKIITP RSNRFIVASR PENLRIEIEK GLKNHLPDIG RLVDCAIISG VQAIKEEYSD
     GKTAEYYLNR VKEDIKLLKK ENKDLKVHFE FASIQNTEMR KKIAESILPE VDCVGMDETE
     IANIIHVLGY EELSEGILKY SRIEDVLKAS KILLERYNLE GMQVHTLYYI MYLCKKGGIL
     SDKSLEKTLE FATILASTKA ALGQISNVGD LKIGLEIPHN KHGQLLKELV EKISKEKELE
     DYRIILVPSR IVENPKSTVG LGDTISAGAF VGYVSELKKL KNK
//