ID A0A0E3SS17_METMT Unreviewed; 486 AA.
AC A0A0E3SS17;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
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 ORFNames=MCMEM_1828 {ECO:0000313|EMBL:AKB85881.1};
OS Methanococcoides methylutens MM1.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanococcoides.
OX NCBI_TaxID=1434104 {ECO:0000313|EMBL:AKB85881.1, ECO:0000313|Proteomes:UP000033048};
RN [1] {ECO:0000313|EMBL:AKB85881.1, ECO:0000313|Proteomes:UP000033048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MM1 {ECO:0000313|EMBL:AKB85881.1,
RC ECO:0000313|Proteomes:UP000033048};
RA Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT "Methanogenic archaea and the global carbon cycle.";
RL Submitted (JUL-2014) 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}.
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DR EMBL; CP009518; AKB85881.1; -; Genomic_DNA.
DR RefSeq; WP_048205917.1; NZ_CP009518.1.
DR AlphaFoldDB; A0A0E3SS17; -.
DR STRING; 1434104.MCMEM_1828; -.
DR GeneID; 24894401; -.
DR KEGG; mmet:MCMEM_1828; -.
DR PATRIC; fig|1434104.5.peg.1984; -.
DR HOGENOM; CLU_046643_0_0_2; -.
DR OrthoDB; 85200at2157; -.
DR UniPathway; UPA00109; -.
DR Proteomes; UP000033048; 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 2; 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|HAMAP-Rule:MF_00561, ECO:0000313|EMBL:AKB85881.1};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00561};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00561};
KW Reference proteome {ECO:0000313|Proteomes:UP000033048};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00561, ECO:0000313|EMBL:AKB85881.1}.
FT ACT_SITE 471
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00561"
FT BINDING 282
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00561"
FT BINDING 313
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00561"
FT BINDING 471
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00561"
SQ SEQUENCE 486 AA; 54426 MW; 2124FF0A84F96796 CRC64;
MEIGEWDSVY HKSYEDIRSS IGNVRGIFVA YNSNIDAIKH VGPGDIEHLL MNVDISEVRE
KVFEYPRQID SPSDLVARLI IAMRDGKAAE VPTNTTEIHD WLTDHLVFDN ARMGGQAGII
SNLLASMDIR KVITYVPWLS EEQAEYFVDS DNLLFPVVEN NELVLKHPKE AFDPENKPKV
NWILEFSKGM EVKFAGEHFI VPRDNRLIIS SRPKWIRIEM APELYERIPQ LQADIDGAIL
AGYQMIKEEY EDGSTYIDYV EKAVNVIEEL KEGNPDIRIH VEFTSIQNKV IRTAILNHIV
RKHVHSLGLD TVEVANVLNV LGFEELAYSV INKGENAIIS LYEGAVKLLR DLQLERVHIH
SLGFYICLVS KDCPVSVEDH RNALLFGSTV AAAKASLGEI LSLESTESGL QVPVSDEGHG
ELEKLEKHLV RSGMSSMEDF ENGCICTPWY DAIIVPTKVV SEPVATVGIG DAISATSFVG
FLSKLK
//