ID Q8PZL9_METMA Unreviewed; 491 AA.
AC Q8PZL9;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 112.
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=MM_0473 {ECO:0000313|EMBL:AAM30169.1};
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952 {ECO:0000313|EMBL:AAM30169.1, ECO:0000313|Proteomes:UP000000595};
RN [1] {ECO:0000313|EMBL:AAM30169.1, ECO:0000313|Proteomes:UP000000595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88
RC {ECO:0000313|Proteomes:UP000000595};
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baumer S., Jacobi C.,
RA Bruggemann H., Lienard T., Christmann A., Bomeke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.P., Gunsalus R.P.,
RA Fritz H.J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
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; AE008384; AAM30169.1; -; Genomic_DNA.
DR RefSeq; WP_011032426.1; NC_003901.1.
DR AlphaFoldDB; Q8PZL9; -.
DR GeneID; 82159483; -.
DR KEGG; mma:MM_0473; -.
DR PATRIC; fig|192952.21.peg.569; -.
DR eggNOG; arCOG03370; Archaea.
DR HOGENOM; CLU_046643_0_0_2; -.
DR BRENDA; 2.7.1.146; 3270.
DR BRENDA; 2.7.1.147; 3270.
DR UniPathway; UPA00109; -.
DR Proteomes; UP000000595; 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 470
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00561"
FT BINDING 281
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00561"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00561"
FT BINDING 470
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00561"
SQ SEQUENCE 491 AA; 55292 MW; 7DCD9C0E9414C731 CRC64;
MDMEEWEQRH NEAFYDAKEA LPYLDGMFVA YNSNIDAIRH LDEEALTKLI GFFDEAEIQE
RVAVYPREIA DPLDFIARLL IAMREGKAAE VPTYTEEIHT WLKEHLGFDY ARMGGQAGII
SNLLARLDLK KVVAYIPWLS AEQAEYFEDN GNILHPKVEN GEVVLKTPAE AFNPGMGSKV
NWIFEFSKDL KVSCAGSTFK VPRDNRLIIS SRPKWIRLDM DRAIYDQLET IFPVDGAMLS
GYQMIKEEYE DGSTYKDYVE HSVEVINKLK SLNPDLRIHV ELTSIQNRVI RKAILTEIVA
RHVHSLGLDT VEVANALNVL GYEELSYSVI RKGENGIMSL YQGAVQLMKD LKLERVHVHS
LGFYICILAK GHPLTLKEHR DALLFSSVLA ASRALHGKIE DLNEAETGLD VPVSAQGLED
LETFKLYCTG RKLCSPDEFE YGYIYGSDHD AILIPSKVVD RPKATVGIGD TISAGAFAAM
LARMKQIKSG K
//
