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Database: UniProt
Entry: A0A0E3SS17_METMT
LinkDB: A0A0E3SS17_METMT
Original site: A0A0E3SS17_METMT 
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
//
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