K6PF_METAC
ID K6PF_METAC Reviewed; 491 AA.
AC P58847;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 06-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=ADP-specific phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_00561};
DE EC=2.7.1.146 {ECO:0000255|HAMAP-Rule:MF_00561};
DE AltName: Full=ADP-dependent phosphofructokinase {ECO:0000255|HAMAP-Rule:MF_00561};
DE Short=ADP-Pfk {ECO:0000255|HAMAP-Rule:MF_00561};
GN Name=pfkC {ECO:0000255|HAMAP-Rule:MF_00561}; Synonyms=pfk;
GN OrderedLocusNames=MA_3563;
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
CC -!- FUNCTION: Catalyzes the phosphorylation of fructose 6-phosphate to
CC fructose 1,6-bisphosphate using ADP as the phosphate donor.
CC {ECO:0000255|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:0000255|HAMAP-
CC Rule:MF_00561};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00561};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00561};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis. {ECO:0000255|HAMAP-
CC Rule:MF_00561}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00561}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkC family.
CC {ECO:0000255|HAMAP-Rule:MF_00561}.
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DR EMBL; AE010299; AAM06924.1; -; Genomic_DNA.
DR RefSeq; WP_011023477.1; NC_003552.1.
DR AlphaFoldDB; P58847; -.
DR SMR; P58847; -.
DR STRING; 188937.MA_3563; -.
DR EnsemblBacteria; AAM06924; AAM06924; MA_3563.
DR GeneID; 1475456; -.
DR KEGG; mac:MA_3563; -.
DR HOGENOM; CLU_046643_0_0_2; -.
DR InParanoid; P58847; -.
DR OMA; NRIFEFR; -.
DR OrthoDB; 15153at2157; -.
DR PhylomeDB; P58847; -.
DR UniPathway; UPA00109; -.
DR Proteomes; UP000002487; 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:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0006000; P:fructose metabolic process; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
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 PANTHER; PTHR21208; PTHR21208; 1.
DR Pfam; PF04587; ADP_PFK_GK; 1.
DR PIRSF; PIRSF015883; ADP-Pfk_glckin; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
DR TIGRFAMs; TIGR02045; P_fruct_ADP; 1.
DR PROSITE; PS51255; ADPK; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Glycolysis; Kinase; Magnesium; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..491
FT /note="ADP-specific phosphofructokinase"
FT /id="PRO_0000184763"
FT DOMAIN 4..486
FT /note="ADPK"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00561"
FT ACT_SITE 470
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00561"
FT BINDING 281
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00561"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00561"
FT BINDING 470
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00561"
SQ SEQUENCE 491 AA; 54937 MW; 70C466A81977677F CRC64;
MDIEEWEQRH AEAFYNAKEA LPYLDGMFVA YNSNIDAIRH LTEEDLSKLV GFFDESDIQD
RVAAYPREIA EPLDFVARLL ISMREGKAAE VPAYTADIHE WLKEHLGFDY ARMGGQAGII
SNLLGRLGLK KVVAYVPWLS EEQAEYFTAT GNILHPKVEN GKVLLKPPGE AFKPGIGSKV
NWILEYSKDM NVTCAGNTFK VPRDNRLIIS SRPKWLRLDM DKQIYEQLDT LLPVDGAMLS
GYQMIKEEYE DGSTYKDYVE NSVKVIEKLK SLNPELRIHV ELTSIQNRLI RKAILTEIVA
RHVHSLGLDT VEVANALNVL GHEELSYSVI RKGENGIMSL YQGAVQLMKD LDLERVHVHS
LGFYICILAK GHPLTLKEHR DSLLFSSVLA AAQALNGNIE NLAEAEAGLE VPVSSIGLED
LENFQLYCTG RKLCTPDEFE YGYVYGSEHD AILIPSKVVE RPKATVGIGD TISAGAFVAM
LAKIKQKHSG K
