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Database: UniProt
Entry: A0A0K1F8I0_9MICO
LinkDB: A0A0K1F8I0_9MICO
Original site: A0A0K1F8I0_9MICO 
ID   A0A0K1F8I0_9MICO        Unreviewed;       748 AA.
AC   A0A0K1F8I0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=6-phosphofructokinase {ECO:0000256|ARBA:ARBA00012055};
DE            EC=2.7.1.11 {ECO:0000256|ARBA:ARBA00012055};
GN   ORFNames=ADJ73_04230 {ECO:0000313|EMBL:AKT50712.1};
OS   Arsenicicoccus sp. oral taxon 190.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Arsenicicoccus.
OX   NCBI_TaxID=1658671 {ECO:0000313|EMBL:AKT50712.1, ECO:0000313|Proteomes:UP000065578};
RN   [1] {ECO:0000313|Proteomes:UP000065578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0371 {ECO:0000313|Proteomes:UP000065578};
RA   Holder M.E., Ajami N.J., Petrosino J.F.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 1,6-
CC         bisphosphate + H(+); Xref=Rhea:RHEA:16109, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:57634,
CC         ChEBI:CHEBI:456216; EC=2.7.1.11;
CC         Evidence={ECO:0000256|ARBA:ARBA00000432};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 3/4.
CC       {ECO:0000256|ARBA:ARBA00004679}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC       {ECO:0000256|ARBA:ARBA00038478}.
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DR   EMBL; CP012070; AKT50712.1; -; Genomic_DNA.
DR   RefSeq; WP_050347234.1; NZ_CP012070.1.
DR   AlphaFoldDB; A0A0K1F8I0; -.
DR   STRING; 1658671.ADJ73_04230; -.
DR   KEGG; ars:ADJ73_04230; -.
DR   PATRIC; fig|1658671.3.peg.849; -.
DR   OrthoDB; 9802503at2; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000065578; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006002; P:fructose 6-phosphate metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.450; -; 2.
DR   Gene3D; 3.40.50.460; Phosphofructokinase domain; 2.
DR   InterPro; IPR009161; 6-Pfructokinase_euk.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR035966; PKF_sf.
DR   NCBIfam; TIGR02478; 6PF1K_euk; 1.
DR   PANTHER; PTHR13697:SF4; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE; 1.
DR   PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1.
DR   Pfam; PF00365; PFK; 2.
DR   PIRSF; PIRSF000533; ATP_PFK_euk; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; Phosphofructokinase; 2.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 2.
PE   3: Inferred from homology;
KW   Allosteric enzyme {ECO:0000256|ARBA:ARBA00022533};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AKT50712.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          12..317
FT                   /note="Phosphofructokinase"
FT                   /evidence="ECO:0000259|Pfam:PF00365"
FT   DOMAIN          397..682
FT                   /note="Phosphofructokinase"
FT                   /evidence="ECO:0000259|Pfam:PF00365"
SQ   SEQUENCE   748 AA;  80544 MW;  4A52213E8B50CC9C CRC64;
     METVHETAPR MRIAVLTSGG DAQGMNAAVR AVVRTALHLG AEVFVIYEGY QGMVDGGDGI
     RLAGWDDVGN VLHRGGTVIG TFRSADFRER AGRMAAAAHL LEHGIDRLVV IGGDGSLSGL
     DLFRQEWPGL LADLVEQGRI SAATAAAHPT LMIAGLVGSI DNDLVGTDMT IGADSALHRI
     VDAIDAIAST AASHQRSFVV EVMGRHCGYL ALMSAIAGGC DYVLIPEHPP APGWEERMCA
     ELRRGRAAGR RDSIVIVAEG AQDRDGRPIT AAYVRDTIEQ RLGEDTRVTI LGHVQRGGRP
     SAFDRWASTW LGYAAAHEVL SATAETVAPV VGIRGNRVVT VPLVEAVERT REVPAAIASG
     DYARAMALRG GSFTEMTQIF TEMSEPPTPQ VDGTPRRIGI LHAGGLAPGM NTAARAAVRL
     GLDRGHTMLG IQGGYPGLRD GDIRELAWGD VEGWTAIGGA ELGVRRSLPE VEHLYPIGRA
     LEEHRVDALL VIGGWNAYVG AQTLWQERDR YPAFRIPMVC VPASIDNNLP GSELAVGADT
     ALNAIVDALD RIKQSASARR RCFVVETMGR YCGYLALMGG LAGGAERVYL HEEGITLDDL
     QRDVQRLRSS FDAGRRLFLA VRNERSSEQY TLDFLARLFD QEGQERYDVR QAVLGHVQQG
     GDPSPFDRIL ATRLVAHAID LLTGELAAGG QEAQLVGLVR GRVRATPLAR MPELMDLVHR
     RPRDQWWLDL RPVVRAVSEP GAAAPTGL
//
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