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Database: UniProt
Entry: K6Z317_9ALTE
LinkDB: K6Z317_9ALTE
Original site: K6Z317_9ALTE 
ID   K6Z317_9ALTE            Unreviewed;       323 AA.
AC   K6Z317;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=6-phosphofructokinase {ECO:0000256|ARBA:ARBA00012055};
DE            EC=2.7.1.11 {ECO:0000256|ARBA:ARBA00012055};
GN   Name=pfkA1 {ECO:0000313|EMBL:GAC30636.1};
GN   ORFNames=GPAL_3796 {ECO:0000313|EMBL:GAC30636.1};
OS   Glaciecola pallidula DSM 14239 = ACAM 615.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Alteromonadaceae; Glaciecola.
OX   NCBI_TaxID=1121922 {ECO:0000313|EMBL:GAC30636.1, ECO:0000313|Proteomes:UP000006251};
RN   [1] {ECO:0000313|EMBL:GAC30636.1, ECO:0000313|Proteomes:UP000006251}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ACAM 615 {ECO:0000313|EMBL:GAC30636.1,
RC   ECO:0000313|Proteomes:UP000006251};
RX   PubMed=25009843;
RA   Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA   Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT   "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT   high degree of genomic diversity and genomic characteristic for cold
RT   adaptation.";
RL   Environ. Microbiol. 16:1642-1653(2014).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAC30636.1}.
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DR   EMBL; BAEQ01000065; GAC30636.1; -; Genomic_DNA.
DR   RefSeq; WP_006015067.1; NZ_KE386819.1.
DR   AlphaFoldDB; K6Z317; -.
DR   STRING; 1121922.GCA_000428905_03326; -.
DR   OrthoDB; 9802503at2; -.
DR   UniPathway; UPA00109; UER00182.
DR   Proteomes; UP000006251; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047334; F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity; IEA:UniProtKB-EC.
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; -; 1.
DR   Gene3D; 3.40.50.460; Phosphofructokinase domain; 1.
DR   InterPro; IPR022953; ATP_PFK.
DR   InterPro; IPR012003; ATP_PFK_prok-type.
DR   InterPro; IPR015912; Phosphofructokinase_CS.
DR   InterPro; IPR000023; Phosphofructokinase_dom.
DR   InterPro; IPR035966; PKF_sf.
DR   PANTHER; PTHR13697:SF4; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE; 1.
DR   PANTHER; PTHR13697; PHOSPHOFRUCTOKINASE; 1.
DR   Pfam; PF00365; PFK; 1.
DR   PIRSF; PIRSF000532; ATP_PFK_prok; 1.
DR   PRINTS; PR00476; PHFRCTKINASE.
DR   SUPFAM; SSF53784; Phosphofructokinase; 1.
DR   PROSITE; PS00433; PHOSPHOFRUCTOKINASE; 1.
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:GAC30636.1};
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          8..279
FT                   /note="Phosphofructokinase"
FT                   /evidence="ECO:0000259|Pfam:PF00365"
SQ   SEQUENCE   323 AA;  34765 MW;  EE0995713E791DCD CRC64;
     MVSKIKHIGI FTSGGDAPGM NAALFAVAKT AESYGIKLSG IRRGFEGLID NDLIPLNSRQ
     LQRIMHLGGT LLKTARSDRF MTALGQQKAL RTVQKNNLDA LIAIGGDGTF RGMLSLANIG
     NTPFIGIPGT IDNDITGTDY TLGFDSAVNT AIKCIDNIRD TAESHNRVFL VEVMGRDSGY
     IGIYSGLSCG ADSILIPESD EDITYLLNKI KNYDSEDAFI VVVAEGDALR VEEVMSQIRN
     VNPHIELRVA KLGHIQRGGN PSAQDRMLGI RLGVLATTAL IEGESGKIAG FCNNKPSLSP
     FEGLVKKHLI NTELKDLLTL FCG
//
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