ID A0A1D7V3N2_9LEPT Unreviewed; 431 AA.
AC A0A1D7V3N2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=ATP-dependent 6-phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01981};
DE Short=ATP-PFK {ECO:0000256|HAMAP-Rule:MF_01981};
DE Short=Phosphofructokinase {ECO:0000256|HAMAP-Rule:MF_01981};
DE EC=2.7.1.11 {ECO:0000256|HAMAP-Rule:MF_01981};
DE AltName: Full=Phosphohexokinase {ECO:0000256|HAMAP-Rule:MF_01981};
GN Name=pfkA {ECO:0000256|HAMAP-Rule:MF_01981};
GN ORFNames=A0128_20720 {ECO:0000313|EMBL:AOP36438.1};
OS Leptospira tipperaryensis.
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=2564040 {ECO:0000313|EMBL:AOP36438.1, ECO:0000313|Proteomes:UP000094197};
RN [1] {ECO:0000313|EMBL:AOP36438.1, ECO:0000313|Proteomes:UP000094197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GWTS #1 {ECO:0000313|EMBL:AOP36438.1,
RC ECO:0000313|Proteomes:UP000094197};
RA Nally J.E., Bayles D.O., Hurley D., Fanning S., McMahon B.J., Arent Z.;
RT "Complete genome seqeunce of Leptospira alstonii serovar Room22.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation of D-fructose 6-phosphate to
CC fructose 1,6-bisphosphate by ATP, the first committing step of
CC glycolysis. {ECO:0000256|HAMAP-Rule:MF_01981}.
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, ECO:0000256|HAMAP-
CC Rule:MF_01981};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|HAMAP-Rule:MF_01981};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 3/4.
CC {ECO:0000256|HAMAP-Rule:MF_01981}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01981}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01981}.
CC -!- SIMILARITY: Belongs to the phosphofructokinase type A (PFKA) family.
CC PPi-dependent PFK group II subfamily. Atypical ATP-dependent clade 'X'
CC sub-subfamily. {ECO:0000256|HAMAP-Rule:MF_01981}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP015218; AOP36438.1; -; Genomic_DNA.
DR RefSeq; WP_069609656.1; NZ_CP015218.1.
DR AlphaFoldDB; A0A1D7V3N2; -.
DR KEGG; laj:A0128_20720; -.
DR OrthoDB; 9802503at2; -.
DR UniPathway; UPA00109; UER00182.
DR Proteomes; UP000094197; Chromosome 2.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003872; F:6-phosphofructokinase activity; IEA:UniProtKB-UniRule.
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; -; 1.
DR HAMAP; MF_01981; Phosphofructokinase_II_X; 1.
DR InterPro; IPR022953; ATP_PFK.
DR InterPro; IPR000023; Phosphofructokinase_dom.
DR InterPro; IPR035966; PKF_sf.
DR InterPro; IPR012004; PyroP-dep_PFK_TP0108.
DR PANTHER; PTHR45770; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 1; 1.
DR PANTHER; PTHR45770:SF11; ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 1; 1.
DR Pfam; PF00365; PFK; 1.
DR PIRSF; PIRSF000534; PPi_PFK_TP0108; 1.
DR PRINTS; PR00476; PHFRCTKINASE.
DR SUPFAM; SSF53784; Phosphofructokinase; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01981};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01981};
KW Glycolysis {ECO:0000256|HAMAP-Rule:MF_01981};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01981};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01981};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01981}; Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01981};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01981}.
FT DOMAIN 70..375
FT /note="Phosphofructokinase"
FT /evidence="ECO:0000259|Pfam:PF00365"
FT ACT_SITE 199
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 143..144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 168..171
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 169
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 197..199
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 242..244
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT BINDING 350..353
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
FT SITE 170
FT /note="Important for substrate specificity; cannot use PPi
FT as phosphoryl donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01981"
SQ SEQUENCE 431 AA; 47598 MW; 77B864A766DE1BC0 CRC64;
METKIKNFGE CTVPSPADYE YYTSDSSRLL FRTVFQSKED WNSYIESGPD FFEQAGPREK
IFFRPKEVTA GIVTCGGLCP GINDVIRGIV MELFYRYGVS RILGFPFGYQ GLVKKYSHKP
IELTPERVAH IVEEGGSMLG SSRGNQSPED MVDYLSLYGV KVLFCIGGDG TLRGAREIVD
EIAKRGEEIS VIGIPKTIDN DINYVQKTFG FSTAFSKAME AVECAHVEAK GAPNGIGLVK
LMGRHSGFIA VNAALASRNV NYCLIPEVNF DLHGNGAFLD ELKKRIQKKG HAVIIAAEGA
GQHFFEITGE RDPSGNLKLK DIGIFLKDTM TDFFKKENIP VNIKYIDPSY IIRSIPADPE
DSVFCGFLAQ NAVHAAMAGK TDMVVGMWNN VFTHLPISVA IQERKVLQPD RSTLWRSLLA
STGQPAHMLA K
//
