ID N0AXG6_9BACI Unreviewed; 308 AA.
AC N0AXG6;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=1-phosphofructokinase {ECO:0000256|ARBA:ARBA00013596, ECO:0000256|RuleBase:RU369061};
DE Short=Fru1PK {ECO:0000256|RuleBase:RU369061};
DE EC=2.7.1.56 {ECO:0000256|ARBA:ARBA00012131, ECO:0000256|RuleBase:RU369061};
DE AltName: Full=Fructose 1-phosphate kinase {ECO:0000256|ARBA:ARBA00032802, ECO:0000256|RuleBase:RU369061};
GN ORFNames=B1NLA3E_06835 {ECO:0000313|EMBL:AGK53131.1};
OS Bacillus sp. 1NLA3E.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=666686 {ECO:0000313|EMBL:AGK53131.1, ECO:0000313|Proteomes:UP000013300};
RN [1] {ECO:0000313|EMBL:AGK53131.1, ECO:0000313|Proteomes:UP000013300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1NLA3E {ECO:0000313|EMBL:AGK53131.1};
RX PubMed=23833140;
RA Venkatramanan R., Prakash O., Woyke T., Chain P., Goodwin L.A., Watson D.,
RA Brooks S., Kostka J.E., Green S.J.;
RT "Genome sequences for three denitrifying bacterial strains isolated from a
RT uranium- and nitrate-contaminated subsurface environment.";
RL Genome Announc. 1:e00449-13(2013).
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of fructose-l-
CC phosphate to fructose-l,6-bisphosphate.
CC {ECO:0000256|RuleBase:RU369061}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-D-fructose 1-phosphate = ADP + beta-D-fructose 1,6-
CC bisphosphate + H(+); Xref=Rhea:RHEA:14213, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:32966, ChEBI:CHEBI:138881,
CC ChEBI:CHEBI:456216; EC=2.7.1.56;
CC Evidence={ECO:0000256|ARBA:ARBA00000823,
CC ECO:0000256|RuleBase:RU369061};
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000256|ARBA:ARBA00010688, ECO:0000256|RuleBase:RU369061}.
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DR EMBL; CP005586; AGK53131.1; -; Genomic_DNA.
DR RefSeq; WP_015593191.1; NC_021171.1.
DR AlphaFoldDB; N0AXG6; -.
DR STRING; 666686.B1NLA3E_06835; -.
DR KEGG; baci:B1NLA3E_06835; -.
DR eggNOG; COG1105; Bacteria.
DR HOGENOM; CLU_050013_1_0_9; -.
DR OrthoDB; 9801219at2; -.
DR Proteomes; UP000013300; Chromosome.
DR GO; GO:0008662; F:1-phosphofructokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR CDD; cd01164; FruK_PfkB_like; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR022463; 1-PFruKinase.
DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR029056; Ribokinase-like.
DR InterPro; IPR017583; Tagatose/fructose_Pkinase.
DR NCBIfam; TIGR03168; 1-PFK; 1.
DR NCBIfam; TIGR03828; pfkB; 1.
DR PANTHER; PTHR46566:SF1; 1-PHOSPHOFRUCTOKINASE; 1.
DR PANTHER; PTHR46566; 1-PHOSPHOFRUCTOKINASE-RELATED; 1.
DR Pfam; PF00294; PfkB; 1.
DR PIRSF; PIRSF000535; 1PFK/6PFK/LacC; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
DR PROSITE; PS00583; PFKB_KINASES_1; 1.
DR PROSITE; PS00584; PFKB_KINASES_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU369061};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU369061};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU369061};
KW Reference proteome {ECO:0000313|Proteomes:UP000013300};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000535}.
FT DOMAIN 7..288
FT /note="Carbohydrate kinase PfkB"
FT /evidence="ECO:0000259|Pfam:PF00294"
SQ SEQUENCE 308 AA; 33470 MW; F34682D1D39E0C58 CRC64;
MIYTVTLNPS VDYIVQIEKV NLGELNRSIN EDKFPGGKGI NVSRVLKEMG VTSKALGFTG
GFTGRYITDY LQTEKIETDF VQVSEDTRIN IKLKTEKETE INASGPSITD ANFVALKDKV
RQLTENDILV LAGSIPSSLP ETTYEELVKI CAENGAKFVV DAEGELLMKV LPYHPFLIKP
NHHELGEIFE TEITTCEQAI HYGKLLIEKG ANNVIVSLAG EGAVFINKES AFIAEVPKGE
VKSSVGAGDS MVAGFLAKFG ETNDVKTAFQ YSVASGSATA FSIGLCTPEK VEKLLPQVKI
KQTSKGRP
//
