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Database: UniProt
Entry: A0A3S9UTJ4_9BACL
LinkDB: A0A3S9UTJ4_9BACL
Original site: A0A3S9UTJ4_9BACL 
ID   A0A3S9UTJ4_9BACL        Unreviewed;       303 AA.
AC   A0A3S9UTJ4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Tagatose-6-phosphate kinase {ECO:0000256|PIRNR:PIRNR000535};
DE            EC=2.7.1.144 {ECO:0000256|PIRNR:PIRNR000535};
GN   Name=pfkB {ECO:0000313|EMBL:AZS13636.1};
GN   ORFNames=EI981_03515 {ECO:0000313|EMBL:AZS13636.1};
OS   Paenibacillus lutimineralis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=2707005 {ECO:0000313|EMBL:AZS13636.1, ECO:0000313|Proteomes:UP000270678};
RN   [1] {ECO:0000313|Proteomes:UP000270678}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MBLB1234 {ECO:0000313|Proteomes:UP000270678};
RA   Nam Y.-D., Kang J., Chung W.-H., Park Y.S.;
RT   "Complete genome sequence of Paenibacillus sp. MBLB1234.";
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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 + D-tagatofuranose 6-phosphate = ADP + D-tagatofuranose
CC         1,6-bisphosphate + H(+); Xref=Rhea:RHEA:12420, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58694, ChEBI:CHEBI:58695,
CC         ChEBI:CHEBI:456216; EC=2.7.1.144;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000535};
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   -!- PATHWAY: Carbohydrate metabolism; D-tagatose 6-phosphate degradation;
CC       D-glyceraldehyde 3-phosphate and glycerone phosphate from D-tagatose 6-
CC       phosphate: step 1/2. {ECO:0000256|PIRNR:PIRNR000535}.
CC   -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family. LacC
CC       subfamily. {ECO:0000256|PIRNR:PIRNR000535}.
CC   -!- SIMILARITY: Belongs to the carbohydrate kinase pfkB family.
CC       {ECO:0000256|ARBA:ARBA00005380}.
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DR   EMBL; CP034346; AZS13636.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S9UTJ4; -.
DR   KEGG; plut:EI981_03515; -.
DR   OrthoDB; 9801219at2; -.
DR   UniPathway; UPA00704; UER00715.
DR   Proteomes; UP000270678; Chromosome.
DR   GO; GO:0008662; F:1-phosphofructokinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009024; F:tagatose-6-phosphate kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:2001059; P:D-tagatose 6-phosphate catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0005988; P:lactose metabolic process; IEA:UniProtKB-KW.
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|PIRNR:PIRNR000535};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU369061};
KW   Lactose metabolism {ECO:0000256|PIRNR:PIRNR000535};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR000535};
KW   Reference proteome {ECO:0000313|Proteomes:UP000270678};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000535}.
FT   DOMAIN          12..280
FT                   /note="Carbohydrate kinase PfkB"
FT                   /evidence="ECO:0000259|Pfam:PF00294"
SQ   SEQUENCE   303 AA;  32628 MW;  8D8843A82AABDBF8 CRC64;
     MIYTITLNPS VDYIVEVEEL NIGGLSRMKR DLKLPGGKGI NVSRVLNQLG AENTALGFLG
     GFTGRYVNDR LQEERMSTDF VTIASDTRIN IKLKHGEETE INGLGPDISE AEAEQLLQKL
     SALQKDDIVI LSGSIPPSLG EDFYERLIRV SKQRGAEFVI DTTGEALLKA LKHRPLLVKP
     NHHELAELYD TELNSMEDVV VYGRKLLGAG AKNVLVSMAA EGALLITESA VYHAKVPAGQ
     VKNSVGAGDS MIAGFVGTLV KTGDPLAAFR TGVAAGSATA FTDDLATRDQ IDQLLPKVVI
     SNR
//
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