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Database: UniProt
Entry: A0A062XE05_9LACO
LinkDB: A0A062XE05_9LACO
Original site: A0A062XE05_9LACO 
ID   A0A062XE05_9LACO        Unreviewed;       304 AA.
AC   A0A062XE05;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 52.
DE   RecName: Full=Tagatose-6-phosphate kinase {ECO:0000256|PIRNR:PIRNR000535};
DE            EC=2.7.1.144 {ECO:0000256|PIRNR:PIRNR000535};
GN   ORFNames=Lani381_0029 {ECO:0000313|EMBL:KDA46815.1};
OS   Ligilactobacillus animalis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Ligilactobacillus.
OX   NCBI_TaxID=1605 {ECO:0000313|EMBL:KDA46815.1, ECO:0000313|Proteomes:UP000027129};
RN   [1] {ECO:0000313|EMBL:KDA46815.1, ECO:0000313|Proteomes:UP000027129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=381-IL-28 {ECO:0000313|EMBL:KDA46815.1,
RC   ECO:0000313|Proteomes:UP000027129};
RA   Sturino J.M., Rajendran M., Altermann E.;
RT   "Draft Genome Sequence of Lactobacillus animalis 381-IL-28.";
RL   Submitted (APR-2014) 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}.
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:KDA46815.1}.
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DR   EMBL; JMHU01000001; KDA46815.1; -; Genomic_DNA.
DR   RefSeq; WP_010690213.1; NZ_POVP01000001.1.
DR   AlphaFoldDB; A0A062XE05; -.
DR   GeneID; 61225651; -.
DR   PATRIC; fig|1605.9.peg.28; -.
DR   eggNOG; COG1105; Bacteria.
DR   OrthoDB; 9801219at2; -.
DR   UniPathway; UPA00704; UER00715.
DR   Proteomes; UP000027129; Unassembled WGS sequence.
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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000535}.
FT   DOMAIN          8..283
FT                   /note="Carbohydrate kinase PfkB"
FT                   /evidence="ECO:0000259|Pfam:PF00294"
SQ   SEQUENCE   304 AA;  33163 MW;  31911E8380272AB6 CRC64;
     MIYTVTVNPS IDYIVQLNEL TLGEVNRMDY DNKLPGGKGI NVSRILKELG LDNTAWGFLG
     GFTGEFVKEA LEKTGLKTNF TPIKADTRIN VKIKAQAETE INGRGPELTK EEIAAFTAQF
     DKLTADDVVI FAGSLVPSLS DDFYFDLIKV IRQKGAQFVI DTTGESLLKT LPENPLVVKP
     NNHELAELFG VKLNSIDDIV KYGKKLLEMG AQHVLISMAG DGGLMITKDK VYRSYAPKGT
     VINSVGAGDS MIGGFTGTYA KTKDPLEAFR YGLACGSATA FSEDLADADK INEILPMIEI
     EEYK
//
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