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Database: UniProt
Entry: R5M014_9FIRM
LinkDB: R5M014_9FIRM
Original site: R5M014_9FIRM 
ID   R5M014_9FIRM            Unreviewed;       306 AA.
AC   R5M014;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Tagatose-6-phosphate kinase {ECO:0000256|PIRNR:PIRNR000535};
DE            EC=2.7.1.144 {ECO:0000256|PIRNR:PIRNR000535};
GN   ORFNames=BN569_00087 {ECO:0000313|EMBL:CCY78562.1};
OS   Butyrivibrio crossotus CAG:259.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Butyrivibrio.
OX   NCBI_TaxID=1263062 {ECO:0000313|EMBL:CCY78562.1, ECO:0000313|Proteomes:UP000018300};
RN   [1] {ECO:0000313|EMBL:CCY78562.1, ECO:0000313|Proteomes:UP000018300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:259 {ECO:0000313|Proteomes:UP000018300};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) 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|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:CCY78562.1}.
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DR   EMBL; CAYU010000109; CCY78562.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5M014; -.
DR   UniPathway; UPA00704; UER00715.
DR   Proteomes; UP000018300; 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; 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.
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:UP000018300};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000535}.
FT   DOMAIN          17..289
FT                   /note="Carbohydrate kinase PfkB"
FT                   /evidence="ECO:0000259|Pfam:PF00294"
SQ   SEQUENCE   306 AA;  33121 MW;  E1D903D8BE5ABB15 CRC64;
     MIYTVTFNPS LDYIVSVRDF KLGITNRTSD ERILPGGKGI NVSTVLKNLG IDNTALGFVS
     GFTGDEIVRR LENMGVKNGF IRLENGFSRI NLKLKSTDGT EINGQGPVIS KENVELLMER
     LSQLKDGDVL FLSGSIPAGM DDDAYKNIME LLKGRDIKIV VDATKELLVK SLPYGPFLIK
     PNNYELGEIF GVRLTTRSSV IPYAKKLQNM GARNVLVSMA GEGAVLVSDD GQVIDAPAPE
     GKLINGVGAG DSMVAGFMAG YLARHDYNHA FCMGVASGSA SAFSENLATK EEIEKVYKTI
     VLEEKV
//
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