UniProt: D4M2W9

Database: UniProt
Entry: D4M2W9_9FIRM

LinkDB:  D4M2W9_9FIRM 
Original site:  D4M2W9_9FIRM

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (5)   
   InterPro (4)   
   Pfam (1)   
All databases (13)   

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ID   D4M2W9_9FIRM            Unreviewed;       318 AA.
AC   D4M2W9;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   RecName: Full=Tagatose-6-phosphate kinase {ECO:0000256|PIRNR:PIRNR000535};
DE            EC=2.7.1.144 {ECO:0000256|PIRNR:PIRNR000535};
GN   ORFNames=RTO_08800 {ECO:0000313|EMBL:CBL25581.1};
OS   [Ruminococcus] torques L2-14.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Mediterraneibacter.
OX   NCBI_TaxID=657313 {ECO:0000313|EMBL:CBL25581.1, ECO:0000313|Proteomes:UP000008956};
RN   [1] {ECO:0000313|EMBL:CBL25581.1, ECO:0000313|Proteomes:UP000008956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L2-14 {ECO:0000313|EMBL:CBL25581.1,
RC   ECO:0000313|Proteomes:UP000008956};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Ruminococcus torques L2-14.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL25581.1, ECO:0000313|Proteomes:UP000008956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L2-14 {ECO:0000313|EMBL:CBL25581.1,
RC   ECO:0000313|Proteomes:UP000008956};
RA   Pajon A.;
RL   Submitted (MAR-2010) 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}.
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DR   EMBL; FP929055; CBL25581.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4M2W9; -.
DR   STRING; 33039.ERS852502_02021; -.
DR   KEGG; rto:RTO_08800; -.
DR   PATRIC; fig|657313.3.peg.554; -.
DR   HOGENOM; CLU_050013_0_2_9; -.
DR   UniPathway; UPA00704; UER00715.
DR   Proteomes; UP000008956; 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; 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:SF5; 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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR000535}.
FT   DOMAIN          17..299
FT                   /note="Carbohydrate kinase PfkB"
FT                   /evidence="ECO:0000259|Pfam:PF00294"
SQ   SEQUENCE   318 AA;  34271 MW;  0A590BAC32A25D54 CRC64;
     MCQSSVPNMI LTVTLNAAID KRYVVEGYQV GEVNRVKECA YTPGGKGLNV SKPASIAGAE
     VVATGFVGGH AGNYIEDALK PFGIKSEFYH LEEESRSCIN IWDEVNHVQT EFLEPGFTVS
     EEEFKGFEKH FTELVKKADV VAMSGSVPKG LDGTAYQRLV RICKEAGKKV ILDTSGKLLE
     MGIEAKPTMI KPNIDEIRML TGKSCDNFQD MVDAAKQIHA DGVEIVAVSL GGDGSFVVCD
     DGIFRARVPK IDAVNTVGCG DSMIAGFALG LSEGLSVEET LKKASAISAA AALREETGFF
     VKEDMEKIYP QVEIEKIG
//

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