ID E3ZSZ4_LISSE Unreviewed; 307 AA.
AC E3ZSZ4;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 63.
DE RecName: Full=Tagatose-6-phosphate kinase {ECO:0000256|PIRNR:PIRNR000535};
DE EC=2.7.1.144 {ECO:0000256|PIRNR:PIRNR000535};
GN ORFNames=NT03LS_2633 {ECO:0000313|EMBL:EFR99248.1};
OS Listeria seeligeri FSL N1-067.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=702453 {ECO:0000313|EMBL:EFR99248.1};
RN [1] {ECO:0000313|EMBL:EFR99248.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL N1-067 {ECO:0000313|EMBL:EFR99248.1};
RX PubMed=21126366; DOI=10.1186/1471-2164-11-688;
RA den Bakker H.C., Cummings C.A., Ferreira V., Vatta P., Orsi R.H.,
RA Degoricija L., Barker M., Petrauskene O., Furtado M.R., Wiedmann M.;
RT "Comparative genomics of the bacterial genus Listeria: Genome evolution is
RT characterized by limited gene acquisition and limited gene loss.";
RL BMC Genomics 11:688-688(2010).
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:EFR99248.1}.
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DR EMBL; ADXJ01000865; EFR99248.1; -; Genomic_DNA.
DR RefSeq; WP_003749266.1; NZ_CM001051.1.
DR AlphaFoldDB; E3ZSZ4; -.
DR PATRIC; fig|702453.3.peg.2216; -.
DR HOGENOM; CLU_050013_1_0_9; -.
DR OrthoDB; 9801219at2; -.
DR UniPathway; UPA00704; UER00715.
DR Proteomes; UP000004302; 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; 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 7..283
FT /note="Carbohydrate kinase PfkB"
FT /evidence="ECO:0000259|Pfam:PF00294"
SQ SEQUENCE 307 AA; 33426 MW; 1538A9F06D64E8AF CRC64;
MIYTITLNPS IDYIVQIDQL NLGELNRMKQ DYKLPGGKGI NVSRVLNQLN VPNLATGFLG
GFTGEFIRDW LREEGVKTGF VTVKGDTRIN IKLKHGEETE INGLGPVISE KEINEFLDAM
DKVTADDIVI LSGSVPPSLG NDFYNRIIQI CKEKQAEFMI DTTGQELLNA LPNNPILIKP
NHHELGELFH VQLNDVNELI PYGKKCLELG AQHVIVSMAG DGALLFTGED VYFAEALQGE
LKNSVGAGDS MIAGFIGTFD KTKDPIKAFA AGVATGGATA FSTDLAEAKL IDELLPQVNI
TKITGRH
//
