KEGG   ENZYME: 2.7.1.234
Entry
EC 2.7.1.234                Enzyme                                 
Name
D-tagatose-1-phosphate kinase;
TagK
Class
Transferases;
Transferring phosphorus-containing groups;
Phosphotransferases with an alcohol group as acceptor
Sysname
ATP:D-tagatopyranse-1-phosphate 6-phosphotransferase
Reaction(IUBMB)
ATP + D-tagatopyranose 1-phosphate = ADP + D-tagatofuranose 1,6-bisphosphate [RN:R12940]
Reaction(KEGG)
R12940
Substrate
ATP [CPD:C00002];
D-tagatopyranose 1-phosphate [CPD:C22459]
Product
ADP [CPD:C00008];
D-tagatofuranose 1,6-bisphosphate
Comment
The enzyme, which has been purified from the bacteria Klebsiella oxytoca and Bacillus licheniformis, is part of a D-tagatose catabolic pathway. The substrate, which occurs in a pyranose form in solution, undergoes a change to the furanose conformation after binding to the enzyme, in order permit phosphorylation at C6.The enzyme has been pruified from the bacterium Bacillus licheniformis and is part of a D-tagatose catabolic pathway.
History
EC 2.7.1.234 created 2021
Orthology
K25602  D-tagatose-1-phosphate kinase
Genes
STYSTY3436
STTt3174
SEXSTBHUCCB_33570
SENTTY21A_16085
STMSTM3254
SEOSTM14_3940
SEVSTMMW_32541
SEYSL1344_3227
SEMSTMDT12_C33110
SEJSTMUK_3242
SEBSTM474_3411
SEFUMN798_3542
SETUSTU288_16475
SETCCFSAN001921_00740
SENRSTMDT2_31471
SENDDT104_32491
SENICY43_16950
SEENSE451236_22395
SPTSPA3123
SEKSSPA2915
SPQSPAB_04064
SENJCFSAN001992_17265
SEEBSEEB0189_003600
SENBBN855_33350
SENEIA1_15745
KPNKPN_03544(pfkB)
KPUKP1_4848(pfkB)
KPMKPHS_46810
KPPA79E_0569
KPHKPNIH24_05495
KPVKPNIH29_23255
KPWKPNIH30_23580
KPGKPNIH32_24460
KPCKPNIH10_23305
KPQKPR0928_22825
KPJN559_0623
KPAKPNJ1_00608
KPSKPNJ2_00646
KPBFH42_14020
KPNEKU54_003005
KPNULI86_03010
KVAKvar_0553
KVDKR75_05250
KVQSP68_11870
KOXKOX_03500
KOEA225_5150
KOYJ415_06265
KMIVW41_10215
KQUAVR78_01570
KQVB8P98_03065(pfkB)
KLLBJF97_25675
KLWDA718_03495(pfkB)
KARLGL98_02920(pfkB)
KGRJJJ10_03120(pfkB)
CNTJT31_02310
CEMLH23_15860
CENLH86_14940
KIENCTC12125_04500(lacC_2)
BFTMNO13_21570(pfkB)
PSGCG163CM_41760(lacC_2)
PSTSE05_51020
TCIA7K98_11385
GAPGAPWK_0478
ORBIPMB12_09245(pfkB)
PMASNCF86_15710(pfkB)
BLIBL01904
BLDBLi03549(fruK2)
BLHBaLi_c36130(fruK2)
BSONS101395_04282(fruK)
BPUBPUM_1770
BPUMBW16_09720
BPUSUP12_09075
BGYBGLY_3939
BALTCFN77_09560(pfkB)
BSAFBSL056_10000
BACWQR42_09010
BCLABC3198
BLEBleG1_3564
VHLBME96_15635
VIGBKP57_09175
VNECFK40_05640(pfkB)
VPNA21D_01740(lacC_2)
VPTKBP50_20680(pfkB)
GRCGI584_19245(pfkB)
MDGK8L98_03780(pfkB)
SEDDERJ70_07280(pfkB)
BVJI5776_03705(pfkB)
BOUI5818_03830(pfkB)
LWElwe0799
BTHSCNY62_05550(pfkB)
PLVERIC2_c16770(fruK)
SAGIMSA_13790
SMUSMU_113
SMCSmuNN2025_0103
SMUTSMUGS5_00480
SMJSMULJ23_0093(fruK-1)
SMUASMUFR_0092(fruK)
SSKSSUD12_1209(fruK)
SPATA0O21_00550
SRATFY406_09765(pfkB)
STRGSRT_01140
SCHJDDV21_002100(pfkB)
SURNNCTC13766_01141(lacC_2)
LJOLJ_0145
LJFFI9785_212(fruK)
LJHLJP_0151
LJNT285_00820
LGALGAS_0148
LPWLpgJCM5343_01500(fruK)
LKLDKL58_02050(pfkB)
LAPIDKL56_01440(pfkB)
LPAIGYM71_02235(pfkB)
LCALSEI_2655
LCZLCAZH_2625
LCSLCBD_2844(tagK)
LCELC2W_2818(tagK)
LCWBN194_27700(fruK_2)
LCLLOCK919_2878
LPQAF91_13170
LPILBPG_01220
LPAPLBPC_2598
LCBLCABL_28220(fruK-1)
LCXLCA12A_0319
LRHLGG_02648(fruK)
LRGLRHM_2542
LRLLC705_02653(fruK)
LRALRHK_2759(pfkB)
LROLOCK900_2648
LRCLOCK908_2731
LCHIKG086_11980(pfkB)
LZEKG087_13190(pfkB)
LNGBSQ50_09180
LMALLM596_11695(pfkB)
PPEPEPE_0141
PPENT256_00800
PDMADU72_2047
PACIA4V11_07425
LHIJP39_05235
LCTBI355_1179
LFMLF20184_07270
LZHD1B17_05515(pfkB)
LFTFG051_06990(pfkB)
CPABG6534_04475(pfkB)
EFAEF0693(fruK-1)
EFLEF62_1066(pfkB_2)
EFIOG1RF_10431(fruK)
EFDEFD32_0512(pfkB_2)
EFSEFS1_0540(fruB-1)
EFNDENG_00729(fruK)
EFQDR75_2644(pfkB)
EFCEFAU004_01953
EFMM7W_1040
EFTM395_04390
ECASECBG_02510
EMUEMQU_0463
EGAAL523_02135(pfkB)
EGVEGCR1_12185(pfkB)
EAVEH197_24005(pfkB)
ESGEsVE80_05490(fruK-1)
ELACI4Q40_01530(pfkB)
ERAFJ9537_14485(pfkB)
EIEENLAB_12050(fruK)
THLTEH_11660(fruK)
TOOC7K38_08600(pfkB)
TKRC7K43_01860(pfkB)
JEHEJN90_04615(pfkB)
GADK8O88_05460(pfkB)
CBOCBO1992
CBACLB_1932(pfkB)
CBHCLC_1938
CBYCLM_2209(pfkB)
CBLCLK_1445(pfkB)
CBBCLD_2632(pfkB)
CBICLJ_B2197(pfkB_2)
CBFCLI_2059(pfkB)
CBMCBF_2045(pfkB)
CBJH04402_02018
CSQCSCA_3249
CLDCLSPO_c19990(fruK2)
ARFAR1Y2_0519
ACACEYQ97_14345(pfkB)
CDFCD630_30760(tagK)
PDCCDIF630_03359(tagK)
CDCCD196_2868(tagK)
CDLCDR20291_2915(tagK)
PDFCD630DERM_30760(tagK)
TEMJW646_04835(pfkB)
TGCL0P85_03525(pfkB)
SELTBCS37_03320
TSGHLK68_02155
FVGI6G91_03380
APVApar_0322
OLSOlsu_0536
ATBJ4859_03910
TIOINP52_01760
CGOCorgl_1662
CAERCSV91_02580
CSTCLK434_02840
FMOC4N19_05880(pfkB)
STRSterm_1965
 » show all
Reference
1  [PMID:26159072]
  Authors
Van der Heiden E, Delmarcelle M, Simon P, Counson M, Galleni M, Freedberg DI, Thompson J, Joris B, Battistel MD.
  Title
Synthesis and Physicochemical Characterization of D-Tagatose-1-Phosphate: The Substrate of the Tagatose-1-Phosphate Kinase in the Phosphotransferase System-Mediated D-Tagatose Catabolic Pathway of Bacillus licheniformis.
  Journal
J Mol Microbiol Biotechnol 25:106-19 (2015)
DOI:10.1159/000370115
  Sequence
[bli:BL01904]
Other DBs
ExplorEnz - The Enzyme Database: 2.7.1.234
IUBMB Enzyme Nomenclature: 2.7.1.234
ExPASy - ENZYME nomenclature database: 2.7.1.234
BRENDA, the Enzyme Database: 2.7.1.234
LinkDB

DBGET integrated database retrieval system