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Conserved domains on  [gi|16129594|ref|NP_416153|]
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pyridoxal kinase 2 [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

pyridoxal kinase PdxY( domain architecture ID 10792681)

pyridoxal kinase PdxY catalyzes the phosphorylation of pyridoxal to PLP in vivo, but shows very low activity compared to PdxK

EC:  2.7.1.35
Gene Ontology:  GO:0008478|GO:0009443|GO:0005829|GO:0005524
PubMed:  15547280|27425248

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05756 PRK05756
pyridoxal kinase PdxY;
2-287 0e+00

pyridoxal kinase PdxY;


:

Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 539.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594    2 MKNILAIQSHVVYGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPSHLTEIVQGIAAIDKLHTCDAVLS 81
Cdd:PRK05756   1 MKNILSIQSHVVYGHVGNSAAVFPMQRLGVNVWPLNTVQFSNHTGYGKWTGCVMPPSHLTEIVQGIADIGWLGECDAVLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594   82 GYLGSAEQGEHILGIVRQVKAANPQAKYFCDPVMGHPEKGCIVAPGVAEFHVRHGLPASDIIAPNLVELEILCEHAVNNV 161
Cdd:PRK05756  81 GYLGSAEQGEAILDAVRRVKAANPQALYFCDPVMGDPEKGCIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594  162 EEAVLAARELIAQGPQIVLVKHLARAGYSRDRFEMLLVTADEAWHISRPLVDFGmRQPVGVGDVTSGLLLVKLLQGATLQ 241
Cdd:PRK05756 161 EDAVAAARALIARGPKIVLVTSLARAGYPADRFEMLLVTADGAWHISRPLVDFM-RQPVGVGDLTSALFLARLLQGGSLE 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 16129594  242 EALEHVTAAVYEIMVTTKAMQEYELQVVAAQDRIAKPEHYFSATKL 287
Cdd:PRK05756 240 EALEHTTAAVYEVMARTKERGSYELQLVAAQDSIATPRAMFQARRL 285
 
Name Accession Description Interval E-value
PRK05756 PRK05756
pyridoxal kinase PdxY;
2-287 0e+00

pyridoxal kinase PdxY;


Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 539.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594    2 MKNILAIQSHVVYGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPSHLTEIVQGIAAIDKLHTCDAVLS 81
Cdd:PRK05756   1 MKNILSIQSHVVYGHVGNSAAVFPMQRLGVNVWPLNTVQFSNHTGYGKWTGCVMPPSHLTEIVQGIADIGWLGECDAVLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594   82 GYLGSAEQGEHILGIVRQVKAANPQAKYFCDPVMGHPEKGCIVAPGVAEFHVRHGLPASDIIAPNLVELEILCEHAVNNV 161
Cdd:PRK05756  81 GYLGSAEQGEAILDAVRRVKAANPQALYFCDPVMGDPEKGCIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594  162 EEAVLAARELIAQGPQIVLVKHLARAGYSRDRFEMLLVTADEAWHISRPLVDFGmRQPVGVGDVTSGLLLVKLLQGATLQ 241
Cdd:PRK05756 161 EDAVAAARALIARGPKIVLVTSLARAGYPADRFEMLLVTADGAWHISRPLVDFM-RQPVGVGDLTSALFLARLLQGGSLE 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 16129594  242 EALEHVTAAVYEIMVTTKAMQEYELQVVAAQDRIAKPEHYFSATKL 287
Cdd:PRK05756 240 EALEHTTAAVYEVMARTKERGSYELQLVAAQDSIATPRAMFQARRL 285
pyridox_kin TIGR00687
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ...
 2-287 0e+00

pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal/pyridoxamine kinase, but mutants lacking PdxK activity retain a specific pyridoxal kinase, PdxY. PdxY acts in the salvage pathway of pyridoxal 5'-phosphate biosynthesis. Mammalian forms of pyridoxal kinase are more similar to PdxY than to PdxK. The PdxK isozyme is omitted from the seed alignment but scores above the trusted cutoff.ThiD and related proteins form an outgroup. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]


Pssm-ID: 273221 [Multi-domain]  Cd Length: 287  Bit Score: 506.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594     2 MKNILAIQSHVVYGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPSHLTEIVQGIAAIDKLHTCDAVLS 81
Cdd:TIGR00687   1 MKNVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLEAINKLNQCDAVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594    82 GYLGSAEQGEHILGIVRQVKAANPQAKYFCDPVMGHPEKGCIVAPGVAEFHVRHGLPASDIIAPNLVELEILCEHAVNNV 161
Cdd:TIGR00687  81 GYLGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKGCYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594   162 EEAVLAARELIAQGPQIVLVKHLARAGYSRDR-FEMLLVTADEAWHISRPLVDFgMRQPVGVGDVTSGLLLVKLLQGATL 240
Cdd:TIGR00687 161 EEALAAADALIAMGPDIVLVTHLIRAGSQRDRsFEGLVATQEGRWHISRPLAVF-DPPPVGTGDLIAALLLATLLHGNSL 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 16129594   241 QEALEHVTAAVYEIMVTTKAMQEYELQVVAAQDRIAKPEHYFSATKL 287
Cdd:TIGR00687 240 KEALEKTVSAVYHVLRTTIQLGKYELQPVAAQLEIRMPQSKFDAEKV 286
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 2-276 3.24e-139

Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal/pyridoxine/pyridoxamine kinase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 441841 [Multi-domain]  Cd Length: 272  Bit Score: 393.36  E-value: 3.24e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594   2 MKNILAIQSHVVYGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPSHLTEIVQGIAAIDKLHTCDAVLS 81
Cdd:COG2240   1 MKRVLSIQSHVVYGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWKELGVLLEFDAVLS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594  82 GYLGSAEQGEHILGIVRQVKAANPQAKYFCDPVMGHPEKGCIVAPGVAEFHVRHGLPASDIIAPNLVELEILCEHAVNNV 161
Cdd:COG2240  81 GYLGSAEQGDIIADFVARVKAANPDALYLCDPVMGDNGKGYYVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594 162 EEAVLAARELIAQGPQIVLVKHLARAGYSRDRFEMLLVTADEAWHISRPLVDFgmrQPVGVGDVTSGLLLVKLLQGATLQ 241
Cdd:COG2240 161 EEALAAARALLALGPKIVVVTSVPLDDTPADKIGNLAVTADGAWLVETPLLPF---SPNGTGDLFAALLLAHLLRGKSLE 237

                       250       260       270
                ....*....|....*....|....*....|....*
gi 16129594 242 EALEHVTAAVYEIMVTTKAMQEYELQVVAAQDRIA 276
Cdd:COG2240 238 EALERAAAFVYEVLERTAAAGSDELLLEAALDELV 272
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 4-258 6.83e-114

Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5'-phosphate (PLP), by catalyzing the phosphorylation of the precursor vitamin B6 in the presence of Zn2+ and ATP. Mammals are unable to synthesize PLP de novo and require its precursors in the form of vitamin B6 (pyridoxal, pyridoxine, and pyridoxamine) from their diet. Pyridoxal kinase encoding genes are also found in many other species including yeast and bacteria.


Pssm-ID: 238578 [Multi-domain]  Cd Length: 254  Bit Score: 328.39  E-value: 6.83e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594   4 NILAIQSHVVYGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPSHLTEIVQGIAAIDKLHTCDAVLSGY 83
Cdd:cd01173   1 RVLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLLLEYDAVLTGY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594  84 LGSAEQGEHILGIVRQVKAANPQAKYFCDPVMGHPEKGCIVAPGVAEFHVRHGLPASDIIAPNLVELEILCEHAVNNVEE 163
Cdd:cd01173  81 LGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGDNGKLYVVAEEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLED 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594 164 AVLAARELIAQGPQIVLVKHLARAGysRDRFEMLLVTADEAWHISRPLVDFgMRQPVGVGDVTSGLLLVKLLQGATLQEA 243
Cdd:cd01173 161 AKAAARALHAKGPKTVVVTSVELAD--DDRIEMLGSTATEAWLVQRPKIPF-PAYFNGTGDLFAALLLARLLKGKSLAEA 237

                       250
                ....*....|....*
gi 16129594 244 LEHVTAAVYEIMVTT 258
Cdd:cd01173 238 LEKALNFVHEVLEAT 252
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 76-251 1.19e-13

Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate (TPP) synthesis pathway, TPP is an essential cofactor for many enzymes.


Pssm-ID: 430062 [Multi-domain]  Cd Length: 246  Bit Score: 69.05  E-value: 1.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594    76 CDAVLSGYLGSAEqgehilgIVRQV--KAANPQAKYFCDPVM----GHPekgcIVAPGVAEFHVRHGLPASDIIAPNLVE 149
Cdd:pfam08543  61 VDAVKTGMLGSAE-------IIEAVaeKLDKYGVPVVLDPVMvaksGDS----LLDDEAIEALKEELLPLATLITPNLPE 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594   150 LEILCEHAVNNVEEAVLAARELIAQGPQIVLVK--HLARAG-YSRDrfemLLVTADEAWHISRPLVDfgMRQPVGVGDVT 226
Cdd:pfam08543 130 AEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKggHLEGEEaVVTD----VLYDGGGFYTLEAPRIP--TKNTHGTGCTL 203

                         170       180
                  ....*....|....*....|....*....
gi 16129594   227 SGLLLVKLLQGATLQEALEH----VTAAV 251
Cdd:pfam08543 204 SAAIAANLAKGLSLPEAVREakeyVTEAI 232
 
Name Accession Description Interval E-value
PRK05756 PRK05756
pyridoxal kinase PdxY;
2-287 0e+00

pyridoxal kinase PdxY;


Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 539.07  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594    2 MKNILAIQSHVVYGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPSHLTEIVQGIAAIDKLHTCDAVLS 81
Cdd:PRK05756   1 MKNILSIQSHVVYGHVGNSAAVFPMQRLGVNVWPLNTVQFSNHTGYGKWTGCVMPPSHLTEIVQGIADIGWLGECDAVLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594   82 GYLGSAEQGEHILGIVRQVKAANPQAKYFCDPVMGHPEKGCIVAPGVAEFHVRHGLPASDIIAPNLVELEILCEHAVNNV 161
Cdd:PRK05756  81 GYLGSAEQGEAILDAVRRVKAANPQALYFCDPVMGDPEKGCIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594  162 EEAVLAARELIAQGPQIVLVKHLARAGYSRDRFEMLLVTADEAWHISRPLVDFGmRQPVGVGDVTSGLLLVKLLQGATLQ 241
Cdd:PRK05756 161 EDAVAAARALIARGPKIVLVTSLARAGYPADRFEMLLVTADGAWHISRPLVDFM-RQPVGVGDLTSALFLARLLQGGSLE 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 16129594  242 EALEHVTAAVYEIMVTTKAMQEYELQVVAAQDRIAKPEHYFSATKL 287
Cdd:PRK05756 240 EALEHTTAAVYEVMARTKERGSYELQLVAAQDSIATPRAMFQARRL 285
pyridox_kin TIGR00687
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ...
 2-287 0e+00

pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal/pyridoxamine kinase, but mutants lacking PdxK activity retain a specific pyridoxal kinase, PdxY. PdxY acts in the salvage pathway of pyridoxal 5'-phosphate biosynthesis. Mammalian forms of pyridoxal kinase are more similar to PdxY than to PdxK. The PdxK isozyme is omitted from the seed alignment but scores above the trusted cutoff.ThiD and related proteins form an outgroup. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]


Pssm-ID: 273221 [Multi-domain]  Cd Length: 287  Bit Score: 506.29  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594     2 MKNILAIQSHVVYGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPSHLTEIVQGIAAIDKLHTCDAVLS 81
Cdd:TIGR00687   1 MKNVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLEAINKLNQCDAVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594    82 GYLGSAEQGEHILGIVRQVKAANPQAKYFCDPVMGHPEKGCIVAPGVAEFHVRHGLPASDIIAPNLVELEILCEHAVNNV 161
Cdd:TIGR00687  81 GYLGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKGCYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594   162 EEAVLAARELIAQGPQIVLVKHLARAGYSRDR-FEMLLVTADEAWHISRPLVDFgMRQPVGVGDVTSGLLLVKLLQGATL 240
Cdd:TIGR00687 161 EEALAAADALIAMGPDIVLVTHLIRAGSQRDRsFEGLVATQEGRWHISRPLAVF-DPPPVGTGDLIAALLLATLLHGNSL 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 16129594   241 QEALEHVTAAVYEIMVTTKAMQEYELQVVAAQDRIAKPEHYFSATKL 287
Cdd:TIGR00687 240 KEALEKTVSAVYHVLRTTIQLGKYELQPVAAQLEIRMPQSKFDAEKV 286
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 2-276 3.24e-139

Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal/pyridoxine/pyridoxamine kinase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 441841 [Multi-domain]  Cd Length: 272  Bit Score: 393.36  E-value: 3.24e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594   2 MKNILAIQSHVVYGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPSHLTEIVQGIAAIDKLHTCDAVLS 81
Cdd:COG2240   1 MKRVLSIQSHVVYGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWKELGVLLEFDAVLS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594  82 GYLGSAEQGEHILGIVRQVKAANPQAKYFCDPVMGHPEKGCIVAPGVAEFHVRHGLPASDIIAPNLVELEILCEHAVNNV 161
Cdd:COG2240  81 GYLGSAEQGDIIADFVARVKAANPDALYLCDPVMGDNGKGYYVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594 162 EEAVLAARELIAQGPQIVLVKHLARAGYSRDRFEMLLVTADEAWHISRPLVDFgmrQPVGVGDVTSGLLLVKLLQGATLQ 241
Cdd:COG2240 161 EEALAAARALLALGPKIVVVTSVPLDDTPADKIGNLAVTADGAWLVETPLLPF---SPNGTGDLFAALLLAHLLRGKSLE 237

                       250       260       270
                ....*....|....*....|....*....|....*
gi 16129594 242 EALEHVTAAVYEIMVTTKAMQEYELQVVAAQDRIA 276
Cdd:COG2240 238 EALERAAAFVYEVLERTAAAGSDELLLEAALDELV 272
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 4-258 6.83e-114

Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5'-phosphate (PLP), by catalyzing the phosphorylation of the precursor vitamin B6 in the presence of Zn2+ and ATP. Mammals are unable to synthesize PLP de novo and require its precursors in the form of vitamin B6 (pyridoxal, pyridoxine, and pyridoxamine) from their diet. Pyridoxal kinase encoding genes are also found in many other species including yeast and bacteria.


Pssm-ID: 238578 [Multi-domain]  Cd Length: 254  Bit Score: 328.39  E-value: 6.83e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594   4 NILAIQSHVVYGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPSHLTEIVQGIAAIDKLHTCDAVLSGY 83
Cdd:cd01173   1 RVLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLLLEYDAVLTGY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594  84 LGSAEQGEHILGIVRQVKAANPQAKYFCDPVMGHPEKGCIVAPGVAEFHVRHGLPASDIIAPNLVELEILCEHAVNNVEE 163
Cdd:cd01173  81 LGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGDNGKLYVVAEEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLED 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594 164 AVLAARELIAQGPQIVLVKHLARAGysRDRFEMLLVTADEAWHISRPLVDFgMRQPVGVGDVTSGLLLVKLLQGATLQEA 243
Cdd:cd01173 161 AKAAARALHAKGPKTVVVTSVELAD--DDRIEMLGSTATEAWLVQRPKIPF-PAYFNGTGDLFAALLLARLLKGKSLAEA 237

                       250
                ....*....|....*
gi 16129594 244 LEHVTAAVYEIMVTT 258
Cdd:cd01173 238 LEKALNFVHEVLEAT 252
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
 1-287 5.17e-54

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 177.20  E-value: 5.17e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594    1 MMKNILAIQSHVVYGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPSHLTEIVQGIAAIDKLHTCDAVL 80
Cdd:PTZ00344   3 MEKKVLSIQSHVTHGYVGNRAATFPLQLLGFDVDFVNTVQLSNHTGYPVIKGHRLDLNELITLMDGLRANNLLSDYTYVL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594   81 SGYLGSAEQGEHILGIVRQVKAANPQAKYFCDPVMGHPEKGCIVAPGVAEFhvRHGLPASDIIAPNLVELEILCEHAVNN 160
Cdd:PTZ00344  83 TGYINSADILREVLATVKEIKELRPKLIFLCDPVMGDDGKLYVKEEVVDAY--RELIPYADVITPNQFEASLLSGVEVKD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594  161 VEEAVLAARELIAQGPQIVLVKHLARAGYSRDRFEMLLVTADEAWHISRplvdFGMRQP------VGVGDVTSGLLLVKL 234
Cdd:PTZ00344 161 LSDALEAIDWFHEQGIPVVVITSFREDEDPTHLRFLLSCRDKDTKNNKR----FTGKVPyiegryTGTGDLFAALLLAFS 236

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16129594  235 LQGAtLQEALEHVTAAVYEIMVTTK--------AMQEYELQVVAAQDRIAKPEHYFSATKL 287
Cdd:PTZ00344 237 HQHP-MDLAVGKAMGVLQDIIKATResggsgssSLMSRELRLIQSPRDLLNPETVFKVTPL 296
pdxK PRK08176
pyridoxine/pyridoxal/pyridoxamine kinase;
4-267 1.74e-43

pyridoxine/pyridoxal/pyridoxamine kinase;


Pssm-ID: 181269 [Multi-domain]  Cd Length: 281  Bit Score: 149.42  E-value: 1.74e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594    4 NILAIQSHVVYGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPSHLTEIVQGIAAIDKLHTCDAVLSGY 83
Cdd:PRK08176  17 DIVAVQSQVVYGSVGNSIAVPAIKANGLRVFAVPTVLLSNTPHYPTFYGGAIPDEWFSGYLRALQERDALRQLRAVTTGY 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594   84 LGSAEQGEHILGIVRQVKAANPQAKYFCDPVMGHPEKGCIVAPGVAEFHVRHGLPASDIIAPNLVELEILCEHAVNNVEE 163
Cdd:PRK08176  97 MGSASQIKILAEWLTALRADHPDLLIMVDPVIGDIDSGIYVKPDLPEAYRQHLLPLAQGLTPNIFELEILTGKPCRTLDS 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594  164 AVLAARELIAQGPQIVLVKHlARAGYSRDRFEMLLVTADEAWHISRPLVDfgmRQPVGVGDVTSGLLLVKLLQGATLQEA 243
Cdd:PRK08176 177 AIAAAKSLLSDTLKWVVITS-AAGNEENQEMQVVVVTADSVNVISHPRVD---TDLKGTGDLFCAELVSGLLKGKALTDA 252

                        250       260
                 ....*....|....*....|....
gi 16129594  244 LEHVTAAVYEIMVTTKAMQEYELQ 267
Cdd:PRK08176 253 AHRAGLRVLEVMRYTQQAGSDELI 276
PLN02978 PLN02978
pyridoxal kinase
 5-287 3.22e-43

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 149.51  E-value: 3.22e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594    5 ILAIQSHVVYGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPSHLTEIVQGIAAIDKLHTCDaVLSGYL 84
Cdd:PLN02978  17 VLSIQSHTVHGYVGNKSAVFPLQLLGFDVDPINSVQFSNHTGYPTFKGQVLDGEQLWALIEGLEANGLLFYTH-LLTGYI 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594   85 GSAEQGEHILGIVRQVKAANPQAKYFCDPVMGHPEKgCIVAPGVAEFHVRHGLPASDIIAPNLVELEILCEHAVNNVEEA 164
Cdd:PLN02978  96 GSVSFLRTVLRVVKKLRSVNPNLTYVCDPVLGDEGK-LYVPPELVPVYREKVVPLATMLTPNQFEAEQLTGIRIVTEEDA 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594  165 VLAARELIAQGPQIVLVKhlaragySRDRFEMLLVTADEAWHISRPLVDFGMRQP------VGVGDVTSGLLL------- 231
Cdd:PLN02978 175 REACAILHAAGPSKVVIT-------SIDIDGKLLLVGSHRKEKGARPEQFKIVIPkipayfTGTGDLMAALLLgwshkyp 247

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16129594  232 ------VKLLQGaTLQeALEHVTAAVYEIMVTTKAMQEYELQVVAAQDRIAKPEHYFSATKL 287
Cdd:PLN02978 248 dnldkaAELAVS-SLQ-AVLRRTLADYKRAGADPKSSSLELRLVQSQDDIRHPQVRFKAERY 307
FruK_PfkB_like cd01164
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ...
 134-250 5.38e-16

1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. FruK plays an important role in the predominant pathway for fructose utilisation.This group also contains tagatose-6-phophate kinase, an enzyme of the tagatose 6-phosphate pathway, which responsible for breakdown of the galactose moiety during lactose metabolism by bacteria such as L. lactis.


Pssm-ID: 238570 [Multi-domain]  Cd Length: 289  Bit Score: 76.03  E-value: 5.38e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594 134 RHGLPAS-DIIAPNLVELEILCEHAVNNVEEAVLAARELIAQGPQIVLVKhLARAGysrdrfeMLLVTADEAWHISRPLV 212
Cdd:cd01164 171 LAALAAKpFLIKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVS-LGADG-------ALLVTKDGVYRASPPKV 242

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 16129594 213 DFgmRQPVGVGDVTSGLLLVKLLQGATLQEALEHVTAA 250
Cdd:cd01164 243 KV--VSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAA 278
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
134-250 7.72e-16

1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 75.94  E-value: 7.72e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594 134 RHGLPAS-DIIAPNLVELEILCEHAVNNVEEAVLAARELIAQGPQIVLVKhLARAGysrdrfeMLLVTADEAWHISRPLV 212
Cdd:COG1105 171 KAALEAGpDLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVS-LGADG-------ALLVTEDGVYRAKPPKV 242

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 16129594 213 DFgmRQPVGVGDVTSGLLLVKLLQGATLQEALEHVTAA 250
Cdd:COG1105 243 EV--VSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAA 278
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 76-251 1.19e-13

Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate (TPP) synthesis pathway, TPP is an essential cofactor for many enzymes.


Pssm-ID: 430062 [Multi-domain]  Cd Length: 246  Bit Score: 69.05  E-value: 1.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594    76 CDAVLSGYLGSAEqgehilgIVRQV--KAANPQAKYFCDPVM----GHPekgcIVAPGVAEFHVRHGLPASDIIAPNLVE 149
Cdd:pfam08543  61 VDAVKTGMLGSAE-------IIEAVaeKLDKYGVPVVLDPVMvaksGDS----LLDDEAIEALKEELLPLATLITPNLPE 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594   150 LEILCEHAVNNVEEAVLAARELIAQGPQIVLVK--HLARAG-YSRDrfemLLVTADEAWHISRPLVDfgMRQPVGVGDVT 226
Cdd:pfam08543 130 AEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKggHLEGEEaVVTD----VLYDGGGFYTLEAPRIP--TKNTHGTGCTL 203

                         170       180
                  ....*....|....*....|....*....
gi 16129594   227 SGLLLVKLLQGATLQEALEH----VTAAV 251
Cdd:pfam08543 204 SAAIAANLAKGLSLPEAVREakeyVTEAI 232
1-PFK TIGR03168
hexose kinase, 1-phosphofructokinase family; This family consists largely of ...
 141-250 1.46e-13

hexose kinase, 1-phosphofructokinase family; This family consists largely of 1-phosphofructokinases, but also includes tagatose-6-kinases and 6-phosphofructokinases.


Pssm-ID: 274464 [Multi-domain]  Cd Length: 303  Bit Score: 69.53  E-value: 1.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594   141 DIIAPNLVELEILCEHAVNNVEEAVLAARELIAQGPQIVLVKhLARAGysrdrfeMLLVTADEAWHISRPLVDfgMRQPV 220
Cdd:TIGR03168 178 FLIKPNHEELEELFGRELKTLEEIIEAARELLDRGAENVLVS-LGADG-------ALLVTKEGALKATPPKVE--VVNTV 247

                          90       100       110
                  ....*....|....*....|....*....|
gi 16129594   221 GVGDVTSGLLLVKLLQGATLQEALEHVTAA 250
Cdd:TIGR03168 248 GAGDSMVAGFLAGLARGLSLEEALRFAVAA 277
PRK07105 PRK07105
pyridoxamine kinase; Validated
 1-258 2.56e-13

pyridoxamine kinase; Validated


Pssm-ID: 180840 [Multi-domain]  Cd Length: 284  Bit Score: 68.40  E-value: 2.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594    1 MMKNILAIQSHVVYGHAGNSAAEFPMRRLGANVWPLNTVQFSNHT----QYGKWTgcvmppshLTEIVQG-IAAIDKLH- 74
Cdd:PRK07105   3 PVKRVAAIHDLSGFGRVALTASIPIMSSMGLQVCPLPTALLSSHTggfqNPSIID--------LTDGMQAfLTHWKSLNl 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594   75 TCDAVLSGYLGSAEQGEHILGIVRQVKaaNPQAKYFCDPVMGhpEKGCiVAPGVAEFHV---RHGLPASDIIAPNLVELE 151
Cdd:PRK07105  75 KFDAIYSGYLGSPRQIQIVSDFIKYFK--KKDLLVVVDPVMG--DNGK-LYQGFDQEMVeemRKLIQKADVITPNLTEAC 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594  152 ILCEHA---VNNVEEAVLA-ARELIAQGPQIVLV-------KHLARAGYSRDrfemllvtADEAWHISRPlvdfgmRQPV 220
Cdd:PRK07105 150 LLLDKPyleKSYSEEEIKQlLRKLADLGPKIVIItsvpfedGKIGVAYYDRA--------TDRFWKVFCK------YIPA 215

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 16129594  221 ---GVGDVTSGLLLVKLLQGATLQEALEHVTAAVYEIMVTT 258
Cdd:PRK07105 216 hypGTGDIFTSVITGSLLQGDSLPIALDRAVQFIEKGIRAT 256
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 77-213 2.99e-12

Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440120 [Multi-domain]  Cd Length: 254  Bit Score: 65.06  E-value: 2.99e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594  77 DAVLSGYLGSAEqgehILGIVRQVKAANPQAKYFCDPVM----GHPekgcIVAPGVAEFHVRHGLPASDIIAPNLVELEI 152
Cdd:COG0351  68 DAIKIGMLGSAE----IIEAVAEILADYPLVPVVLDPVMvaksGDR----LLDEDAVEALRELLLPLATVVTPNLPEAEA 139

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16129594 153 LCEHAVNNVEEAVLAARELIAQGPQIVLVK--HLArAGYSRDrfemLLVTADEAWHISRPLVD 213
Cdd:COG0351 140 LLGIEITTLDDMREAAKALLELGAKAVLVKggHLP-GDEAVD----VLYDGDGVREFSAPRID 197
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 133-250 3.72e-12

pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 65.44  E-value: 3.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594   133 VRHGLPASDIIAPNLVELEILCEHAVNNVEEAVLAARELIAQGPQIVLVKhLARAGysrdrfeMLLVTADEAWHISRP-- 210
Cdd:pfam00294 174 LLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVT-LGADG-------ALVVEGDGEVHVPAVpk 245

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 16129594   211 --LVDfgmrqPVGVGDVTSGLLLVKLLQGATLQEALEHVTAA 250
Cdd:pfam00294 246 vkVVD-----TTGAGDSFVGGFLAGLLAGKSLEEALRFANAA 282
PRK14713 PRK14713
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
63-262 4.88e-09

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 237797 [Multi-domain]  Cd Length: 530  Bit Score: 56.72  E-value: 4.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594   63 IVQGIAAIDKLHTCDAVLSGYLGSAEqgehILGIVRQVKAANPQAKYFCDPVMGHPEKGCIVAPGvAEFHVRHGLPASDI 142
Cdd:PRK14713  86 LRAQLDAVSDDVTVDAVKIGMLGDAE----VIDAVRTWLAEHRPPVVVLDPVMVATSGDRLLEED-AEAALRELVPRADL 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594  143 IAPNLVELEILCEHAVNNVEEAVLA-ARELIAQGPQIVLVK--HLAragySRDRFEMLLVTADEAWHISRPLVDfgMRQP 219
Cdd:PRK14713 161 ITPNLPELAVLLGEPPATTWEEALAqARRLAAETGTTVLVKggHLD----GQRAPDALVGPDGAVTEVPGPRVD--TRNT 234

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 16129594  220 VGVGDVTSGLLLVKLLQGATLQEALEHVTAAVYEIMVTTKAMQ 262
Cdd:PRK14713 235 HGTGCSLSSALATRLGRGGDWAAALRWATAWLHGAIAAGAALQ 277
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 77-251 8.06e-09

bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 55.13  E-value: 8.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594   77 DAVLSGYLGSAEqgehILGIVRQVKAANPQAKYFCDPVM----GHPekgcIVAPGVAEFHVRHGLPASDIIAPNLVELEI 152
Cdd:PRK06427  75 DAVKIGMLASAE----IIETVAEALKRYPIPPVVLDPVMiaksGDP----LLADDAVAALRERLLPLATLITPNLPEAEA 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594  153 LCEHAVNNVEEAVLAARELI-AQGPQIVLVK--HLARAGYSRDRfemlLVTADEAWHISRPLVDfgMRQPVGVGDVTSGL 229
Cdd:PRK06427 147 LTGLPIADTEDEMKAAARALhALGCKAVLIKggHLLDGEESVDW----LFDGEGEERFSAPRIP--TKNTHGTGCTLSAA 220

                        170       180
                 ....*....|....*....|....*.
gi 16129594  230 LLVKLLQGATLQEALEH----VTAAV 251
Cdd:PRK06427 221 IAAELAKGASLLDAVQTakdyVTRAI 246
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 71-250 1.29e-08

Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar or nucleoside kinase, ribokinase family is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 440290 [Multi-domain]  Cd Length: 301  Bit Score: 54.89  E-value: 1.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594  71 DKLHTCDAV-LSGYLGSAEQG-EHILGIVRQVKAANpqAKYFCDPVMGHpekgCIVAPGVAEFhvRHGLPASDIIAPNLV 148
Cdd:COG0524 123 ALLAGADILhLGGITLASEPPrEALLAALEAARAAG--VPVSLDPNYRP----ALWEPARELL--RELLALVDILFPNEE 194

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594 149 ELEILCEHavnnvEEAVLAARELIAQGPQIVLVKHLARAGYsrdrfemlLVTADEAWHISRP---LVDfgmrqPVGVGDV 225
Cdd:COG0524 195 EAELLTGE-----TDPEEAAAALLARGVKLVVVTLGAEGAL--------LYTGGEVVHVPAFpveVVD-----TTGAGDA 256

                       170       180
                ....*....|....*....|....*
gi 16129594 226 TSGLLLVKLLQGATLQEALEHVTAA 250
Cdd:COG0524 257 FAAGFLAGLLEGLDLEEALRFANAA 281
PRK11142 PRK11142
ribokinase; Provisional
 141-262 1.79e-05

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 45.25  E-value: 1.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594  141 DIIAPNLVELEILCEHAVNNVEEAVLAARELIAQGPQIVLVKHLARAGY-SRDRFEMLL----VTAdeawhisrplVDfg 215
Cdd:PRK11142 180 DIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRGVWlSENGEGQRVpgfrVQA----------VD-- 247

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 16129594  216 mrqPVGVGDVTSGLLLVKLLQGATLQEALE--HVTAAvyeIMVTTKAMQ 262
Cdd:PRK11142 248 ---TIAAGDTFNGALVTALLEGKPLPEAIRfaHAAAA---IAVTRKGAQ 290
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 73-235 1.83e-05

ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).


Pssm-ID: 238177 [Multi-domain]  Cd Length: 196  Bit Score: 44.39  E-value: 1.83e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594  73 LHTCDAV-LSGYLGSAEQGEHILGIVRQVKAAnpqakYFCDPVMghpekgcivaPGVAEFH--VRHGLPASDIIAPNLVE 149
Cdd:cd00287  55 LVGADAVvISGLSPAPEAVLDALEEARRRGVP-----VVLDPGP----------RAVRLDGeeLEKLLPGVDILTPNEEE 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594 150 LEILCEHAVNNVEEAVLAARELIAQGPQIVLVKHLARAGysrdrfemLLVTADEaWHISRPLVDFGMRQPVGVGDVTSGL 229
Cdd:cd00287 120 AEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGA--------IVATRGG-TEVHVPAFPVKVVDTTGAGDAFLAA 190


                ....*.
gi 16129594 230 LLVKLL 235
Cdd:cd00287 191 LAAGLA 196
PRK09517 PRK09517
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ...
 75-262 3.93e-05

multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 169939 [Multi-domain]  Cd Length: 755  Bit Score: 44.96  E-value: 3.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594   75 TCDAVLSGYLGSAEqgehilgIVRQVKA---ANPQAKYFCDPVMGHPEKGCIVAPGVAEfHVRHGLPASDIIAPNLVELE 151
Cdd:PRK09517 310 TVDAVKLGMLGSAD-------TVDLVASwlgSHEHGPVVLDPVMVATSGDRLLDADATE-ALRRLAVHVDVVTPNIPELA 381

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594  152 ILC-EHAVNNVEEAVLAARELIAQGPQIVLVK--HLaragySRDRFEMLLVTADEAWH-ISRPLVDfgMRQPVGVGDVTS 227
Cdd:PRK09517 382 VLCgEAPAITMDEAIAQARGFARTHGTIVIVKggHL-----TGDLADNAVVRPDGSVHqVENPRVN--TTNSHGTGCSLS 454

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 16129594  228 GLLLVKLLQGATLQEALEHVTAAVYEIMVTTKAMQ 262
Cdd:PRK09517 455 AALATLIAAGESVEKALEWATRWLNEALRHADHLA 489
PRK12413 PRK12413
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
137-182 1.19e-04

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183513 [Multi-domain]  Cd Length: 253  Bit Score: 42.74  E-value: 1.19e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 16129594  137 LPASDIIAPNLVELEILCEHAVNNVEEAVLAARELIAQGPQIVLVK 182
Cdd:PRK12413 127 FPYVTVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAVVIK 172
fruK PRK09513
1-phosphofructokinase; Provisional
 136-249 2.39e-04

1-phosphofructokinase; Provisional


Pssm-ID: 181923 [Multi-domain]  Cd Length: 312  Bit Score: 41.99  E-value: 2.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594  136 GLPASD-IIAPNLVELEILCEHAVNNVEEAVLAARELIAQGPQIVLVKHLARAGysrdrfemLLVTADEAWHISRPLVDf 214
Cdd:PRK09513 176 GLKAAPwLVKPNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGA--------LWVNASGEWIAKPPACD- 246

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 16129594  215 gMRQPVGVGDVTSGLLLVKLLQGATLQEALEHVTA 249
Cdd:PRK09513 247 -VVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATA 280
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
 118-244 3.74e-04

YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.


Pssm-ID: 238916 [Multi-domain]  Cd Length: 288  Bit Score: 41.15  E-value: 3.74e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594 118 PEKGCIVApgvaefHVRHGLPASDIIAPNLVELEILCEHAVNNVEEAVLAARELIAQGPQIVLVKHLARAGYSRDRFEml 197
Cdd:cd01941 161 PTSAPKLK------KLFYLLHAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSREG-- 232

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 16129594 198 lvtADEAWHISRPLVDfgmrQPV---GVGDVTSGLLLVKLLQGATLQEAL 244
Cdd:cd01941 233 ---GVETKLFPAPQPE----TVVnvtGAGDAFVAGLVAGLLEGMSLDDSL 275
PRK08573 PRK08573
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
77-184 3.39e-03

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 236297 [Multi-domain]  Cd Length: 448  Bit Score: 38.56  E-value: 3.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594   77 DAVLSGYLGSAEqgehilgIVRQVkaANPQAKY----FCDPVM----GHPekgcIVAPGVAEFHVRHGLPASDIIAPNLV 148
Cdd:PRK08573  73 DAAKTGMLSNRE-------IIEAV--AKTVSKYgfplVVDPVMiaksGAP----LLREDAVDALIKRLLPLATVVTPNRP 139

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 16129594  149 ELEILCEHAVNNVEEAVLAARELIAQ-GPQIVLVK--HL 184
Cdd:PRK08573 140 EAEKLTGMKIRSVEDARKAAKYIVEElGAEAVVVKggHL 178
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
 77-182 3.82e-03

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 38.60  E-value: 3.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16129594   77 DAVLSGYLGSAEqgehILGIVRQVKAANPQAKYFCDPVMGHPEKGCIVAPGVAEFHVRHGLPASDIIAPNLVELE-ILCE 155
Cdd:PLN02898  80 DVVKTGMLPSAE----IVKVLCQALKEFPVKALVVDPVMVSTSGDVLAGPSILSALREELLPLATIVTPNVKEASaLLGG 155

                         90       100
                 ....*....|....*....|....*..
gi 16129594  156 HAVNNVEEAVLAARELIAQGPQIVLVK 182
Cdd:PLN02898 156 DPLETVADMRSAAKELHKLGPRYVLVK 182
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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