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Conserved domains on  [gi|555038100|gb|ESL82415|]
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pyridoxamine kinase [Enterobacter roggenkampii]

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;
1-286 0e+00

pyridoxal kinase PdxY;


:

Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 535.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100   1 MKNILAIQSHVVFGHAGNSAAEFPMRRLGVNVWPLNTVQFSNHTQYGKWAGCVMPPSHLTEVVQGIADIDQLKRCDAVLS 80
Cdd:PRK05756   1 MKNILSIQSHVVYGHVGNSAAVFPMQRLGVNVWPLNTVQFSNHTGYGKWTGCVMPPSHLTEIVQGIADIGWLGECDAVLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100  81 GYLGSAEQGEHILGIVRQVKAANPSAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHPVNSV 160
Cdd:PRK05756  81 GYLGSAEQGEAILDAVRRVKAANPQALYFCDPVMGDPEKGCIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100 161 EEAVSASRELIAQGPEVVLVKHLARAGLSQDRFEMLLVTKEDAWHISRPLVDFGtRQPVGVGDVTSGLLLVKLLQGATVR 240
Cdd:PRK05756 161 EDAVAAARALIARGPKIVLVTSLARAGYPADRFEMLLVTADGAWHISRPLVDFM-RQPVGVGDLTSALFLARLLQGGSLE 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 555038100 241 DALEHVTAAVYEIMIATKEMQEYELQVVAAQDRIAKPEHYFSATQL 286
Cdd:PRK05756 240 EALEHTTAAVYEVMARTKERGSYELQLVAAQDSIATPRAMFQARRL 285
 
Name Accession Description Interval E-value
PRK05756 PRK05756
pyridoxal kinase PdxY;
1-286 0e+00

pyridoxal kinase PdxY;


Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 535.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100   1 MKNILAIQSHVVFGHAGNSAAEFPMRRLGVNVWPLNTVQFSNHTQYGKWAGCVMPPSHLTEVVQGIADIDQLKRCDAVLS 80
Cdd:PRK05756   1 MKNILSIQSHVVYGHVGNSAAVFPMQRLGVNVWPLNTVQFSNHTGYGKWTGCVMPPSHLTEIVQGIADIGWLGECDAVLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100  81 GYLGSAEQGEHILGIVRQVKAANPSAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHPVNSV 160
Cdd:PRK05756  81 GYLGSAEQGEAILDAVRRVKAANPQALYFCDPVMGDPEKGCIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100 161 EEAVSASRELIAQGPEVVLVKHLARAGLSQDRFEMLLVTKEDAWHISRPLVDFGtRQPVGVGDVTSGLLLVKLLQGATVR 240
Cdd:PRK05756 161 EDAVAAARALIARGPKIVLVTSLARAGYPADRFEMLLVTADGAWHISRPLVDFM-RQPVGVGDLTSALFLARLLQGGSLE 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 555038100 241 DALEHVTAAVYEIMIATKEMQEYELQVVAAQDRIAKPEHYFSATQL 286
Cdd:PRK05756 240 EALEHTTAAVYEVMARTKERGSYELQLVAAQDSIATPRAMFQARRL 285
pyridox_kin TIGR00687
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ...
 1-286 9.97e-170

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: 471.24  E-value: 9.97e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100    1 MKNILAIQSHVVFGHAGNSAAEFPMRRLGVNVWPLNTVQFSNHTQYGKWAGCVMPPSHLTEVVQGIADIDQLKRCDAVLS 80
Cdd:TIGR00687   1 MKNVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLEAINKLNQCDAVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100   81 GYLGSAEQGEHILGIVRQVKAANPSAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHPVNSV 160
Cdd:TIGR00687  81 GYLGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKGCYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100  161 EEAVSASRELIAQGPEVVLVKHLARAGLSQDR-FEMLLVTKEDAWHISRPLVDFgTRQPVGVGDVTSGLLLVKLLQGATV 239
Cdd:TIGR00687 161 EEALAAADALIAMGPDIVLVTHLIRAGSQRDRsFEGLVATQEGRWHISRPLAVF-DPPPVGTGDLIAALLLATLLHGNSL 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 555038100  240 RDALEHVTAAVYEIMIATKEMQEYELQVVAAQDRIAKPEHYFSATQL 286
Cdd:TIGR00687 240 KEALEKTVSAVYHVLRTTIQLGKYELQPVAAQLEIRMPQSKFDAEKV 286
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 1-275 2.16e-138

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: 391.05  E-value: 2.16e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100   1 MKNILAIQSHVVFGHAGNSAAEFPMRRLGVNVWPLNTVQFSNHTQYGKWAGCVMPPSHLTEVVQGIADIDQLKRCDAVLS 80
Cdd:COG2240    1 MKRVLSIQSHVVYGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWKELGVLLEFDAVLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100  81 GYLGSAEQGEHILGIVRQVKAANPSAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHPVNSV 160
Cdd:COG2240   81 GYLGSAEQGDIIADFVARVKAANPDALYLCDPVMGDNGKGYYVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100 161 EEAVSASRELIAQGPEVVLVKHLARAGLSQDRFEMLLVTKEDAWHISRPLVDFgtrQPVGVGDVTSGLLLVKLLQGATVR 240
Cdd:COG2240  161 EEALAAARALLALGPKIVVVTSVPLDDTPADKIGNLAVTADGAWLVETPLLPF---SPNGTGDLFAALLLAHLLRGKSLE 237

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 555038100 241 DALEHVTAAVYEIMIATKEMQEYELQVVAAQDRIA 275
Cdd:COG2240  238 EALERAAAFVYEVLERTAAAGSDELLLEAALDELV 272
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 3-259 2.31e-111

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: 321.84  E-value: 2.31e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100   3 NILAIQSHVVFGHAGNSAAEFPMRRLGVNVWPLNTVQFSNHTQYGKWAGCVMPPSHLTEVVQGIADIDQLKRCDAVLSGY 82
Cdd:cd01173    1 RVLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLLLEYDAVLTGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100  83 LGSAEQGEHILGIVRQVKAANPSAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHPVNSVEE 162
Cdd:cd01173   81 LGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGDNGKLYVVAEEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLED 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100 163 AVSASRELIAQGPEVVLVKHLARAGlsQDRFEMLLVTKEDAWHISRPLVDFGTrQPVGVGDVTSGLLLVKLLQGATVRDA 242
Cdd:cd01173  161 AKAAARALHAKGPKTVVVTSVELAD--DDRIEMLGSTATEAWLVQRPKIPFPA-YFNGTGDLFAALLLARLLKGKSLAEA 237

                        250
                 ....*....|....*..
gi 555038100 243 LEHVTAAVYEIMIATKE 259
Cdd:cd01173  238 LEKALNFVHEVLEATYE 254
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 63-250 4.35e-15

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: 72.90  E-value: 4.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100   63 VQGIADID------QLK------RCDAVLSGYLGSAEqgehilgIVRQV--KAANPSAKYFCDPVM----GHPekgcIVA 124
Cdd:pfam08543  37 VQGVHPLPpefvaaQLDavlediPVDAVKTGMLGSAE-------IIEAVaeKLDKYGVPVVLDPVMvaksGDS----LLD 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100  125 PGVAEFHVRHALPASDIIAPNLVELEILCEHPVNSVEEAVSASRELIAQGPEVVLVK--HLAragLSQDRFEMLLVTKED 202
Cdd:pfam08543 106 DEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKggHLE---GEEAVVTDVLYDGGG 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 555038100  203 AWHISRPLVDfgTRQPVGVGDVTSGLLLVKLLQGATVRDALEH----VTAAV 250
Cdd:pfam08543 183 FYTLEAPRIP--TKNTHGTGCTLSAAIAANLAKGLSLPEAVREakeyVTEAI 232
 
Name Accession Description Interval E-value
PRK05756 PRK05756
pyridoxal kinase PdxY;
1-286 0e+00

pyridoxal kinase PdxY;


Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 535.99  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100   1 MKNILAIQSHVVFGHAGNSAAEFPMRRLGVNVWPLNTVQFSNHTQYGKWAGCVMPPSHLTEVVQGIADIDQLKRCDAVLS 80
Cdd:PRK05756   1 MKNILSIQSHVVYGHVGNSAAVFPMQRLGVNVWPLNTVQFSNHTGYGKWTGCVMPPSHLTEIVQGIADIGWLGECDAVLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100  81 GYLGSAEQGEHILGIVRQVKAANPSAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHPVNSV 160
Cdd:PRK05756  81 GYLGSAEQGEAILDAVRRVKAANPQALYFCDPVMGDPEKGCIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100 161 EEAVSASRELIAQGPEVVLVKHLARAGLSQDRFEMLLVTKEDAWHISRPLVDFGtRQPVGVGDVTSGLLLVKLLQGATVR 240
Cdd:PRK05756 161 EDAVAAARALIARGPKIVLVTSLARAGYPADRFEMLLVTADGAWHISRPLVDFM-RQPVGVGDLTSALFLARLLQGGSLE 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 555038100 241 DALEHVTAAVYEIMIATKEMQEYELQVVAAQDRIAKPEHYFSATQL 286
Cdd:PRK05756 240 EALEHTTAAVYEVMARTKERGSYELQLVAAQDSIATPRAMFQARRL 285
pyridox_kin TIGR00687
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ...
 1-286 9.97e-170

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: 471.24  E-value: 9.97e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100    1 MKNILAIQSHVVFGHAGNSAAEFPMRRLGVNVWPLNTVQFSNHTQYGKWAGCVMPPSHLTEVVQGIADIDQLKRCDAVLS 80
Cdd:TIGR00687   1 MKNVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLEAINKLNQCDAVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100   81 GYLGSAEQGEHILGIVRQVKAANPSAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHPVNSV 160
Cdd:TIGR00687  81 GYLGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKGCYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100  161 EEAVSASRELIAQGPEVVLVKHLARAGLSQDR-FEMLLVTKEDAWHISRPLVDFgTRQPVGVGDVTSGLLLVKLLQGATV 239
Cdd:TIGR00687 161 EEALAAADALIAMGPDIVLVTHLIRAGSQRDRsFEGLVATQEGRWHISRPLAVF-DPPPVGTGDLIAALLLATLLHGNSL 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 555038100  240 RDALEHVTAAVYEIMIATKEMQEYELQVVAAQDRIAKPEHYFSATQL 286
Cdd:TIGR00687 240 KEALEKTVSAVYHVLRTTIQLGKYELQPVAAQLEIRMPQSKFDAEKV 286
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 1-275 2.16e-138

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: 391.05  E-value: 2.16e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100   1 MKNILAIQSHVVFGHAGNSAAEFPMRRLGVNVWPLNTVQFSNHTQYGKWAGCVMPPSHLTEVVQGIADIDQLKRCDAVLS 80
Cdd:COG2240    1 MKRVLSIQSHVVYGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWKELGVLLEFDAVLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100  81 GYLGSAEQGEHILGIVRQVKAANPSAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHPVNSV 160
Cdd:COG2240   81 GYLGSAEQGDIIADFVARVKAANPDALYLCDPVMGDNGKGYYVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100 161 EEAVSASRELIAQGPEVVLVKHLARAGLSQDRFEMLLVTKEDAWHISRPLVDFgtrQPVGVGDVTSGLLLVKLLQGATVR 240
Cdd:COG2240  161 EEALAAARALLALGPKIVVVTSVPLDDTPADKIGNLAVTADGAWLVETPLLPF---SPNGTGDLFAALLLAHLLRGKSLE 237

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 555038100 241 DALEHVTAAVYEIMIATKEMQEYELQVVAAQDRIA 275
Cdd:COG2240  238 EALERAAAFVYEVLERTAAAGSDELLLEAALDELV 272
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 3-259 2.31e-111

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: 321.84  E-value: 2.31e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100   3 NILAIQSHVVFGHAGNSAAEFPMRRLGVNVWPLNTVQFSNHTQYGKWAGCVMPPSHLTEVVQGIADIDQLKRCDAVLSGY 82
Cdd:cd01173    1 RVLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLLLEYDAVLTGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100  83 LGSAEQGEHILGIVRQVKAANPSAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHPVNSVEE 162
Cdd:cd01173   81 LGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGDNGKLYVVAEEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLED 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100 163 AVSASRELIAQGPEVVLVKHLARAGlsQDRFEMLLVTKEDAWHISRPLVDFGTrQPVGVGDVTSGLLLVKLLQGATVRDA 242
Cdd:cd01173  161 AKAAARALHAKGPKTVVVTSVELAD--DDRIEMLGSTATEAWLVQRPKIPFPA-YFNGTGDLFAALLLARLLKGKSLAEA 237

                        250
                 ....*....|....*..
gi 555038100 243 LEHVTAAVYEIMIATKE 259
Cdd:cd01173  238 LEKALNFVHEVLEATYE 254
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
 2-286 1.89e-52

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 173.34  E-value: 1.89e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100   2 KNILAIQSHVVFGHAGNSAAEFPMRRLGVNVWPLNTVQFSNHTQYGKWAGCVMPPSHLTEVVQGIADIDQLKRCDAVLSG 81
Cdd:PTZ00344   5 KKVLSIQSHVTHGYVGNRAATFPLQLLGFDVDFVNTVQLSNHTGYPVIKGHRLDLNELITLMDGLRANNLLSDYTYVLTG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100  82 YLGSAEQGEHILGIVRQVKAANPSAKYFCDPVMGHPEKGCIVAPGVAEFhvRHALPASDIIAPNLVELEILCEHPVNSVE 161
Cdd:PTZ00344  85 YINSADILREVLATVKEIKELRPKLIFLCDPVMGDDGKLYVKEEVVDAY--RELIPYADVITPNQFEASLLSGVEVKDLS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100 162 EAVSASRELIAQGPEVVLVKHLARAGLSQD-RFEMLLVTKEDA----WHISRPLVDFgtrQPVGVGDVTSGLLLVKLLQG 236
Cdd:PTZ00344 163 DALEAIDWFHEQGIPVVVITSFREDEDPTHlRFLLSCRDKDTKnnkrFTGKVPYIEG---RYTGTGDLFAALLLAFSHQH 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 555038100 237 AtVRDALEHVTAAVYEIMIATKE--------MQEYELQVVAAQDRIAKPEHYFSATQL 286
Cdd:PTZ00344 240 P-MDLAVGKAMGVLQDIIKATREsggsgsssLMSRELRLIQSPRDLLNPETVFKVTPL 296
pdxK PRK08176
pyridoxine/pyridoxal/pyridoxamine kinase;
3-266 2.64e-44

pyridoxine/pyridoxal/pyridoxamine kinase;


Pssm-ID: 181269 [Multi-domain]  Cd Length: 281  Bit Score: 151.73  E-value: 2.64e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100   3 NILAIQSHVVFGHAGNSAAEFPMRRLGVNVWPLNTVQFSNHTQYGKWAGCVMPPSHLTEVVQGIADIDQLKRCDAVLSGY 82
Cdd:PRK08176  17 DIVAVQSQVVYGSVGNSIAVPAIKANGLRVFAVPTVLLSNTPHYPTFYGGAIPDEWFSGYLRALQERDALRQLRAVTTGY 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100  83 LGSAEQGEHILGIVRQVKAANPSAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHPVNSVEE 162
Cdd:PRK08176  97 MGSASQIKILAEWLTALRADHPDLLIMVDPVIGDIDSGIYVKPDLPEAYRQHLLPLAQGLTPNIFELEILTGKPCRTLDS 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100 163 AVSASRELIAQGPEVVLVKHlARAGLSQDRFEMLLVTKEDAWHISRPLVDfgtRQPVGVGDVTSGLLLVKLLQGATVRDA 242
Cdd:PRK08176 177 AIAAAKSLLSDTLKWVVITS-AAGNEENQEMQVVVVTADSVNVISHPRVD---TDLKGTGDLFCAELVSGLLKGKALTDA 252

                        250       260
                 ....*....|....*....|....
gi 555038100 243 LEHVTAAVYEIMIATKEMQEYELQ 266
Cdd:PRK08176 253 AHRAGLRVLEVMRYTQQAGSDELI 276
PLN02978 PLN02978
pyridoxal kinase
 4-286 2.98e-41

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 144.50  E-value: 2.98e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100   4 ILAIQSHVVFGHAGNSAAEFPMRRLGVNVWPLNTVQFSNHTQYGKWAGCVMPPSHLTEVVQGIADIDQLKRCDaVLSGYL 83
Cdd:PLN02978  17 VLSIQSHTVHGYVGNKSAVFPLQLLGFDVDPINSVQFSNHTGYPTFKGQVLDGEQLWALIEGLEANGLLFYTH-LLTGYI 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100  84 GSAEQGEHILGIVRQVKAANPSAKYFCDPVMGHPEKgCIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHPVNSVEEA 163
Cdd:PLN02978  96 GSVSFLRTVLRVVKKLRSVNPNLTYVCDPVLGDEGK-LYVPPELVPVYREKVVPLATMLTPNQFEAEQLTGIRIVTEEDA 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100 164 VSASRELIAQGPEVVLVKHLARAGlsqdrfEMLLV--------TKEDAWHISRPlvdfgtRQP---VGVGDVTSGLLL-- 230
Cdd:PLN02978 175 REACAILHAAGPSKVVITSIDIDG------KLLLVgshrkekgARPEQFKIVIP------KIPayfTGTGDLMAALLLgw 242

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 555038100 231 ---------------VKLLQgatvrdALEHVTAAVYEIMIATKEMQEYELQVVAAQDRIAKPEHYFSATQL 286
Cdd:PLN02978 243 shkypdnldkaaelaVSSLQ------AVLRRTLADYKRAGADPKSSSLELRLVQSQDDIRHPQVRFKAERY 307
FruK_PfkB_like cd01164
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ...
 133-249 4.39e-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: 76.42  E-value: 4.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100 133 RHALPAS-DIIAPNLVELEILCEHPVNSVEEAVSASRELIAQGPEVVLVKhLARAGlsqdrfeMLLVTKEDAWHISRPLV 211
Cdd:cd01164  171 LAALAAKpFLIKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVS-LGADG-------ALLVTKDGVYRASPPKV 242

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 555038100 212 DfgTRQPVGVGDVTSGLLLVKLLQGATVRDALEHVTAA 249
Cdd:cd01164  243 K--VVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAA 278
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
133-249 7.10e-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: 7.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100 133 RHALPAS-DIIAPNLVELEILCEHPVNSVEEAVSASRELIAQGPEVVLVKhLARAGlsqdrfeMLLVTKEDAWHISRPLV 211
Cdd:COG1105  171 KAALEAGpDLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVS-LGADG-------ALLVTEDGVYRAKPPKV 242

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 555038100 212 DfgTRQPVGVGDVTSGLLLVKLLQGATVRDALEHVTAA 249
Cdd:COG1105  243 E--VVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAA 278
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 63-250 4.35e-15

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: 72.90  E-value: 4.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100   63 VQGIADID------QLK------RCDAVLSGYLGSAEqgehilgIVRQV--KAANPSAKYFCDPVM----GHPekgcIVA 124
Cdd:pfam08543  37 VQGVHPLPpefvaaQLDavlediPVDAVKTGMLGSAE-------IIEAVaeKLDKYGVPVVLDPVMvaksGDS----LLD 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100  125 PGVAEFHVRHALPASDIIAPNLVELEILCEHPVNSVEEAVSASRELIAQGPEVVLVK--HLAragLSQDRFEMLLVTKED 202
Cdd:pfam08543 106 DEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKggHLE---GEEAVVTDVLYDGGG 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 555038100  203 AWHISRPLVDfgTRQPVGVGDVTSGLLLVKLLQGATVRDALEH----VTAAV 250
Cdd:pfam08543 183 FYTLEAPRIP--TKNTHGTGCTLSAAIAANLAKGLSLPEAVREakeyVTEAI 232
PRK07105 PRK07105
pyridoxamine kinase; Validated
 1-257 1.43e-13

pyridoxamine kinase; Validated


Pssm-ID: 180840 [Multi-domain]  Cd Length: 284  Bit Score: 69.17  E-value: 1.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100   1 MKNILAIQSHVVFGHAGNSAAEFPMRRLGVNVWPLNTVQFSNHTQYGKwagcvmPPS--HLTEVVQGIadIDQLKR---- 74
Cdd:PRK07105   4 VKRVAAIHDLSGFGRVALTASIPIMSSMGLQVCPLPTALLSSHTGGFQ------NPSiiDLTDGMQAF--LTHWKSlnlk 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100  75 CDAVLSGYLGSAEQGEHILGIVRQVKaaNPSAKYFCDPVMGhpEKGCiVAPGVAEFHV---RHALPASDIIAPNLVELEI 151
Cdd:PRK07105  76 FDAIYSGYLGSPRQIQIVSDFIKYFK--KKDLLVVVDPVMG--DNGK-LYQGFDQEMVeemRKLIQKADVITPNLTEACL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100 152 LCEHPV----NSVEEAVSASRELIAQGPEVVLVkhlarAGLSQDRFEMLLV----TKEDAWHIsrplvdFGTRQPV---G 220
Cdd:PRK07105 151 LLDKPYleksYSEEEIKQLLRKLADLGPKIVII-----TSVPFEDGKIGVAyydrATDRFWKV------FCKYIPAhypG 219

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 555038100 221 VGDVTSGLLLVKLLQGATVRDALEHVTAAVYEIMIAT 257
Cdd:PRK07105 220 TGDIFTSVITGSLLQGDSLPIALDRAVQFIEKGIRAT 256
HMPP_kinase cd01169
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ...
 74-250 3.00e-13

4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two consecutive phosphorylation steps in the thiamine phosphate biosynthesis pathway, leading to the synthesis of vitamin B1. The first step is the phosphorylation of the hydroxyl group of HMP to form 4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate (HMP-P) and then the phophorylation of HMP-P to form 4-amino-5-hydroxymethyl-2-methyl-pyrimidine pyrophosphate (HMP-PP), which is the substrate for the thiamine synthase coupling reaction.


Pssm-ID: 238574 [Multi-domain]  Cd Length: 242  Bit Score: 67.53  E-value: 3.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100  74 RCDAVLSGYLGSAEqgehILGIVRQVKAANPSAKYFCDPVM----GHPekgcIVAPGVAEFHVRHALPASDIIAPNLVEL 149
Cdd:cd01169   68 PVDAIKIGMLGSAE----IIEAVAEALKDYPDIPVVLDPVMvaksGDS----LLDDDAIEALRELLLPLATLITPNLPEA 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100 150 EILCEHPVNSVEEAVSASRELIAQGPEVVLVK--HLaRAGLSQDrfemLLVTKEDAWHISRPLVDfgTRQPVGVGDVTSG 227
Cdd:cd01169  140 ELLTGLEIATEEDMMKAAKALLALGAKAVLIKggHL-PGDEAVD----VLYDGGGFFEFESPRID--TKNTHGTGCTLSS 212

                        170       180
                 ....*....|....*....|....*..
gi 555038100 228 LLLVKLLQGAT----VRDALEHVTAAV 250
Cdd:cd01169  213 AIAANLAKGLSleeaVREAKEYVTQAI 239
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 60-249 1.25e-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: 66.22  E-value: 1.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100  60 TEVVQGIADID------QLkrcDAVLS---------GYLGSAEQGEHILGIVRQVKAANpsakYFCDPVM----GHPekg 120
Cdd:COG0351   40 TLGVTGVHPVPpefvaaQL---RAVLEdipvdaikiGMLGSAEIIEAVAEILADYPLVP----VVLDPVMvaksGDR--- 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100 121 cIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHPVNSVEEAVSASRELIAQGPEVVLVK--HLArAGLSQDrfemLLV 198
Cdd:COG0351  110 -LLDEDAVEALRELLLPLATVVTPNLPEAEALLGIEITTLDDMREAAKALLELGAKAVLVKggHLP-GDEAVD----VLY 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 555038100 199 TKEDAWHISRPLVDfgTRQPVGVGDVTSGLLLVKLLQGATVRDALEH----VTAA 249
Cdd:COG0351  184 DGDGVREFSAPRID--TGNTHGTGCTLSSAIAALLAKGLDLEEAVREakeyVTQA 236
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 132-249 1.57e-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: 66.21  E-value: 1.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100  132 VRHALPASDIIAPNLVELEILCEHPVNSVEEAVSASRELIAQGPEVVLVKhLARAGlsqdrfeMLLVTKEDAWHISRP-- 209
Cdd:pfam00294 174 LLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVT-LGADG-------ALVVEGDGEVHVPAVpk 245

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 555038100  210 --LVDfgtrqPVGVGDVTSGLLLVKLLQGATVRDALEHVTAA 249
Cdd:pfam00294 246 vkVVD-----TTGAGDSFVGGFLAGLLAGKSLEEALRFANAA 282
1-PFK TIGR03168
hexose kinase, 1-phosphofructokinase family; This family consists largely of ...
 140-249 1.58e-12

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: 66.44  E-value: 1.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100  140 DIIAPNLVELEILCEHPVNSVEEAVSASRELIAQGPEVVLVKhLARAGlsqdrfeMLLVTKEDAWHISRPLVDFGTrqPV 219
Cdd:TIGR03168 178 FLIKPNHEELEELFGRELKTLEEIIEAARELLDRGAENVLVS-LGADG-------ALLVTKEGALKATPPKVEVVN--TV 247

                          90       100       110
                  ....*....|....*....|....*....|
gi 555038100  220 GVGDVTSGLLLVKLLQGATVRDALEHVTAA 249
Cdd:TIGR03168 248 GAGDSMVAGFLAGLARGLSLEEALRFAVAA 277
PRK14713 PRK14713
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
76-248 6.68e-10

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 237797 [Multi-domain]  Cd Length: 530  Bit Score: 59.42  E-value: 6.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100  76 DAVLSGYLGSAEqgehILGIVRQVKAANPSAKYFCDPVMGHPEKGCIVAPGvAEFHVRHALPASDIIAPNLVELEILCEH 155
Cdd:PRK14713 100 DAVKIGMLGDAE----VIDAVRTWLAEHRPPVVVLDPVMVATSGDRLLEED-AEAALRELVPRADLITPNLPELAVLLGE 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100 156 PVNSV-EEAVSASRELIAQGPEVVLVK--HLAraglSQDRFEMLLVTKEDAWHISRPLVDfgTRQPVGVGDVTSGLLLVK 232
Cdd:PRK14713 175 PPATTwEEALAQARRLAAETGTTVLVKggHLD----GQRAPDALVGPDGAVTEVPGPRVD--TRNTHGTGCSLSSALATR 248

                        170
                 ....*....|....*.
gi 555038100 233 LLQGATVRDALEHVTA 248
Cdd:PRK14713 249 LGRGGDWAAALRWATA 264
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 76-250 3.67e-09

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 56.29  E-value: 3.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100  76 DAVLSGYLGSAEqgehILGIVRQVKAANPSAKYFCDPVM----GHPekgcIVAPGVAEFHVRHALPASDIIAPNLVELEI 151
Cdd:PRK06427  75 DAVKIGMLASAE----IIETVAEALKRYPIPPVVLDPVMiaksGDP----LLADDAVAALRERLLPLATLITPNLPEAEA 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100 152 LCEHPVNSVEEAV-SASRELIAQGPEVVLVK--HLARAGLSQDRfemlLVTKEDAWHISRPLVDfgTRQPVGVGDVTSGL 228
Cdd:PRK06427 147 LTGLPIADTEDEMkAAARALHALGCKAVLIKggHLLDGEESVDW----LFDGEGEERFSAPRIP--TKNTHGTGCTLSAA 220

                        170       180
                 ....*....|....*....|....*.
gi 555038100 229 LLVKLLQGATVRDALEH----VTAAV 250
Cdd:PRK06427 221 IAAELAKGASLLDAVQTakdyVTRAI 246
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 68-249 1.00e-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: 55.28  E-value: 1.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100  68 DIDQLKRCDAV-LSGYLGSAEQG-EHILGIVRQVKAANpsAKYFCDPVMGHpekgCIVAPGVAEFhvRHALPASDIIAPN 145
Cdd:COG0524  121 DEALLAGADILhLGGITLASEPPrEALLAALEAARAAG--VPVSLDPNYRP----ALWEPARELL--RELLALVDILFPN 192

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100 146 LVELEILCEHPvnSVEEAVsasRELIAQGPEVVLVKhLARAGLsqdrfemLLVTKEDAWHISRP---LVDfgtrqPVGVG 222
Cdd:COG0524  193 EEEAELLTGET--DPEEAA---AALLARGVKLVVVT-LGAEGA-------LLYTGGEVVHVPAFpveVVD-----TTGAG 254

                        170       180
                 ....*....|....*....|....*..
gi 555038100 223 DVTSGLLLVKLLQGATVRDALEHVTAA 249
Cdd:COG0524  255 DAFAAGFLAGLLEGLDLEEALRFANAA 281
PRK09517 PRK09517
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ...
 76-248 2.96e-07

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


Pssm-ID: 169939 [Multi-domain]  Cd Length: 755  Bit Score: 51.51  E-value: 2.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100  76 DAVLSGYLGSAEqgehilgIVRQVKA---ANPSAKYFCDPVMGHPEKGCIVAPGVAEfHVRHALPASDIIAPNLVELEIL 152
Cdd:PRK09517 312 DAVKLGMLGSAD-------TVDLVASwlgSHEHGPVVLDPVMVATSGDRLLDADATE-ALRRLAVHVDVVTPNIPELAVL 383

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100 153 C-EHPVNSVEEAVSASRELIAQGPEVVLVKHlarAGLSQDRFEMLLVTKEDAWH-ISRPLVDfgTRQPVGVGDVTSGLLL 230
Cdd:PRK09517 384 CgEAPAITMDEAIAQARGFARTHGTIVIVKG---GHLTGDLADNAVVRPDGSVHqVENPRVN--TTNSHGTGCSLSAALA 458

                        170
                 ....*....|....*...
gi 555038100 231 VKLLQGATVRDALEHVTA 248
Cdd:PRK09517 459 TLIAAGESVEKALEWATR 476
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 77-234 2.25e-06

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: 47.09  E-value: 2.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100  77 AVLSGYLGSAEQGEHILGIVRQVKAAnpsakYFCDPVMghpekgcivaPGVAEFH--VRHALPASDIIAPNLVELEILCE 154
Cdd:cd00287   61 VVISGLSPAPEAVLDALEEARRRGVP-----VVLDPGP----------RAVRLDGeeLEKLLPGVDILTPNEEEAEALTG 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100 155 HPVNSVEEAVSASRELIAQGPEVVLVKHLARAGLSQDRfemllvtkeDAWHISRPLVDFGTRQPVGVGDVTSGLLLVKLL 234
Cdd:cd00287  126 RRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATR---------GGTEVHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
PRK12413 PRK12413
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
136-252 3.63e-05

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183513 [Multi-domain]  Cd Length: 253  Bit Score: 44.28  E-value: 3.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100 136 LPASDIIAPNLVELEILCEHPVNSVEEAVSASRELIAQGPEVVLVKHLARagLSQDRFEMLLVTKEDAWHISRPLVDfgt 215
Cdd:PRK12413 127 FPYVTVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAVVIKGGNR--LSQKKAIDLFYDGKEFVILESPVLE--- 201

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 555038100 216 RQPVGVGDVTSGLLLVKLLQGATVRDALEHVTAAVYE 252
Cdd:PRK12413 202 KNNIGAGCTFASSIASQLVKGKSPLEAVKNSKDFVYQ 238
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
 76-181 3.90e-04

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 41.68  E-value: 3.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100  76 DAVLSGYLGSAEqgehILGIVRQVKAANPSAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLVELE-ILCE 154
Cdd:PLN02898  80 DVVKTGMLPSAE----IVKVLCQALKEFPVKALVVDPVMVSTSGDVLAGPSILSALREELLPLATIVTPNVKEASaLLGG 155

                         90       100
                 ....*....|....*....|....*..
gi 555038100 155 HPVNSVEEAVSASRELIAQGPEVVLVK 181
Cdd:PLN02898 156 DPLETVADMRSAAKELHKLGPRYVLVK 182
fruK PRK09513
1-phosphofructokinase; Provisional
 141-248 5.25e-04

1-phosphofructokinase; Provisional


Pssm-ID: 181923 [Multi-domain]  Cd Length: 312  Bit Score: 40.83  E-value: 5.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100 141 IIAPNLVELEILCEHPVNSVEEAVSASRELIAQGPEVVLVKHLARAGlsqdrfemLLVTKEDAWHISRPLVDFGTrqPVG 220
Cdd:PRK09513 183 LVKPNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGA--------LWVNASGEWIAKPPACDVVS--TVG 252

                         90       100
                 ....*....|....*....|....*...
gi 555038100 221 VGDVTSGLLLVKLLQGATVRDALEHVTA 248
Cdd:PRK09513 253 AGDSMVGGLIYGLLMRESSEHTLRLATA 280
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
 101-243 1.19e-03

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: 39.60  E-value: 1.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 555038100 101 AANPSAKYFCDPVmghpeKGCIVApgvaefHVRHALPASDIIAPNLVELEILCEHPVNSVEEAVSASRELIAQGPEVVLV 180
Cdd:cd01941  150 AAKHGVPVAFEPT-----SAPKLK------KLFYLLHAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIV 218

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 555038100 181 KHLARAGLSQDRfEMLLVTKEDAWHISRPLVDfgtrqpV-GVGDVTSGLLLVKLLQGATVRDAL 243
Cdd:cd01941  219 TLGAKGVLLSSR-EGGVETKLFPAPQPETVVN------VtGAGDAFVAGLVAGLLEGMSLDDSL 275
 
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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