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Conserved domains on  [gi|1049326242|ref|WP_065822973|]
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pyridoxal kinase PdxY [Photorhabdus australis]

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;
1-287 0e+00

pyridoxal kinase PdxY;


:

Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 543.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242   1 MKNILSIQSHVVFGHAGNSAAEFPMRRMGVNVWPLNTVQFSNHTQYAQWKGCVMPAGHLTEVVQGIEEIGQLKSCHAVLS 80
Cdd:PRK05756    1 MKNILSIQSHVVYGHVGNSAAVFPMQRLGVNVWPLNTVQFSNHTGYGKWTGCVMPPSHLTEIVQGIADIGWLGECDAVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242  81 GYIGSPEQGSHIIDIVKRVKAANPDAWYFCDPVMGHPEKGCIVAPGVTEFLCEKALPASDVIAPNLLELETLSMQKVTNV 160
Cdd:PRK05756   81 GYLGSAEQGEAILDAVRRVKAANPQALYFCDPVMGDPEKGCIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242 161 EQAVTAARTLCEKGPGIVLVKHLSRAGYQTDCFEMLLVTQEHSWHVSRPLVDFGGcQPVGVGDLTSGLLLVNLLKGESLQ 240
Cdd:PRK05756  161 EDAVAAARALIARGPKIVLVTSLARAGYPADRFEMLLVTADGAWHISRPLVDFMR-QPVGVGDLTSALFLARLLQGGSLE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1049326242 241 TALEHVAAAVYEVMVTTKDMDEYELQIVAAQDRMVAPDHKFCATQLD 287
Cdd:PRK05756  240 EALEHTTAAVYEVMARTKERGSYELQLVAAQDSIATPRAMFQARRLA 286
 
Name Accession Description Interval E-value
PRK05756 PRK05756
pyridoxal kinase PdxY;
1-287 0e+00

pyridoxal kinase PdxY;


Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 543.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242   1 MKNILSIQSHVVFGHAGNSAAEFPMRRMGVNVWPLNTVQFSNHTQYAQWKGCVMPAGHLTEVVQGIEEIGQLKSCHAVLS 80
Cdd:PRK05756    1 MKNILSIQSHVVYGHVGNSAAVFPMQRLGVNVWPLNTVQFSNHTGYGKWTGCVMPPSHLTEIVQGIADIGWLGECDAVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242  81 GYIGSPEQGSHIIDIVKRVKAANPDAWYFCDPVMGHPEKGCIVAPGVTEFLCEKALPASDVIAPNLLELETLSMQKVTNV 160
Cdd:PRK05756   81 GYLGSAEQGEAILDAVRRVKAANPQALYFCDPVMGDPEKGCIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242 161 EQAVTAARTLCEKGPGIVLVKHLSRAGYQTDCFEMLLVTQEHSWHVSRPLVDFGGcQPVGVGDLTSGLLLVNLLKGESLQ 240
Cdd:PRK05756  161 EDAVAAARALIARGPKIVLVTSLARAGYPADRFEMLLVTADGAWHISRPLVDFMR-QPVGVGDLTSALFLARLLQGGSLE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1049326242 241 TALEHVAAAVYEVMVTTKDMDEYELQIVAAQDRMVAPDHKFCATQLD 287
Cdd:PRK05756  240 EALEHTTAAVYEVMARTKERGSYELQLVAAQDSIATPRAMFQARRLA 286
pyridox_kin TIGR00687
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ...
 1-287 1.42e-152

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: 427.71  E-value: 1.42e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242   1 MKNILSIQSHVVFGHAGNSAAEFPMRRMGVNVWPLNTVQFSNHTQYAQWKGCVMPAGHLTEVVQGIEEIGQLKSCHAVLS 80
Cdd:TIGR00687   1 MKNVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLEAINKLNQCDAVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242  81 GYIGSPEQGSHIIDIVKRVKAANPDAWYFCDPVMGHPEKGCIVAPGVTEFLCEKALPASDVIAPNLLELETLSMQKVTNV 160
Cdd:TIGR00687  81 GYLGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKGCYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242 161 EQAVTAARTLCEKGPGIVLVKHLSRAGYQTD-CFEMLLVTQEHSWHVSRPLVDFGGcQPVGVGDLTSGLLLVNLLKGESL 239
Cdd:TIGR00687 161 EEALAAADALIAMGPDIVLVTHLIRAGSQRDrSFEGLVATQEGRWHISRPLAVFDP-PPVGTGDLIAALLLATLLHGNSL 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1049326242 240 QTALEHVAAAVYEVMVTTKDMDEYELQIVAAQDRMVAPDHKFCATQLD 287
Cdd:TIGR00687 240 KEALEKTVSAVYHVLRTTIQLGKYELQPVAAQLEIRMPQSKFDAEKVE 287
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 1-275 7.48e-141

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: 397.21  E-value: 7.48e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242   1 MKNILSIQSHVVFGHAGNSAAEFPMRRMGVNVWPLNTVQFSNHTQYAQWKGCVMPAGHLTEVVQGIEEIGQLKSCHAVLS 80
Cdd:COG2240     1 MKRVLSIQSHVVYGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWKELGVLLEFDAVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242  81 GYIGSPEQGSHIIDIVKRVKAANPDAWYFCDPVMGHPEKGCIVAPGVTEFLCEKALPASDVIAPNLLELETLSMQKVTNV 160
Cdd:COG2240    81 GYLGSAEQGDIIADFVARVKAANPDALYLCDPVMGDNGKGYYVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242 161 EQAVTAARTLCEKGPGIVLVKHLSRAGYQTDCFEMLLVTQEHSWHVSRPLVDFggcQPVGVGDLTSGLLLVNLLKGESLQ 240
Cdd:COG2240   161 EEALAAARALLALGPKIVVVTSVPLDDTPADKIGNLAVTADGAWLVETPLLPF---SPNGTGDLFAALLLAHLLRGKSLE 237

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1049326242 241 TALEHVAAAVYEVMVTTKDMDEYELQIVAAQDRMV 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 1.87e-110

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: 319.53  E-value: 1.87e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242   3 NILSIQSHVVFGHAGNSAAEFPMRRMGVNVWPLNTVQFSNHTQYAQWKGCVMPAGHLTEVVQGIEEIGQLKSCHAVLSGY 82
Cdd:cd01173     1 RVLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLLLEYDAVLTGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242  83 IGSPEQGSHIIDIVKRVKAANPDAWYFCDPVMGHPEKGCIVAPGVTEFLCEKALPASDVIAPNLLELETLSMQKVTNVEQ 162
Cdd:cd01173    81 LGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGDNGKLYVVAEEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLED 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242 163 AVTAARTLCEKGPGIVLVKHLSRAGyqTDCFEMLLVTQEHSWHVSRPLVDFgGCQPVGVGDLTSGLLLVNLLKGESLQTA 242
Cdd:cd01173   161 AKAAARALHAKGPKTVVVTSVELAD--DDRIEMLGSTATEAWLVQRPKIPF-PAYFNGTGDLFAALLLARLLKGKSLAEA 237

                         250
                  ....*....|....*..
gi 1049326242 243 LEHVAAAVYEVMVTTKD 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 ...
 63-245 1.76e-14

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: 71.36  E-value: 1.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242  63 VQGIEEI------GQLKS------CHAVLSGYIGSPEqgshIIDIVKRvKAANPDAWYFCDPVM----GHPekgcIVAPG 126
Cdd:pfam08543  37 VQGVHPLppefvaAQLDAvledipVDAVKTGMLGSAE----IIEAVAE-KLDKYGVPVVLDPVMvaksGDS----LLDDE 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242 127 VTEFLCEKALPASDVIAPNLLELETLSMQKVTNVEQAVTAARTLCEKGPGIVLVK--HLSRAG-YQTDcfemLLVTQEHS 203
Cdd:pfam08543 108 AIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKggHLEGEEaVVTD----VLYDGGGF 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1049326242 204 WHVSRPLVDFGGCQpvGVGDLTSGLLLVNLLKGESLQTALEH 245
Cdd:pfam08543 184 YTLEAPRIPTKNTH--GTGCTLSAAIAANLAKGLSLPEAVRE 223
 
Name Accession Description Interval E-value
PRK05756 PRK05756
pyridoxal kinase PdxY;
1-287 0e+00

pyridoxal kinase PdxY;


Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 543.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242   1 MKNILSIQSHVVFGHAGNSAAEFPMRRMGVNVWPLNTVQFSNHTQYAQWKGCVMPAGHLTEVVQGIEEIGQLKSCHAVLS 80
Cdd:PRK05756    1 MKNILSIQSHVVYGHVGNSAAVFPMQRLGVNVWPLNTVQFSNHTGYGKWTGCVMPPSHLTEIVQGIADIGWLGECDAVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242  81 GYIGSPEQGSHIIDIVKRVKAANPDAWYFCDPVMGHPEKGCIVAPGVTEFLCEKALPASDVIAPNLLELETLSMQKVTNV 160
Cdd:PRK05756   81 GYLGSAEQGEAILDAVRRVKAANPQALYFCDPVMGDPEKGCIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242 161 EQAVTAARTLCEKGPGIVLVKHLSRAGYQTDCFEMLLVTQEHSWHVSRPLVDFGGcQPVGVGDLTSGLLLVNLLKGESLQ 240
Cdd:PRK05756  161 EDAVAAARALIARGPKIVLVTSLARAGYPADRFEMLLVTADGAWHISRPLVDFMR-QPVGVGDLTSALFLARLLQGGSLE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1049326242 241 TALEHVAAAVYEVMVTTKDMDEYELQIVAAQDRMVAPDHKFCATQLD 287
Cdd:PRK05756  240 EALEHTTAAVYEVMARTKERGSYELQLVAAQDSIATPRAMFQARRLA 286
pyridox_kin TIGR00687
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ...
 1-287 1.42e-152

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: 427.71  E-value: 1.42e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242   1 MKNILSIQSHVVFGHAGNSAAEFPMRRMGVNVWPLNTVQFSNHTQYAQWKGCVMPAGHLTEVVQGIEEIGQLKSCHAVLS 80
Cdd:TIGR00687   1 MKNVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLEAINKLNQCDAVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242  81 GYIGSPEQGSHIIDIVKRVKAANPDAWYFCDPVMGHPEKGCIVAPGVTEFLCEKALPASDVIAPNLLELETLSMQKVTNV 160
Cdd:TIGR00687  81 GYLGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKGCYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242 161 EQAVTAARTLCEKGPGIVLVKHLSRAGYQTD-CFEMLLVTQEHSWHVSRPLVDFGGcQPVGVGDLTSGLLLVNLLKGESL 239
Cdd:TIGR00687 161 EEALAAADALIAMGPDIVLVTHLIRAGSQRDrSFEGLVATQEGRWHISRPLAVFDP-PPVGTGDLIAALLLATLLHGNSL 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1049326242 240 QTALEHVAAAVYEVMVTTKDMDEYELQIVAAQDRMVAPDHKFCATQLD 287
Cdd:TIGR00687 240 KEALEKTVSAVYHVLRTTIQLGKYELQPVAAQLEIRMPQSKFDAEKVE 287
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 1-275 7.48e-141

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: 397.21  E-value: 7.48e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242   1 MKNILSIQSHVVFGHAGNSAAEFPMRRMGVNVWPLNTVQFSNHTQYAQWKGCVMPAGHLTEVVQGIEEIGQLKSCHAVLS 80
Cdd:COG2240     1 MKRVLSIQSHVVYGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWKELGVLLEFDAVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242  81 GYIGSPEQGSHIIDIVKRVKAANPDAWYFCDPVMGHPEKGCIVAPGVTEFLCEKALPASDVIAPNLLELETLSMQKVTNV 160
Cdd:COG2240    81 GYLGSAEQGDIIADFVARVKAANPDALYLCDPVMGDNGKGYYVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242 161 EQAVTAARTLCEKGPGIVLVKHLSRAGYQTDCFEMLLVTQEHSWHVSRPLVDFggcQPVGVGDLTSGLLLVNLLKGESLQ 240
Cdd:COG2240   161 EEALAAARALLALGPKIVVVTSVPLDDTPADKIGNLAVTADGAWLVETPLLPF---SPNGTGDLFAALLLAHLLRGKSLE 237

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1049326242 241 TALEHVAAAVYEVMVTTKDMDEYELQIVAAQDRMV 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 1.87e-110

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: 319.53  E-value: 1.87e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242   3 NILSIQSHVVFGHAGNSAAEFPMRRMGVNVWPLNTVQFSNHTQYAQWKGCVMPAGHLTEVVQGIEEIGQLKSCHAVLSGY 82
Cdd:cd01173     1 RVLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLLLEYDAVLTGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242  83 IGSPEQGSHIIDIVKRVKAANPDAWYFCDPVMGHPEKGCIVAPGVTEFLCEKALPASDVIAPNLLELETLSMQKVTNVEQ 162
Cdd:cd01173    81 LGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGDNGKLYVVAEEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLED 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242 163 AVTAARTLCEKGPGIVLVKHLSRAGyqTDCFEMLLVTQEHSWHVSRPLVDFgGCQPVGVGDLTSGLLLVNLLKGESLQTA 242
Cdd:cd01173   161 AKAAARALHAKGPKTVVVTSVELAD--DDRIEMLGSTATEAWLVQRPKIPF-PAYFNGTGDLFAALLLARLLKGKSLAEA 237

                         250
                  ....*....|....*..
gi 1049326242 243 LEHVAAAVYEVMVTTKD 259
Cdd:cd01173   238 LEKALNFVHEVLEATYE 254
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
 2-286 1.95e-49

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 165.25  E-value: 1.95e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242   2 KNILSIQSHVVFGHAGNSAAEFPMRRMGVNVWPLNTVQFSNHTQYAQWKGCVMPAGHLTEVVQGIEEIGQLKSCHAVLSG 81
Cdd:PTZ00344    5 KKVLSIQSHVTHGYVGNRAATFPLQLLGFDVDFVNTVQLSNHTGYPVIKGHRLDLNELITLMDGLRANNLLSDYTYVLTG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242  82 YIGSPEQGSHIIDIVKRVKAANPDAWYFCDPVMGhpEKGCIVAPgvtEFLCE---KALPASDVIAPNLLELETLSMQKVT 158
Cdd:PTZ00344   85 YINSADILREVLATVKEIKELRPKLIFLCDPVMG--DDGKLYVK---EEVVDayrELIPYADVITPNQFEASLLSGVEVK 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242 159 NVEQAVTAARTLCEKGPGIVLVKHLSRAGYQTDCFEMLLVTQEHSWHVSRplvdFGGCQP------VGVGDLTSGLLLVN 232
Cdd:PTZ00344  160 DLSDALEAIDWFHEQGIPVVVITSFREDEDPTHLRFLLSCRDKDTKNNKR----FTGKVPyiegryTGTGDLFAALLLAF 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1049326242 233 LLKGEsLQTALEHVAAAVYEVMVTTKD--------MDEYELQIVAAQDRMVAPDHKFCATQL 286
Cdd:PTZ00344  236 SHQHP-MDLAVGKAMGVLQDIIKATREsggsgsssLMSRELRLIQSPRDLLNPETVFKVTPL 296
PLN02978 PLN02978
pyridoxal kinase
 4-287 5.90e-48

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 161.83  E-value: 5.90e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242   4 ILSIQSHVVFGHAGNSAAEFPMRRMGVNVWPLNTVQFSNHTQYAQWKGCVMPAGHLTEVVQGIEEIGQLKSCHaVLSGYI 83
Cdd:PLN02978   17 VLSIQSHTVHGYVGNKSAVFPLQLLGFDVDPINSVQFSNHTGYPTFKGQVLDGEQLWALIEGLEANGLLFYTH-LLTGYI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242  84 GSPEQGSHIIDIVKRVKAANPDAWYFCDPVMGHPEKgCIVAPGVTEFLCEKALPASDVIAPNLLELETLSMQKVTNVEQA 163
Cdd:PLN02978   96 GSVSFLRTVLRVVKKLRSVNPNLTYVCDPVLGDEGK-LYVPPELVPVYREKVVPLATMLTPNQFEAEQLTGIRIVTEEDA 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242 164 VTAARTLCEKGPGIVLVKHLSRAGyqtdcfEMLLV-----TQEHS---WHVSRPLVDfggCQPVGVGDLTSGLLLVNLLK 235
Cdd:PLN02978  175 REACAILHAAGPSKVVITSIDIDG------KLLLVgshrkEKGARpeqFKIVIPKIP---AYFTGTGDLMAALLLGWSHK 245

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1049326242 236 G-ESLQTALEHVAAAVYEVMV-TTKDMDEY---------ELQIVAAQDRMVAPDHKFCATQLD 287
Cdd:PLN02978  246 YpDNLDKAAELAVSSLQAVLRrTLADYKRAgadpkssslELRLVQSQDDIRHPQVRFKAERYS 308
pdxK PRK08176
pyridoxine/pyridoxal/pyridoxamine kinase;
3-267 7.34e-47

pyridoxine/pyridoxal/pyridoxamine kinase;


Pssm-ID: 181269 [Multi-domain]  Cd Length: 281  Bit Score: 158.28  E-value: 7.34e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242   3 NILSIQSHVVFGHAGNSAAEFPMRRMGVNVWPLNTVQFSNHTQYAQWKGCVMPAGHLTEVVQGIEEIGQLKSCHAVLSGY 82
Cdd:PRK08176   17 DIVAVQSQVVYGSVGNSIAVPAIKANGLRVFAVPTVLLSNTPHYPTFYGGAIPDEWFSGYLRALQERDALRQLRAVTTGY 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242  83 IGSPEQGSHIIDIVKRVKAANPDAWYFCDPVMGHPEKGCIVAPGVTEFLCEKALPASDVIAPNLLELETLSMQKVTNVEQ 162
Cdd:PRK08176   97 MGSASQIKILAEWLTALRADHPDLLIMVDPVIGDIDSGIYVKPDLPEAYRQHLLPLAQGLTPNIFELEILTGKPCRTLDS 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242 163 AVTAARTLCEKGPGIVLVkhlSRAGYQTDCFEM--LLVTQEHSWHVSRPLVDfggCQPVGVGDLTSGLLLVNLLKGESLQ 240
Cdd:PRK08176  177 AIAAAKSLLSDTLKWVVI---TSAAGNEENQEMqvVVVTADSVNVISHPRVD---TDLKGTGDLFCAELVSGLLKGKALT 250

                         250       260
                  ....*....|....*....|....*..
gi 1049326242 241 TALEHVAAAVYEVMVTTKDMDEYELQI 267
Cdd:PRK08176  251 DAAHRAGLRVLEVMRYTQQAGSDELIL 277
PRK07105 PRK07105
pyridoxamine kinase; Validated
 1-257 1.29e-15

pyridoxamine kinase; Validated


Pssm-ID: 180840 [Multi-domain]  Cd Length: 284  Bit Score: 74.95  E-value: 1.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242   1 MKNILSIQSHVVFGHAGNSAAEFPMRRMGVNVWPLNTVQFSNHT----QYAQWKgcvmpaghLTEVVQGIeeIGQLKS-- 74
Cdd:PRK07105    4 VKRVAAIHDLSGFGRVALTASIPIMSSMGLQVCPLPTALLSSHTggfqNPSIID--------LTDGMQAF--LTHWKSln 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242  75 --CHAVLSGYIGSPEQGSHIIDIVKRVKaaNPDAWYFCDPVMGhpEKGCiVAPGVTE-------FLCEKAlpasDVIAPN 145
Cdd:PRK07105   74 lkFDAIYSGYLGSPRQIQIVSDFIKYFK--KKDLLVVVDPVMG--DNGK-LYQGFDQemveemrKLIQKA----DVITPN 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242 146 LLE----LETLSMQKVTNVEQAVTAARTLCEKGPGIVLV-------KHLSRAGYQTDcfemllvtQEHSWHVSRPLVdfg 214
Cdd:PRK07105  145 LTEacllLDKPYLEKSYSEEEIKQLLRKLADLGPKIVIItsvpfedGKIGVAYYDRA--------TDRFWKVFCKYI--- 213

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1049326242 215 gcqPV---GVGDLTSGLLLVNLLKGESLQTALEHVAAAVYEVMVTT 257
Cdd:PRK07105  214 ---PAhypGTGDIFTSVITGSLLQGDSLPIALDRAVQFIEKGIRAT 256
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 63-245 1.76e-14

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: 71.36  E-value: 1.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242  63 VQGIEEI------GQLKS------CHAVLSGYIGSPEqgshIIDIVKRvKAANPDAWYFCDPVM----GHPekgcIVAPG 126
Cdd:pfam08543  37 VQGVHPLppefvaAQLDAvledipVDAVKTGMLGSAE----IIEAVAE-KLDKYGVPVVLDPVMvaksGDS----LLDDE 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242 127 VTEFLCEKALPASDVIAPNLLELETLSMQKVTNVEQAVTAARTLCEKGPGIVLVK--HLSRAG-YQTDcfemLLVTQEHS 203
Cdd:pfam08543 108 AIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKggHLEGEEaVVTD----VLYDGGGF 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1049326242 204 WHVSRPLVDFGGCQpvGVGDLTSGLLLVNLLKGESLQTALEH 245
Cdd:pfam08543 184 YTLEAPRIPTKNTH--GTGCTLSAAIAANLAKGLSLPEAVRE 223
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 60-245 2.42e-14

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: 70.84  E-value: 2.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242  60 TEVVQGIEEI------GQLKSC------HAVLSGYIGSPEqgshIIDIVKRVKAANPDAWYFCDPVM----GHPekgcIV 123
Cdd:COG0351    40 TLGVTGVHPVppefvaAQLRAVledipvDAIKIGMLGSAE----IIEAVAEILADYPLVPVVLDPVMvaksGDR----LL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242 124 APGVTEFLCEKALPASDVIAPNLLELETLSMQKVTNVEQAVTAARTLCEKGPGIVLVK--HLsRAGYQTDcfemLLVTQE 201
Cdd:COG0351   112 DEDAVEALRELLLPLATVVTPNLPEAEALLGIEITTLDDMREAAKALLELGAKAVLVKggHL-PGDEAVD----VLYDGD 186

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1049326242 202 HSWHVSRPLVDFGGCQpvGVGDLTSGLLLVNLLKGESLQTALEH 245
Cdd:COG0351   187 GVREFSAPRIDTGNTH--GTGCTLSSAIAALLAKGLDLEEAVRE 228
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 63-249 1.66e-13

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 68.61  E-value: 1.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242  63 VQGIEEI------GQLKSC------HAVLSGYIGSPEqgshIIDIVKRVKAANPDAWYFCDPVM----GHPekgcIVAPG 126
Cdd:PRK06427   50 VQRVHPIppefvaAQLDAVfsdiriDAVKIGMLASAE----IIETVAEALKRYPIPPVVLDPVMiaksGDP----LLADD 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242 127 VTEFLCEKALPASDVIAPNLLELETLS-MQKVTNVEQAVTAARTLCEKGPGIVLVK--HLSRAGYQTDcfemLLVTQEHS 203
Cdd:PRK06427  122 AVAALRERLLPLATLITPNLPEAEALTgLPIADTEDEMKAAARALHALGCKAVLIKggHLLDGEESVD----WLFDGEGE 197

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1049326242 204 WHVSRPLVDfgGCQPVGVGDLTSGLLLVNLLKGESLQTAlehVAAA 249
Cdd:PRK06427  198 ERFSAPRIP--TKNTHGTGCTLSAAIAAELAKGASLLDA---VQTA 238
HMPP_kinase cd01169
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ...
 63-252 2.22e-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: 67.91  E-value: 2.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242  63 VQGIEEIG------QLKS------CHAVLSGYIGSPEqgshIIDIVKRVKAANPDAWYFCDPVM----GHPekgcIVAPG 126
Cdd:cd01169    45 VFGVHPVPpefvaaQLDAvledipVDAIKIGMLGSAE----IIEAVAEALKDYPDIPVVLDPVMvaksGDS----LLDDD 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242 127 VTEFLCEKALPASDVIAPNLLELETLSMQKVTNVEQAVTAARTLCEKGPGIVLVK--HLsRAGYQTDcfemLLVTQEHSW 204
Cdd:cd01169   117 AIEALRELLLPLATLITPNLPEAELLTGLEIATEEDMMKAAKALLALGAKAVLIKggHL-PGDEAVD----VLYDGGGFF 191

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1049326242 205 HVSRPLVDFGGCQpvGVGDLTSGLLLVNLLKGESLQTALEHVAAAVYE 252
Cdd:cd01169   192 EFESPRIDTKNTH--GTGCTLSSAIAANLAKGLSLEEAVREAKEYVTQ 237
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
133-249 1.85e-11

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


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 63.23  E-value: 1.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242 133 EKALPAS-DVIAPNLLELETLSMQKVTNVEQAVTAARTLCEKGPGIVLVkhlSRAGYqtdcfEMLLVTQEHSWHVSRPLV 211
Cdd:COG1105   171 KAALEAGpDLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVV---SLGAD-----GALLVTEDGVYRAKPPKV 242

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1049326242 212 DFGgcQPVGVGD-LTSGLLLvNLLKGESLQTALEH-VAAA 249
Cdd:COG1105   243 EVV--STVGAGDsMVAGFLA-GLARGLDLEEALRLaVAAG 279
FruK_PfkB_like cd01164
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ...
 134-249 2.66e-11

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: 62.55  E-value: 2.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242 134 KALPasDVIAPNLLELETLSMQKVTNVEQAVTAARTLCEKGPGIVLVkhlSRAGYqtdcfEMLLVTQEHSWHVSRPLVDf 213
Cdd:cd01164   175 AAKP--FLIKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLV---SLGAD-----GALLVTKDGVYRASPPKVK- 243

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1049326242 214 gGCQPVGVGDLTSGLLLVNLLKGESLQTALEH-VAAA 249
Cdd:cd01164   244 -VVSTVGAGDSMVAGFVAGLAQGLSLEEALRLaVAAG 279
1-PFK TIGR03168
hexose kinase, 1-phosphofructokinase family; This family consists largely of ...
 134-249 2.11e-10

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: 60.28  E-value: 2.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242 134 KALPAS-DVIAPNLLELETLSMQKVTNVEQAVTAARTLCEKGPGIVLVkhlSRAGYQtdcfeMLLVTQEHSWHVSRPLVD 212
Cdd:TIGR03168 171 EALAAKpFLIKPNHEELEELFGRELKTLEEIIEAARELLDRGAENVLV---SLGADG-----ALLVTKEGALKATPPKVE 242

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1049326242 213 FGGcqPVGVGDLTSGLLLVNLLKGESLQTALEHVAAA 249
Cdd:TIGR03168 243 VVN--TVGAGDSMVAGFLAGLARGLSLEEALRFAVAA 277
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 132-249 1.01e-08

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 55.04  E-value: 1.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242 132 CEKALPASDVIAPNLLELETLSMQKVTNVEQAVTAARTLCEKGPGIVLVKhLSRAGyqtdcfeMLLVTQEHSWHVSRP-- 209
Cdd:pfam00294 174 LLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVT-LGADG-------ALVVEGDGEVHVPAVpk 245

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1049326242 210 --LVDfggcqPVGVGDLTSGLLLVNLLKGESLQTALEHVAAA 249
Cdd:pfam00294 246 vkVVD-----TTGAGDSFVGGFLAGLLAGKSLEEALRFANAA 282
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 76-249 2.57e-07

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: 51.04  E-value: 2.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242  76 HAVLSGYIGSPEQG-SHIIDIVKRVKAANpdAWYFCDPVMGHPekgciVAPGVTEFLcEKALPASDVIAPNLLELETLsm 154
Cdd:COG0524   130 ILHLGGITLASEPPrEALLAALEAARAAG--VPVSLDPNYRPA-----LWEPARELL-RELLALVDILFPNEEEAELL-- 199

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242 155 qkvTNVEQAVTAARTLCEKGPGIVLVKhLSRAGyqtdcfeMLLVTQEHSWHVSRP---LVDfggcqPVGVGDLTSGLLLV 231
Cdd:COG0524   200 ---TGETDPEEAAAALLARGVKLVVVT-LGAEG-------ALLYTGGEVVHVPAFpveVVD-----TTGAGDAFAAGFLA 263

                         170       180
                  ....*....|....*....|
gi 1049326242 232 NLLKGESLQTALE--HVAAA 249
Cdd:COG0524   264 GLLEGLDLEEALRfaNAAAA 283
PRK08573 PRK08573
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
111-244 1.00e-05

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 236297 [Multi-domain]  Cd Length: 448  Bit Score: 46.64  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242 111 DPVM----GHPekgcIVAPGVTEFLCEKALPASDVIAPNLLELETLSMQKVTNVEQAVTAARTLCEK-GPGIVLVK--HL 183
Cdd:PRK08573  103 DPVMiaksGAP----LLREDAVDALIKRLLPLATVVTPNRPEAEKLTGMKIRSVEDARKAAKYIVEElGAEAVVVKggHL 178

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1049326242 184 sRAGYQTDcfemlLVTQEHSWHVSR-PLVDfGGCQPvGVGDLTSGLLLVNLLKGESLQTALE 244
Cdd:PRK08573  179 -EGEEAVD-----VLYHNGTFREFRaPRVE-SGCTH-GTGCSFSAAIAAGLAKGLDPEEAIK 232
PRK14713 PRK14713
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
77-184 5.55e-05

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 237797 [Multi-domain]  Cd Length: 530  Bit Score: 44.39  E-value: 5.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242  77 AVLSGYIGSPEqgshIIDIVKRVKAANPDAWYFCDPVMghpekgciVAPGVTEFLCEKA-------LPASDVIAPNLLEL 149
Cdd:PRK14713  101 AVKIGMLGDAE----VIDAVRTWLAEHRPPVVVLDPVM--------VATSGDRLLEEDAeaalrelVPRADLITPNLPEL 168

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1049326242 150 ETLSMQKV-TNVEQAVTAARTLCEKGPGIVLVK--HLS 184
Cdd:PRK14713  169 AVLLGEPPaTTWEEALAQARRLAAETGTTVLVKggHLD 206
PRK11142 PRK11142
ribokinase; Provisional
 140-250 7.02e-05

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 43.70  E-value: 7.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242 140 DVIAPNLLELETLSMQKVTNVEQAVTAARTLCEKGPGIVLVKHLSRAGYqtdcfemllvtqehswhVSRPlvDFGGCQP- 218
Cdd:PRK11142  180 DIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRGVW-----------------LSEN--GEGQRVPg 240

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1049326242 219 --------VGVGDLTSGLLLVNLLKGESLQTALE--HVAAAV 250
Cdd:PRK11142  241 frvqavdtIAAGDTFNGALVTALLEGKPLPEAIRfaHAAAAI 282
PRK12412 PRK12412
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
48-250 9.01e-04

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183512 [Multi-domain]  Cd Length: 268  Bit Score: 39.95  E-value: 9.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242  48 QWKGCVMPAgHLTEVVQGIEEIGQLKSCHAVLSGYIGSPEqgshIIDIVKRVKAANPDAWYFCDPVMGHPEKGCIVAPGV 127
Cdd:PRK12412   47 GWAHNVFPI-PASTLKPQLETTIEGVGVDALKTGMLGSVE----IIEMVAETIEKHNFKNVVVDPVMVCKGADEALHPET 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242 128 TEFLCEKALPASDVIAPNLLELETLSMQKVTNVEQAVTAARTLCEKGPGIVLVKHLSRAG--------YQTDCFEMLlvt 199
Cdd:PRK12412  122 NDCLRDVLVPKALVVTPNLFEAYQLSGVKINSLEDMKEAAKKIHALGAKYVLIKGGSKLGtetaidvlYDGETFDLL--- 198

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1049326242 200 qeHSWHVSRPLVDFGGCQpvgvgdlTSGLLLVNLLKG----ESLQTALEHVAAAV 250
Cdd:PRK12412  199 --ESEKIDTTNTHGAGCT-------YSAAITAELAKGkpvkEAVKTAKEFITAAI 244
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 77-234 1.04e-03

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: 39.39  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242  77 AVLSGYIGSPEQGSHIIDIVKRVKAAnpdawYFCDPVMGhpekgcIVAPgvTEFLCEKALPASDVIAPNLLELETLSMQK 156
Cdd:cd00287    61 VVISGLSPAPEAVLDALEEARRRGVP-----VVLDPGPR------AVRL--DGEELEKLLPGVDILTPNEEEAEALTGRR 127

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1049326242 157 VTNVEQAVTAARTLCEKGPGIVLVKHlSRAGYqtdcfemlLVTQEHSWHVSRPLVDFGGCQPVGVGDLTSGLLLVNLL 234
Cdd:cd00287   128 DLEVKEAAEAAALLLSKGPKVVIVTL-GEKGA--------IVATRGGTEVHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
 63-181 1.60e-03

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 39.75  E-value: 1.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242  63 VQGIEEI------GQLKSC------HAVLSGYIGSPEQGSHIIDIVKR--VKAAnpdawyFCDPVMGHPEKGCIVAPGVT 128
Cdd:PLN02898   55 VQGVHAVpldfvaEQLKSVlsdmpvDVVKTGMLPSAEIVKVLCQALKEfpVKAL------VVDPVMVSTSGDVLAGPSIL 128

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1049326242 129 EFLCEKALPASDVIAPNLLELETL-SMQKVTNVEQAVTAARTLCEKGPGIVLVK 181
Cdd:PLN02898  129 SALREELLPLATIVTPNVKEASALlGGDPLETVADMRSAAKELHKLGPRYVLVK 182
PRK09517 PRK09517
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ...
 77-260 6.23e-03

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


Pssm-ID: 169939 [Multi-domain]  Cd Length: 755  Bit Score: 38.03  E-value: 6.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242  77 AVLSGYIGSPEqgshIIDIVKRVKAANPDAWYFCDPVMGHPEKGCIVAPGVTEFLcEKALPASDVIAPNLLELETL-SMQ 155
Cdd:PRK09517  313 AVKLGMLGSAD----TVDLVASWLGSHEHGPVVLDPVMVATSGDRLLDADATEAL-RRLAVHVDVVTPNIPELAVLcGEA 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1049326242 156 KVTNVEQAVTAARTLCEKGPGIVLVK--HLSRAgyqtDCfEMLLVTQEHSWH-VSRPLVDFGGCQpvGVGDLTSGLLLVN 232
Cdd:PRK09517  388 PAITMDEAIAQARGFARTHGTIVIVKggHLTGD----LA-DNAVVRPDGSVHqVENPRVNTTNSH--GTGCSLSAALATL 460

                         170       180
                  ....*....|....*....|....*...
gi 1049326242 233 LLKGESLQTALEHVAAAVYEVMVTTKDM 260
Cdd:PRK09517  461 IAAGESVEKALEWATRWLNEALRHADHL 488
 
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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