NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|499214665|ref|WP_010912205|]
View 

MULTISPECIES: pyridoxal kinase PdxY [Mesorhizobium]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK05756 PRK05756
pyridoxal kinase PdxY;
9-285 1.18e-140

pyridoxal kinase PdxY;


:

Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 397.70  E-value: 1.18e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665   9 PRAVIVISSHVARGSVGNRAAVFALETLGFPVWAVPTVILPWHPGHGRATRIVPPLDQFKAFMADLERAPWLGEVGAVLS 88
Cdd:PRK05756   1 MKNILSIQSHVVYGHVGNSAAVFPMQRLGVNVWPLNTVQFSNHTGYGKWTGCVMPPSHLTEIVQGIADIGWLGECDAVLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665  89 GYLGEAGQAEAVASLVAAVKARTPDAVYICDPVMGDSG-GLYVPEATAAAMRDRLVPIADIATPNRYELEWMAGAPLPDL 167
Cdd:PRK05756  81 GYLGSAEQGEAILDAVRRVKAANPQALYFCDPVMGDPEkGCIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665 168 KSVIAAALHA---GPSTMLVTSAQSM--MIGGTGNLLLDGTQALLAEHRVID--KPPNGLGDLTAAVYLARILSGQPPIK 240
Cdd:PRK05756 161 EDAVAAARALiarGPKIVLVTSLARAgyPADRFEMLLVTADGAWHISRPLVDfmRQPVGVGDLTSALFLARLLQGGSLEE 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 499214665 241 ALQSTTAAVYEILARTAKRGGDELQLETDAQSLSHPMAMVQLRHL 285
Cdd:PRK05756 241 ALEHTTAAVYEVMARTKERGSYELQLVAAQDSIATPRAMFQARRL 285
 
Name Accession Description Interval E-value
PRK05756 PRK05756
pyridoxal kinase PdxY;
9-285 1.18e-140

pyridoxal kinase PdxY;


Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 397.70  E-value: 1.18e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665   9 PRAVIVISSHVARGSVGNRAAVFALETLGFPVWAVPTVILPWHPGHGRATRIVPPLDQFKAFMADLERAPWLGEVGAVLS 88
Cdd:PRK05756   1 MKNILSIQSHVVYGHVGNSAAVFPMQRLGVNVWPLNTVQFSNHTGYGKWTGCVMPPSHLTEIVQGIADIGWLGECDAVLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665  89 GYLGEAGQAEAVASLVAAVKARTPDAVYICDPVMGDSG-GLYVPEATAAAMRDRLVPIADIATPNRYELEWMAGAPLPDL 167
Cdd:PRK05756  81 GYLGSAEQGEAILDAVRRVKAANPQALYFCDPVMGDPEkGCIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665 168 KSVIAAALHA---GPSTMLVTSAQSM--MIGGTGNLLLDGTQALLAEHRVID--KPPNGLGDLTAAVYLARILSGQPPIK 240
Cdd:PRK05756 161 EDAVAAARALiarGPKIVLVTSLARAgyPADRFEMLLVTADGAWHISRPLVDfmRQPVGVGDLTSALFLARLLQGGSLEE 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 499214665 241 ALQSTTAAVYEILARTAKRGGDELQLETDAQSLSHPMAMVQLRHL 285
Cdd:PRK05756 241 ALEHTTAAVYEVMARTKERGSYELQLVAAQDSIATPRAMFQARRL 285
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 9-273 1.80e-109

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: 318.25  E-value: 1.80e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665   9 PRAVIVISSHVARGSVGNRAAVFALETLGFPVWAVPTVILPWHPGHGRATRIVPPLDQFKAFMADLERAPWLGEVGAVLS 88
Cdd:COG2240    1 MKRVLSIQSHVVYGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWKELGVLLEFDAVLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665  89 GYLGEAGQAEAVASLVAAVKARTPDAVYICDPVMGDSG-GLYVPEATAAAMRDRLVPIADIATPNRYELEWMAGAPLPDL 167
Cdd:COG2240   81 GYLGSAEQGDIIADFVARVKAANPDALYLCDPVMGDNGkGYYVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665 168 KSVIAAA--LHA-GPSTMLVTSAQSM--MIGGTGNLLLDGTQALLAEHRVIDKPPNGLGDLTAAVYLARILSGQPPIKAL 242
Cdd:COG2240  161 EEALAAAraLLAlGPKIVVVTSVPLDdtPADKIGNLAVTADGAWLVETPLLPFSPNGTGDLFAALLLAHLLRGKSLEEAL 240

                        250       260       270
                 ....*....|....*....|....*....|.
gi 499214665 243 QSTTAAVYEILARTAKRGGDELQLETDAQSL 273
Cdd:COG2240  241 ERAAAFVYEVLERTAAAGSDELLLEAALDEL 271
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 12-258 6.54e-93

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: 275.62  E-value: 6.54e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665  12 VIVISSHVARGSVGNRAAVFALETLGFPVWAVPTVILPWHPGHGRATRIVPPLDQFKAFMADLERAPWLGEVGAVLSGYL 91
Cdd:cd01173    2 VLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLLLEYDAVLTGYL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665  92 GEAGQAEAVASLVAAVKARTPDAVYICDPVMGDSGGLYV-PEATAAAMRDRLVPIADIATPNRYELEWMAGAPLPDLKSV 170
Cdd:cd01173   82 GSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGDNGKLYVvAEEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLEDA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665 171 IAAA--LHA-GPSTMLVTSAQSMMIGGTGNLLLDGTQALLAEHRVIDKP--PNGLGDLTAAVYLARILSGQPPIKALQST 245
Cdd:cd01173  162 KAAAraLHAkGPKTVVVTSVELADDDRIEMLGSTATEAWLVQRPKIPFPayFNGTGDLFAALLLARLLKGKSLAEALEKA 241

                        250
                 ....*....|...
gi 499214665 246 TAAVYEILARTAK 258
Cdd:cd01173  242 LNFVHEVLEATYE 254
pyridox_kin TIGR00687
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ...
 9-266 2.35e-60

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: 193.51  E-value: 2.35e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665    9 PRAVIVISSHVARGSVGNRAAVFALETLGFPVWAVPTVILPWHPGHGRATRIVPPLDQFKAFMADLERAPWLGEVGAVLS 88
Cdd:TIGR00687   1 MKNVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLEAINKLNQCDAVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665   89 GYLGEAGQAEAVASLVAAVKARTPDAVYICDPVMGDSG-GLYVPEATAAAMRDRLVPIADIATPNRYELEWMAGAPLPDL 167
Cdd:TIGR00687  81 GYLGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWkGCYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665  168 KSVIAAA--LHA-GPSTMLVTSAQSM---------MIGGTGNLLLDGTQALLaehrVIDKPPNGLGDLTAAVYLARILSG 235
Cdd:TIGR00687 161 EEALAAAdaLIAmGPDIVLVTHLIRAgsqrdrsfeGLVATQEGRWHISRPLA----VFDPPPVGTGDLIAALLLATLLHG 236

                         250       260       270
                  ....*....|....*....|....*....|.
gi 499214665  236 QPPIKALQSTTAAVYEILARTAKRGGDELQL 266
Cdd:TIGR00687 237 NSLKEALEKTVSAVYHVLRTTIQLGKYELQP 267
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 65-255 1.04e-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: 1.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665   65 DQFKAFMADLErapwlgeVGAVLSGYLGEAGQAEAVASLVaavkaRTPDAVYICDPVM-GDSGGLYVPEATAAAMRDRLV 143
Cdd:pfam08543  50 AQLDAVLEDIP-------VDAVKTGMLGSAEIIEAVAEKL-----DKYGVPVVLDPVMvAKSGDSLLDDEAIEALKEELL 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665  144 PIADIATPNRYELEWMAGAPLPDLKSVIAAA--LHA-GPSTMLVTsaqsmmiGG--------TGNLLLDGTQALLAEHRV 212
Cdd:pfam08543 118 PLATLITPNLPEAEALTGRKIKTLEDMKEAAkkLLAlGAKAVLIK-------GGhlegeeavVTDVLYDGGGFYTLEAPR 190

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 499214665  213 IDKP-PNGLGD-LTAAV--YLARilsGQPPIKALQSTTAAVYEILAR 255
Cdd:pfam08543 191 IPTKnTHGTGCtLSAAIaaNLAK---GLSLPEAVREAKEYVTEAIRD 234
 
Name Accession Description Interval E-value
PRK05756 PRK05756
pyridoxal kinase PdxY;
9-285 1.18e-140

pyridoxal kinase PdxY;


Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 397.70  E-value: 1.18e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665   9 PRAVIVISSHVARGSVGNRAAVFALETLGFPVWAVPTVILPWHPGHGRATRIVPPLDQFKAFMADLERAPWLGEVGAVLS 88
Cdd:PRK05756   1 MKNILSIQSHVVYGHVGNSAAVFPMQRLGVNVWPLNTVQFSNHTGYGKWTGCVMPPSHLTEIVQGIADIGWLGECDAVLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665  89 GYLGEAGQAEAVASLVAAVKARTPDAVYICDPVMGDSG-GLYVPEATAAAMRDRLVPIADIATPNRYELEWMAGAPLPDL 167
Cdd:PRK05756  81 GYLGSAEQGEAILDAVRRVKAANPQALYFCDPVMGDPEkGCIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665 168 KSVIAAALHA---GPSTMLVTSAQSM--MIGGTGNLLLDGTQALLAEHRVID--KPPNGLGDLTAAVYLARILSGQPPIK 240
Cdd:PRK05756 161 EDAVAAARALiarGPKIVLVTSLARAgyPADRFEMLLVTADGAWHISRPLVDfmRQPVGVGDLTSALFLARLLQGGSLEE 240

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 499214665 241 ALQSTTAAVYEILARTAKRGGDELQLETDAQSLSHPMAMVQLRHL 285
Cdd:PRK05756 241 ALEHTTAAVYEVMARTKERGSYELQLVAAQDSIATPRAMFQARRL 285
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 9-273 1.80e-109

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: 318.25  E-value: 1.80e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665   9 PRAVIVISSHVARGSVGNRAAVFALETLGFPVWAVPTVILPWHPGHGRATRIVPPLDQFKAFMADLERAPWLGEVGAVLS 88
Cdd:COG2240    1 MKRVLSIQSHVVYGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWKELGVLLEFDAVLS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665  89 GYLGEAGQAEAVASLVAAVKARTPDAVYICDPVMGDSG-GLYVPEATAAAMRDRLVPIADIATPNRYELEWMAGAPLPDL 167
Cdd:COG2240   81 GYLGSAEQGDIIADFVARVKAANPDALYLCDPVMGDNGkGYYVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665 168 KSVIAAA--LHA-GPSTMLVTSAQSM--MIGGTGNLLLDGTQALLAEHRVIDKPPNGLGDLTAAVYLARILSGQPPIKAL 242
Cdd:COG2240  161 EEALAAAraLLAlGPKIVVVTSVPLDdtPADKIGNLAVTADGAWLVETPLLPFSPNGTGDLFAALLLAHLLRGKSLEEAL 240

                        250       260       270
                 ....*....|....*....|....*....|.
gi 499214665 243 QSTTAAVYEILARTAKRGGDELQLETDAQSL 273
Cdd:COG2240  241 ERAAAFVYEVLERTAAAGSDELLLEAALDEL 271
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 12-258 6.54e-93

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: 275.62  E-value: 6.54e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665  12 VIVISSHVARGSVGNRAAVFALETLGFPVWAVPTVILPWHPGHGRATRIVPPLDQFKAFMADLERAPWLGEVGAVLSGYL 91
Cdd:cd01173    2 VLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLLLEYDAVLTGYL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665  92 GEAGQAEAVASLVAAVKARTPDAVYICDPVMGDSGGLYV-PEATAAAMRDRLVPIADIATPNRYELEWMAGAPLPDLKSV 170
Cdd:cd01173   82 GSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGDNGKLYVvAEEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLEDA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665 171 IAAA--LHA-GPSTMLVTSAQSMMIGGTGNLLLDGTQALLAEHRVIDKP--PNGLGDLTAAVYLARILSGQPPIKALQST 245
Cdd:cd01173  162 KAAAraLHAkGPKTVVVTSVELADDDRIEMLGSTATEAWLVQRPKIPFPayFNGTGDLFAALLLARLLKGKSLAEALEKA 241

                        250
                 ....*....|...
gi 499214665 246 TAAVYEILARTAK 258
Cdd:cd01173  242 LNFVHEVLEATYE 254
pyridox_kin TIGR00687
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ...
 9-266 2.35e-60

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: 193.51  E-value: 2.35e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665    9 PRAVIVISSHVARGSVGNRAAVFALETLGFPVWAVPTVILPWHPGHGRATRIVPPLDQFKAFMADLERAPWLGEVGAVLS 88
Cdd:TIGR00687   1 MKNVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLEAINKLNQCDAVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665   89 GYLGEAGQAEAVASLVAAVKARTPDAVYICDPVMGDSG-GLYVPEATAAAMRDRLVPIADIATPNRYELEWMAGAPLPDL 167
Cdd:TIGR00687  81 GYLGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWkGCYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665  168 KSVIAAA--LHA-GPSTMLVTSAQSM---------MIGGTGNLLLDGTQALLaehrVIDKPPNGLGDLTAAVYLARILSG 235
Cdd:TIGR00687 161 EEALAAAdaLIAmGPDIVLVTHLIRAgsqrdrsfeGLVATQEGRWHISRPLA----VFDPPPVGTGDLIAALLLATLLHG 236

                         250       260       270
                  ....*....|....*....|....*....|.
gi 499214665  236 QPPIKALQSTTAAVYEILARTAKRGGDELQL 266
Cdd:TIGR00687 237 NSLKEALEKTVSAVYHVLRTTIQLGKYELQP 267
pdxK PRK08176
pyridoxine/pyridoxal/pyridoxamine kinase;
12-266 7.37e-47

pyridoxine/pyridoxal/pyridoxamine kinase;


Pssm-ID: 181269 [Multi-domain]  Cd Length: 281  Bit Score: 158.66  E-value: 7.37e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665  12 VIVISSHVARGSVGNRAAVFALETLGFPVWAVPTVIL---PWHPG-HGRATrivpPLDQFKAFMADLERAPWLGEVGAVL 87
Cdd:PRK08176  18 IVAVQSQVVYGSVGNSIAVPAIKANGLRVFAVPTVLLsntPHYPTfYGGAI----PDEWFSGYLRALQERDALRQLRAVT 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665  88 SGYLGEAGQAEAVASLVAAVKARTPDAVYICDPVMGDSG-GLYVPEATAAAMRDRLVPIADIATPNRYELEWMAGAPLPD 166
Cdd:PRK08176  94 TGYMGSASQIKILAEWLTALRADHPDLLIMVDPVIGDIDsGIYVKPDLPEAYRQHLLPLAQGLTPNIFELEILTGKPCRT 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665 167 LKSVIAAA---LHAGPSTMLVTSAQSMMIGGTGNLLL---DGTQALlaEHRVIDKPPNGLGDLTAAVYLARILSGQPPIK 240
Cdd:PRK08176 174 LDSAIAAAkslLSDTLKWVVITSAAGNEENQEMQVVVvtaDSVNVI--SHPRVDTDLKGTGDLFCAELVSGLLKGKALTD 251

                        250       260
                 ....*....|....*....|....*.
gi 499214665 241 ALQSTTAAVYEILARTAKRGGDELQL 266
Cdd:PRK08176 252 AAHRAGLRVLEVMRYTQQAGSDELIL 277
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
 12-276 1.00e-44

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 153.31  E-value: 1.00e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665  12 VIVISSHVARGSVGNRAAVFALETLGFPVWAVPTVILPWHPGHG--RATRIVppLDQFKAFMADLERAPWLGEVGAVLSG 89
Cdd:PTZ00344   7 VLSIQSHVTHGYVGNRAATFPLQLLGFDVDFVNTVQLSNHTGYPviKGHRLD--LNELITLMDGLRANNLLSDYTYVLTG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665  90 YLGEAGQAEAVASLVAAVKARTPDAVYICDPVMGDSGGLYVPEATAAAMRdRLVPIADIATPNRYELEWMAGAPLPDLKS 169
Cdd:PTZ00344  85 YINSADILREVLATVKEIKELRPKLIFLCDPVMGDDGKLYVKEEVVDAYR-ELIPYADVITPNQFEASLLSGVEVKDLSD 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665 170 VIAAA--LHA-GPSTMLVTSAQ------------SMMIGGTGNllldgTQALLAEHRVIDKPPNGLGDLTAAVYLARILS 234
Cdd:PTZ00344 164 ALEAIdwFHEqGIPVVVITSFRededpthlrfllSCRDKDTKN-----NKRFTGKVPYIEGRYTGTGDLFAALLLAFSHQ 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499214665 235 GqpPIK-ALQSTTAAVYEILARTAKRGGD--------ELQLETDAQSLSHP 276
Cdd:PTZ00344 239 H--PMDlAVGKAMGVLQDIIKATRESGGSgssslmsrELRLIQSPRDLLNP 287
PLN02978 PLN02978
pyridoxal kinase
 6-276 3.85e-43

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 149.51  E-value: 3.85e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665   6 PDAPRaVIVISSHVARGSVGNRAAVFALETLGFPVWAVPTVILPWHPGHGRATRIVPPLDQFKAFMADLERAPWLgEVGA 85
Cdd:PLN02978  12 SSTGR-VLSIQSHTVHGYVGNKSAVFPLQLLGFDVDPINSVQFSNHTGYPTFKGQVLDGEQLWALIEGLEANGLL-FYTH 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665  86 VLSGYLGEAGQAEAVASLVAAVKARTPDAVYICDPVMGDSGGLYVPEATAAAMRDRLVPIADIATPNRYELEWMAGAPLP 165
Cdd:PLN02978  90 LLTGYIGSVSFLRTVLRVVKKLRSVNPNLTYVCDPVLGDEGKLYVPPELVPVYREKVVPLATMLTPNQFEAEQLTGIRIV 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665 166 DLKSVIAA--ALHA-GPSTMLVTSaqsmmIGGTGNLLLDGTQALLAEHR------VIDKPP---NGLGDLTAAVYLAriL 233
Cdd:PLN02978 170 TEEDAREAcaILHAaGPSKVVITS-----IDIDGKLLLVGSHRKEKGARpeqfkiVIPKIPayfTGTGDLMAALLLG--W 242

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 499214665 234 SGQPP---IKALQSTTAAVYEILARTA---KRGGD-------ELQLETDAQSLSHP 276
Cdd:PLN02978 243 SHKYPdnlDKAAELAVSSLQAVLRRTLadyKRAGAdpkssslELRLVQSQDDIRHP 298
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 65-255 1.04e-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: 1.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665   65 DQFKAFMADLErapwlgeVGAVLSGYLGEAGQAEAVASLVaavkaRTPDAVYICDPVM-GDSGGLYVPEATAAAMRDRLV 143
Cdd:pfam08543  50 AQLDAVLEDIP-------VDAVKTGMLGSAEIIEAVAEKL-----DKYGVPVVLDPVMvAKSGDSLLDDEAIEALKEELL 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665  144 PIADIATPNRYELEWMAGAPLPDLKSVIAAA--LHA-GPSTMLVTsaqsmmiGG--------TGNLLLDGTQALLAEHRV 212
Cdd:pfam08543 118 PLATLITPNLPEAEALTGRKIKTLEDMKEAAkkLLAlGAKAVLIK-------GGhlegeeavVTDVLYDGGGFYTLEAPR 190

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 499214665  213 IDKP-PNGLGD-LTAAV--YLARilsGQPPIKALQSTTAAVYEILAR 255
Cdd:pfam08543 191 IPTKnTHGTGCtLSAAIaaNLAK---GLSLPEAVREAKEYVTEAIRD 234
PRK07105 PRK07105
pyridoxamine kinase; Validated
 12-186 5.52e-13

pyridoxamine kinase; Validated


Pssm-ID: 180840 [Multi-domain]  Cd Length: 284  Bit Score: 67.63  E-value: 5.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665  12 VIVISSHVARGSVGNRAAVFALETLGFPVWAVPTVILPWHPGHGRATRIVPPLDQFKAFMADLERapwLG-EVGAVLSGY 90
Cdd:PRK07105   7 VAAIHDLSGFGRVALTASIPIMSSMGLQVCPLPTALLSSHTGGFQNPSIIDLTDGMQAFLTHWKS---LNlKFDAIYSGY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665  91 LGEAGQAEAVASLVaaVKARTPDAVYICDPVMGDSGGLYVP--EATAAAMRdRLVPIADIATPNRYELEWMAGAPLP--- 165
Cdd:PRK07105  84 LGSPRQIQIVSDFI--KYFKKKDLLVVVDPVMGDNGKLYQGfdQEMVEEMR-KLIQKADVITPNLTEACLLLDKPYLeks 160

                        170       180
                 ....*....|....*....|....*
gi 499214665 166 ----DLKSVIAAALHAGPSTMLVTS 186
Cdd:PRK07105 161 yseeEIKQLLRKLADLGPKIVIITS 185
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 140-249 4.27e-10

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 59.28  E-value: 4.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665  140 DRLVPIADIATPNRYELEWMAGAPLPDLKSVIAAA---LHAGPSTMLVTSaqsmmiGGTGNLLLDGTQALLA----EHRV 212
Cdd:pfam00294 175 LELLPLADLLKPNEEELEALTGAKLDDIEEALAALhklLAKGIKTVIVTL------GADGALVVEGDGEVHVpavpKVKV 248

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 499214665  213 IDkpPNGLGDLTAAVYLARILSGQPPIKALQ--STTAAV 249
Cdd:pfam00294 249 VD--TTGAGDSFVGGFLAGLLAGKSLEEALRfaNAAAAL 285
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 58-185 7.54e-10

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 58.21  E-value: 7.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665  58 TRIVPP-----LDQFKAFMADLErapwlgeVGAVLSGYLGEAGQAEAVASLVAavkaRTPDAVYICDPVM----GDSGGl 128
Cdd:PRK06427  51 QRVHPIppefvAAQLDAVFSDIR-------IDAVKIGMLASAEIIETVAEALK----RYPIPPVVLDPVMiaksGDPLL- 118

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 499214665 129 yvPEATAAAMRDRLVPIADIATPNRYELEWMAGAPLPDLKSVIAAA---LHA-GPSTMLVT 185
Cdd:PRK06427 119 --ADDAVAALRERLLPLATLITPNLPEAEALTGLPIADTEDEMKAAaraLHAlGCKAVLIK 177
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 72-248 3.41e-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: 50.65  E-value: 3.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665  72 ADLERAPWLgevgaVLSGY-LGEAGQAEAVASLVAAVKARtpDAVYICDPvmgdSGGLYVPEATAAAMRDrLVPIADIAT 150
Cdd:COG0524  123 ALLAGADIL-----HLGGItLASEPPREALLAALEAARAA--GVPVSLDP----NYRPALWEPARELLRE-LLALVDILF 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665 151 PNRYELEWMAGAplPDLKSVIAAALHAGPSTMLVTsaqsmmIGGTGNLLLDGTQALLA---EHRVIDkpPNGLGDLTAAV 227
Cdd:COG0524  191 PNEEEAELLTGE--TDPEEAAAALLARGVKLVVVT------LGAEGALLYTGGEVVHVpafPVEVVD--TTGAGDAFAAG 260

                        170       180
                 ....*....|....*....|...
gi 499214665 228 YLARILSGQPPIKALQ--STTAA 248
Cdd:COG0524  261 FLAGLLEGLDLEEALRfaNAAAA 283
1-PFK TIGR03168
hexose kinase, 1-phosphofructokinase family; This family consists largely of ...
 55-248 2.50e-06

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: 47.96  E-value: 2.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665   55 GRATRIVPP--------LDQFK-AFMADLERAPWLgevgaVLSGYLGEAGQAEAVASLVAAVKARtpDAVYICDpvmgds 125
Cdd:TIGR03168  97 GEETELNEPgpeiseeeLEQLLeKLRELLASGDIV-----VISGSLPPGVPPDFYAQLIAIARKK--GAKVILD------ 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665  126 gglyvpeATAAAMRDRLVPIADIATPNRYELEWMAGAPLPDLKSVIAAA---LHAGPSTMLVtsaqSMmiGGTGNLLLDG 202
Cdd:TIGR03168 164 -------TSGEALREALAAKPFLIKPNHEELEELFGRELKTLEEIIEAArelLDRGAENVLV----SL--GADGALLVTK 230

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 499214665  203 TQALLAEHRVID-KPPNGLGDLTAAVYLARILSGQPPIKALQSTTAA 248
Cdd:TIGR03168 231 EGALKATPPKVEvVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAA 277
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
 63-184 5.65e-06

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 47.46  E-value: 5.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665  63 PLD----QFKAFMADLErapwlgeVGAVLSGYLGEAGQAEAVASlvaAVKARTPDAVyICDPVMGDSGGLYVPEATA-AA 137
Cdd:PLN02898  62 PLDfvaeQLKSVLSDMP-------VDVVKTGMLPSAEIVKVLCQ---ALKEFPVKAL-VVDPVMVSTSGDVLAGPSIlSA 130

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499214665 138 MRDRLVPIADIATPNRYELEWMAGA----PLPDLKSViAAALHA-GPSTMLV 184
Cdd:PLN02898 131 LREELLPLATIVTPNVKEASALLGGdpleTVADMRSA-AKELHKlGPRYVLV 181
PRK14713 PRK14713
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
61-254 6.75e-06

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 237797 [Multi-domain]  Cd Length: 530  Bit Score: 47.09  E-value: 6.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665  61 VPPLD----QFKAFMADLErapwlgeVGAVLSGYLGEAGQAEAVASLVAAVKArtpdAVYICDPVM-GDSGGLYVPEATA 135
Cdd:PRK14713  80 VPPADflraQLDAVSDDVT-------VDAVKIGMLGDAEVIDAVRTWLAEHRP----PVVVLDPVMvATSGDRLLEEDAE 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665 136 AAMRDrLVPIADIATPNRYELEWMAGAPLPDlksVIAAALHAGPSTMLVTSAQSMMIGG------TGNLLL--DGTQALL 207
Cdd:PRK14713 149 AALRE-LVPRADLITPNLPELAVLLGEPPAT---TWEEALAQARRLAAETGTTVLVKGGhldgqrAPDALVgpDGAVTEV 224

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 499214665 208 AEHRVIDKPPNGLGDLTAAVYLARILSGQPPIKALQSTTAAVYEILA 254
Cdd:PRK14713 225 PGPRVDTRNTHGTGCSLSSALATRLGRGGDWAAALRWATAWLHGAIA 271
PRK12616 PRK12616
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
117-251 7.38e-06

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183624  Cd Length: 270  Bit Score: 46.58  E-value: 7.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665 117 ICDPVM---GDSGGLYvPEAtAAAMRDRLVPIADIATPNRYELEWMAGapLPDLKSV-----IAAALHA-GPSTMLVTSA 187
Cdd:PRK12616 105 VIDPVMvckGANEVLY-PEH-AEALREQLAPLATVITPNLFEAGQLSG--MGEIKTVeqmkeAAKKIHElGAQYVVITGG 180

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499214665 188 QSMMIGGTGNLLLDGTQALLAEHRVIDKP-PNGLGDLTAAVYLARILSGQPPIKALQST----TAAVYE 251
Cdd:PRK12616 181 GKLKHEKAVDVLYDGETAEVLESEMIDTPyTHGAGCTFSAAVTAELAKGSEVKEAIYAAkefiTAAIKE 249
PRK08573 PRK08573
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
83-174 7.53e-06

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 236297 [Multi-domain]  Cd Length: 448  Bit Score: 47.03  E-value: 7.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665  83 VGAVLSGYLGEAGQAEAVASLVAavKARTPDAVyicDPVM-GDSGGLYVPEATAAAMRDRLVPIADIATPNRYELEWMAG 161
Cdd:PRK08573  72 IDAAKTGMLSNREIIEAVAKTVS--KYGFPLVV---DPVMiAKSGAPLLREDAVDALIKRLLPLATVVTPNRPEAEKLTG 146

                         90
                 ....*....|...
gi 499214665 162 APLPDLKSVIAAA 174
Cdd:PRK08573 147 MKIRSVEDARKAA 159
PRK09517 PRK09517
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ...
 54-294 9.24e-06

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


Pssm-ID: 169939 [Multi-domain]  Cd Length: 755  Bit Score: 46.89  E-value: 9.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665  54 HGRATRIVPPLD----QFKAFMADLErapwlgeVGAVLSGYLGEAGQAEAVASLVAAVkartPDAVYICDPVMGDSGGLY 129
Cdd:PRK09517 285 HGVNTIHTPPLTfleeQLEAVFSDVT-------VDAVKLGMLGSADTVDLVASWLGSH----EHGPVVLDPVMVATSGDR 353

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665 130 VPEATAAAMRDRLVPIADIATPNRYELEWMAG-APLPDLKSVIAAA--LHAGPSTMLVTSAQSMMIGGTGNLLL--DGTQ 204
Cdd:PRK09517 354 LLDADATEALRRLAVHVDVVTPNIPELAVLCGeAPAITMDEAIAQArgFARTHGTIVIVKGGHLTGDLADNAVVrpDGSV 433

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665 205 ALLAEHRVIDKPPNGLGDLTAAVYLARILSGQPPIKALQSTTAAVYEILartakRGGDELQLETDAQSLSHPMAMVQLRH 284
Cdd:PRK09517 434 HQVENPRVNTTNSHGTGCSLSAALATLIAAGESVEKALEWATRWLNEAL-----RHADHLAVGSGNGPVDHGHLARRLTH 508

                        250
                 ....*....|..
gi 499214665 285 L--THPGRDRRA 294
Cdd:PRK09517 509 AaeTTPWAHLRA 520
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
151-248 1.63e-05

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


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 45.51  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665 151 PNRYELEWMAGAPLPDLKSVIAAA--LHAGPSTMLVTSAqsmmiGGTGNLLLDGTQALLAEHRVID-KPPNGLGDLTAAV 227
Cdd:COG1105  183 PNLEELEELLGRPLETLEDIIAAAreLLERGAENVVVSL-----GADGALLVTEDGVYRAKPPKVEvVSTVGAGDSMVAG 257

                         90       100
                 ....*....|....*....|.
gi 499214665 228 YLARILSGQPPIKALQSTTAA 248
Cdd:COG1105  258 FLAGLARGLDLEEALRLAVAA 278
FruK_PfkB_like cd01164
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ...
 55-248 2.17e-05

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: 45.22  E-value: 2.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665  55 GRATRIV---PPLD--QFKAFMADLERAPWLGEVgAVLSGYLGEAGQAEAVASLVAAVKARTPdavyicdPVMGDSGGly 129
Cdd:cd01164   98 GTETEINepgPEISeeELEALLEKLKALLKKGDI-VVLSGSLPPGVPADFYAELVRLAREKGA-------RVILDTSG-- 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665 130 vpeataAAMRDRLVPIADIATPNRYELEWMAGAPLPDLKSVIAAA---LHAGPSTMLVtsaqSMmiGGTGNLLLDGTQAL 206
Cdd:cd01164  168 ------EALLAALAAKPFLIKPNREELEELFGRPLGDEEDVIAAArklIERGAENVLV----SL--GADGALLVTKDGVY 235

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 499214665 207 LAehrvidKPPN-------GLGDLTAAVYLARILSGQPPIKALQSTTAA 248
Cdd:cd01164  236 RA------SPPKvkvvstvGAGDSMVAGFVAGLAQGLSLEEALRLAVAA 278
PRK12412 PRK12412
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
9-251 1.49e-04

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183512 [Multi-domain]  Cd Length: 268  Bit Score: 42.65  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665   9 PRAVIVISSHvARGSVGNRAAVFALETLGFPVWAVPTVILPWHPGHGRATRIVP-PLDQFKAfmaDLERAPWLGEVGAVL 87
Cdd:PRK12412   2 NKALTIAGSD-TSGGAGIQADLKTFQELGVYGMTSLTTIVTMDPHNGWAHNVFPiPASTLKP---QLETTIEGVGVDALK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665  88 SGYLGEAGQAEAVASLVAavKARTPDAVyiCDPVM---GDSGGLYvPEATAAaMRDRLVPIADIATPNRYELEWMAGAPL 164
Cdd:PRK12412  78 TGMLGSVEIIEMVAETIE--KHNFKNVV--VDPVMvckGADEALH-PETNDC-LRDVLVPKALVVTPNLFEAYQLSGVKI 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499214665 165 PDLKSVIAAA--LHA-GPSTMLVTSAQSMMIGGTGNLLLDG-TQALLAEHRVIDKPPNGLGDLTAAVYLARILSGQPPIK 240
Cdd:PRK12412 152 NSLEDMKEAAkkIHAlGAKYVLIKGGSKLGTETAIDVLYDGeTFDLLESEKIDTTNTHGAGCTYSAAITAELAKGKPVKE 231

                        250
                 ....*....|.
gi 499214665 241 ALQSTTAAVYE 251
Cdd:PRK12412 232 AVKTAKEFITA 242
fruK PRK09513
1-phosphofructokinase; Provisional
 151-217 2.03e-04

1-phosphofructokinase; Provisional


Pssm-ID: 181923 [Multi-domain]  Cd Length: 312  Bit Score: 42.37  E-value: 2.03e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499214665 151 PNRYELEWMAGAPLPDLKSVIAAA--LHAGPSTMLVTSaqsmmIGGTGNLLLDGTQALLAehrvidKPP 217
Cdd:PRK09513 186 PNRRELEIWAGRKLPELKDVIEAAhaLREQGIAHVVIS-----LGAEGALWVNASGEWIA------KPP 243
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH