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Conserved domains on  [gi|754952465|ref|WP_042308629|]
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MULTISPECIES: pyridoxal kinase PdxY [Citrobacter]

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

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: 534.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465   1 MKNILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPTHLTEIVKGIADIDKLQTCDAVLS 80
Cdd:PRK05756   1 MKNILSIQSHVVYGHVGNSAAVFPMQRLGVNVWPLNTVQFSNHTGYGKWTGCVMPPSHLTEIVQGIADIGWLGECDAVLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465  81 GYLGSAEQGEHILGIVRQVKAANPRAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHAVHNV 160
Cdd:PRK05756  81 GYLGSAEQGEAILDAVRRVKAANPQALYFCDPVMGDPEKGCIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 161 TEAVMAARELIAQGPEIVLVKHLARAGISTDRFEMLLVTAEQAWHISRPLVDFGaRQPVGVGDVTSGLLLVKLLQGASLQ 240
Cdd:PRK05756 161 EDAVAAARALIARGPKIVLVTSLARAGYPADRFEMLLVTADGAWHISRPLVDFM-RQPVGVGDLTSALFLARLLQGGSLE 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 754952465 241 QALEHVTAAVYEVMIATKEMHEYELQVVAAQDRIAKPEHYFSATQL 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: 534.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465   1 MKNILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPTHLTEIVKGIADIDKLQTCDAVLS 80
Cdd:PRK05756   1 MKNILSIQSHVVYGHVGNSAAVFPMQRLGVNVWPLNTVQFSNHTGYGKWTGCVMPPSHLTEIVQGIADIGWLGECDAVLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465  81 GYLGSAEQGEHILGIVRQVKAANPRAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHAVHNV 160
Cdd:PRK05756  81 GYLGSAEQGEAILDAVRRVKAANPQALYFCDPVMGDPEKGCIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 161 TEAVMAARELIAQGPEIVLVKHLARAGISTDRFEMLLVTAEQAWHISRPLVDFGaRQPVGVGDVTSGLLLVKLLQGASLQ 240
Cdd:PRK05756 161 EDAVAAARALIARGPKIVLVTSLARAGYPADRFEMLLVTADGAWHISRPLVDFM-RQPVGVGDLTSALFLARLLQGGSLE 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 754952465 241 QALEHVTAAVYEVMIATKEMHEYELQVVAAQDRIAKPEHYFSATQL 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 6.17e-173

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: 479.33  E-value: 6.17e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465    1 MKNILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPTHLTEIVKGIADIDKLQTCDAVLS 80
Cdd:TIGR00687   1 MKNVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLEAINKLNQCDAVLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465   81 GYLGSAEQGEHILGIVRQVKAANPRAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHAVHNV 160
Cdd:TIGR00687  81 GYLGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKGCYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465  161 TEAVMAARELIAQGPEIVLVKHLARAGISTDR-FEMLLVTAEQAWHISRPLVDFGaRQPVGVGDVTSGLLLVKLLQGASL 239
Cdd:TIGR00687 161 EEALAAADALIAMGPDIVLVTHLIRAGSQRDRsFEGLVATQEGRWHISRPLAVFD-PPPVGTGDLIAALLLATLLHGNSL 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 754952465  240 QQALEHVTAAVYEVMIATKEMHEYELQVVAAQDRIAKPEHYFSATQL 286
Cdd:TIGR00687 240 KEALEKTVSAVYHVLRTTIQLGKYELQPVAAQLEIRMPQSKFDAEKV 286
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
1-275 1.85e-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: 391.43  E-value: 1.85e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465   1 MKNILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPTHLTEIVKGIADIDKLQTCDAVLS 80
Cdd:COG2240    1 MKRVLSIQSHVVYGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWKELGVLLEFDAVLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465  81 GYLGSAEQGEHILGIVRQVKAANPRAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHAVHNV 160
Cdd:COG2240   81 GYLGSAEQGDIIADFVARVKAANPDALYLCDPVMGDNGKGYYVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 161 TEAVMAARELIAQGPEIVLVKHLARAGISTDRFEMLLVTAEQAWHISRPLVDFgarQPVGVGDVTSGLLLVKLLQGASLQ 240
Cdd:COG2240  161 EEALAAARALLALGPKIVVVTSVPLDDTPADKIGNLAVTADGAWLVETPLLPF---SPNGTGDLFAALLLAHLLRGKSLE 237
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 754952465 241 QALEHVTAAVYEVMIATKEMHEYELQVVAAQDRIA 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 1.06e-112

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: 325.31  E-value: 1.06e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465   3 NILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPTHLTEIVKGIADIDKLQTCDAVLSGY 82
Cdd:cd01173    1 RVLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLLLEYDAVLTGY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465  83 LGSAEQGEHILGIVRQVKAANPRAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHAVHNVTE 162
Cdd:cd01173   81 LGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGDNGKLYVVAEEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLED 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 163 AVMAARELIAQGPEIVLVKHLARAGisTDRFEMLLVTAEQAWHISRPLVDFGArQPVGVGDVTSGLLLVKLLQGASLQQA 242
Cdd:cd01173  161 AKAAARALHAKGPKTVVVTSVELAD--DDRIEMLGSTATEAWLVQRPKIPFPA-YFNGTGDLFAALLLARLLKGKSLAEA 237
                        250
                 ....*....|....*..
gi 754952465 243 LEHVTAAVYEVMIATKE 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 ...
53-250 3.50e-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: 67.51  E-value: 3.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465   53 VMPPTHLTEIVKGI-ADIDklqtCDAVLSGYLGSAEqgehilgIVRQV--KAANPRAKYFCDPVM----GHPekgcIVAP 125
Cdd:pfam08543  42 PLPPEFVAAQLDAVlEDIP----VDAVKTGMLGSAE-------IIEAVaeKLDKYGVPVVLDPVMvaksGDS----LLDD 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465  126 GVAEFHVRHALPASDIIAPNLVELEILCEHAVHNVTEAVMAARELIAQGPEIVLVK--HLARAG-ISTDrfemLLVTAEQ 202
Cdd:pfam08543 107 EAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKggHLEGEEaVVTD----VLYDGGG 182
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 754952465  203 AWHISRPLVDfgARQPVGVGDVTSGLLLVKLLQGASLQQALEH----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: 534.06  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465   1 MKNILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPTHLTEIVKGIADIDKLQTCDAVLS 80
Cdd:PRK05756   1 MKNILSIQSHVVYGHVGNSAAVFPMQRLGVNVWPLNTVQFSNHTGYGKWTGCVMPPSHLTEIVQGIADIGWLGECDAVLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465  81 GYLGSAEQGEHILGIVRQVKAANPRAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHAVHNV 160
Cdd:PRK05756  81 GYLGSAEQGEAILDAVRRVKAANPQALYFCDPVMGDPEKGCIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 161 TEAVMAARELIAQGPEIVLVKHLARAGISTDRFEMLLVTAEQAWHISRPLVDFGaRQPVGVGDVTSGLLLVKLLQGASLQ 240
Cdd:PRK05756 161 EDAVAAARALIARGPKIVLVTSLARAGYPADRFEMLLVTADGAWHISRPLVDFM-RQPVGVGDLTSALFLARLLQGGSLE 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 754952465 241 QALEHVTAAVYEVMIATKEMHEYELQVVAAQDRIAKPEHYFSATQL 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 6.17e-173

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: 479.33  E-value: 6.17e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465    1 MKNILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPTHLTEIVKGIADIDKLQTCDAVLS 80
Cdd:TIGR00687   1 MKNVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLEAINKLNQCDAVLS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465   81 GYLGSAEQGEHILGIVRQVKAANPRAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHAVHNV 160
Cdd:TIGR00687  81 GYLGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKGCYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465  161 TEAVMAARELIAQGPEIVLVKHLARAGISTDR-FEMLLVTAEQAWHISRPLVDFGaRQPVGVGDVTSGLLLVKLLQGASL 239
Cdd:TIGR00687 161 EEALAAADALIAMGPDIVLVTHLIRAGSQRDRsFEGLVATQEGRWHISRPLAVFD-PPPVGTGDLIAALLLATLLHGNSL 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 754952465  240 QQALEHVTAAVYEVMIATKEMHEYELQVVAAQDRIAKPEHYFSATQL 286
Cdd:TIGR00687 240 KEALEKTVSAVYHVLRTTIQLGKYELQPVAAQLEIRMPQSKFDAEKV 286
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
1-275 1.85e-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: 391.43  E-value: 1.85e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465   1 MKNILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPTHLTEIVKGIADIDKLQTCDAVLS 80
Cdd:COG2240    1 MKRVLSIQSHVVYGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWKELGVLLEFDAVLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465  81 GYLGSAEQGEHILGIVRQVKAANPRAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHAVHNV 160
Cdd:COG2240   81 GYLGSAEQGDIIADFVARVKAANPDALYLCDPVMGDNGKGYYVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 161 TEAVMAARELIAQGPEIVLVKHLARAGISTDRFEMLLVTAEQAWHISRPLVDFgarQPVGVGDVTSGLLLVKLLQGASLQ 240
Cdd:COG2240  161 EEALAAARALLALGPKIVVVTSVPLDDTPADKIGNLAVTADGAWLVETPLLPF---SPNGTGDLFAALLLAHLLRGKSLE 237
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 754952465 241 QALEHVTAAVYEVMIATKEMHEYELQVVAAQDRIA 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 1.06e-112

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: 325.31  E-value: 1.06e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465   3 NILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPTHLTEIVKGIADIDKLQTCDAVLSGY 82
Cdd:cd01173    1 RVLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLLLEYDAVLTGY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465  83 LGSAEQGEHILGIVRQVKAANPRAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHAVHNVTE 162
Cdd:cd01173   81 LGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGDNGKLYVVAEEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLED 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 163 AVMAARELIAQGPEIVLVKHLARAGisTDRFEMLLVTAEQAWHISRPLVDFGArQPVGVGDVTSGLLLVKLLQGASLQQA 242
Cdd:cd01173  161 AKAAARALHAKGPKTVVVTSVELAD--DDRIEMLGSTATEAWLVQRPKIPFPA-YFNGTGDLFAALLLARLLKGKSLAEA 237
                        250
                 ....*....|....*..
gi 754952465 243 LEHVTAAVYEVMIATKE 259
Cdd:cd01173  238 LEKALNFVHEVLEATYE 254
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
2-286 1.54e-52

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 173.34  E-value: 1.54e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465   2 KNILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPTHLTEIVKGIADIDKLQTCDAVLSG 81
Cdd:PTZ00344   5 KKVLSIQSHVTHGYVGNRAATFPLQLLGFDVDFVNTVQLSNHTGYPVIKGHRLDLNELITLMDGLRANNLLSDYTYVLTG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465  82 YLGSAEQGEHILGIVRQVKAANPRAKYFCDPVMGHPEKGCIVAPGVAEFhvRHALPASDIIAPNLVELEILCEHAVHNVT 161
Cdd:PTZ00344  85 YINSADILREVLATVKEIKELRPKLIFLCDPVMGDDGKLYVKEEVVDAY--RELIPYADVITPNQFEASLLSGVEVKDLS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 162 EAVMAARELIAQGPEIVLVKHLARAGISTDRFEMLLVTAEQAWHISRplvdFGARQP------VGVGDVTSGLLLVKLLQ 235
Cdd:PTZ00344 163 DALEAIDWFHEQGIPVVVITSFREDEDPTHLRFLLSCRDKDTKNNKR----FTGKVPyiegryTGTGDLFAALLLAFSHQ 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 754952465 236 GaSLQQALEHVTAAVYEVMIATKEMH--------EYELQVVAAQDRIAKPEHYFSATQL 286
Cdd:PTZ00344 239 H-PMDLAVGKAMGVLQDIIKATRESGgsgssslmSRELRLIQSPRDLLNPETVFKVTPL 296
PLN02978 PLN02978
pyridoxal kinase
4-286 5.44e-43

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 149.12  E-value: 5.44e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465   4 ILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPTHLTEIVKGIaDIDKLQTCDAVLSGYL 83
Cdd:PLN02978  17 VLSIQSHTVHGYVGNKSAVFPLQLLGFDVDPINSVQFSNHTGYPTFKGQVLDGEQLWALIEGL-EANGLLFYTHLLTGYI 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465  84 GSAEQGEHILGIVRQVKAANPRAKYFCDPVMGHPEKgCIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHAVHNVTEA 163
Cdd:PLN02978  96 GSVSFLRTVLRVVKKLRSVNPNLTYVCDPVLGDEGK-LYVPPELVPVYREKVVPLATMLTPNQFEAEQLTGIRIVTEEDA 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 164 VMAARELIAQGPEIVLVKhlaragiSTDRFEMLLVTA---------EQAWHISRPLVdfgARQPVGVGDVTSGLLLV--- 231
Cdd:PLN02978 175 REACAILHAAGPSKVVIT-------SIDIDGKLLLVGshrkekgarPEQFKIVIPKI---PAYFTGTGDLMAALLLGwsh 244
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754952465 232 ----KLLQGASLQ----QALEHVTAAVYEVMIATKEMHEYELQVVAAQDRIAKPEHYFSATQL 286
Cdd:PLN02978 245 kypdNLDKAAELAvsslQAVLRRTLADYKRAGADPKSSSLELRLVQSQDDIRHPQVRFKAERY 307
pdxK PRK08176
pyridoxine/pyridoxal/pyridoxamine kinase;
3-266 1.07e-40

pyridoxine/pyridoxal/pyridoxamine kinase;


Pssm-ID: 181269 [Multi-domain]  Cd Length: 281  Bit Score: 142.10  E-value: 1.07e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465   3 NILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPTHLTEIVKGIADIDKLQTCDAVLSGY 82
Cdd:PRK08176  17 DIVAVQSQVVYGSVGNSIAVPAIKANGLRVFAVPTVLLSNTPHYPTFYGGAIPDEWFSGYLRALQERDALRQLRAVTTGY 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465  83 LGSAEQGEHILGIVRQVKAANPRAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHAVHNVTE 162
Cdd:PRK08176  97 MGSASQIKILAEWLTALRADHPDLLIMVDPVIGDIDSGIYVKPDLPEAYRQHLLPLAQGLTPNIFELEILTGKPCRTLDS 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 163 AVMAARELIAQGPEIVLVKHlARAGISTDRFEMLLVTAEQAWHISRPLVDfgaRQPVGVGDVTSGLLLVKLLQGASLQQA 242
Cdd:PRK08176 177 AIAAAKSLLSDTLKWVVITS-AAGNEENQEMQVVVVTADSVNVISHPRVD---TDLKGTGDLFCAELVSGLLKGKALTDA 252
                        250       260
                 ....*....|....*....|....
gi 754952465 243 LEHVTAAVYEVMIATKEMHEYELQ 266
Cdd:PRK08176 253 AHRAGLRVLEVMRYTQQAGSDELI 276
PRK07105 PRK07105
pyridoxamine kinase; Validated
1-265 2.81e-16

pyridoxamine kinase; Validated


Pssm-ID: 180840 [Multi-domain]  Cd Length: 284  Bit Score: 76.88  E-value: 2.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465   1 MKNILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHT----QYGKWTgcvmppthLTEIVKGI------ADID 70
Cdd:PRK07105   4 VKRVAAIHDLSGFGRVALTASIPIMSSMGLQVCPLPTALLSSHTggfqNPSIID--------LTDGMQAFlthwksLNLK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465  71 klqtCDAVLSGYLGSAEQGEHILGIVRQVKaaNPRAKYFCDPVMGhpEKGCiVAPGVAEFHV---RHALPASDIIAPNLV 147
Cdd:PRK07105  76 ----FDAIYSGYLGSPRQIQIVSDFIKYFK--KKDLLVVVDPVMG--DNGK-LYQGFDQEMVeemRKLIQKADVITPNLT 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 148 ELEILCEHA---VHNVTEAVMA-ARELIAQGPEIVLVkhlarAGISTDRFEMLLV----TAEQAWHISRPlvdfgaRQPV 219
Cdd:PRK07105 147 EACLLLDKPyleKSYSEEEIKQlLRKLADLGPKIVII-----TSVPFEDGKIGVAyydrATDRFWKVFCK------YIPA 215
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 754952465 220 ---GVGDVTSGLLLVKLLQGASLQQALEHVTAAVYEVMIATkEMHEYEL 265
Cdd:PRK07105 216 hypGTGDIFTSVITGSLLQGDSLPIALDRAVQFIEKGIRAT-LGLKYDL 263
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
133-249 1.58e-15

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


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 75.17  E-value: 1.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 133 RHALPAS-DIIAPNLVELEILCEHAVHNVTEAVMAARELIAQGPEIVLVKhLARAGistdrfeMLLVTAEQAWHISRPLV 211
Cdd:COG1105  171 KAALEAGpDLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVS-LGADG-------ALLVTEDGVYRAKPPKV 242
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 754952465 212 DfgARQPVGVGDVTSGLLLVKLLQGASLQQALEHVTAA 249
Cdd:COG1105  243 E--VVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAA 278
FruK_PfkB_like cd01164
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ...
133-249 6.36e-15

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: 72.95  E-value: 6.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 133 RHALPAS-DIIAPNLVELEILCEHAVHNVTEAVMAARELIAQGPEIVLVKhLARAGistdrfeMLLVTAEQAWHISRPLV 211
Cdd:cd01164  171 LAALAAKpFLIKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVS-LGADG-------ALLVTKDGVYRASPPKV 242
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 754952465 212 DfgARQPVGVGDVTSGLLLVKLLQGASLQQALEHVTAA 249
Cdd:cd01164  243 K--VVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAA 278
HMPP_kinase cd01169
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ...
75-250 1.25e-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: 68.68  E-value: 1.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465  75 CDAVLSGYLGSAEqgehILGIVRQVKAANPRAKYFCDPVM----GHPekgcIVAPGVAEFHVRHALPASDIIAPNLVELE 150
Cdd:cd01169   69 VDAIKIGMLGSAE----IIEAVAEALKDYPDIPVVLDPVMvaksGDS----LLDDDAIEALRELLLPLATLITPNLPEAE 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 151 ILCEHAVHNVTEAVMAARELIAQGPEIVLVK--HLaRAGISTDrfemLLVTAEQAWHISRPLVDfgARQPVGVGDVTSGL 228
Cdd:cd01169  141 LLTGLEIATEEDMMKAAKALLALGAKAVLIKggHL-PGDEAVD----VLYDGGGFFEFESPRID--TKNTHGTGCTLSSA 213
                        170       180
                 ....*....|....*....|....*.
gi 754952465 229 LLVKLLQGASL----QQALEHVTAAV 250
Cdd:cd01169  214 IAANLAKGLSLeeavREAKEYVTQAI 239
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
53-250 3.50e-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: 67.51  E-value: 3.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465   53 VMPPTHLTEIVKGI-ADIDklqtCDAVLSGYLGSAEqgehilgIVRQV--KAANPRAKYFCDPVM----GHPekgcIVAP 125
Cdd:pfam08543  42 PLPPEFVAAQLDAVlEDIP----VDAVKTGMLGSAE-------IIEAVaeKLDKYGVPVVLDPVMvaksGDS----LLDD 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465  126 GVAEFHVRHALPASDIIAPNLVELEILCEHAVHNVTEAVMAARELIAQGPEIVLVK--HLARAG-ISTDrfemLLVTAEQ 202
Cdd:pfam08543 107 EAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKggHLEGEEaVVTD----VLYDGGG 182
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 754952465  203 AWHISRPLVDfgARQPVGVGDVTSGLLLVKLLQGASLQQALEH----VTAAV 250
Cdd:pfam08543 183 FYTLEAPRIP--TKNTHGTGCTLSAAIAANLAKGLSLPEAVREakeyVTEAI 232
1-PFK TIGR03168
hexose kinase, 1-phosphofructokinase family; This family consists largely of ...
140-249 9.98e-13

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


Pssm-ID: 274464 [Multi-domain]  Cd Length: 303  Bit Score: 66.83  E-value: 9.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465  140 DIIAPNLVELEILCEHAVHNVTEAVMAARELIAQGPEIVLVKhLARAGistdrfeMLLVTAEQAWHISRPLVDfgARQPV 219
Cdd:TIGR03168 178 FLIKPNHEELEELFGRELKTLEEIIEAARELLDRGAENVLVS-LGADG-------ALLVTKEGALKATPPKVE--VVNTV 247
                          90       100       110
                  ....*....|....*....|....*....|
gi 754952465  220 GVGDVTSGLLLVKLLQGASLQQALEHVTAA 249
Cdd:TIGR03168 248 GAGDSMVAGFLAGLARGLSLEEALRFAVAA 277
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
76-249 6.56e-11

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: 61.21  E-value: 6.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465  76 DAVLSGYLGSAEQGEHILGIVRQVKAANprakYFCDPVM----GHPekgcIVAPGVAEFHVRHALPASDIIAPNLVELEI 151
Cdd:COG0351   68 DAIKIGMLGSAEIIEAVAEILADYPLVP----VVLDPVMvaksGDR----LLDEDAVEALRELLLPLATVVTPNLPEAEA 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 152 LCEHAVHNVTEAVMAARELIAQGPEIVLVK--HLArAGISTDrfemLLVTAEQAWHISRPLVDfgARQPVGVGDVTSGLL 229
Cdd:COG0351  140 LLGIEITTLDDMREAAKALLELGAKAVLVKggHLP-GDEAVD----VLYDGDGVREFSAPRID--TGNTHGTGCTLSSAI 212
                        170       180
                 ....*....|....*....|....
gi 754952465 230 LVKLLQGASL----QQALEHVTAA 249
Cdd:COG0351  213 AALLAKGLDLeeavREAKEYVTQA 236
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
132-249 1.62e-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: 60.43  E-value: 1.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465  132 VRHALPASDIIAPNLVELEILCEHAVHNVTEAVMAARELIAQGPEIVLVKhLARAGistdrfeMLLVTAEQAWHISRP-- 209
Cdd:pfam00294 174 LLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVT-LGADG-------ALVVEGDGEVHVPAVpk 245
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 754952465  210 --LVDfgarqPVGVGDVTSGLLLVKLLQGASLQQALEHVTAA 249
Cdd:pfam00294 246 vkVVD-----TTGAGDSFVGGFLAGLLAGKSLEEALRFANAA 282
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
68-249 8.30e-10

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: 58.36  E-value: 8.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465  68 DIDKLQTCDAV-LSGYLGSAEQG-EHILGIVRQVKAANprAKYFCDPVMGHpekgCIVAPGVAEFhvRHALPASDIIAPN 145
Cdd:COG0524  121 DEALLAGADILhLGGITLASEPPrEALLAALEAARAAG--VPVSLDPNYRP----ALWEPARELL--RELLALVDILFPN 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 146 LVELEILCEHavhnvTEAVMAARELIAQGPEIVLVKhLARAGIstdrfemLLVTAEQAWHISRPLVDfgARQPVGVGDVT 225
Cdd:COG0524  193 EEEAELLTGE-----TDPEEAAAALLARGVKLVVVT-LGAEGA-------LLYTGGEVVHVPAFPVE--VVDTTGAGDAF 257
                        170       180
                 ....*....|....*....|....
gi 754952465 226 SGLLLVKLLQGASLQQALEHVTAA 249
Cdd:COG0524  258 AAGFLAGLLEGLDLEEALRFANAA 281
PRK14713 PRK14713
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
74-248 4.31e-08

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 237797 [Multi-domain]  Cd Length: 530  Bit Score: 54.02  E-value: 4.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465  74 TCDAVLSGYLGSAEqgehILGIVRQVKAANPRAKYFCDPVMGHPEKGCIVAPGvAEFHVRHALPASDIIAPNLVELEILC 153
Cdd:PRK14713  98 TVDAVKIGMLGDAE----VIDAVRTWLAEHRPPVVVLDPVMVATSGDRLLEED-AEAALRELVPRADLITPNLPELAVLL 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 154 EHAVHNV-TEAVMAARELIAQGPEIVLVK--HLarAGISTDrfEMLLVTAEQAWHISRPLVDfgARQPVGVGDVTSGLLL 230
Cdd:PRK14713 173 GEPPATTwEEALAQARRLAAETGTTVLVKggHL--DGQRAP--DALVGPDGAVTEVPGPRVD--TRNTHGTGCSLSSALA 246
                        170
                 ....*....|....*...
gi 754952465 231 VKLLQGASLQQALEHVTA 248
Cdd:PRK14713 247 TRLGRGGDWAAALRWATA 264
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
76-250 7.79e-08

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 52.05  E-value: 7.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465  76 DAVLSGYLGSAEqgehILGIVRQVKAANPRAKYFCDPVM----GHPekgcIVAPGVAEFHVRHALPASDIIAPNLVELEI 151
Cdd:PRK06427  75 DAVKIGMLASAE----IIETVAEALKRYPIPPVVLDPVMiaksGDP----LLADDAVAALRERLLPLATLITPNLPEAEA 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 152 LCEHAVHNvTEAVM--AARELIAQGPEIVLVK--HLARAGISTDRfemlLVTAEQAWHISRPLVDfgARQPVGVGDVTSG 227
Cdd:PRK06427 147 LTGLPIAD-TEDEMkaAARALHALGCKAVLIKggHLLDGEESVDW----LFDGEGEERFSAPRIP--TKNTHGTGCTLSA 219
                        170       180
                 ....*....|....*....|....*..
gi 754952465 228 LLLVKLLQGASLQQALEH----VTAAV 250
Cdd:PRK06427 220 AIAAELAKGASLLDAVQTakdyVTRAI 246
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
77-234 1.46e-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: 47.86  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465  77 AVLSGYLGSAEQGEHILGIVRQVKAAnprakYFCDPVMghpekgcivaPGVAEFH--VRHALPASDIIAPNLVELEILCE 154
Cdd:cd00287   61 VVISGLSPAPEAVLDALEEARRRGVP-----VVLDPGP----------RAVRLDGeeLEKLLPGVDILTPNEEEAEALTG 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 155 HAVHNVTEAVMAARELIAQGPEIVLVKHLARAGISTDRfemllvtaeQAWHISRPLVDFGARQPVGVGDVTSGLLLVKLL 234
Cdd:cd00287  126 RRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATR---------GGTEVHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
PRK09517 PRK09517
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ...
74-248 7.20e-05

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


Pssm-ID: 169939 [Multi-domain]  Cd Length: 755  Bit Score: 44.19  E-value: 7.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465  74 TCDAVLSGYLGSAEqgehilgIVRQVKA---ANPRAKYFCDPVMGHPEKGCIVAPGVAEfHVRHALPASDIIAPNLVELE 150
Cdd:PRK09517 310 TVDAVKLGMLGSAD-------TVDLVASwlgSHEHGPVVLDPVMVATSGDRLLDADATE-ALRRLAVHVDVVTPNIPELA 381
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 151 ILC-EHAVHNVTEAVMAARELIAQGPEIVLVK--HLaragiSTDRFEMLLVTAEQAWH-ISRPLVDFGARQpvGVGDVTS 226
Cdd:PRK09517 382 VLCgEAPAITMDEAIAQARGFARTHGTIVIVKggHL-----TGDLADNAVVRPDGSVHqVENPRVNTTNSH--GTGCSLS 454
                        170       180
                 ....*....|....*....|..
gi 754952465 227 GLLLVKLLQGASLQQALEHVTA 248
Cdd:PRK09517 455 AALATLIAAGESVEKALEWATR 476
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
117-243 3.71e-04

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


Pssm-ID: 238916 [Multi-domain]  Cd Length: 288  Bit Score: 41.15  E-value: 3.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 117 PEKGCIVApgvaefHVRHALPASDIIAPNLVELEILCEHAVHNVTEAVMAARELIAQGPEIVLVKHLARAGISTDRFEML 196
Cdd:cd01941  161 PTSAPKLK------KLFYLLHAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSREGGV 234
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 754952465 197 LVTAEQAWHISRPLVDFGArqpvgvGDVTSGLLLVKLLQGASLQQAL 243
Cdd:cd01941  235 ETKLFPAPQPETVVNVTGA------GDAFVAGLVAGLLEGMSLDDSL 275
PRK11142 PRK11142
ribokinase; Provisional
140-250 4.49e-04

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 41.01  E-value: 4.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 140 DIIAPNLVELEILCEHAVHNVTEAVMAARELIAQGPEIVLVKHLAR-AGISTDRFEMLlvtaeqawhISRPLVDfgARQP 218
Cdd:PRK11142 180 DIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRgVWLSENGEGQR---------VPGFRVQ--AVDT 248
                         90       100       110
                 ....*....|....*....|....*....|....
gi 754952465 219 VGVGDVTSGLLLVKLLQGASLQQALE--HVTAAV 250
Cdd:PRK11142 249 IAAGDTFNGALVTALLEGKPLPEAIRfaHAAAAI 282
fruK PRK09513
1-phosphofructokinase; Provisional
141-248 5.74e-04

1-phosphofructokinase; Provisional


Pssm-ID: 181923 [Multi-domain]  Cd Length: 312  Bit Score: 40.83  E-value: 5.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 141 IIAPNLVELEILCEHAVHNVTEAVMAARELIAQGPEIVLvkhlaragISTDRFEMLLVTAEQAWHISRPLVDFGArqPVG 220
Cdd:PRK09513 183 LVKPNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVV--------ISLGAEGALWVNASGEWIAKPPACDVVS--TVG 252
                         90       100
                 ....*....|....*....|....*...
gi 754952465 221 VGDVTSGLLLVKLLQGASLQQALEHVTA 248
Cdd:PRK09513 253 AGDSMVGGLIYGLLMRESSEHTLRLATA 280
PRK12413 PRK12413
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
136-181 1.23e-03

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183513 [Multi-domain]  Cd Length: 253  Bit Score: 39.66  E-value: 1.23e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 754952465 136 LPASDIIAPNLVELEILCEHAVHNVTEAVMAARELIAQGPEIVLVK 181
Cdd:PRK12413 127 FPYVTVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAVVIK 172
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
76-193 2.29e-03

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 39.37  E-value: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465  76 DAVLSGYLGSAEqgehILGIVRQVKAANPRAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLVELE-ILCE 154
Cdd:PLN02898  80 DVVKTGMLPSAE----IVKVLCQALKEFPVKALVVDPVMVSTSGDVLAGPSILSALREELLPLATIVTPNVKEASaLLGG 155
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 754952465 155 HAVHNVTEAVMAARELIAQGPEIVLVK--HLARAGISTDRF 193
Cdd:PLN02898 156 DPLETVADMRSAAKELHKLGPRYVLVKggHLPDSLDAVDVL 196
PRK10294 PRK10294
6-phosphofructokinase 2; Provisional
140-249 7.40e-03

6-phosphofructokinase 2; Provisional


Pssm-ID: 182361 [Multi-domain]  Cd Length: 309  Bit Score: 37.46  E-value: 7.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 140 DIIAPNLVELEILCEHAVHNVTEAVMAARELIAQGPEIVLVKHLARAGistdrfeMLLVTAEQAWHISRPLVDfgARQPV 219
Cdd:PRK10294 182 ELVKPNQKELSALVNRDLTQPDDVRKAAQELVNSGKAKRVVVSLGPQG-------ALGVDSENCIQVVPPPVK--SQSTV 252
                         90       100       110
                 ....*....|....*....|....*....|
gi 754952465 220 GVGDVTSGLLLVKLLQGASLQQALEHVTAA 249
Cdd:PRK10294 253 GAGDSMVGAMTLKLAENASLEEMVRFGVAA 282
 
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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