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Conserved domains on  [gi|1737388516|emb|VAL08794|]
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pyridoxamine kinase [Enterobacter hormaechei]

Protein Classification

pyridoxal kinase PdxY( domain architecture ID 10792681)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK05756 PRK05756
pyridoxal kinase PdxY;
1-286 0e+00

pyridoxal kinase PdxY;


:

Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 534.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516   1 MKNILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMLPSHLTEIVQGIADIDQLKRCDAVLS 80
Cdd:PRK05756    1 MKNILSIQSHVVYGHVGNSAAVFPMQRLGVNVWPLNTVQFSNHTGYGKWTGCVMPPSHLTEIVQGIADIGWLGECDAVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516  81 GYLGSAEQGEHILGIVRQVKAANPAAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLIELEILCEHPVNSV 160
Cdd:PRK05756   81 GYLGSAEQGEAILDAVRRVKAANPQALYFCDPVMGDPEKGCIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516 161 EEAVRASRELLAQGPEIVLVKHLARAGLSQDRFEMLLVTKDEAWHISRPLVDFGtRQPVGVGDVTSGLLLVKLLQSASLR 240
Cdd:PRK05756  161 EDAVAAARALIARGPKIVLVTSLARAGYPADRFEMLLVTADGAWHISRPLVDFM-RQPVGVGDLTSALFLARLLQGGSLE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1737388516 241 DALEHVTAAVYEIMIATKTMQEYELQVVAAQDRIAKPEHYFSATQL 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: 534.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516   1 MKNILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMLPSHLTEIVQGIADIDQLKRCDAVLS 80
Cdd:PRK05756    1 MKNILSIQSHVVYGHVGNSAAVFPMQRLGVNVWPLNTVQFSNHTGYGKWTGCVMPPSHLTEIVQGIADIGWLGECDAVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516  81 GYLGSAEQGEHILGIVRQVKAANPAAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLIELEILCEHPVNSV 160
Cdd:PRK05756   81 GYLGSAEQGEAILDAVRRVKAANPQALYFCDPVMGDPEKGCIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516 161 EEAVRASRELLAQGPEIVLVKHLARAGLSQDRFEMLLVTKDEAWHISRPLVDFGtRQPVGVGDVTSGLLLVKLLQSASLR 240
Cdd:PRK05756  161 EDAVAAARALIARGPKIVLVTSLARAGYPADRFEMLLVTADGAWHISRPLVDFM-RQPVGVGDLTSALFLARLLQGGSLE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1737388516 241 DALEHVTAAVYEIMIATKTMQEYELQVVAAQDRIAKPEHYFSATQL 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 1.60e-169

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: 470.47  E-value: 1.60e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516   1 MKNILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMLPSHLTEIVQGIADIDQLKRCDAVLS 80
Cdd:TIGR00687   1 MKNVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLEAINKLNQCDAVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516  81 GYLGSAEQGEHILGIVRQVKAANPAAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLIELEILCEHPVNSV 160
Cdd:TIGR00687  81 GYLGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKGCYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516 161 EEAVRASRELLAQGPEIVLVKHLARAGLSQDR-FEMLLVTKDEAWHISRPLVDFgTRQPVGVGDVTSGLLLVKLLQSASL 239
Cdd:TIGR00687 161 EEALAAADALIAMGPDIVLVTHLIRAGSQRDRsFEGLVATQEGRWHISRPLAVF-DPPPVGTGDLIAALLLATLLHGNSL 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1737388516 240 RDALEHVTAAVYEIMIATKTMQEYELQVVAAQDRIAKPEHYFSATQL 286
Cdd:TIGR00687 240 KEALEKTVSAVYHVLRTTIQLGKYELQPVAAQLEIRMPQSKFDAEKV 286
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 1-275 1.56e-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: 1.56e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516   1 MKNILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMLPSHLTEIVQGIADIDQLKRCDAVLS 80
Cdd:COG2240     1 MKRVLSIQSHVVYGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWKELGVLLEFDAVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516  81 GYLGSAEQGEHILGIVRQVKAANPAAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLIELEILCEHPVNSV 160
Cdd:COG2240    81 GYLGSAEQGDIIADFVARVKAANPDALYLCDPVMGDNGKGYYVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516 161 EEAVRASRELLAQGPEIVLVKHLARAGLSQDRFEMLLVTKDEAWHISRPLVDFgtrQPVGVGDVTSGLLLVKLLQSASLR 240
Cdd:COG2240   161 EEALAAARALLALGPKIVVVTSVPLDDTPADKIGNLAVTADGAWLVETPLLPF---SPNGTGDLFAALLLAHLLRGKSLE 237

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1737388516 241 DALEHVTAAVYEIMIATKTMQEYELQVVAAQDRIA 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 ...
 3-257 1.09e-113

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


Pssm-ID: 238578 [Multi-domain]  Cd Length: 254  Bit Score: 328.00  E-value: 1.09e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516   3 NILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMLPSHLTEIVQGIADIDQLKRCDAVLSGY 82
Cdd:cd01173     1 RVLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLLLEYDAVLTGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516  83 LGSAEQGEHILGIVRQVKAANPAAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLIELEILCEHPVNSVEE 162
Cdd:cd01173    81 LGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGDNGKLYVVAEEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLED 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516 163 AVRASRELLAQGPEIVLVKHLARAGlsQDRFEMLLVTKDEAWHISRPLVDFGTrQPVGVGDVTSGLLLVKLLQSASLRDA 242
Cdd:cd01173   161 AKAAARALHAKGPKTVVVTSVELAD--DDRIEMLGSTATEAWLVQRPKIPFPA-YFNGTGDLFAALLLARLLKGKSLAEA 237

                         250
                  ....*....|....*
gi 1737388516 243 LEHVTAAVYEIMIAT 257
Cdd:cd01173   238 LEKALNFVHEVLEAT 252
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 63-250 2.22e-15

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


Pssm-ID: 430062 [Multi-domain]  Cd Length: 246  Bit Score: 73.67  E-value: 2.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516  63 VQGIADID------QLK------RCDAVLSGYLGSAEqgehilgIVRQV--KAANPAAKYFCDPVM----GHPekgcIVA 124
Cdd:pfam08543  37 VQGVHPLPpefvaaQLDavlediPVDAVKTGMLGSAE-------IIEAVaeKLDKYGVPVVLDPVMvaksGDS----LLD 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516 125 PGVAEFHVRHALPASDIIAPNLIELEILCEHPVNSVEEAVRASRELLAQGPEIVLVK--HLAragLSQDRFEMLLVTKDE 202
Cdd:pfam08543 106 DEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKggHLE---GEEAVVTDVLYDGGG 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1737388516 203 AWHISRPLVDfgTRQPVGVGDVTSGLLLVKLLQSASLRDALEH----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: 534.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516   1 MKNILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMLPSHLTEIVQGIADIDQLKRCDAVLS 80
Cdd:PRK05756    1 MKNILSIQSHVVYGHVGNSAAVFPMQRLGVNVWPLNTVQFSNHTGYGKWTGCVMPPSHLTEIVQGIADIGWLGECDAVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516  81 GYLGSAEQGEHILGIVRQVKAANPAAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLIELEILCEHPVNSV 160
Cdd:PRK05756   81 GYLGSAEQGEAILDAVRRVKAANPQALYFCDPVMGDPEKGCIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516 161 EEAVRASRELLAQGPEIVLVKHLARAGLSQDRFEMLLVTKDEAWHISRPLVDFGtRQPVGVGDVTSGLLLVKLLQSASLR 240
Cdd:PRK05756  161 EDAVAAARALIARGPKIVLVTSLARAGYPADRFEMLLVTADGAWHISRPLVDFM-RQPVGVGDLTSALFLARLLQGGSLE 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1737388516 241 DALEHVTAAVYEIMIATKTMQEYELQVVAAQDRIAKPEHYFSATQL 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 1.60e-169

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: 470.47  E-value: 1.60e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516   1 MKNILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMLPSHLTEIVQGIADIDQLKRCDAVLS 80
Cdd:TIGR00687   1 MKNVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLEAINKLNQCDAVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516  81 GYLGSAEQGEHILGIVRQVKAANPAAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLIELEILCEHPVNSV 160
Cdd:TIGR00687  81 GYLGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKGCYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516 161 EEAVRASRELLAQGPEIVLVKHLARAGLSQDR-FEMLLVTKDEAWHISRPLVDFgTRQPVGVGDVTSGLLLVKLLQSASL 239
Cdd:TIGR00687 161 EEALAAADALIAMGPDIVLVTHLIRAGSQRDRsFEGLVATQEGRWHISRPLAVF-DPPPVGTGDLIAALLLATLLHGNSL 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1737388516 240 RDALEHVTAAVYEIMIATKTMQEYELQVVAAQDRIAKPEHYFSATQL 286
Cdd:TIGR00687 240 KEALEKTVSAVYHVLRTTIQLGKYELQPVAAQLEIRMPQSKFDAEKV 286
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 1-275 1.56e-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: 1.56e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516   1 MKNILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMLPSHLTEIVQGIADIDQLKRCDAVLS 80
Cdd:COG2240     1 MKRVLSIQSHVVYGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWKELGVLLEFDAVLS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516  81 GYLGSAEQGEHILGIVRQVKAANPAAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLIELEILCEHPVNSV 160
Cdd:COG2240    81 GYLGSAEQGDIIADFVARVKAANPDALYLCDPVMGDNGKGYYVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516 161 EEAVRASRELLAQGPEIVLVKHLARAGLSQDRFEMLLVTKDEAWHISRPLVDFgtrQPVGVGDVTSGLLLVKLLQSASLR 240
Cdd:COG2240   161 EEALAAARALLALGPKIVVVTSVPLDDTPADKIGNLAVTADGAWLVETPLLPF---SPNGTGDLFAALLLAHLLRGKSLE 237

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1737388516 241 DALEHVTAAVYEIMIATKTMQEYELQVVAAQDRIA 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 ...
 3-257 1.09e-113

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


Pssm-ID: 238578 [Multi-domain]  Cd Length: 254  Bit Score: 328.00  E-value: 1.09e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516   3 NILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMLPSHLTEIVQGIADIDQLKRCDAVLSGY 82
Cdd:cd01173     1 RVLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLLLEYDAVLTGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516  83 LGSAEQGEHILGIVRQVKAANPAAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLIELEILCEHPVNSVEE 162
Cdd:cd01173    81 LGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGDNGKLYVVAEEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLED 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516 163 AVRASRELLAQGPEIVLVKHLARAGlsQDRFEMLLVTKDEAWHISRPLVDFGTrQPVGVGDVTSGLLLVKLLQSASLRDA 242
Cdd:cd01173   161 AKAAARALHAKGPKTVVVTSVELAD--DDRIEMLGSTATEAWLVQRPKIPFPA-YFNGTGDLFAALLLARLLKGKSLAEA 237

                         250
                  ....*....|....*
gi 1737388516 243 LEHVTAAVYEIMIAT 257
Cdd:cd01173   238 LEKALNFVHEVLEAT 252
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
 2-286 2.18e-52

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 172.96  E-value: 2.18e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516   2 KNILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMLPSHLTEIVQGIADIDQLKRCDAVLSG 81
Cdd:PTZ00344    5 KKVLSIQSHVTHGYVGNRAATFPLQLLGFDVDFVNTVQLSNHTGYPVIKGHRLDLNELITLMDGLRANNLLSDYTYVLTG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516  82 YLGSAEQGEHILGIVRQVKAANPAAKYFCDPVMGHPEKGCIVAPGVAEFhvRHALPASDIIAPNLIELEILCEHPVNSVE 161
Cdd:PTZ00344   85 YINSADILREVLATVKEIKELRPKLIFLCDPVMGDDGKLYVKEEVVDAY--RELIPYADVITPNQFEASLLSGVEVKDLS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516 162 EAVRASRELLAQGPEIVLVKHLARAGLSQD-RFEMLLVTKDEA----WHISRPLVDFgtrQPVGVGDVTSGLLLVkLLQS 236
Cdd:PTZ00344  163 DALEAIDWFHEQGIPVVVITSFREDEDPTHlRFLLSCRDKDTKnnkrFTGKVPYIEG---RYTGTGDLFAALLLA-FSHQ 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1737388516 237 ASLRDALEHVTAAVYEIMIATK--------TMQEYELQVVAAQDRIAKPEHYFSATQL 286
Cdd:PTZ00344  239 HPMDLAVGKAMGVLQDIIKATResggsgssSLMSRELRLIQSPRDLLNPETVFKVTPL 296
pdxK PRK08176
pyridoxine/pyridoxal/pyridoxamine kinase;
3-266 5.41e-42

pyridoxine/pyridoxal/pyridoxamine kinase;


Pssm-ID: 181269 [Multi-domain]  Cd Length: 281  Bit Score: 145.57  E-value: 5.41e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516   3 NILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMLPSHLTEIVQGIADIDQLKRCDAVLSGY 82
Cdd:PRK08176   17 DIVAVQSQVVYGSVGNSIAVPAIKANGLRVFAVPTVLLSNTPHYPTFYGGAIPDEWFSGYLRALQERDALRQLRAVTTGY 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516  83 LGSAEQGEHILGIVRQVKAANPAAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLIELEILCEHPVNSVEE 162
Cdd:PRK08176   97 MGSASQIKILAEWLTALRADHPDLLIMVDPVIGDIDSGIYVKPDLPEAYRQHLLPLAQGLTPNIFELEILTGKPCRTLDS 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516 163 AVRASRELLAQGPEIVLVKHlARAGLSQDRFEMLLVTKDEAWHISRPLVDfgtRQPVGVGDVTSGLLLVKLLQSASLRDA 242
Cdd:PRK08176  177 AIAAAKSLLSDTLKWVVITS-AAGNEENQEMQVVVVTADSVNVISHPRVD---TDLKGTGDLFCAELVSGLLKGKALTDA 252

                         250       260
                  ....*....|....*....|....
gi 1737388516 243 LEHVTAAVYEIMIATKTMQEYELQ 266
Cdd:PRK08176  253 AHRAGLRVLEVMRYTQQAGSDELI 276
PLN02978 PLN02978
pyridoxal kinase
 4-286 2.29e-41

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 144.88  E-value: 2.29e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516   4 ILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMLPSHLTEIVQGIADIDQLKRCDaVLSGYL 83
Cdd:PLN02978   17 VLSIQSHTVHGYVGNKSAVFPLQLLGFDVDPINSVQFSNHTGYPTFKGQVLDGEQLWALIEGLEANGLLFYTH-LLTGYI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516  84 GSAEQGEHILGIVRQVKAANPAAKYFCDPVMGHPEKgCIVAPGVAEFHVRHALPASDIIAPNLIELEILCEHPVNSVEEA 163
Cdd:PLN02978   96 GSVSFLRTVLRVVKKLRSVNPNLTYVCDPVLGDEGK-LYVPPELVPVYREKVVPLATMLTPNQFEAEQLTGIRIVTEEDA 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516 164 VRASRELLAQGPEIVLVKHLARAGlsqdrfEMLLV--------TKDEAWHISRPlvdfgtRQP---VGVGDVTSGLLLVk 232
Cdd:PLN02978  175 REACAILHAAGPSKVVITSIDIDG------KLLLVgshrkekgARPEQFKIVIP------KIPayfTGTGDLMAALLLG- 241

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1737388516 233 llQSA----SLRDALE----------HVTAAVYEIMIATKTMQEYELQVVAAQDRIAKPEHYFSATQL 286
Cdd:PLN02978  242 --WSHkypdNLDKAAElavsslqavlRRTLADYKRAGADPKSSSLELRLVQSQDDIRHPQVRFKAERY 307
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
133-249 1.95e-16

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


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 77.48  E-value: 1.95e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516 133 RHALPAS-DIIAPNLIELEILCEHPVNSVEEAVRASRELLAQGPEIVLVKhLARAGlsqdrfeMLLVTKDEAWHISRPLV 211
Cdd:COG1105   171 KAALEAGpDLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVS-LGADG-------ALLVTEDGVYRAKPPKV 242

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1737388516 212 DfgTRQPVGVGDVTSGLLLVKLLQSASLRDALEHVTAA 249
Cdd:COG1105   243 E--VVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAA 278
FruK_PfkB_like cd01164
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ...
 133-249 9.18e-16

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


Pssm-ID: 238570 [Multi-domain]  Cd Length: 289  Bit Score: 75.65  E-value: 9.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516 133 RHALPAS-DIIAPNLIELEILCEHPVNSVEEAVRASRELLAQGPEIVLVKhLARAGlsqdrfeMLLVTKDEAWHISRPLV 211
Cdd:cd01164   171 LAALAAKpFLIKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVS-LGADG-------ALLVTKDGVYRASPPKV 242

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1737388516 212 DfgTRQPVGVGDVTSGLLLVKLLQSASLRDALEHVTAA 249
Cdd:cd01164   243 K--VVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAA 278
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 63-250 2.22e-15

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


Pssm-ID: 430062 [Multi-domain]  Cd Length: 246  Bit Score: 73.67  E-value: 2.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516  63 VQGIADID------QLK------RCDAVLSGYLGSAEqgehilgIVRQV--KAANPAAKYFCDPVM----GHPekgcIVA 124
Cdd:pfam08543  37 VQGVHPLPpefvaaQLDavlediPVDAVKTGMLGSAE-------IIEAVaeKLDKYGVPVVLDPVMvaksGDS----LLD 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516 125 PGVAEFHVRHALPASDIIAPNLIELEILCEHPVNSVEEAVRASRELLAQGPEIVLVK--HLAragLSQDRFEMLLVTKDE 202
Cdd:pfam08543 106 DEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKggHLE---GEEAVVTDVLYDGGG 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1737388516 203 AWHISRPLVDfgTRQPVGVGDVTSGLLLVKLLQSASLRDALEH----VTAAV 250
Cdd:pfam08543 183 FYTLEAPRIP--TKNTHGTGCTLSAAIAANLAKGLSLPEAVREakeyVTEAI 232
PRK07105 PRK07105
pyridoxamine kinase; Validated
 1-257 8.21e-15

pyridoxamine kinase; Validated


Pssm-ID: 180840 [Multi-domain]  Cd Length: 284  Bit Score: 72.64  E-value: 8.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516   1 MKNILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHT----QYGKWTgcvmlpshLTEIVQGIadIDQLKR-- 74
Cdd:PRK07105    4 VKRVAAIHDLSGFGRVALTASIPIMSSMGLQVCPLPTALLSSHTggfqNPSIID--------LTDGMQAF--LTHWKSln 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516  75 --CDAVLSGYLGSAEQGEHILGIVRQVKAANPAAkyFCDPVMGhpEKGCiVAPGVAEFHV---RHALPASDIIAPNLIEL 149
Cdd:PRK07105   74 lkFDAIYSGYLGSPRQIQIVSDFIKYFKKKDLLV--VVDPVMG--DNGK-LYQGFDQEMVeemRKLIQKADVITPNLTEA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516 150 EILCEHPV----NSVEEAVRASRELLAQGPEIVLVkhlarAGLSQDRFEMLLV----TKDEAWHIsrplvdFGTRQPV-- 219
Cdd:PRK07105  149 CLLLDKPYleksYSEEEIKQLLRKLADLGPKIVII-----TSVPFEDGKIGVAyydrATDRFWKV------FCKYIPAhy 217

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1737388516 220 -GVGDVTSGLLLVKLLQSASLRDALEHVTAAVYEIMIAT 257
Cdd:PRK07105  218 pGTGDIFTSVITGSLLQGDSLPIALDRAVQFIEKGIRAT 256
HMPP_kinase cd01169
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ...
 74-256 2.86e-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: 2.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516  74 RCDAVLSGYLGSAEqgehILGIVRQVKAANPAAKYFCDPVM----GHPekgcIVAPGVAEFHVRHALPASDIIAPNLIEL 149
Cdd:cd01169    68 PVDAIKIGMLGSAE----IIEAVAEALKDYPDIPVVLDPVMvaksGDS----LLDDDAIEALRELLLPLATLITPNLPEA 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516 150 EILCEHPVNSVEEAVRASRELLAQGPEIVLVK--HLaRAGLSQDrfemLLVTKDEAWHISRPLVDfgTRQPVGVGDVTSG 227
Cdd:cd01169   140 ELLTGLEIATEEDMMKAAKALLALGAKAVLIKggHL-PGDEAVD----VLYDGGGFFEFESPRID--TKNTHGTGCTLSS 212

                         170       180
                  ....*....|....*....|....*....
gi 1737388516 228 LLLVKLLQSASLRDALEHVTAAVYEIMIA 256
Cdd:cd01169   213 AIAANLAKGLSLEEAVREAKEYVTQAIRN 241
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 132-249 3.17e-13

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 68.52  E-value: 3.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516 132 VRHALPASDIIAPNLIELEILCEHPVNSVEEAVRASRELLAQGPEIVLVKhLARAGlsqdrfeMLLVTKDEAWHISRP-- 209
Cdd:pfam00294 174 LLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVT-LGADG-------ALVVEGDGEVHVPAVpk 245

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1737388516 210 --LVDfgtrqPVGVGDVTSGLLLVKLLQSASLRDALEHVTAA 249
Cdd:pfam00294 246 vkVVD-----TTGAGDSFVGGFLAGLLAGKSLEEALRFANAA 282
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 63-249 5.11e-13

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: 67.37  E-value: 5.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516  63 VQGIADID------QLkrcDAVLS---------GYLGSAEqgehILGIVRQVKAANPAAKYFCDPVM----GHPekgcIV 123
Cdd:COG0351    43 VTGVHPVPpefvaaQL---RAVLEdipvdaikiGMLGSAE----IIEAVAEILADYPLVPVVLDPVMvaksGDR----LL 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516 124 APGVAEFHVRHALPASDIIAPNLIELEILCEHPVNSVEEAVRASRELLAQGPEIVLVK--HLArAGLSQDrfemLLVTKD 201
Cdd:COG0351   112 DEDAVEALRELLLPLATVVTPNLPEAEALLGIEITTLDDMREAAKALLELGAKAVLVKggHLP-GDEAVD----VLYDGD 186

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1737388516 202 EAWHISRPLVDfgTRQPVGVGDVTSGLLLVKLLQSASLRDALEH----VTAA 249
Cdd:COG0351   187 GVREFSAPRID--TGNTHGTGCTLSSAIAALLAKGLDLEEAVREakeyVTQA 236
1-PFK TIGR03168
hexose kinase, 1-phosphofructokinase family; This family consists largely of ...
 140-249 5.16e-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: 67.99  E-value: 5.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516 140 DIIAPNLIELEILCEHPVNSVEEAVRASRELLAQGPEIVLVKhLARAGlsqdrfeMLLVTKDEAWHISRPLVDFGTrqPV 219
Cdd:TIGR03168 178 FLIKPNHEELEELFGRELKTLEEIIEAARELLDRGAENVLVS-LGADG-------ALLVTKEGALKATPPKVEVVN--TV 247

                          90       100       110
                  ....*....|....*....|....*....|
gi 1737388516 220 GVGDVTSGLLLVKLLQSASLRDALEHVTAA 249
Cdd:TIGR03168 248 GAGDSMVAGFLAGLARGLSLEEALRFAVAA 277
PRK14713 PRK14713
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
76-261 7.91e-11

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 237797 [Multi-domain]  Cd Length: 530  Bit Score: 62.11  E-value: 7.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516  76 DAVLSGYLGSAEqgehILGIVRQVKAANPAAKYFCDPVMGHPEKGCIVAPGvAEFHVRHALPASDIIAPNLIELEILCEH 155
Cdd:PRK14713  100 DAVKIGMLGDAE----VIDAVRTWLAEHRPPVVVLDPVMVATSGDRLLEED-AEAALRELVPRADLITPNLPELAVLLGE 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516 156 PVNSV-EEAVRASRELLAQGPEIVLVK--HLAraglSQDRFEMLLVTKDEAWHISRPLVDfgTRQPVGVGDVTSGLLLVK 232
Cdd:PRK14713  175 PPATTwEEALAQARRLAAETGTTVLVKggHLD----GQRAPDALVGPDGAVTEVPGPRVD--TRNTHGTGCSLSSALATR 248

                         170       180
                  ....*....|....*....|....*....
gi 1737388516 233 LLQSASLRDALEHVTAAVYEIMIATKTMQ 261
Cdd:PRK14713  249 LGRGGDWAAALRWATAWLHGAIAAGAALQ 277
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 76-250 6.79e-10

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 58.21  E-value: 6.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516  76 DAVLSGYLGSAEqgehILGIVRQVKAANPAAKYFCDPVM----GHPekgcIVAPGVAEFHVRHALPASDIIAPNLIELEI 151
Cdd:PRK06427   75 DAVKIGMLASAE----IIETVAEALKRYPIPPVVLDPVMiaksGDP----LLADDAVAALRERLLPLATLITPNLPEAEA 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516 152 LCEHPVNSVEEAVR-ASRELLAQGPEIVLVK--HLARAGLSQDRfemlLVTKDEAWHISRPLVDfgTRQPVGVGD----- 223
Cdd:PRK06427  147 LTGLPIADTEDEMKaAARALHALGCKAVLIKggHLLDGEESVDW----LFDGEGEERFSAPRIP--TKNTHGTGCtlsaa 220

                         170       180
                  ....*....|....*....|....*..
gi 1737388516 224 VTSGLLLVKLLQSAsLRDALEHVTAAV 250
Cdd:PRK06427  221 IAAELAKGASLLDA-VQTAKDYVTRAI 246
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 68-249 1.35e-09

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: 57.59  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516  68 DIDQLKRCDAV-LSGYLGSAEQG-EHILGIVRQVKAANpaAKYFCDPVMGHpekgCIVAPGVAEFhvRHALPASDIIAPN 145
Cdd:COG0524   121 DEALLAGADILhLGGITLASEPPrEALLAALEAARAAG--VPVSLDPNYRP----ALWEPARELL--RELLALVDILFPN 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516 146 LIELEILCEHpvnsvEEAVRASRELLAQGPEIVLVKhLARAGLsqdrfemLLVTKDEAWHISRP---LVDfgtrqPVGVG 222
Cdd:COG0524   193 EEEAELLTGE-----TDPEEAAAALLARGVKLVVVT-LGAEGA-------LLYTGGEVVHVPAFpveVVD-----TTGAG 254

                         170       180
                  ....*....|....*....|....*..
gi 1737388516 223 DVTSGLLLVKLLQSASLRDALEHVTAA 249
Cdd:COG0524   255 DAFAAGFLAGLLEGLDLEEALRFANAA 281
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 77-234 8.82e-07

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: 48.25  E-value: 8.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516  77 AVLSGYLGSAEQGEHILGIVRQVKAAnpaakYFCDPVMghpekgcivaPGVAEFH--VRHALPASDIIAPNLIELEILCE 154
Cdd:cd00287    61 VVISGLSPAPEAVLDALEEARRRGVP-----VVLDPGP----------RAVRLDGeeLEKLLPGVDILTPNEEEAEALTG 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516 155 HPVNSVEEAVRASRELLAQGPEIVLVKHLARAGlsqdrfemLLVTKDEaWHISRPLVDFGTRQPVGVGDVTSGLLLVKLL 234
Cdd:cd00287   126 RRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGA--------IVATRGG-TEVHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
PRK09517 PRK09517
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ...
 76-248 1.06e-06

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


Pssm-ID: 169939 [Multi-domain]  Cd Length: 755  Bit Score: 49.59  E-value: 1.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516  76 DAVLSGYLGSAEqgehilgIVRQVKA---ANPAAKYFCDPVMGHPEKGCIVAPGVAEfHVRHALPASDIIAPNLIELEIL 152
Cdd:PRK09517  312 DAVKLGMLGSAD-------TVDLVASwlgSHEHGPVVLDPVMVATSGDRLLDADATE-ALRRLAVHVDVVTPNIPELAVL 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516 153 C-EHPVNSVEEAVRASRELLAQGPEIVLVKHlarAGLSQDRFEMLLVTKDEAWH-ISRPLVDfgTRQPVGVGDVTSGLLL 230
Cdd:PRK09517  384 CgEAPAITMDEAIAQARGFARTHGTIVIVKG---GHLTGDLADNAVVRPDGSVHqVENPRVN--TTNSHGTGCSLSAALA 458

                         170
                  ....*....|....*...
gi 1737388516 231 VKLLQSASLRDALEHVTA 248
Cdd:PRK09517  459 TLIAAGESVEKALEWATR 476
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
 76-181 9.75e-04

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 40.52  E-value: 9.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516  76 DAVLSGYLGSAEqgehILGIVRQVKAANPAAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLIELE-ILCE 154
Cdd:PLN02898   80 DVVKTGMLPSAE----IVKVLCQALKEFPVKALVVDPVMVSTSGDVLAGPSILSALREELLPLATIVTPNVKEASaLLGG 155

                          90       100
                  ....*....|....*....|....*..
gi 1737388516 155 HPVNSVEEAVRASRELLAQGPEIVLVK 181
Cdd:PLN02898  156 DPLETVADMRSAAKELHKLGPRYVLVK 182
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
 117-243 1.27e-03

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


Pssm-ID: 238916 [Multi-domain]  Cd Length: 288  Bit Score: 39.60  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516 117 PEKGCIVApgvaefHVRHALPASDIIAPNLIELEILCEHPVNSVEEAVRASRELLAQGPEIVLVKHLARAGLSQDRFEML 196
Cdd:cd01941   161 PTSAPKLK------KLFYLLHAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSREGGV 234

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1737388516 197 lvtkdEAWHISRPLVDfgTRQPV-GVGDVTSGLLLVKLLQSASLRDAL 243
Cdd:cd01941   235 -----ETKLFPAPQPE--TVVNVtGAGDAFVAGLVAGLLEGMSLDDSL 275
fruK PRK09513
1-phosphofructokinase; Provisional
 141-248 1.66e-03

1-phosphofructokinase; Provisional


Pssm-ID: 181923 [Multi-domain]  Cd Length: 312  Bit Score: 39.29  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516 141 IIAPNLIELEILCEHPVNSVEEAVRASRELLAQGPEIVLVKHLARAGlsqdrfemLLVTKDEAWHISRPLVDFGTrqPVG 220
Cdd:PRK09513  183 LVKPNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGA--------LWVNASGEWIAKPPACDVVS--TVG 252

                          90       100
                  ....*....|....*....|....*...
gi 1737388516 221 VGDVTSGLLLVKLLQSASLRDALEHVTA 248
Cdd:PRK09513  253 AGDSMVGGLIYGLLMRESSEHTLRLATA 280
PRK11142 PRK11142
ribokinase; Provisional
 140-250 3.28e-03

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 38.31  E-value: 3.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1737388516 140 DIIAPNLIELEILCEHPVNSVEEAVRASRELLAQGPEIVLVKHLAR-AGLSQDRFEMLLVT-KDEAwhisrplVDfgtrq 217
Cdd:PRK11142  180 DIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRgVWLSENGEGQRVPGfRVQA-------VD----- 247

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1737388516 218 PVGVGDVTSGLLLVKLLQSASLRDALE--HVTAAV 250
Cdd:PRK11142  248 TIAAGDTFNGALVTALLEGKPLPEAIRfaHAAAAI 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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