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Conserved domains on  [gi|1061899879|ref|NP_001317959|]
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pyridoxal kinase isoform 2 [Homo sapiens]

Protein Classification

carbohydrate kinase family protein( domain architecture ID 399)

carbohydrate kinase family protein that accepts a wide variety of substrates, including carbohydrates and aromatic small molecules, all being phosphorylated at a hydroxyl group; belongs to the ribokinase/pfkB sugar kinase superfamily

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ribokinase_pfkB_like super family cl00192
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 8-264 5.67e-115

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).


The actual alignment was detected with superfamily member TIGR00687:

Pssm-ID: 469648 [Multi-domain]  Cd Length: 287  Bit Score: 331.79  E-value: 5.67e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879   8 GYAHWKGQVLNSDELQELYEGL-RLNNMNKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDKWDGegsM 86
Cdd:TIGR00687  45 GYGKWTGQVLPPDELHELVEGLeAINKLNQCDAVLSGYLGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKG---C 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879  87 YVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITssdlpspqgsnYLIVLGSQR 166
Cdd:TIGR00687 122 YVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTEEEALAAADALIAMGPDIVLVT-----------HLIRAGSQR 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879 167 RRNPAGSVVMERIRMDIRKVDAVF----VGTGDLFAAMLLAwTHKHPNNLKVACEKTVSTLHHVLQRTIQCAKAQagegV 242
Cdd:TIGR00687 191 DRSFEGLVATQEGRWHISRPLAVFdpppVGTGDLIAALLLA-TLLHGNSLKEALEKTVSAVYHVLRTTIQLGKYE----L 265

                         250       260
                  ....*....|....*....|..
gi 1061899879 243 RPSPMQLELRMVQSKRDIEDPE 264
Cdd:TIGR00687 266 QPVAAQLEIRMPQSKFDAEKVE 287
 
Name Accession Description Interval E-value
pyridox_kin TIGR00687
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ...
 8-264 5.67e-115

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: 331.79  E-value: 5.67e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879   8 GYAHWKGQVLNSDELQELYEGL-RLNNMNKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDKWDGegsM 86
Cdd:TIGR00687  45 GYGKWTGQVLPPDELHELVEGLeAINKLNQCDAVLSGYLGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKG---C 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879  87 YVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITssdlpspqgsnYLIVLGSQR 166
Cdd:TIGR00687 122 YVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTEEEALAAADALIAMGPDIVLVT-----------HLIRAGSQR 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879 167 RRNPAGSVVMERIRMDIRKVDAVF----VGTGDLFAAMLLAwTHKHPNNLKVACEKTVSTLHHVLQRTIQCAKAQagegV 242
Cdd:TIGR00687 191 DRSFEGLVATQEGRWHISRPLAVFdpppVGTGDLIAALLLA-TLLHGNSLKEALEKTVSAVYHVLRTTIQLGKYE----L 265

                         250       260
                  ....*....|....*....|..
gi 1061899879 243 RPSPMQLELRMVQSKRDIEDPE 264
Cdd:TIGR00687 266 QPVAAQLEIRMPQSKFDAEKVE 287
PLN02978 PLN02978
pyridoxal kinase
 4-270 1.81e-102

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 300.89  E-value: 1.81e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879   4 SRPPGYAHWKGQVLNSDELQELYEGLRLNNMNKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwdgE 83
Cdd:PLN02978   54 SNHTGYPTFKGQVLDGEQLWALIEGLEANGLLFYTHLLTGYIGSVSFLRTVLRVVKKLRSVNPNLTYVCDPVLGD----E 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879  84 GSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITSSDLPspqgsNYLIVLG 163
Cdd:PLN02978  130 GKLYVPPELVPVYREKVVPLATMLTPNQFEAEQLTGIRIVTEEDAREACAILHAAGPSKVVITSIDID-----GKLLLVG 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879 164 SQRRRNPAGSvvmERIRMDIRKVDAVFVGTGDLFAAMLLAWTHKHPNNLKVACEKTVSTLHHVLQRTIQCAKAqagEGVR 243
Cdd:PLN02978  205 SHRKEKGARP---EQFKIVIPKIPAYFTGTGDLMAALLLGWSHKYPDNLDKAAELAVSSLQAVLRRTLADYKR---AGAD 278

                         250       260
                  ....*....|....*....|....*..
gi 1061899879 244 PSPMQLELRMVQSKRDIEDPEIVVQAT 270
Cdd:PLN02978  279 PKSSSLELRLVQSQDDIRHPQVRFKAE 305
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 7-232 6.31e-84

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: 251.74  E-value: 6.31e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879   7 PGYAHWKGQVLNSDELQELYEGLRLNNM-NKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwdgEGS 85
Cdd:cd01173    42 TGYGTWTGFVLSAEELEDLLEGLEALGLlLEYDAVLTGYLGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGD----NGK 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879  86 MYV-PEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITSSDLPSPqgsnylivlgs 164
Cdd:cd01173   118 LYVvAEEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVTSVELADD----------- 186

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879 165 qRRRNPAGSVVMERIRMDIRKVD--AVFVGTGDLFAAMLLAWTHKHPnNLKVACEKTVSTLHHVLQRTIQ 232
Cdd:cd01173   187 -DRIEMLGSTATEAWLVQRPKIPfpAYFNGTGDLFAALLLARLLKGK-SLAEALEKALNFVHEVLEATYE 254
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 7-232 2.04e-57

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: 184.58  E-value: 2.04e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879   7 PGYAHWKGQVLNSDELQELYEGL-RLNNMNKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwDGEGs 85
Cdd:COG2240    44 TGYGTFTGRDLPTDDIADILDGWkELGVLLEFDAVLSGYLGSAEQGDIIADFVARVKAANPDALYLCDPVMGD--NGKG- 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879  86 MYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITS---SDLPSPQGSNYLIvl 162
Cdd:COG2240   121 YYVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETLEEALAAARALLALGPKIVVVTSvplDDTPADKIGNLAV-- 198

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1061899879 163 gsqrrrNPAGSVVMERirmdiRKVDAVFVGTGDLFAAMLLA-WTHKHPnnLKVACEKTVSTLHHVLQRTIQ 232
Cdd:COG2240   199 ------TADGAWLVET-----PLLPFSPNGTGDLFAALLLAhLLRGKS--LEEALERAAAFVYEVLERTAA 256
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 57-155 4.59e-17

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: 78.29  E-value: 4.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879  57 IVQELKQQNPRLVyvCDPVLGDKwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLH 136
Cdd:pfam08543  78 VAEKLDKYGVPVV--LDPVMVAK---SGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLL 152

                          90
                  ....*....|....*....
gi 1061899879 137 SMGPDTVVITSSDLPSPQG 155
Cdd:pfam08543 153 ALGAKAVLIKGGHLEGEEA 171
 
Name Accession Description Interval E-value
pyridox_kin TIGR00687
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ...
 8-264 5.67e-115

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: 331.79  E-value: 5.67e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879   8 GYAHWKGQVLNSDELQELYEGL-RLNNMNKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDKWDGegsM 86
Cdd:TIGR00687  45 GYGKWTGQVLPPDELHELVEGLeAINKLNQCDAVLSGYLGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKG---C 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879  87 YVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITssdlpspqgsnYLIVLGSQR 166
Cdd:TIGR00687 122 YVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTEEEALAAADALIAMGPDIVLVT-----------HLIRAGSQR 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879 167 RRNPAGSVVMERIRMDIRKVDAVF----VGTGDLFAAMLLAwTHKHPNNLKVACEKTVSTLHHVLQRTIQCAKAQagegV 242
Cdd:TIGR00687 191 DRSFEGLVATQEGRWHISRPLAVFdpppVGTGDLIAALLLA-TLLHGNSLKEALEKTVSAVYHVLRTTIQLGKYE----L 265

                         250       260
                  ....*....|....*....|..
gi 1061899879 243 RPSPMQLELRMVQSKRDIEDPE 264
Cdd:TIGR00687 266 QPVAAQLEIRMPQSKFDAEKVE 287
PLN02978 PLN02978
pyridoxal kinase
 4-270 1.81e-102

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 300.89  E-value: 1.81e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879   4 SRPPGYAHWKGQVLNSDELQELYEGLRLNNMNKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwdgE 83
Cdd:PLN02978   54 SNHTGYPTFKGQVLDGEQLWALIEGLEANGLLFYTHLLTGYIGSVSFLRTVLRVVKKLRSVNPNLTYVCDPVLGD----E 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879  84 GSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITSSDLPspqgsNYLIVLG 163
Cdd:PLN02978  130 GKLYVPPELVPVYREKVVPLATMLTPNQFEAEQLTGIRIVTEEDAREACAILHAAGPSKVVITSIDID-----GKLLLVG 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879 164 SQRRRNPAGSvvmERIRMDIRKVDAVFVGTGDLFAAMLLAWTHKHPNNLKVACEKTVSTLHHVLQRTIQCAKAqagEGVR 243
Cdd:PLN02978  205 SHRKEKGARP---EQFKIVIPKIPAYFTGTGDLMAALLLGWSHKYPDNLDKAAELAVSSLQAVLRRTLADYKR---AGAD 278

                         250       260
                  ....*....|....*....|....*..
gi 1061899879 244 PSPMQLELRMVQSKRDIEDPEIVVQAT 270
Cdd:PLN02978  279 PKSSSLELRLVQSQDDIRHPQVRFKAE 305
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
 8-272 1.58e-87

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 262.32  E-value: 1.58e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879   8 GYAHWKGQVLNSDELQELYEGLRLNNM-NKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwdgEGSM 86
Cdd:PTZ00344   48 GYPVIKGHRLDLNELITLMDGLRANNLlSDYTYVLTGYINSADILREVLATVKEIKELRPKLIFLCDPVMGD----DGKL 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879  87 YVPEDLLPVYKEkVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITSSDLpsPQGSNYLIVLGSQR 166
Cdd:PTZ00344  124 YVKEEVVDAYRE-LIPYADVITPNQFEASLLSGVEVKDLSDALEAIDWFHEQGIPVVVITSFRE--DEDPTHLRFLLSCR 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879 167 RRNPAGSvvmERIRMDIRKVDAVFVGTGDLFAAMLLAWTHKHPnnLKVACEKTVSTLHHVLQRTIqcakaQAGEGVRPSP 246
Cdd:PTZ00344  201 DKDTKNN---KRFTGKVPYIEGRYTGTGDLFAALLLAFSHQHP--MDLAVGKAMGVLQDIIKATR-----ESGGSGSSSL 270

                         250       260
                  ....*....|....*....|....*.
gi 1061899879 247 MQLELRMVQSKRDIEDPEIVVQATVL 272
Cdd:PTZ00344  271 MSRELRLIQSPRDLLNPETVFKVTPL 296
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 7-232 6.31e-84

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: 251.74  E-value: 6.31e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879   7 PGYAHWKGQVLNSDELQELYEGLRLNNM-NKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwdgEGS 85
Cdd:cd01173    42 TGYGTWTGFVLSAEELEDLLEGLEALGLlLEYDAVLTGYLGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGD----NGK 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879  86 MYV-PEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITSSDLPSPqgsnylivlgs 164
Cdd:cd01173   118 LYVvAEEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVTSVELADD----------- 186

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879 165 qRRRNPAGSVVMERIRMDIRKVD--AVFVGTGDLFAAMLLAWTHKHPnNLKVACEKTVSTLHHVLQRTIQ 232
Cdd:cd01173   187 -DRIEMLGSTATEAWLVQRPKIPfpAYFNGTGDLFAALLLARLLKGK-SLAEALEKALNFVHEVLEATYE 254
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 7-232 2.04e-57

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: 184.58  E-value: 2.04e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879   7 PGYAHWKGQVLNSDELQELYEGL-RLNNMNKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwDGEGs 85
Cdd:COG2240    44 TGYGTFTGRDLPTDDIADILDGWkELGVLLEFDAVLSGYLGSAEQGDIIADFVARVKAANPDALYLCDPVMGD--NGKG- 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879  86 MYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITS---SDLPSPQGSNYLIvl 162
Cdd:COG2240   121 YYVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETLEEALAAARALLALGPKIVVVTSvplDDTPADKIGNLAV-- 198

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1061899879 163 gsqrrrNPAGSVVMERirmdiRKVDAVFVGTGDLFAAMLLA-WTHKHPnnLKVACEKTVSTLHHVLQRTIQ 232
Cdd:COG2240   199 ------TADGAWLVET-----PLLPFSPNGTGDLFAALLLAhLLRGKS--LEEALERAAAFVYEVLERTAA 256
PRK05756 PRK05756
pyridoxal kinase PdxY;
7-272 9.81e-47

pyridoxal kinase PdxY;


Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 157.72  E-value: 9.81e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879   7 PGYAHWKGQVLNSDELQELYEGL-RLNNMNKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDKwdgEGS 85
Cdd:PRK05756   44 TGYGKWTGCVMPPSHLTEIVQGIaDIGWLGECDAVLSGYLGSAEQGEAILDAVRRVKAANPQALYFCDPVMGDP---EKG 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879  86 MYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITSSDLP-SPQGSNYLIVLgs 164
Cdd:PRK05756  121 CIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETLEDAVAAARALIARGPKIVLVTSLARAgYPADRFEMLLV-- 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879 165 qrrrNPAGSVVMERIRMDIRKVDavfVGTGDLFAAMLLAWtHKHPNNLKVACEKTVSTLHHVLQRTIQCakaqageGVRp 244
Cdd:PRK05756  199 ----TADGAWHISRPLVDFMRQP---VGVGDLTSALFLAR-LLQGGSLEEALEHTTAAVYEVMARTKER-------GSY- 262

                         250       260
                  ....*....|....*....|....*...
gi 1061899879 245 spmqlELRMVQSKRDIEDPEIVVQATVL 272
Cdd:PRK05756  263 -----ELQLVAAQDSIATPRAMFQARRL 285
pdxK PRK08176
pyridoxine/pyridoxal/pyridoxamine kinase;
40-233 8.44e-24

pyridoxine/pyridoxal/pyridoxamine kinase;


Pssm-ID: 181269 [Multi-domain]  Cd Length: 281  Bit Score: 97.03  E-value: 8.44e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879  40 VLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDKWDGegsMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSG 119
Cdd:PRK08176   92 VTTGYMGSASQIKILAEWLTALRADHPDLLIMVDPVIGDIDSG---IYVKPDLPEAYRQHLLPLAQGLTPNIFELEILTG 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879 120 RKIHSQEEALRVMDMLHSMGPDTVVITSSDLPSPQGS-NYLIVLGSQRrrnpagsVVMERIRmdirkVDAVFVGTGDLFA 198
Cdd:PRK08176  169 KPCRTLDSAIAAAKSLLSDTLKWVVITSAAGNEENQEmQVVVVTADSV-------NVISHPR-----VDTDLKGTGDLFC 236

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1061899879 199 AMLLA-WTHKHPnnLKVACEKTVSTLHHVLQRTIQC 233
Cdd:PRK08176  237 AELVSgLLKGKA--LTDAAHRAGLRVLEVMRYTQQA 270
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 37-204 7.66e-20

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: 84.84  E-value: 7.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879  37 YDYVLTGYTRDKsfLAMVVDIVQELKQQNPRlvYVCDPVLGDK-WDGEGsmyvpedllpvyKEKVVPLADIITPNQFEAE 115
Cdd:cd00287    58 ADAVVISGLSPA--PEAVLDALEEARRRGVP--VVLDPGPRAVrLDGEE------------LEKLLPGVDILTPNEEEAE 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879 116 LLSGRKIHSQEEALRVMDMLHSMGPDTVVITssdlpspQGSNYLIVLGSQRRRNPAGSVvmerirmdirKVDAV-FVGTG 194
Cdd:cd00287   122 ALTGRRDLEVKEAAEAAALLLSKGPKVVIVT-------LGEKGAIVATRGGTEVHVPAF----------PVKVVdTTGAG 184

                         170
                  ....*....|
gi 1061899879 195 DLFAAMLLAW 204
Cdd:cd00287   185 DAFLAALAAG 194
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 52-199 3.76e-19

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: 83.93  E-value: 3.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879  52 AMVVDIVQELKQQNprlvYVCDPVLGDKWDGEGSmyvPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRV 131
Cdd:COG0351    82 EAVAEILADYPLVP----VVLDPVMVAKSGDRLL---DEDAVEALRELLLPLATVVTPNLPEAEALLGIEITTLDDMREA 154

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1061899879 132 MDMLHSMGPDTVVITSSDLPSPQGSNYLiVLGSQRRRnpagsVVMERIRmdirkvDAVFVGTGDLFAA 199
Cdd:COG0351   155 AKALLELGAKAVLVKGGHLPGDEAVDVL-YDGDGVRE-----FSAPRID------TGNTHGTGCTLSS 210
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 57-155 4.59e-17

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: 78.29  E-value: 4.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879  57 IVQELKQQNPRLVyvCDPVLGDKwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLH 136
Cdd:pfam08543  78 VAEKLDKYGVPVV--LDPVMVAK---SGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLL 152

                          90
                  ....*....|....*....
gi 1061899879 137 SMGPDTVVITSSDLPSPQG 155
Cdd:pfam08543 153 ALGAKAVLIKGGHLEGEEA 171
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 54-203 7.30e-14

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 69.38  E-value: 7.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879  54 VVDIVQELKQQNPRLVYVCDPVL----GDkwdgegsmyvP---EDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQE 126
Cdd:PRK06427   87 IIETVAEALKRYPIPPVVLDPVMiaksGD----------PllaDDAVAALRERLLPLATLITPNLPEAEALTGLPIADTE 156

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1061899879 127 EALRVM-DMLHSMGPDTVVITSS-DLPSPQGSNYLIvlgsqrrrNPAGSVVMERIRMDIRKVDavfvGTGDLFAAMLLA 203
Cdd:PRK06427  157 DEMKAAaRALHALGCKAVLIKGGhLLDGEESVDWLF--------DGEGEERFSAPRIPTKNTH----GTGCTLSAAIAA 223
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 55-204 3.60e-11

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 61.98  E-value: 3.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879  55 VDIVQELKQQNPRLVYVCDPVLGDKWDgegsmyvpedLLPVYKEkVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDM 134
Cdd:pfam00294 143 EATLEELIEAAKNGGTFDPNLLDPLGA----------AREALLE-LLPLADLLKPNEEELEALTGAKLDDIEEALAALHK 211

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1061899879 135 LHSMGPDTVVITSsdlpSPQGSnyLIVLGSQRRRNPAgsvvmerirmdIRKVDAV-FVGTGDLFAAMLLAW 204
Cdd:pfam00294 212 LLAKGIKTVIVTL----GADGA--LVVEGDGEVHVPA-----------VPKVKVVdTTGAGDSFVGGFLAG 265
PRK07105 PRK07105
pyridoxamine kinase; Validated
 36-230 6.27e-11

pyridoxamine kinase; Validated


Pssm-ID: 180840 [Multi-domain]  Cd Length: 284  Bit Score: 61.47  E-value: 6.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879  36 KYDYVLTGY---TRDksflamvVDIVQELKQ--QNPRLVYVCDPVLGDKwdgeGSMYVP--EDLLPVYKeKVVPLADIIT 108
Cdd:PRK07105   75 KFDAIYSGYlgsPRQ-------IQIVSDFIKyfKKKDLLVVVDPVMGDN----GKLYQGfdQEMVEEMR-KLIQKADVIT 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879 109 PNQFEAELLSG---RKIHSQEEalRVMDMLH---SMGPDTVVITSSdlpsPQGSNYLIVLGSQRRRNpagsvvmERIRMD 182
Cdd:PRK07105  143 PNLTEACLLLDkpyLEKSYSEE--EIKQLLRklaDLGPKIVIITSV----PFEDGKIGVAYYDRATD-------RFWKVF 209

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1061899879 183 IRKVDAVFVGTGDLFAAMLLAWTHkHPNNLKVACEKTVSTLHHVLQRT 230
Cdd:PRK07105  210 CKYIPAHYPGTGDIFTSVITGSLL-QGDSLPIALDRAVQFIEKGIRAT 256
PRK11142 PRK11142
ribokinase; Provisional
 103-146 1.16e-10

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 60.65  E-value: 1.16e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1061899879 103 LADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVIT 146
Cdd:PRK11142  178 LVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLIT 221
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 98-203 1.49e-10

Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This reaction is the first step in the ribose metabolism. It traps ribose within the cell after uptake and also prepares the sugar for use in the synthesis of nucleotides and histidine, and for entry into the pentose phosphate pathway. Ribokinase is dimeric in solution.


Pssm-ID: 238579 [Multi-domain]  Cd Length: 292  Bit Score: 60.26  E-value: 1.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879  98 EKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITssdlpspqgsnylivLGSQrrrnpaGSVVM- 176
Cdd:cd01174   170 AELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVT---------------LGAK------GALLAs 228

                          90       100       110
                  ....*....|....*....|....*....|
gi 1061899879 177 --ERIRMDIRKVDAV-FVGTGDLFAAMLLA 203
Cdd:cd01174   229 ggEVEHVPAFKVKAVdTTGAGDTFIGALAA 258
PRK08573 PRK08573
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
71-166 2.57e-09

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 236297 [Multi-domain]  Cd Length: 448  Bit Score: 57.43  E-value: 2.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879  71 VCDPVLGDKwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLH-SMGPDTVVITSSD 149
Cdd:PRK08573  101 VVDPVMIAK---SGAPLLREDAVDALIKRLLPLATVVTPNRPEAEKLTGMKIRSVEDARKAAKYIVeELGAEAVVVKGGH 177

                          90
                  ....*....|....*..
gi 1061899879 150 LPSPQGSNYLIVLGSQR 166
Cdd:PRK08573  178 LEGEEAVDVLYHNGTFR 194
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 40-203 7.80e-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: 55.28  E-value: 7.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879  40 VLTGYT-RDKSFLAMVVDIVQELKQQNPRLVYvcDPVLGDKwdgegsmyVPEDLLPVYKEkVVPLADIITPNQFEAELLS 118
Cdd:COG0524   132 HLGGITlASEPPREALLAALEAARAAGVPVSL--DPNYRPA--------LWEPARELLRE-LLALVDILFPNEEEAELLT 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879 119 GrkIHSQEEALRVmdmLHSMGPDTVVITssdlpspqgsnylivLGSQrrrnpaGSVVM---ERIRMDIRKVDAVF-VGTG 194
Cdd:COG0524   201 G--ETDPEEAAAA---LLARGVKLVVVT---------------LGAE------GALLYtggEVVHVPAFPVEVVDtTGAG 254


                  ....*....
gi 1061899879 195 DLFAAMLLA 203
Cdd:COG0524   255 DAFAAGFLA 263
PRK12616 PRK12616
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
11-146 8.01e-08

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183624  Cd Length: 270  Bit Score: 51.97  E-value: 8.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879  11 HWKGQVLNSD------ELQELYEGLRLNNMNkydyvlTGYTRDKSFLAMVVDIVQELKQQNprlvYVCDPVLGDKwdGEG 84
Cdd:PRK12616   49 SWDHQVFPIDtdtiraQLSTIVDGIGVDAMK------TGMLPTVDIIELAADTIKEKQLKN----VVIDPVMVCK--GAN 116

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1061899879  85 SMYVPEDLlPVYKEKVVPLADIITPNQFEAELLSGR-KIHSQEEALRVMDMLHSMGPDTVVIT 146
Cdd:PRK12616  117 EVLYPEHA-EALREQLAPLATVITPNLFEAGQLSGMgEIKTVEQMKEAAKKIHELGAQYVVIT 178
PRK12413 PRK12413
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
99-145 8.47e-08

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183513 [Multi-domain]  Cd Length: 253  Bit Score: 51.99  E-value: 8.47e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1061899879  99 KVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVI 145
Cdd:PRK12413  125 QFFPYVTVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAVVI 171
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
 38-152 2.76e-07

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 51.31  E-value: 2.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879  38 DYVLTGYTRDKSFLAMVVDIVQELKQQNprlvYVCDPVLGDKwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAE-L 116
Cdd:PLN02898   80 DVVKTGMLPSAEIVKVLCQALKEFPVKA----LVVDPVMVST---SGDVLAGPSILSALREELLPLATIVTPNVKEASaL 152

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1061899879 117 LSGRKIHSqeealrVMDM------LHSMGPDTVVITSSDLPS 152
Cdd:PLN02898  153 LGGDPLET------VADMrsaakeLHKLGPRYVLVKGGHLPD 188
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
13-209 1.51e-06

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


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 48.59  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879  13 KGQVLNSDELQELYEGLRlNNMNKYDY-VLTGytrdkSFLAMV-----VDIVQELKQQNPRLVyvcdpvlgdkWDGEGsm 86
Cdd:COG1105   106 PGPEISEEELEALLERLE-ELLKEGDWvVLSG-----SLPPGVppdfyAELIRLARARGAKVV----------LDTSG-- 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879  87 yvpEDLLPVYKEKVvplaDIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITssdlpspqgsnylivLGSQr 166
Cdd:COG1105   168 ---EALKAALEAGP----DLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVS---------------LGAD- 224

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1061899879 167 rrnpaGSVVM---ERIRMDIRKVDAVF-VGTGD-LFAAMLLAWTHKHP 209
Cdd:COG1105   225 -----GALLVtedGVYRAKPPKVEVVStVGAGDsMVAGFLAGLARGLD 267
PRK12412 PRK12412
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
38-145 3.03e-06

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183512 [Multi-domain]  Cd Length: 268  Bit Score: 47.27  E-value: 3.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879  38 DYVLTGYTRDKSFLAMVVDIVQELKQQNprlvYVCDPVLGDKwdGEGSMYVPEDLLpVYKEKVVPLADIITPNQFEAELL 117
Cdd:PRK12412   74 DALKTGMLGSVEIIEMVAETIEKHNFKN----VVVDPVMVCK--GADEALHPETND-CLRDVLVPKALVVTPNLFEAYQL 146

                          90       100
                  ....*....|....*....|....*...
gi 1061899879 118 SGRKIHSQEEALRVMDMLHSMGPDTVVI 145
Cdd:PRK12412  147 SGVKINSLEDMKEAAKKIHALGAKYVLI 174
PTZ00347 PTZ00347
phosphomethylpyrimidine kinase; Provisional
 57-241 6.68e-06

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240375 [Multi-domain]  Cd Length: 504  Bit Score: 46.88  E-value: 6.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879  57 IVQELKQqnprLVYVCDPVL----GDKWDGEGSMyvpEDLLPVYKEKVVPLADIITPNQFEAELLSGRK-IHSQEEALRV 131
Cdd:PTZ00347  317 VIEKLKN----LPMVVDPVLvatsGDDLVAQKNA---DDVLAMYKERIFPMATIITPNIPEAERILGRKeITGVYEARAA 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879 132 MDMLhsmgpdtvvitssdlpSPQGSNYLIVLGSQRRRNP--AGSVVMERIRMDIRKVDAVFV------GTGDLFAAMLLA 203
Cdd:PTZ00347  390 AQAL----------------AQYGSRYVLVKGGHDLIDPeaCRDVLYDREKDRFYEFTANRIatinthGTGCTLASAISS 453

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1061899879 204 WTHKHpNNLKVACEKTVSTLHHVLQRTIQCAKAQAGEG 241
Cdd:PTZ00347  454 FLARG-YTVPDAVERAIGYVHEAIVRSCGVPLGQGTNR 490
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
 96-209 4.64e-04

Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside analogues at the 5'-hydroxyl using ATP or GTP as the phosphate donor.The physiological function of AK is associated with the regulation of extracellular adenosine levels and the preservation of intracellular adenylate pools. Adenosine kinase is involved in the purine salvage pathway.


Pssm-ID: 238573 [Multi-domain]  Cd Length: 312  Bit Score: 41.06  E-value: 4.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879  96 YKE---KVVPLADIITPNQFEAELLSGRKI-HSQEEALRVMdmlhSMGPDTVVITssdlpspQGSNYLIVLgSQRRRNPA 171
Cdd:cd01168   190 FKEallELLPYVDILFGNEEEAEALAEAETtDDLEAALKLL----ALRCRIVVIT-------QGAKGAVVV-EGGEVYPV 257

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1061899879 172 GSVVMERIrmdirkVDAvfVGTGDLFAA-MLLAWTHKHP 209
Cdd:cd01168   258 PAIPVEKI------VDT--NGAGDAFAGgFLYGLVQGEP 288
KdgK cd01166
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ...
 89-203 1.44e-03

2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form 2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the common intermediate product, that allows organisms to channel D-glucuronate and/or D-galacturinate into the glycolysis and therefore use polymers, like pectin and xylan as carbon sources.


Pssm-ID: 238571 [Multi-domain]  Cd Length: 294  Bit Score: 39.48  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879  89 PEDLLPVYKEkVVPLADIITPNQFEAELLSGRKIHSQ-EEALRvmdmLHSMGPDTVVItssdlpspqgsnylivlgsqrR 167
Cdd:cd01166   172 AEEAREALEE-LLPYVDIVLPSEEEAEALLGDEDPTDaAERAL----ALALGVKAVVV---------------------K 225

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1061899879 168 RNPAGSVVM---ERIRMDIRKVDAV-FVGTGDLFAAMLLA 203
Cdd:cd01166   226 LGAEGALVYtggGRVFVPAYPVEVVdTTGAGDAFAAGFLA 265
FruK_PfkB_like cd01164
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ...
 55-215 7.31e-03

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: 37.13  E-value: 7.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879  55 VDIVQELKQQNPRLVyvCDPvlgdkwDGEGsmyvpedLLPVYKEKVvplaDIITPNQFEAELLSGRKIHSQEEALRVMDM 134
Cdd:cd01164   148 AELVRLAREKGARVI--LDT------SGEA-------LLAALAAKP----FLIKPNREELEELFGRPLGDEEDVIAAARK 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1061899879 135 LHSMGPDTVVITssdlpspqgsnylivLGSQrrrnpaGSVVMER---IRMDIRKVDAV-FVGTGD-LFAAMLLAWTHKHP 209
Cdd:cd01164   209 LIERGAENVLVS---------------LGAD------GALLVTKdgvYRASPPKVKVVsTVGAGDsMVAGFVAGLAQGLS 267


                  ....*...
gi 1061899879 210 --NNLKVA 215
Cdd:cd01164   268 leEALRLA 275
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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