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Conserved domains on  [gi|4505701|ref|NP_003672|]
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pyridoxal kinase isoform 1 [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 ...
 6-304 2.50e-149

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: 420.39  E-value: 2.50e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701      6 RVLSIQSHVIRGYVGNRAATFPLQVLGFEIDAVNSVQFSNHTGYAHWKGQVLNSDELQELYEGL-RLNNMNKYDYVLTGY 84
Cdd:TIGR00687   3 NVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLeAINKLNQCDAVLSGY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701     85 TRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDKWDGegsMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHS 164
Cdd:TIGR00687  83 LGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKG---CYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701    165 QEEALRVMDMLHSMGPDTVVITssdlpspqgsnYLIVLGSQRRRNPAGSVVMERIRMDIRKVDAVF----VGTGDLFAAM 240
Cdd:TIGR00687 160 EEEALAAADALIAMGPDIVLVT-----------HLIRAGSQRDRSFEGLVATQEGRWHISRPLAVFdpppVGTGDLIAAL 228

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4505701    241 LLAwTHKHPNNLKVACEKTVSTLHHVLQRTIQCAKAQagegVRPSPMQLELRMVQSKRDIEDPE 304
Cdd:TIGR00687 229 LLA-TLLHGNSLKEALEKTVSAVYHVLRTTIQLGKYE----LQPVAAQLEIRMPQSKFDAEKVE 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 ...
 6-304 2.50e-149

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: 420.39  E-value: 2.50e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701      6 RVLSIQSHVIRGYVGNRAATFPLQVLGFEIDAVNSVQFSNHTGYAHWKGQVLNSDELQELYEGL-RLNNMNKYDYVLTGY 84
Cdd:TIGR00687   3 NVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLeAINKLNQCDAVLSGY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701     85 TRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDKWDGegsMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHS 164
Cdd:TIGR00687  83 LGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKG---CYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701    165 QEEALRVMDMLHSMGPDTVVITssdlpspqgsnYLIVLGSQRRRNPAGSVVMERIRMDIRKVDAVF----VGTGDLFAAM 240
Cdd:TIGR00687 160 EEEALAAADALIAMGPDIVLVT-----------HLIRAGSQRDRSFEGLVATQEGRWHISRPLAVFdpppVGTGDLIAAL 228

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4505701    241 LLAwTHKHPNNLKVACEKTVSTLHHVLQRTIQCAKAQagegVRPSPMQLELRMVQSKRDIEDPE 304
Cdd:TIGR00687 229 LLA-TLLHGNSLKEALEKTVSAVYHVLRTTIQLGKYE----LQPVAAQLEIRMPQSKFDAEKVE 287
PLN02978 PLN02978
pyridoxal kinase
 6-310 1.05e-137

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 391.80  E-value: 1.05e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701     6 RVLSIQSHVIRGYVGNRAATFPLQVLGFEIDAVNSVQFSNHTGYAHWKGQVLNSDELQELYEGLRLNNMNKYDYVLTGYT 85
Cdd:PLN02978  16 RVLSIQSHTVHGYVGNKSAVFPLQLLGFDVDPINSVQFSNHTGYPTFKGQVLDGEQLWALIEGLEANGLLFYTHLLTGYI 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701    86 RDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQ 165
Cdd:PLN02978  96 GSVSFLRTVLRVVKKLRSVNPNLTYVCDPVLGD----EGKLYVPPELVPVYREKVVPLATMLTPNQFEAEQLTGIRIVTE 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701   166 EEALRVMDMLHSMGPDTVVITSSDLPspqgsNYLIVLGSQRRRNPAGSvvmERIRMDIRKVDAVFVGTGDLFAAMLLAWT 245
Cdd:PLN02978 172 EDAREACAILHAAGPSKVVITSIDID-----GKLLLVGSHRKEKGARP---EQFKIVIPKIPAYFTGTGDLMAALLLGWS 243

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4505701   246 HKHPNNLKVACEKTVSTLHHVLQRTIQCAKAqagEGVRPSPMQLELRMVQSKRDIEDPEIVVQAT 310
Cdd:PLN02978 244 HKYPDNLDKAAELAVSSLQAVLRRTLADYKR---AGADPKSSSLELRLVQSQDDIRHPQVRFKAE 305
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 6-272 9.29e-117

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: 336.86  E-value: 9.29e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701    6 RVLSIQSHVIRGYVGNRAATFPLQVLGFEIDAVNSVQFSNHTGYAHWKGQVLNSDELQELYEGLRLNNM-NKYDYVLTGY 84
Cdd:cd01173   1 RVLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLlLEYDAVLTGY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701   85 TRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwdgEGSMYV-PEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIH 163
Cdd:cd01173  81 LGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGD----NGKLYVvAEEIVPVYRDLLVPLADIITPNQFELELLTGKKIN 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701  164 SQEEALRVMDMLHSMGPDTVVITSSDLPSPqgsnylivlgsqRRRNPAGSVVMERIRMDIRKVD--AVFVGTGDLFAAML 241
Cdd:cd01173 157 DLEDAKAAARALHAKGPKTVVVTSVELADD------------DRIEMLGSTATEAWLVQRPKIPfpAYFNGTGDLFAALL 224

                       250       260       270
                ....*....|....*....|....*....|.
gi 4505701  242 LAWTHKHPnNLKVACEKTVSTLHHVLQRTIQ 272
Cdd:cd01173 225 LARLLKGK-SLAEALEKALNFVHEVLEATYE 254
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 6-272 2.92e-84

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: 254.69  E-value: 2.92e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701    6 RVLSIQSHVIRGYVGNRAATFPLQVLGFEIDAVNSVQFSNHTGYAHWKGQVLNSDELQELYEGL-RLNNMNKYDYVLTGY 84
Cdd:COG2240   3 RVLSIQSHVVYGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWkELGVLLEFDAVLSGY 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701   85 TRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwDGEGsMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHS 164
Cdd:COG2240  83 LGSAEQGDIIADFVARVKAANPDALYLCDPVMGD--NGKG-YYVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYET 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701  165 QEEALRVMDMLHSMGPDTVVITS---SDLPSPQGSNYLIvlgsqrrrNPAGSVVMERirmdiRKVDAVFVGTGDLFAAML 241
Cdd:COG2240 160 LEEALAAARALLALGPKIVVVTSvplDDTPADKIGNLAV--------TADGAWLVET-----PLLPFSPNGTGDLFAALL 226

                       250       260       270
                ....*....|....*....|....*....|..
gi 4505701  242 LA-WTHKHPnnLKVACEKTVSTLHHVLQRTIQ 272
Cdd:COG2240 227 LAhLLRGKS--LEEALERAAAFVYEVLERTAA 256
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 97-195 9.27e-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: 77.91  E-value: 9.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701     97 IVQELKQQNPRLVyvCDPVLGDKwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLH 176
Cdd:pfam08543  78 VAEKLDKYGVPVV--LDPVMVAK---SGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLL 152

                          90
                  ....*....|....*....
gi 4505701    177 SMGPDTVVITSSDLPSPQG 195
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 ...
 6-304 2.50e-149

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: 420.39  E-value: 2.50e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701      6 RVLSIQSHVIRGYVGNRAATFPLQVLGFEIDAVNSVQFSNHTGYAHWKGQVLNSDELQELYEGL-RLNNMNKYDYVLTGY 84
Cdd:TIGR00687   3 NVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLeAINKLNQCDAVLSGY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701     85 TRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDKWDGegsMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHS 164
Cdd:TIGR00687  83 LGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKG---CYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701    165 QEEALRVMDMLHSMGPDTVVITssdlpspqgsnYLIVLGSQRRRNPAGSVVMERIRMDIRKVDAVF----VGTGDLFAAM 240
Cdd:TIGR00687 160 EEEALAAADALIAMGPDIVLVT-----------HLIRAGSQRDRSFEGLVATQEGRWHISRPLAVFdpppVGTGDLIAAL 228

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4505701    241 LLAwTHKHPNNLKVACEKTVSTLHHVLQRTIQCAKAQagegVRPSPMQLELRMVQSKRDIEDPE 304
Cdd:TIGR00687 229 LLA-TLLHGNSLKEALEKTVSAVYHVLRTTIQLGKYE----LQPVAAQLEIRMPQSKFDAEKVE 287
PLN02978 PLN02978
pyridoxal kinase
 6-310 1.05e-137

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 391.80  E-value: 1.05e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701     6 RVLSIQSHVIRGYVGNRAATFPLQVLGFEIDAVNSVQFSNHTGYAHWKGQVLNSDELQELYEGLRLNNMNKYDYVLTGYT 85
Cdd:PLN02978  16 RVLSIQSHTVHGYVGNKSAVFPLQLLGFDVDPINSVQFSNHTGYPTFKGQVLDGEQLWALIEGLEANGLLFYTHLLTGYI 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701    86 RDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQ 165
Cdd:PLN02978  96 GSVSFLRTVLRVVKKLRSVNPNLTYVCDPVLGD----EGKLYVPPELVPVYREKVVPLATMLTPNQFEAEQLTGIRIVTE 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701   166 EEALRVMDMLHSMGPDTVVITSSDLPspqgsNYLIVLGSQRRRNPAGSvvmERIRMDIRKVDAVFVGTGDLFAAMLLAWT 245
Cdd:PLN02978 172 EDAREACAILHAAGPSKVVITSIDID-----GKLLLVGSHRKEKGARP---EQFKIVIPKIPAYFTGTGDLMAALLLGWS 243

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4505701   246 HKHPNNLKVACEKTVSTLHHVLQRTIQCAKAqagEGVRPSPMQLELRMVQSKRDIEDPEIVVQAT 310
Cdd:PLN02978 244 HKYPDNLDKAAELAVSSLQAVLRRTLADYKR---AGADPKSSSLELRLVQSQDDIRHPQVRFKAE 305
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
 1-312 2.22e-123

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 355.16  E-value: 2.22e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701     1 MEEECRVLSIQSHVIRGYVGNRAATFPLQVLGFEIDAVNSVQFSNHTGYAHWKGQVLNSDELQELYEGLRLNNM-NKYDY 79
Cdd:PTZ00344   1 MSMEKKVLSIQSHVTHGYVGNRAATFPLQLLGFDVDFVNTVQLSNHTGYPVIKGHRLDLNELITLMDGLRANNLlSDYTY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701    80 VLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwdgEGSMYVPEDLLPVYKEkVVPLADIITPNQFEAELLSG 159
Cdd:PTZ00344  81 VLTGYINSADILREVLATVKEIKELRPKLIFLCDPVMGD----DGKLYVKEEVVDAYRE-LIPYADVITPNQFEASLLSG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701   160 RKIHSQEEALRVMDMLHSMGPDTVVITSSDLpsPQGSNYLIVLGSQRRRNPAGSvvmERIRMDIRKVDAVFVGTGDLFAA 239
Cdd:PTZ00344 156 VEVKDLSDALEAIDWFHEQGIPVVVITSFRE--DEDPTHLRFLLSCRDKDTKNN---KRFTGKVPYIEGRYTGTGDLFAA 230

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4505701   240 MLLAWTHKHPnnLKVACEKTVSTLHHVLQRTIqcakaQAGEGVRPSPMQLELRMVQSKRDIEDPEIVVQATVL 312
Cdd:PTZ00344 231 LLLAFSHQHP--MDLAVGKAMGVLQDIIKATR-----ESGGSGSSSLMSRELRLIQSPRDLLNPETVFKVTPL 296
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 6-272 9.29e-117

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: 336.86  E-value: 9.29e-117
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701    6 RVLSIQSHVIRGYVGNRAATFPLQVLGFEIDAVNSVQFSNHTGYAHWKGQVLNSDELQELYEGLRLNNM-NKYDYVLTGY 84
Cdd:cd01173   1 RVLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLlLEYDAVLTGY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701   85 TRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwdgEGSMYV-PEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIH 163
Cdd:cd01173  81 LGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGD----NGKLYVvAEEIVPVYRDLLVPLADIITPNQFELELLTGKKIN 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701  164 SQEEALRVMDMLHSMGPDTVVITSSDLPSPqgsnylivlgsqRRRNPAGSVVMERIRMDIRKVD--AVFVGTGDLFAAML 241
Cdd:cd01173 157 DLEDAKAAARALHAKGPKTVVVTSVELADD------------DRIEMLGSTATEAWLVQRPKIPfpAYFNGTGDLFAALL 224

                       250       260       270
                ....*....|....*....|....*....|.
gi 4505701  242 LAWTHKHPnNLKVACEKTVSTLHHVLQRTIQ 272
Cdd:cd01173 225 LARLLKGK-SLAEALEKALNFVHEVLEATYE 254
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 6-272 2.92e-84

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: 254.69  E-value: 2.92e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701    6 RVLSIQSHVIRGYVGNRAATFPLQVLGFEIDAVNSVQFSNHTGYAHWKGQVLNSDELQELYEGL-RLNNMNKYDYVLTGY 84
Cdd:COG2240   3 RVLSIQSHVVYGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWkELGVLLEFDAVLSGY 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701   85 TRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDkwDGEGsMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHS 164
Cdd:COG2240  83 LGSAEQGDIIADFVARVKAANPDALYLCDPVMGD--NGKG-YYVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYET 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701  165 QEEALRVMDMLHSMGPDTVVITS---SDLPSPQGSNYLIvlgsqrrrNPAGSVVMERirmdiRKVDAVFVGTGDLFAAML 241
Cdd:COG2240 160 LEEALAAARALLALGPKIVVVTSvplDDTPADKIGNLAV--------TADGAWLVET-----PLLPFSPNGTGDLFAALL 226

                       250       260       270
                ....*....|....*....|....*....|..
gi 4505701  242 LA-WTHKHPnnLKVACEKTVSTLHHVLQRTIQ 272
Cdd:COG2240 227 LAhLLRGKS--LEEALERAAAFVYEVLERTAA 256
PRK05756 PRK05756
pyridoxal kinase PdxY;
7-312 8.73e-78

pyridoxal kinase PdxY;


Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 238.62  E-value: 8.73e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701     7 VLSIQSHVIRGYVGNRAATFPLQVLGFEIDAVNSVQFSNHTGYAHWKGQVLNSDELQELYEGL-RLNNMNKYDYVLTGYT 85
Cdd:PRK05756   4 ILSIQSHVVYGHVGNSAAVFPMQRLGVNVWPLNTVQFSNHTGYGKWTGCVMPPSHLTEIVQGIaDIGWLGECDAVLSGYL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701    86 RDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDKwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQ 165
Cdd:PRK05756  84 GSAEQGEAILDAVRRVKAANPQALYFCDPVMGDP---EKGCIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701   166 EEALRVMDMLHSMGPDTVVITSSDLP-SPQGSNYLIVLgsqrrrNPAGSVVMERIRMDIRKVDavfVGTGDLFAAMLLAW 244
Cdd:PRK05756 161 EDAVAAARALIARGPKIVLVTSLARAgYPADRFEMLLV------TADGAWHISRPLVDFMRQP---VGVGDLTSALFLAR 231

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4505701   245 tHKHPNNLKVACEKTVSTLHHVLQRTIQCakaqageGVRpspmqlELRMVQSKRDIEDPEIVVQATVL 312
Cdd:PRK05756 232 -LLQGGSLEEALEHTTAAVYEVMARTKER-------GSY------ELQLVAAQDSIATPRAMFQARRL 285
pdxK PRK08176
pyridoxine/pyridoxal/pyridoxamine kinase;
7-273 2.33e-33

pyridoxine/pyridoxal/pyridoxamine kinase;


Pssm-ID: 181269 [Multi-domain]  Cd Length: 281  Bit Score: 123.61  E-value: 2.33e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701     7 VLSIQSHVIRGYVGNRAATFPLQVLGFEIDAVNSVQFSNHTGYAHWKGQVLNSD----ELQELYE--GLRlnnmnKYDYV 80
Cdd:PRK08176  18 IVAVQSQVVYGSVGNSIAVPAIKANGLRVFAVPTVLLSNTPHYPTFYGGAIPDEwfsgYLRALQErdALR-----QLRAV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701    81 LTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDKWDGegsMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGR 160
Cdd:PRK08176  93 TTGYMGSASQIKILAEWLTALRADHPDLLIMVDPVIGDIDSG---IYVKPDLPEAYRQHLLPLAQGLTPNIFELEILTGK 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701   161 KIHSQEEALRVMDMLHSMGPDTVVITSSDLPSPQGS-NYLIVLGSQRrrnpagsVVMERIRmdirkVDAVFVGTGDLFAA 239
Cdd:PRK08176 170 PCRTLDSAIAAAKSLLSDTLKWVVITSAAGNEENQEmQVVVVTADSV-------NVISHPR-----VDTDLKGTGDLFCA 237

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 4505701   240 MLLA-WTHKHPnnLKVACEKTVSTLHHVLQRTIQC 273
Cdd:PRK08176 238 ELVSgLLKGKA--LTDAAHRAGLRVLEVMRYTQQA 270
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 77-244 2.90e-19

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: 84.07  E-value: 2.90e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701   77 YDYVLTGYTRDKsfLAMVVDIVQELKQQNPRlvYVCDPVLGDK-WDGEGsmyvpedllpvyKEKVVPLADIITPNQFEAE 155
Cdd:cd00287  58 ADAVVISGLSPA--PEAVLDALEEARRRGVP--VVLDPGPRAVrLDGEE------------LEKLLPGVDILTPNEEEAE 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701  156 LLSGRKIHSQEEALRVMDMLHSMGPDTVVITssdlpspQGSNYLIVLGSQRRRNPAGSVvmerirmdirKVDAV-FVGTG 234
Cdd:cd00287 122 ALTGRRDLEVKEAAEAAALLLSKGPKVVIVT-------LGEKGAIVATRGGTEVHVPAF----------PVKVVdTTGAG 184

                       170
                ....*....|
gi 4505701  235 DLFAAMLLAW 244
Cdd:cd00287 185 DAFLAALAAG 194
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 92-239 1.02e-18

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: 83.55  E-value: 1.02e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701   92 AMVVDIVQELKQQNprlvYVCDPVLGDKWDGEGSmyvPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRV 171
Cdd:COG0351  82 EAVAEILADYPLVP----VVLDPVMVAKSGDRLL---DEDAVEALRELLLPLATVVTPNLPEAEALLGIEITTLDDMREA 154

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4505701  172 MDMLHSMGPDTVVITSSDLPSPQGSNYLiVLGSQRRRnpagsVVMERIRmdirkvDAVFVGTGDLFAA 239
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 ...
 97-195 9.27e-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: 77.91  E-value: 9.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701     97 IVQELKQQNPRLVyvCDPVLGDKwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLH 176
Cdd:pfam08543  78 VAEKLDKYGVPVV--LDPVMVAK---SGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLL 152

                          90
                  ....*....|....*....
gi 4505701    177 SMGPDTVVITSSDLPSPQG 195
Cdd:pfam08543 153 ALGAKAVLIKGGHLEGEEA 171
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 94-243 1.21e-13

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 69.38  E-value: 1.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701    94 VVDIVQELKQQNPRLVYVCDPVL----GDkwdgegsmyvP---EDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQE 166
Cdd:PRK06427  87 IIETVAEALKRYPIPPVVLDPVMiaksGD----------PllaDDAVAALRERLLPLATLITPNLPEAEALTGLPIADTE 156

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4505701   167 EALRVM-DMLHSMGPDTVVITSS-DLPSPQGSNYLIvlgsqrrrNPAGSVVMERIRMDIRKVDavfvGTGDLFAAMLLA 243
Cdd:PRK06427 157 DEMKAAaRALHALGCKAVLIKGGhLLDGEESVDWLF--------DGEGEERFSAPRIPTKNTH----GTGCTLSAAIAA 223
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 95-244 5.50e-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: 5.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701     95 VDIVQELKQQNPRLVYVCDPVLGDKWDgegsmyvpedLLPVYKEkVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDM 174
Cdd:pfam00294 143 EATLEELIEAAKNGGTFDPNLLDPLGA----------AREALLE-LLPLADLLKPNEEELEALTGAKLDDIEEALAALHK 211

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4505701    175 LHSMGPDTVVITSsdlpSPQGSnyLIVLGSQRRRNPAgsvvmerirmdIRKVDAV-FVGTGDLFAAMLLAW 244
Cdd:pfam00294 212 LLAKGIKTVIVTL----GADGA--LVVEGDGEVHVPA-----------VPKVKVVdTTGAGDSFVGGFLAG 265
PRK07105 PRK07105
pyridoxamine kinase; Validated
 76-270 7.99e-11

pyridoxamine kinase; Validated


Pssm-ID: 180840 [Multi-domain]  Cd Length: 284  Bit Score: 61.47  E-value: 7.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701    76 KYDYVLTGY---TRDksflamvVDIVQELKQ--QNPRLVYVCDPVLGDKwdgeGSMYVP--EDLLPVYKeKVVPLADIIT 148
Cdd:PRK07105  75 KFDAIYSGYlgsPRQ-------IQIVSDFIKyfKKKDLLVVVDPVMGDN----GKLYQGfdQEMVEEMR-KLIQKADVIT 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701   149 PNQFEAELLSG---RKIHSQEEalRVMDMLH---SMGPDTVVITSSdlpsPQGSNYLIVLGSQRRRNpagsvvmERIRMD 222
Cdd:PRK07105 143 PNLTEACLLLDkpyLEKSYSEE--EIKQLLRklaDLGPKIVIITSV----PFEDGKIGVAYYDRATD-------RFWKVF 209

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 4505701   223 IRKVDAVFVGTGDLFAAMLLAWTHkHPNNLKVACEKTVSTLHHVLQRT 270
Cdd:PRK07105 210 CKYIPAHYPGTGDIFTSVITGSLL-QGDSLPIALDRAVQFIEKGIRAT 256
PRK11142 PRK11142
ribokinase; Provisional
 143-186 1.76e-10

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 60.65  E-value: 1.76e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 4505701   143 LADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVIT 186
Cdd:PRK11142 178 LVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLIT 221
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 138-243 2.23e-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: 2.23e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701  138 EKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITssdlpspqgsnylivLGSQrrrnpaGSVVM- 216
Cdd:cd01174 170 AELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVT---------------LGAK------GALLAs 228

                        90       100       110
                ....*....|....*....|....*....|
gi 4505701  217 --ERIRMDIRKVDAV-FVGTGDLFAAMLLA 243
Cdd:cd01174 229 ggEVEHVPAFKVKAVdTTGAGDTFIGALAA 258
PRK08573 PRK08573
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
111-206 3.93e-09

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 236297 [Multi-domain]  Cd Length: 448  Bit Score: 57.43  E-value: 3.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701   111 VCDPVLGDKwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLH-SMGPDTVVITSSD 189
Cdd:PRK08573 101 VVDPVMIAK---SGAPLLREDAVDALIKRLLPLATVVTPNRPEAEKLTGMKIRSVEDARKAAKYIVeELGAEAVVVKGGH 177

                         90
                 ....*....|....*..
gi 4505701   190 LPSPQGSNYLIVLGSQR 206
Cdd:PRK08573 178 LEGEEAVDVLYHNGTFR 194
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 80-243 1.12e-08

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: 1.12e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701   80 VLTGYT-RDKSFLAMVVDIVQELKQQNPRLVYvcDPVLGDKwdgegsmyVPEDLLPVYKEkVVPLADIITPNQFEAELLS 158
Cdd:COG0524 132 HLGGITlASEPPREALLAALEAARAAGVPVSL--DPNYRPA--------LWEPARELLRE-LLALVDILFPNEEEAELLT 200

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701  159 GrkIHSQEEALRVmdmLHSMGPDTVVITssdlpspqgsnylivLGSQrrrnpaGSVVM---ERIRMDIRKVDAVF-VGTG 234
Cdd:COG0524 201 G--ETDPEEAAAA---LLARGVKLVVVT---------------LGAE------GALLYtggEVVHVPAFPVEVVDtTGAG 254


                ....*....
gi 4505701  235 DLFAAMLLA 243
Cdd:COG0524 255 DAFAAGFLA 263
PRK12616 PRK12616
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
51-186 1.10e-07

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183624  Cd Length: 270  Bit Score: 51.97  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701    51 HWKGQVLNSD------ELQELYEGLRLNNMNkydyvlTGYTRDKSFLAMVVDIVQELKQQNprlvYVCDPVLGDKwdGEG 124
Cdd:PRK12616  49 SWDHQVFPIDtdtiraQLSTIVDGIGVDAMK------TGMLPTVDIIELAADTIKEKQLKN----VVIDPVMVCK--GAN 116

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 4505701   125 SMYVPEDLlPVYKEKVVPLADIITPNQFEAELLSGR-KIHSQEEALRVMDMLHSMGPDTVVIT 186
Cdd:PRK12616 117 EVLYPEHA-EALREQLAPLATVITPNLFEAGQLSGMgEIKTVEQMKEAAKKIHELGAQYVVIT 178
PRK12413 PRK12413
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
139-185 1.15e-07

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183513 [Multi-domain]  Cd Length: 253  Bit Score: 51.99  E-value: 1.15e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 4505701   139 KVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVI 185
Cdd:PRK12413 125 QFFPYVTVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAVVI 171
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
 78-192 3.99e-07

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 51.31  E-value: 3.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701    78 DYVLTGYTRDKSFLAMVVDIVQELKQQNprlvYVCDPVLGDKwdgEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAE-L 156
Cdd:PLN02898  80 DVVKTGMLPSAEIVKVLCQALKEFPVKA----LVVDPVMVST---SGDVLAGPSILSALREELLPLATIVTPNVKEASaL 152

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 4505701   157 LSGRKIHSqeealrVMDM------LHSMGPDTVVITSSDLPS 192
Cdd:PLN02898 153 LGGDPLET------VADMrsaakeLHKLGPRYVLVKGGHLPD 188
PRK12412 PRK12412
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
6-185 1.31e-06

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183512 [Multi-domain]  Cd Length: 268  Bit Score: 48.81  E-value: 1.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701     6 RVLSIQSHVIRGYVGNRAATFPLQVLG-FEIDAVNS-VQFSNHTGYAHwkgQVLNSD------ELQELYEGLRLNNMNky 77
Cdd:PRK12412   3 KALTIAGSDTSGGAGIQADLKTFQELGvYGMTSLTTiVTMDPHNGWAH---NVFPIPastlkpQLETTIEGVGVDALK-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701    78 dyvlTGYTRDKSFLAMVVDIVQELKQQNprlvYVCDPVLGDKwdGEGSMYVPEDLLpVYKEKVVPLADIITPNQFEAELL 157
Cdd:PRK12412  78 ----TGMLGSVEIIEMVAETIEKHNFKN----VVVDPVMVCK--GADEALHPETND-CLRDVLVPKALVVTPNLFEAYQL 146

                        170       180
                 ....*....|....*....|....*...
gi 4505701   158 SGRKIHSQEEALRVMDMLHSMGPDTVVI 185
Cdd:PRK12412 147 SGVKINSLEDMKEAAKKIHALGAKYVLI 174
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
53-249 2.17e-06

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


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 48.21  E-value: 2.17e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701   53 KGQVLNSDELQELYEGLRlNNMNKYDY-VLTGytrdkSFLAMV-----VDIVQELKQQNPRLVyvcdpvlgdkWDGEGsm 126
Cdd:COG1105 106 PGPEISEEELEALLERLE-ELLKEGDWvVLSG-----SLPPGVppdfyAELIRLARARGAKVV----------LDTSG-- 167

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701  127 yvpEDLLPVYKEKVvplaDIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITssdlpspqgsnylivLGSQr 206
Cdd:COG1105 168 ---EALKAALEAGP----DLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVS---------------LGAD- 224

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 4505701  207 rrnpaGSVVM---ERIRMDIRKVDAVF-VGTGD-LFAAMLLAWTHKHP 249
Cdd:COG1105 225 -----GALLVtedGVYRAKPPKVEVVStVGAGDsMVAGFLAGLARGLD 267
PTZ00347 PTZ00347
phosphomethylpyrimidine kinase; Provisional
 97-281 9.26e-06

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240375 [Multi-domain]  Cd Length: 504  Bit Score: 46.88  E-value: 9.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701    97 IVQELKQqnprLVYVCDPVL----GDKWDGEGSMyvpEDLLPVYKEKVVPLADIITPNQFEAELLSGRK-IHSQEEALRV 171
Cdd:PTZ00347 317 VIEKLKN----LPMVVDPVLvatsGDDLVAQKNA---DDVLAMYKERIFPMATIITPNIPEAERILGRKeITGVYEARAA 389

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701   172 MDMLhsmgpdtvvitssdlpSPQGSNYLIVLGSQRRRNP--AGSVVMERIRMDIRKVDAVFV------GTGDLFAAMLLA 243
Cdd:PTZ00347 390 AQAL----------------AQYGSRYVLVKGGHDLIDPeaCRDVLYDREKDRFYEFTANRIatinthGTGCTLASAISS 453

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 4505701   244 WTHKHpNNLKVACEKTVSTLHHVLQRTIQCAKAQAGEG 281
Cdd:PTZ00347 454 FLARG-YTVPDAVERAIGYVHEAIVRSCGVPLGQGTNR 490
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
 136-249 6.00e-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: 6.00e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701  136 YKE---KVVPLADIITPNQFEAELLSGRKI-HSQEEALRVMdmlhSMGPDTVVITssdlpspQGSNYLIVLgSQRRRNPA 211
Cdd:cd01168 190 FKEallELLPYVDILFGNEEEAEALAEAETtDDLEAALKLL----ALRCRIVVIT-------QGAKGAVVV-EGGEVYPV 257

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 4505701  212 GSVVMERIrmdirkVDAvfVGTGDLFAA-MLLAWTHKHP 249
Cdd:cd01168 258 PAIPVEKI------VDT--NGAGDAFAGgFLYGLVQGEP 288
KdgK cd01166
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ...
 129-243 1.84e-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: 1.84e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4505701  129 PEDLLPVYKEkVVPLADIITPNQFEAELLSGRKIHSQ-EEALRvmdmLHSMGPDTVVItssdlpspqgsnylivlgsqrR 207
Cdd:cd01166 172 AEEAREALEE-LLPYVDIVLPSEEEAEALLGDEDPTDaAERAL----ALALGVKAVVV---------------------K 225

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 4505701  208 RNPAGSVVM---ERIRMDIRKVDAV-FVGTGDLFAAMLLA 243
Cdd:cd01166 226 LGAEGALVYtggGRVFVPAYPVEVVdTTGAGDAFAAGFLA 265
 
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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