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Conserved domains on  [gi|334188058|ref|NP_001190432|]
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pfkB-like carbohydrate kinase family protein [Arabidopsis thaliana]

Protein Classification

pyridoxal kinase( domain architecture ID 10010958)

pyridoxal kinase catalyzes the transfer of a phosphate group from ATP to the 5-hydroxylmethyl group of pyridoxal to form the biologically active pyridoxal phosphate, an active form of vitamin B6

CATH:  3.40.1190.20
EC:  2.7.1.35
Gene Ontology:  GO:0005524|GO:0046872|GO:0008478|GO:0009443|GO:0008615
PubMed:  8382990|7748903|15581583|8690703|15189147|17109392
SCOP:  4000759

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02978 PLN02978
pyridoxal kinase
 36-315 0e+00

pyridoxal kinase


:

Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 562.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058  36 TTPPVLSLALPSDTGRVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLE 115
Cdd:PLN02978   1 MAPPVLSLALPSSTGRVLSIQSHTVHGYVGNKSAVFPLQLLGFDVDPINSVQFSNHTGYPTFKGQVLDGEQLWALIEGLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058 116 ANDLLFYTHVLT----------------------------VCDPVMGDEGKLYVPEELVHVYREKVVPLASMLTPNQFEA 167
Cdd:PLN02978  81 ANGLLFYTHLLTgyigsvsflrtvlrvvkklrsvnpnltyVCDPVLGDEGKLYVPPELVPVYREKVVPLATMLTPNQFEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058 168 EKLTGLRINSEEDGREACAILHAAGPSKVVITSITIGGILLLIGSHQKEKGLKPEQFKILIHKIPAYFTGTGDLMTALLL 247
Cdd:PLN02978 161 EQLTGIRIVTEEDAREACAILHAAGPSKVVITSIDIDGKLLLVGSHRKEKGARPEQFKIVIPKIPAYFTGTGDLMAALLL 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334188058 248 GWSNKYPDNLDKAAELAVSTLQALLRRTLDDYKRAGYDPTSSSLEIRLIQSQEDIRNPKVELKAERYS 315
Cdd:PLN02978 241 GWSHKYPDNLDKAAELAVSSLQAVLRRTLADYKRAGADPKSSSLELRLVQSQDDIRHPQVRFKAERYS 308
 
Name Accession Description Interval E-value
PLN02978 PLN02978
pyridoxal kinase
 36-315 0e+00

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 562.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058  36 TTPPVLSLALPSDTGRVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLE 115
Cdd:PLN02978   1 MAPPVLSLALPSSTGRVLSIQSHTVHGYVGNKSAVFPLQLLGFDVDPINSVQFSNHTGYPTFKGQVLDGEQLWALIEGLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058 116 ANDLLFYTHVLT----------------------------VCDPVMGDEGKLYVPEELVHVYREKVVPLASMLTPNQFEA 167
Cdd:PLN02978  81 ANGLLFYTHLLTgyigsvsflrtvlrvvkklrsvnpnltyVCDPVLGDEGKLYVPPELVPVYREKVVPLATMLTPNQFEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058 168 EKLTGLRINSEEDGREACAILHAAGPSKVVITSITIGGILLLIGSHQKEKGLKPEQFKILIHKIPAYFTGTGDLMTALLL 247
Cdd:PLN02978 161 EQLTGIRIVTEEDAREACAILHAAGPSKVVITSIDIDGKLLLVGSHRKEKGARPEQFKIVIPKIPAYFTGTGDLMAALLL 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334188058 248 GWSNKYPDNLDKAAELAVSTLQALLRRTLDDYKRAGYDPTSSSLEIRLIQSQEDIRNPKVELKAERYS 315
Cdd:PLN02978 241 GWSHKYPDNLDKAAELAVSSLQAVLRRTLADYKRAGADPKSSSLELRLVQSQDDIRHPQVRFKAERYS 308
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 51-277 1.57e-95

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: 282.94  E-value: 1.57e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058  51 RVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLEANDLL-FYTHVLT-- 127
Cdd:cd01173    1 RVLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLLlEYDAVLTgy 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058 128 --------------------------VCDPVMGDEGKLYV-PEELVHVYREKVVPLASMLTPNQFEAEKLTGLRINSEED 180
Cdd:cd01173   81 lgsaeqveavaeivkrlkeknpnllyVCDPVMGDNGKLYVvAEEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLED 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058 181 GREACAILHAAGPSKVVITSITIG--GILLLIGSHQKEKGLkpeqFKILIHKIPAYFTGTGDLMTALLLGWSNKYPDnLD 258
Cdd:cd01173  161 AKAAARALHAKGPKTVVVTSVELAddDRIEMLGSTATEAWL----VQRPKIPFPAYFNGTGDLFAALLLARLLKGKS-LA 235

                        250
                 ....*....|....*....
gi 334188058 259 KAAELAVSTLQALLRRTLD 277
Cdd:cd01173  236 EALEKALNFVHEVLEATYE 254
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 51-302 8.85e-73

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: 225.41  E-value: 8.85e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058  51 RVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLEANDLLF-----YT-- 123
Cdd:COG2240    3 RVLSIQSHVVYGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWKELGVLLefdavLSgy 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058 124 ----------------------HVLTVCDPVMGDEGKLY-VPEELVHVYREKVVPLASMLTPNQFEAEKLTGLRINSEED 180
Cdd:COG2240   83 lgsaeqgdiiadfvarvkaanpDALYLCDPVMGDNGKGYyVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETLEE 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058 181 GREACAILHAAGPSKVVITSITIGGI------LLLIGshqkekglkPEQFKILIH-KIPAYFTGTGDLMTALLLGWSNKY 253
Cdd:COG2240  163 ALAAARALLALGPKIVVVTSVPLDDTpadkigNLAVT---------ADGAWLVETpLLPFSPNGTGDLFAALLLAHLLRG 233

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 334188058 254 pDNLDKAAELAVSTLQALLRRTLDdykrAGYDptssslEIRLIQSQEDI 302
Cdd:COG2240  234 -KSLEEALERAAAFVYEVLERTAA----AGSD------ELLLEAALDEL 271
pyridox_kin TIGR00687
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ...
 51-313 1.21e-69

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: 218.16  E-value: 1.21e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058   51 RVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLEA-NDLLFYTHVLT-- 127
Cdd:TIGR00687   3 NVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLEAiNKLNQCDAVLSgy 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058  128 --------------------------VCDPVMGDEGK-LYVPEELVHVYREKVVPLASMLTPNQFEAEKLTGLRINSEED 180
Cdd:TIGR00687  83 lgsaeqvamvvgivrqvkqanpqalyVCDPVMGDPWKgCYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTEEE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058  181 GREACAILHAAGPSKVVITSITIGGillLIGSHQKEKGLKPEQFKILIHKIPAYF----TGTGDLMTALLLGwSNKYPDN 256
Cdd:TIGR00687 163 ALAAADALIAMGPDIVLVTHLIRAG---SQRDRSFEGLVATQEGRWHISRPLAVFdpppVGTGDLIAALLLA-TLLHGNS 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 334188058  257 LDKAAELAVSTLQALLRRTlddyKRAGydptssSLEIRLIQSQEDIRNPKVELKAER 313
Cdd:TIGR00687 239 LKEALEKTVSAVYHVLRTT----IQLG------KYELQPVAAQLEIRMPQSKFDAEK 285
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 128-199 3.56e-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: 3.56e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334188058  128 VCDPVM--GDEGKLyVPEELVHVYREKVVPLASMLTPNQFEAEKLTGLRINSEEDGREACAILHAAGPSKVVIT 199
Cdd:pfam08543  90 VLDPVMvaKSGDSL-LDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIK 162
 
Name Accession Description Interval E-value
PLN02978 PLN02978
pyridoxal kinase
 36-315 0e+00

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 562.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058  36 TTPPVLSLALPSDTGRVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLE 115
Cdd:PLN02978   1 MAPPVLSLALPSSTGRVLSIQSHTVHGYVGNKSAVFPLQLLGFDVDPINSVQFSNHTGYPTFKGQVLDGEQLWALIEGLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058 116 ANDLLFYTHVLT----------------------------VCDPVMGDEGKLYVPEELVHVYREKVVPLASMLTPNQFEA 167
Cdd:PLN02978  81 ANGLLFYTHLLTgyigsvsflrtvlrvvkklrsvnpnltyVCDPVLGDEGKLYVPPELVPVYREKVVPLATMLTPNQFEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058 168 EKLTGLRINSEEDGREACAILHAAGPSKVVITSITIGGILLLIGSHQKEKGLKPEQFKILIHKIPAYFTGTGDLMTALLL 247
Cdd:PLN02978 161 EQLTGIRIVTEEDAREACAILHAAGPSKVVITSIDIDGKLLLVGSHRKEKGARPEQFKIVIPKIPAYFTGTGDLMAALLL 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 334188058 248 GWSNKYPDNLDKAAELAVSTLQALLRRTLDDYKRAGYDPTSSSLEIRLIQSQEDIRNPKVELKAERYS 315
Cdd:PLN02978 241 GWSHKYPDNLDKAAELAVSSLQAVLRRTLADYKRAGADPKSSSLELRLVQSQDDIRHPQVRFKAERYS 308
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
 47-305 1.84e-105

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 309.70  E-value: 1.84e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058  47 SDTGRVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLEANDLLF-YTHV 125
Cdd:PTZ00344   2 SMEKKVLSIQSHVTHGYVGNRAATFPLQLLGFDVDFVNTVQLSNHTGYPVIKGHRLDLNELITLMDGLRANNLLSdYTYV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058 126 LT----------------------------VCDPVMGDEGKLYVPEELVHVYREkVVPLASMLTPNQFEAEKLTGLRINS 177
Cdd:PTZ00344  82 LTgyinsadilrevlatvkeikelrpklifLCDPVMGDDGKLYVKEEVVDAYRE-LIPYADVITPNQFEASLLSGVEVKD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058 178 EEDGREACAILHAAGPSKVVITSITIG----GILLLIGSHQKEKGlKPEQFKILIHKIPAYFTGTGDLMTALLLGWSNKY 253
Cdd:PTZ00344 161 LSDALEAIDWFHEQGIPVVVITSFREDedptHLRFLLSCRDKDTK-NNKRFTGKVPYIEGRYTGTGDLFAALLLAFSHQH 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 334188058 254 PdnLDKAAELAVSTLQALLRRTlDDYKRAGyDPTSSSLEIRLIQSQEDIRNP 305
Cdd:PTZ00344 240 P--MDLAVGKAMGVLQDIIKAT-RESGGSG-SSSLMSRELRLIQSPRDLLNP 287
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 51-277 1.57e-95

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: 282.94  E-value: 1.57e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058  51 RVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLEANDLL-FYTHVLT-- 127
Cdd:cd01173    1 RVLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLLlEYDAVLTgy 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058 128 --------------------------VCDPVMGDEGKLYV-PEELVHVYREKVVPLASMLTPNQFEAEKLTGLRINSEED 180
Cdd:cd01173   81 lgsaeqveavaeivkrlkeknpnllyVCDPVMGDNGKLYVvAEEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLED 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058 181 GREACAILHAAGPSKVVITSITIG--GILLLIGSHQKEKGLkpeqFKILIHKIPAYFTGTGDLMTALLLGWSNKYPDnLD 258
Cdd:cd01173  161 AKAAARALHAKGPKTVVVTSVELAddDRIEMLGSTATEAWL----VQRPKIPFPAYFNGTGDLFAALLLARLLKGKS-LA 235

                        250
                 ....*....|....*....
gi 334188058 259 KAAELAVSTLQALLRRTLD 277
Cdd:cd01173  236 EALEKALNFVHEVLEATYE 254
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 51-302 8.85e-73

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: 225.41  E-value: 8.85e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058  51 RVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLEANDLLF-----YT-- 123
Cdd:COG2240    3 RVLSIQSHVVYGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWKELGVLLefdavLSgy 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058 124 ----------------------HVLTVCDPVMGDEGKLY-VPEELVHVYREKVVPLASMLTPNQFEAEKLTGLRINSEED 180
Cdd:COG2240   83 lgsaeqgdiiadfvarvkaanpDALYLCDPVMGDNGKGYyVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETLEE 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058 181 GREACAILHAAGPSKVVITSITIGGI------LLLIGshqkekglkPEQFKILIH-KIPAYFTGTGDLMTALLLGWSNKY 253
Cdd:COG2240  163 ALAAARALLALGPKIVVVTSVPLDDTpadkigNLAVT---------ADGAWLVETpLLPFSPNGTGDLFAALLLAHLLRG 233

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 334188058 254 pDNLDKAAELAVSTLQALLRRTLDdykrAGYDptssslEIRLIQSQEDI 302
Cdd:COG2240  234 -KSLEEALERAAAFVYEVLERTAA----AGSD------ELLLEAALDEL 271
pyridox_kin TIGR00687
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ...
 51-313 1.21e-69

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: 218.16  E-value: 1.21e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058   51 RVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLEA-NDLLFYTHVLT-- 127
Cdd:TIGR00687   3 NVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLEAiNKLNQCDAVLSgy 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058  128 --------------------------VCDPVMGDEGK-LYVPEELVHVYREKVVPLASMLTPNQFEAEKLTGLRINSEED 180
Cdd:TIGR00687  83 lgsaeqvamvvgivrqvkqanpqalyVCDPVMGDPWKgCYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTEEE 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058  181 GREACAILHAAGPSKVVITSITIGGillLIGSHQKEKGLKPEQFKILIHKIPAYF----TGTGDLMTALLLGwSNKYPDN 256
Cdd:TIGR00687 163 ALAAADALIAMGPDIVLVTHLIRAG---SQRDRSFEGLVATQEGRWHISRPLAVFdpppVGTGDLIAALLLA-TLLHGNS 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 334188058  257 LDKAAELAVSTLQALLRRTlddyKRAGydptssSLEIRLIQSQEDIRNPKVELKAER 313
Cdd:TIGR00687 239 LKEALEKTVSAVYHVLRTT----IQLG------KYELQPVAAQLEIRMPQSKFDAEK 285
PRK05756 PRK05756
pyridoxal kinase PdxY;
49-313 3.54e-63

pyridoxal kinase PdxY;


Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 201.64  E-value: 3.54e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058  49 TGRVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGLEANDLLF------- 121
Cdd:PRK05756   1 MKNILSIQSHVVYGHVGNSAAVFPMQRLGVNVWPLNTVQFSNHTGYGKWTGCVMPPSHLTEIVQGIADIGWLGecdavls 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058 122 -Y-------THVLT--------------VCDPVMGDEGK-LYVPEELVHVYREKVVPLASMLTPNQFEAEKLTGLRINSE 178
Cdd:PRK05756  81 gYlgsaeqgEAILDavrrvkaanpqalyFCDPVMGDPEKgCIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058 179 EDGREACAILHAAGPSKVVITSIT-----IGGILLLIGShqkekglkPEQFKILIH-KIPAYF--TGTGDLMTALLLGWS 250
Cdd:PRK05756 161 EDAVAAARALIARGPKIVLVTSLAragypADRFEMLLVT--------ADGAWHISRpLVDFMRqpVGVGDLTSALFLARL 232

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334188058 251 NKyPDNLDKAAELAVSTLQALLRRTlddyKRAGydptssSLEIRLIQSQEDIRNPKVELKAER 313
Cdd:PRK05756 233 LQ-GGSLEEALEHTTAAVYEVMART----KERG------SYELQLVAAQDSIATPRAMFQARR 284
pdxK PRK08176
pyridoxine/pyridoxal/pyridoxamine kinase;
35-285 3.08e-30

pyridoxine/pyridoxal/pyridoxamine kinase;


Pssm-ID: 181269 [Multi-domain]  Cd Length: 281  Bit Score: 115.52  E-value: 3.08e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058  35 MTTPPVLSLALPSDtgrVLSIQSHTVQGYVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTFKGQVLNGQQLCDLIEGL 114
Cdd:PRK08176   4 LLLFNDKSRALQAD---IVAVQSQVVYGSVGNSIAVPAIKANGLRVFAVPTVLLSNTPHYPTFYGGAIPDEWFSGYLRAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058 115 EANDLL-----------------------------FYTHVLTVCDPVMGDEGK-LYVPEELVHVYREKVVPLASMLTPNQ 164
Cdd:PRK08176  81 QERDALrqlravttgymgsasqikilaewltalraDHPDLLIMVDPVIGDIDSgIYVKPDLPEAYRQHLLPLAQGLTPNI 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058 165 FEAEKLTGLRINSEEDGREACAILHAAGPSKVVITS----ITIGGILLLIGSHqkekglkpEQFKILIH-KIPAYFTGTG 239
Cdd:PRK08176 161 FELEILTGKPCRTLDSAIAAAKSLLSDTLKWVVITSaagnEENQEMQVVVVTA--------DSVNVISHpRVDTDLKGTG 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 334188058 240 DLMTA-----LLLGWSnkypdnLDKAAELAVSTLQALLRRTlddyKRAGYD 285
Cdd:PRK08176 233 DLFCAelvsgLLKGKA------LTDAAHRAGLRVLEVMRYT----QQAGSD 273
PRK07105 PRK07105
pyridoxamine kinase; Validated
 109-281 4.28e-19

pyridoxamine kinase; Validated


Pssm-ID: 180840 [Multi-domain]  Cd Length: 284  Bit Score: 85.35  E-value: 4.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058 109 DLIEGLEANDLLFythvltVCDPVMGDEGKLYVP--EELVHVYReKVVPLASMLTPNQFEAEKLTG----LRINSEEDGR 182
Cdd:PRK07105  95 DFIKYFKKKDLLV------VVDPVMGDNGKLYQGfdQEMVEEMR-KLIQKADVITPNLTEACLLLDkpylEKSYSEEEIK 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058 183 EACAILHAAGPSKVVITSITIGGILLLIGSHQKEKGlkpeQFKILIHK-IPAYFTGTGDLMTALLLGwSNKYPDNLDKAA 261
Cdd:PRK07105 168 QLLRKLADLGPKIVIITSVPFEDGKIGVAYYDRATD----RFWKVFCKyIPAHYPGTGDIFTSVITG-SLLQGDSLPIAL 242

                        170       180
                 ....*....|....*....|
gi 334188058 262 ELAVSTLQALLRRTLdDYKR 281
Cdd:PRK07105 243 DRAVQFIEKGIRATL-GLKY 261
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 128-277 3.32e-16

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: 76.62  E-value: 3.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058 128 VCDPVM----GDEGklyVPEELVHVYREKVVPLASMLTPNQFEAEKLTGLRINSEEDGREACAILHAAGPSKVVITsiti 203
Cdd:COG0351   97 VLDPVMvaksGDRL---LDEDAVEALRELLLPLATVVTPNLPEAEALLGIEITTLDDMREAAKALLELGAKAVLVK---- 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058 204 GGIL-------LLIGshqkekglkPEQFKILIHK--IPAYFTGTGDL----MTALL-LGWSnkypdnLDKAAELAVSTLQ 269
Cdd:COG0351  170 GGHLpgdeavdVLYD---------GDGVREFSAPriDTGNTHGTGCTlssaIAALLaKGLD------LEEAVREAKEYVT 234


                 ....*...
gi 334188058 270 ALLRRTLD 277
Cdd:COG0351  235 QAIRAALR 242
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 128-199 3.56e-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: 3.56e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334188058  128 VCDPVM--GDEGKLyVPEELVHVYREKVVPLASMLTPNQFEAEKLTGLRINSEEDGREACAILHAAGPSKVVIT 199
Cdd:pfam08543  90 VLDPVMvaKSGDSL-LDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIK 162
PRK08573 PRK08573
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
128-198 1.00e-13

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 236297 [Multi-domain]  Cd Length: 448  Bit Score: 71.30  E-value: 1.00e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334188058 128 VCDPVM-GDEGKLYVPEELVHVYREKVVPLASMLTPNQFEAEKLTGLRINSEEDGREACAILHAAGPSKVVI 198
Cdd:PRK08573 101 VVDPVMiAKSGAPLLREDAVDALIKRLLPLATVVTPNRPEAEKLTGMKIRSVEDARKAAKYIVEELGAEAVV 172
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 112-208 5.23e-13

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 67.84  E-value: 5.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058 112 EGLEANDLLFYthvltVCDPVM----GDEGklyVPEELVHVYREKVVPLASMLTPNQFEAEKLTGLRINSEEDG-REACA 186
Cdd:PRK06427  93 EALKRYPIPPV-----VLDPVMiaksGDPL---LADDAVAALRERLLPLATLITPNLPEAEALTGLPIADTEDEmKAAAR 164

                         90       100
                 ....*....|....*....|..
gi 334188058 187 ILHAAGPSKVVITsitiGGILL 208
Cdd:PRK06427 165 ALHALGCKAVLIK----GGHLL 182
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 96-249 1.24e-11

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: 62.50  E-value: 1.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058  96 TFKGQVLNGQQlCDLIEGLEANDLLFYTHVLTVCDPVMGdeGKLYVPEELvhvyrEKVVPLASMLTPNQFEAEKLTGLRI 175
Cdd:cd00287   57 GADAVVISGLS-PAPEAVLDALEEARRRGVPVVLDPGPR--AVRLDGEEL-----EKLLPGVDILTPNEEEAEALTGRRD 128

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334188058 176 NSEEDGREACAILHAAGPSKVVITSITIGGILLLIGSHQKEKGLKPEQfkilihkiPAYFTGTGDLMTALLLGW 249
Cdd:cd00287  129 LEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGGTEVHVPAFPVK--------VVDTTGAGDAFLAALAAG 194
PRK12412 PRK12412
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
128-198 3.06e-11

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183512 [Multi-domain]  Cd Length: 268  Bit Score: 62.68  E-value: 3.06e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334188058 128 VCDPVM---GDEGKLYvPEELVhVYREKVVPLASMLTPNQFEAEKLTGLRINSEEDGREACAILHAAGPSKVVI 198
Cdd:PRK12412 103 VVDPVMvckGADEALH-PETND-CLRDVLVPKALVVTPNLFEAYQLSGVKINSLEDMKEAAKKIHALGAKYVLI 174
PRK11142 PRK11142
ribokinase; Provisional
 159-248 8.76e-11

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 61.81  E-value: 8.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058 159 MLTPNQFEAEKLTGLRINSEEDGREACAILHAAGPSKVVitsITIG--GILLligSHQKEKGLKPeQFKI-LIHKIPAYF 235
Cdd:PRK11142 181 IITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVL---ITLGsrGVWL---SENGEGQRVP-GFRVqAVDTIAAGD 253

                         90
                 ....*....|...
gi 334188058 236 TGTGDLMTALLLG 248
Cdd:PRK11142 254 TFNGALVTALLEG 266
PRK12616 PRK12616
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
109-215 6.94e-10

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183624  Cd Length: 270  Bit Score: 58.90  E-value: 6.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058 109 DLIEgLEANDLLFYTHVLTVCDPVM---GDEGKLYvPEElVHVYREKVVPLASMLTPNQFEAEKLTGL-RINSEEDGREA 184
Cdd:PRK12616  87 DIIE-LAADTIKEKQLKNVVIDPVMvckGANEVLY-PEH-AEALREQLAPLATVITPNLFEAGQLSGMgEIKTVEQMKEA 163

                         90       100       110
                 ....*....|....*....|....*....|.
gi 334188058 185 CAILHAAGPSKVVITSitiGGILlligSHQK 215
Cdd:PRK12616 164 AKKIHELGAQYVVITG---GGKL----KHEK 187
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 150-199 3.95e-08

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: 53.71  E-value: 3.95e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 334188058 150 REKVVPLASMLTPNQFEAEKLTGLRINSEEDGREACAILHAAGPSKVVIT 199
Cdd:cd01174  169 PAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVT 218
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 63-265 4.95e-08

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 53.50  E-value: 4.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058   63 YVGNKSAVFPLQLLGYDVDPINSVQFSNHTGYPTfkgQVLNGQQLCDLIEGLEANDllfyTHVLTVCDPVMGDEGKLyvp 142
Cdd:pfam00294 105 FNRGAAADLTPEELEENEDLLENADLLYISGSLP---LGLPEATLEELIEAAKNGG----TFDPNLLDPLGAAREAL--- 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058  143 eelvhvyrEKVVPLASMLTPNQFEAEKLTGLRINSEEDGREACAILHAAGPSKVVITSITIGGILLLIGSHQKEKGLKPE 222
Cdd:pfam00294 175 --------LELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEVHVPAVPKV 246

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 334188058  223 QfkilihkiPAYFTGTGDLMTA-LLLGWSNKYPdnLDKAAELAV 265
Cdd:pfam00294 247 K--------VVDTTGAGDSFVGgFLAGLLAGKS--LEEALRFAN 280
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
 128-198 1.60e-07

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 52.46  E-value: 1.60e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334188058 128 VCDPVM----GDEgkLYVPEELvHVYREKVVPLASMLTPNQFEAEKLTGL-RINSEEDGREACAILHAAGPSKVVI 198
Cdd:PLN02898 109 VVDPVMvstsGDV--LAGPSIL-SALREELLPLATIVTPNVKEASALLGGdPLETVADMRSAAKELHKLGPRYVLV 181
PRK12413 PRK12413
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
143-198 4.12e-07

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183513 [Multi-domain]  Cd Length: 253  Bit Score: 50.45  E-value: 4.12e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 334188058 143 EELVhvyreKVVPLASMLTPNQFEAEKLTGLRINSEEDGREACAILHAAGPSKVVI 198
Cdd:PRK12413 121 QELI-----QFFPYVTVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAVVI 171
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 125-265 8.86e-07

Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar or nucleoside kinase, ribokinase family is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 440290 [Multi-domain]  Cd Length: 301  Bit Score: 49.50  E-value: 8.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058 125 VLTVCDPVMGDEGKLYVPEELvhvyrEKVVPLASMLTPNQFEAEKLTGlrinsEEDGREACAILHAAGPSKVVitsITIG 204
Cdd:COG0524  159 VPVSLDPNYRPALWEPARELL-----RELLALVDILFPNEEEAELLTG-----ETDPEEAAAALLARGVKLVV---VTLG 225

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 334188058 205 --GILLLIGSHqkekglkpeqfkilIHKIPAYF------TGTGD-----LMTALLLGWSnkypdnLDKAAELAV 265
Cdd:COG0524  226 aeGALLYTGGE--------------VVHVPAFPvevvdtTGAGDafaagFLAGLLEGLD------LEEALRFAN 279
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
 160-269 8.90e-07

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: 49.62  E-value: 8.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058 160 LTPNQFEAEKLTGLRINSEEDGREACAILHAAGPSKVVitsITIG--GILLLIGSHQKEKGLKPEqfkILIHKIpAYFTG 237
Cdd:cd01941  180 LTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVI---VTLGakGVLLSSREGGVETKLFPA---PQPETV-VNVTG 252

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 334188058 238 TGD-LMTALLLGWSNKYP--DNLDKAAELAVSTLQ 269
Cdd:cd01941  253 AGDaFVAGLVAGLLEGMSldDSLRFAQAAAALTLE 287
PTZ00347 PTZ00347
phosphomethylpyrimidine kinase; Provisional
 99-198 1.57e-03

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240375 [Multi-domain]  Cd Length: 504  Bit Score: 39.95  E-value: 1.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058  99 GQVLNGQQLCDLIEGLEAndllfythVLTVCDPVM----GDE-GKLYVPEELVHVYREKVVPLASMLTPNQFEAEKLTGL 173
Cdd:PTZ00347 306 GLVPTARQLEIVIEKLKN--------LPMVVDPVLvatsGDDlVAQKNADDVLAMYKERIFPMATIITPNIPEAERILGR 377

                         90       100
                 ....*....|....*....|....*.
gi 334188058 174 R-INSEEDGREACAILHAAGPSKVVI 198
Cdd:PTZ00347 378 KeITGVYEARAAAQALAQYGSRYVLV 403
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
162-265 3.57e-03

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


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 38.58  E-value: 3.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334188058 162 PNQFEAEKLTGLRINSEEDGREACAILHAAGpSKVVITSITIGGILLLIGShqkekglkpEQFKILIHKIPAYFT-GTGD 240
Cdd:COG1105  183 PNLEELEELLGRPLETLEDIIAAARELLERG-AENVVVSLGADGALLVTED---------GVYRAKPPKVEVVSTvGAGD 252

                         90       100
                 ....*....|....*....|....*.
gi 334188058 241 LMTA-LLLGWSNKYPdnLDKAAELAV 265
Cdd:COG1105  253 SMVAgFLAGLARGLD--LEEALRLAV 276
 
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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