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Conserved domains on  [gi|1596687012|gb|TDT44611|]
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hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Halospina denitrificans]

Protein Classification

hydroxymethylpyrimidine/phosphomethylpyrimidine kinase( domain architecture ID 10100230)

bifunctional enzyme, phosphomethylpyrimidine (HMP-P) kinase/hydroxymethylpyrimidine (HMP) kinase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 9-252 1.67e-95

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: 280.77  E-value: 1.67e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012   9 LVLSGLDPSGGAGIQADIQAITALGCHPLPVLTCLTVQDTRNVYGAEPVDADLIHRQLLHLEADTPIHAIKTGALGDETV 88
Cdd:COG0351     1 LTIAGSDPSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVTGVHPVPPEFVAAQLRAVLEDIPVDAIKIGMLGSAEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  89 IQALTEFLDNREPIPYVLDPVIKAAGGGELADEKLIAAMLEQLFPRASLVTPNGPELTQLGGNPDETTS-----AKTLLE 163
Cdd:COG0351    81 IEAVAEILADYPLVPVVLDPVMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALLGIEITTLDdmreaAKALLE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012 164 YGCGAVLATGGHGTGEFIENRLFTSDGGdRTWQQPRI-GGEYHGSGCTLAAGISAGMARGQALEAAIETGQEFVAASIRS 242
Cdd:COG0351   161 LGAKAVLVKGGHLPGDEAVDVLYDGDGV-REFSAPRIdTGNTHGTGCTLSSAIAALLAKGLDLEEAVREAKEYVTQAIRA 239

                         250
                  ....*....|.
gi 1596687012 243 ALRVGHGQ-PV 252
Cdd:COG0351   240 ALRLGMGHgPV 250
 
Name Accession Description Interval E-value
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 9-252 1.67e-95

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: 280.77  E-value: 1.67e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012   9 LVLSGLDPSGGAGIQADIQAITALGCHPLPVLTCLTVQDTRNVYGAEPVDADLIHRQLLHLEADTPIHAIKTGALGDETV 88
Cdd:COG0351     1 LTIAGSDPSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVTGVHPVPPEFVAAQLRAVLEDIPVDAIKIGMLGSAEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  89 IQALTEFLDNREPIPYVLDPVIKAAGGGELADEKLIAAMLEQLFPRASLVTPNGPELTQLGGNPDETTS-----AKTLLE 163
Cdd:COG0351    81 IEAVAEILADYPLVPVVLDPVMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALLGIEITTLDdmreaAKALLE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012 164 YGCGAVLATGGHGTGEFIENRLFTSDGGdRTWQQPRI-GGEYHGSGCTLAAGISAGMARGQALEAAIETGQEFVAASIRS 242
Cdd:COG0351   161 LGAKAVLVKGGHLPGDEAVDVLYDGDGV-REFSAPRIdTGNTHGTGCTLSSAIAALLAKGLDLEEAVREAKEYVTQAIRA 239

                         250
                  ....*....|.
gi 1596687012 243 ALRVGHGQ-PV 252
Cdd:COG0351   240 ALRLGMGHgPV 250
HMPP_kinase cd01169
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ...
 7-243 2.43e-88

4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two consecutive phosphorylation steps in the thiamine phosphate biosynthesis pathway, leading to the synthesis of vitamin B1. The first step is the phosphorylation of the hydroxyl group of HMP to form 4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate (HMP-P) and then the phophorylation of HMP-P to form 4-amino-5-hydroxymethyl-2-methyl-pyrimidine pyrophosphate (HMP-PP), which is the substrate for the thiamine synthase coupling reaction.


Pssm-ID: 238574 [Multi-domain]  Cd Length: 242  Bit Score: 262.05  E-value: 2.43e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012   7 HVLVLSGLDPSGGAGIQADIQAITALGCHPLPVLTCLTVQDTRNVYGAEPVDADLIHRQLLHLEADTPIHAIKTGALGDE 86
Cdd:cd01169     1 VVLTIAGSDSSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVFGVHPVPPEFVAAQLDAVLEDIPVDAIKIGMLGSA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  87 TVIQALTEFLDNREPIPYVLDPVIKAAGGGELADEKLIAAMLEQLFPRASLVTPNGPELTQLGGNPDETT-----SAKTL 161
Cdd:cd01169    81 EIIEAVAEALKDYPDIPVVLDPVMVAKSGDSLLDDDAIEALRELLLPLATLITPNLPEAELLTGLEIATEedmmkAAKAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012 162 LEYGCGAVLATGGHGTGEFIENRLFTSDGGDRTWQQPRIGGEYHGSGCTLAAGISAGMARGQALEAAIETGQEFVAASIR 241
Cdd:cd01169   161 LALGAKAVLIKGGHLPGDEAVDVLYDGGGFFEFESPRIDTKNTHGTGCTLSSAIAANLAKGLSLEEAVREAKEYVTQAIR 240


                  ..
gi 1596687012 242 SA 243
Cdd:cd01169   241 NA 242
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 15-249 5.54e-87

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: 258.57  E-value: 5.54e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  15 DPSGGAGIQADIQAITALGCHPLPVLTCLTVQDTRNVYGAEPVDADLIHRQLLHLEADTPIHAIKTGALGDETVIQALTE 94
Cdd:pfam08543   1 DSSGGAGIQADLKTFSALGVYGMSVITALTAQNTLGVQGVHPLPPEFVAAQLDAVLEDIPVDAVKTGMLGSAEIIEAVAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  95 FLDnREPIPYVLDPVIKAAGGGELADEKLIAAMLEQLFPRASLVTPNGPELTQLGGNPDETTS-----AKTLLEYGCGAV 169
Cdd:pfam08543  81 KLD-KYGVPVVLDPVMVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEdmkeaAKKLLALGAKAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012 170 LATGGHGTGE--FIENRLFTsDGGDRTWQQPRI-GGEYHGSGCTLAAGISAGMARGQALEAAIETGQEFVAASIRSALRV 246
Cdd:pfam08543 160 LIKGGHLEGEeaVVTDVLYD-GGGFYTLEAPRIpTKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKEYVTEAIRDALNL 238


                  ...
gi 1596687012 247 GHG 249
Cdd:pfam08543 239 GKG 241
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 6-251 5.61e-76

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 231.55  E-value: 5.61e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012   6 PHVLVLSGLDPSGGAGIQADIQAITALGCHPLPVLTCLTVQDTRNVYGAEPVDADLIHRQLLHLEADTPIHAIKTGALGD 85
Cdd:PRK06427    5 PIALTIAGSDSGGGAGIQADLKTFQALGVYGMSAITALTAQNTLGVQRVHPIPPEFVAAQLDAVFSDIRIDAVKIGMLAS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  86 ETVIQALTEFLDNREPIPYVLDPVIKAAGGGELADEKLIAAMLEQLFPRASLVTPNGPELTQLGGNPDETT------SAK 159
Cdd:PRK06427   85 AEIIETVAEALKRYPIPPVVLDPVMIAKSGDPLLADDAVAALRERLLPLATLITPNLPEAEALTGLPIADTedemkaAAR 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012 160 TLLEYGCGAVLATGGH-GTGEFIENRLFTSDgGDRTWQQPRIGGE-YHGSGCTLAAGISAGMARGQALEAAIETGQEFVA 237
Cdd:PRK06427  165 ALHALGCKAVLIKGGHlLDGEESVDWLFDGE-GEERFSAPRIPTKnTHGTGCTLSAAIAAELAKGASLLDAVQTAKDYVT 243

                         250
                  ....*....|....
gi 1596687012 238 ASIRSALRVGHGQP 251
Cdd:PRK06427  244 RAIRHALEIGQGHG 257
HMP-P_kinase TIGR00097
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ...
 8-250 1.99e-61

hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a bifunctional enzyme, phosphomethylpyrimidine kinase (EC 2.7.4.7)/Hydroxymethylpyrimidine kinase (EC 2.7.1.49), the ThiD/J protein of thiamine biosynthesis. The protein is commonly observed within operons containing other thiamine biosynthesis genes. Numerous examples are fusion proteins with other thiamine-biosynthetic domains. Saccaromyces has three recent paralogs, two of which are isofunctional and score above the trusted cutoff. The third shows a longer branch length in a phylogenetic tree and scores below the trusted cutoff, as do putative second copies in a number of species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 272904 [Multi-domain]  Cd Length: 254  Bit Score: 194.05  E-value: 1.99e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012   8 VLVLSGLDPSGGAGIQADIQAITALGCHPLPVLTCLTVQDTRNVYGAEPVDADLIHRQLLHLEADTPIHAIKTGALGDET 87
Cdd:TIGR00097   1 ALTIAGSDSGGGAGIQADLKTFSALGVFGTSVITALTAQNTRGVTGVYPIPPDFVEAQLDAVFSDIPVDAAKTGMLASAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  88 VIQALTEFLDNREPIPYVLDPVIKAAGGGELADEKLIAAMLEQLFPRASLVTPNGPELTQLGGNP-----DETTSAKTLL 162
Cdd:TIGR00097  81 IVEAVARKLREYPVRPLVVDPVMVAKSGAPLLEEEAIEALRKRLLPLATLITPNLPEAEALLGTKirteqDMIKAAKKLR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012 163 EYGCGAVLATGGHGTGEFIENRLFTsDGGDRTWQQPRIGGEY-HGSGCTLAAGISAGMARGQALEAAIETGQEFVAASIR 241
Cdd:TIGR00097 161 ELGPKAVLIKGGHLEGDQAVDVLFD-GGEIHILKAPRIETKNtHGTGCTLSAAIAANLAKGLSLKEAVKEAKEFVTGAIR 239


                  ....*....
gi 1596687012 242 SALRVGHGQ 250
Cdd:TIGR00097 240 YGLNIGHGH 248
 
Name Accession Description Interval E-value
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 9-252 1.67e-95

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: 280.77  E-value: 1.67e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012   9 LVLSGLDPSGGAGIQADIQAITALGCHPLPVLTCLTVQDTRNVYGAEPVDADLIHRQLLHLEADTPIHAIKTGALGDETV 88
Cdd:COG0351     1 LTIAGSDPSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVTGVHPVPPEFVAAQLRAVLEDIPVDAIKIGMLGSAEI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  89 IQALTEFLDNREPIPYVLDPVIKAAGGGELADEKLIAAMLEQLFPRASLVTPNGPELTQLGGNPDETTS-----AKTLLE 163
Cdd:COG0351    81 IEAVAEILADYPLVPVVLDPVMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALLGIEITTLDdmreaAKALLE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012 164 YGCGAVLATGGHGTGEFIENRLFTSDGGdRTWQQPRI-GGEYHGSGCTLAAGISAGMARGQALEAAIETGQEFVAASIRS 242
Cdd:COG0351   161 LGAKAVLVKGGHLPGDEAVDVLYDGDGV-REFSAPRIdTGNTHGTGCTLSSAIAALLAKGLDLEEAVREAKEYVTQAIRA 239

                         250
                  ....*....|.
gi 1596687012 243 ALRVGHGQ-PV 252
Cdd:COG0351   240 ALRLGMGHgPV 250
HMPP_kinase cd01169
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ...
 7-243 2.43e-88

4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two consecutive phosphorylation steps in the thiamine phosphate biosynthesis pathway, leading to the synthesis of vitamin B1. The first step is the phosphorylation of the hydroxyl group of HMP to form 4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate (HMP-P) and then the phophorylation of HMP-P to form 4-amino-5-hydroxymethyl-2-methyl-pyrimidine pyrophosphate (HMP-PP), which is the substrate for the thiamine synthase coupling reaction.


Pssm-ID: 238574 [Multi-domain]  Cd Length: 242  Bit Score: 262.05  E-value: 2.43e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012   7 HVLVLSGLDPSGGAGIQADIQAITALGCHPLPVLTCLTVQDTRNVYGAEPVDADLIHRQLLHLEADTPIHAIKTGALGDE 86
Cdd:cd01169     1 VVLTIAGSDSSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVFGVHPVPPEFVAAQLDAVLEDIPVDAIKIGMLGSA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  87 TVIQALTEFLDNREPIPYVLDPVIKAAGGGELADEKLIAAMLEQLFPRASLVTPNGPELTQLGGNPDETT-----SAKTL 161
Cdd:cd01169    81 EIIEAVAEALKDYPDIPVVLDPVMVAKSGDSLLDDDAIEALRELLLPLATLITPNLPEAELLTGLEIATEedmmkAAKAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012 162 LEYGCGAVLATGGHGTGEFIENRLFTSDGGDRTWQQPRIGGEYHGSGCTLAAGISAGMARGQALEAAIETGQEFVAASIR 241
Cdd:cd01169   161 LALGAKAVLIKGGHLPGDEAVDVLYDGGGFFEFESPRIDTKNTHGTGCTLSSAIAANLAKGLSLEEAVREAKEYVTQAIR 240


                  ..
gi 1596687012 242 SA 243
Cdd:cd01169   241 NA 242
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 15-249 5.54e-87

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: 258.57  E-value: 5.54e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  15 DPSGGAGIQADIQAITALGCHPLPVLTCLTVQDTRNVYGAEPVDADLIHRQLLHLEADTPIHAIKTGALGDETVIQALTE 94
Cdd:pfam08543   1 DSSGGAGIQADLKTFSALGVYGMSVITALTAQNTLGVQGVHPLPPEFVAAQLDAVLEDIPVDAVKTGMLGSAEIIEAVAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  95 FLDnREPIPYVLDPVIKAAGGGELADEKLIAAMLEQLFPRASLVTPNGPELTQLGGNPDETTS-----AKTLLEYGCGAV 169
Cdd:pfam08543  81 KLD-KYGVPVVLDPVMVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEdmkeaAKKLLALGAKAV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012 170 LATGGHGTGE--FIENRLFTsDGGDRTWQQPRI-GGEYHGSGCTLAAGISAGMARGQALEAAIETGQEFVAASIRSALRV 246
Cdd:pfam08543 160 LIKGGHLEGEeaVVTDVLYD-GGGFYTLEAPRIpTKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKEYVTEAIRDALNL 238


                  ...
gi 1596687012 247 GHG 249
Cdd:pfam08543 239 GKG 241
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 6-251 5.61e-76

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 231.55  E-value: 5.61e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012   6 PHVLVLSGLDPSGGAGIQADIQAITALGCHPLPVLTCLTVQDTRNVYGAEPVDADLIHRQLLHLEADTPIHAIKTGALGD 85
Cdd:PRK06427    5 PIALTIAGSDSGGGAGIQADLKTFQALGVYGMSAITALTAQNTLGVQRVHPIPPEFVAAQLDAVFSDIRIDAVKIGMLAS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  86 ETVIQALTEFLDNREPIPYVLDPVIKAAGGGELADEKLIAAMLEQLFPRASLVTPNGPELTQLGGNPDETT------SAK 159
Cdd:PRK06427   85 AEIIETVAEALKRYPIPPVVLDPVMIAKSGDPLLADDAVAALRERLLPLATLITPNLPEAEALTGLPIADTedemkaAAR 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012 160 TLLEYGCGAVLATGGH-GTGEFIENRLFTSDgGDRTWQQPRIGGE-YHGSGCTLAAGISAGMARGQALEAAIETGQEFVA 237
Cdd:PRK06427  165 ALHALGCKAVLIKGGHlLDGEESVDWLFDGE-GEERFSAPRIPTKnTHGTGCTLSAAIAAELAKGASLLDAVQTAKDYVT 243

                         250
                  ....*....|....
gi 1596687012 238 ASIRSALRVGHGQP 251
Cdd:PRK06427  244 RAIRHALEIGQGHG 257
HMP-P_kinase TIGR00097
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ...
 8-250 1.99e-61

hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a bifunctional enzyme, phosphomethylpyrimidine kinase (EC 2.7.4.7)/Hydroxymethylpyrimidine kinase (EC 2.7.1.49), the ThiD/J protein of thiamine biosynthesis. The protein is commonly observed within operons containing other thiamine biosynthesis genes. Numerous examples are fusion proteins with other thiamine-biosynthetic domains. Saccaromyces has three recent paralogs, two of which are isofunctional and score above the trusted cutoff. The third shows a longer branch length in a phylogenetic tree and scores below the trusted cutoff, as do putative second copies in a number of species. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 272904 [Multi-domain]  Cd Length: 254  Bit Score: 194.05  E-value: 1.99e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012   8 VLVLSGLDPSGGAGIQADIQAITALGCHPLPVLTCLTVQDTRNVYGAEPVDADLIHRQLLHLEADTPIHAIKTGALGDET 87
Cdd:TIGR00097   1 ALTIAGSDSGGGAGIQADLKTFSALGVFGTSVITALTAQNTRGVTGVYPIPPDFVEAQLDAVFSDIPVDAAKTGMLASAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  88 VIQALTEFLDNREPIPYVLDPVIKAAGGGELADEKLIAAMLEQLFPRASLVTPNGPELTQLGGNP-----DETTSAKTLL 162
Cdd:TIGR00097  81 IVEAVARKLREYPVRPLVVDPVMVAKSGAPLLEEEAIEALRKRLLPLATLITPNLPEAEALLGTKirteqDMIKAAKKLR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012 163 EYGCGAVLATGGHGTGEFIENRLFTsDGGDRTWQQPRIGGEY-HGSGCTLAAGISAGMARGQALEAAIETGQEFVAASIR 241
Cdd:TIGR00097 161 ELGPKAVLIKGGHLEGDQAVDVLFD-GGEIHILKAPRIETKNtHGTGCTLSAAIAANLAKGLSLKEAVKEAKEFVTGAIR 239


                  ....*....
gi 1596687012 242 SALRVGHGQ 250
Cdd:TIGR00097 240 YGLNIGHGH 248
PRK08573 PRK08573
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
6-252 7.80e-50

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 236297 [Multi-domain]  Cd Length: 448  Bit Score: 169.52  E-value: 7.80e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012   6 PHVLVLSGLDPSGGAGIQADIQAITALGCHPLPVLTCLTVQDTRNVYGAEPVDADLIHRQLLHLEADTPIHAIKTGALGD 85
Cdd:PRK08573    3 PVALTIAGSDSGGGAGIEADLKTFAALGVHGAVAITSVTAQNTYEVRAIHDLPPEVVAAQIEAVWEDMGIDAAKTGMLSN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  86 ETVIQALTEFLDNREpIPYVLDPVIKAAGGGELADEKLIAAMLEQLFPRASLVTPNGPELTQLGGNP-----DETTSAKT 160
Cdd:PRK08573   83 REIIEAVAKTVSKYG-FPLVVDPVMIAKSGAPLLREDAVDALIKRLLPLATVVTPNRPEAEKLTGMKirsveDARKAAKY 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012 161 LL-EYGCGAVLATGGHGTGEFIENRLFTsDGGDRTWQQPRI-GGEYHGSGCTLAAGISAGMARGQALEAAIETGQEFVAA 238
Cdd:PRK08573  162 IVeELGAEAVVVKGGHLEGEEAVDVLYH-NGTFREFRAPRVeSGCTHGTGCSFSAAIAAGLAKGLDPEEAIKTAKKFITM 240

                         250
                  ....*....|....*
gi 1596687012 239 SIRSALRVGHGQ-PV 252
Cdd:PRK08573  241 AIKYGVKIGKGHcPV 255
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
 6-253 1.30e-45

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 159.55  E-value: 1.30e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012   6 PHVLVLSGLDPSGGAGIQADIQAITALGCHPLPVLTCLTVQDTRNVYGAEPVDADLIHRQLLHLEADTPIHAIKTGALGD 85
Cdd:PLN02898   10 PHVLTVAGSDSGAGAGIQADIKACAARGVYCTTAITAVTAQNTVGVQGVHAVPLDFVAEQLKSVLSDMPVDVVKTGMLPS 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  86 ETVIQALTEFLDNREPIPYVLDPVIKAAGGGELADEKLIAAMLEQLFPRASLVTPNGPELTQL-GGNPDET-----TSAK 159
Cdd:PLN02898   90 AEIVKVLCQALKEFPVKALVVDPVMVSTSGDVLAGPSILSALREELLPLATIVTPNVKEASALlGGDPLETvadmrSAAK 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012 160 TLLEYGCGAVLATGGH--GTGEFIENrLFtsDGGD-RTWQQPRIGGEY-HGSGCTLAAGISAGMARGQALEAAIETGQEF 235
Cdd:PLN02898  170 ELHKLGPRYVLVKGGHlpDSLDAVDV-LY--DGTEfHELRSSRIKTRNtHGTGCTLASCIAAELAKGSDMLSAVKVAKRY 246

                         250       260
                  ....*....|....*....|
gi 1596687012 236 VAASIRSA--LRVGHGQPVP 253
Cdd:PLN02898  247 VETALEYSkdIGIGNGAQGP 266
PRK14713 PRK14713
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
6-252 9.48e-45

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 237797 [Multi-domain]  Cd Length: 530  Bit Score: 157.64  E-value: 9.48e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012   6 PHVLVLSGLDPSGGAGIQADIQAITALGCHPLPVLTCLTVQDTRNVYGAEPVDADLIHRQLLHLEADTPIHAIKTGALGD 85
Cdd:PRK14713   30 PRVLSIAGTDPSGGAGIQADLKSIAAAGGYGMAVITALVAQNTRGVRAVHVPPADFLRAQLDAVSDDVTVDAVKIGMLGD 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  86 ETVIQALTEFLDNREPIPYVLDPVIKAAGGGELADEKLIAAMLEqLFPRASLVTPNGPELTQLGGNPDETT------SAK 159
Cdd:PRK14713  110 AEVIDAVRTWLAEHRPPVVVLDPVMVATSGDRLLEEDAEAALRE-LVPRADLITPNLPELAVLLGEPPATTweealaQAR 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012 160 TLLEYGCGAVLATGGHGTGEFIENRLFTSDGGDRTWQQPRIGG-EYHGSGCTLAAGISAGMARGQALEAAIETGQEFVAA 238
Cdd:PRK14713  189 RLAAETGTTVLVKGGHLDGQRAPDALVGPDGAVTEVPGPRVDTrNTHGTGCSLSSALATRLGRGGDWAAALRWATAWLHG 268

                         250
                  ....*....|....*..
gi 1596687012 239 SIR--SALRVGHGQ-PV 252
Cdd:PRK14713  269 AIAagAALQVGTGNgPV 285
PTZ00347 PTZ00347
phosphomethylpyrimidine kinase; Provisional
 6-250 4.44e-41

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240375 [Multi-domain]  Cd Length: 504  Bit Score: 147.42  E-value: 4.44e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012   6 PHVLVLSGLDPSGGAGIQADIQAITALGCHPLPVLTCLTVQDTRNVYGAEPVDADLIHRQLLHLEADTPIHAIKTGALGD 85
Cdd:PTZ00347  231 PTVLTVSGSDSGGGAGHQADLKTLEALGVYSTSALTSLTAQNTKGVQQIQVVNEDFFAAQIDSVMSDFNISVVKLGLVPT 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  86 ETVIQALTEFLDNrepIPYVLDPVIKAAGGGELADEK----LIAAMLEQLFPRASLVTPNGPELTQLGGNPDETT----- 156
Cdd:PTZ00347  311 ARQLEIVIEKLKN---LPMVVDPVLVATSGDDLVAQKnaddVLAMYKERIFPMATIITPNIPEAERILGRKEITGvyear 387

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012 157 -SAKTLLEYGCGAVLATGGHG--TGEFIENRLFTSDgGDR--TWQQPRIGG-EYHGSGCTLAAGISAGMARGQALEAAIE 230
Cdd:PTZ00347  388 aAAQALAQYGSRYVLVKGGHDliDPEACRDVLYDRE-KDRfyEFTANRIATiNTHGTGCTLASAISSFLARGYTVPDAVE 466

                         250       260
                  ....*....|....*....|
gi 1596687012 231 TGQEFVAASIRSALRVGHGQ 250
Cdd:PTZ00347  467 RAIGYVHEAIVRSCGVPLGQ 486
PRK09517 PRK09517
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ...
 6-249 1.93e-34

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


Pssm-ID: 169939 [Multi-domain]  Cd Length: 755  Bit Score: 130.86  E-value: 1.93e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012   6 PHVLVLSGLDPSGGAGIQADIQAITALGCHPLPVLTCLTVQDTRNVYGAEPVDADLIHRQLLHLEADTPIHAIKTGALGD 85
Cdd:PRK09517  242 PRVLSIAGTDPTGGAGIQADLKSIAAGGGYGMCVVTALVAQNTHGVNTIHTPPLTFLEEQLEAVFSDVTVDAVKLGMLGS 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  86 ETVIQALTEFLDNREPIPYVLDPVIKAAGGGELADEKLIAAMLEqLFPRASLVTPNGPELTQLGGNPDETT------SAK 159
Cdd:PRK09517  322 ADTVDLVASWLGSHEHGPVVLDPVMVATSGDRLLDADATEALRR-LAVHVDVVTPNIPELAVLCGEAPAITmdeaiaQAR 400

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012 160 TLLEYGCGAVLATGGHGTGEFIENRLFTSDGGDRTWQQPRIG-GEYHGSGCTLAAGISAGMARGQALEAAIETGQEFVAA 238
Cdd:PRK09517  401 GFARTHGTIVIVKGGHLTGDLADNAVVRPDGSVHQVENPRVNtTNSHGTGCSLSAALATLIAAGESVEKALEWATRWLNE 480

                         250
                  ....*....|...
gi 1596687012 239 SIRSA--LRVGHG 249
Cdd:PRK09517  481 ALRHAdhLAVGSG 493
PRK12413 PRK12413
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
1-247 1.26e-32

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183513 [Multi-domain]  Cd Length: 253  Bit Score: 119.78  E-value: 1.26e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012   1 MLNEKphVLVLSGLDPSGGAGIQADIQAITALGCHPLPVLTCLTVQdTRNVYGAEPVDADLIHRQLLHLeADTPIHAIKT 80
Cdd:PRK12413    1 MKTNY--ILAISGNDIFSGGGLHADLATYTRNGLHGFVAVTCLTAM-TEKGFEVFPVDKEIFQQQLDSL-KDVPFSAIKI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  81 GALGDETVIQALTEFLDNREPIPYVLDPVIKAAgggELADEKlIAAM---LEQLFPRASLVTPNGPE---LTQLGGNP-- 152
Cdd:PRK12413   77 GLLPNVEIAEQALDFIKGHPGIPVVLDPVLVCK---ETHDVE-VSELrqeLIQFFPYVTVITPNLVEaelLSGKEIKTle 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012 153 DETTSAKTLLEYGCGAVLATGGhgtgefieNRL-------FTSDGGD-RTWQQPRIGGEYHGSGCTLAAGISAGMARGQA 224
Cdd:PRK12413  153 DMKEAAKKLYDLGAKAVVIKGG--------NRLsqkkaidLFYDGKEfVILESPVLEKNNIGAGCTFASSIASQLVKGKS 224

                         250       260
                  ....*....|....*....|...
gi 1596687012 225 LEAAIETGQEFVAASIRSALRVG 247
Cdd:PRK12413  225 PLEAVKNSKDFVYQAIQQSDQYG 247
PRK12412 PRK12412
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
6-246 1.28e-31

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183512 [Multi-domain]  Cd Length: 268  Bit Score: 117.38  E-value: 1.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012   6 PHVLVLSGLDPSGGAGIQADIQAITALGCHPLPVLTCLTVQDTRNVYGAE--PVDADLIHRQLLHLEADTPIHAIKTGAL 83
Cdd:PRK12412    2 NKALTIAGSDTSGGAGIQADLKTFQELGVYGMTSLTTIVTMDPHNGWAHNvfPIPASTLKPQLETTIEGVGVDALKTGML 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  84 GDETVIQALTEFLDNREPIPYVLDPVIKAAGGGELADEKLIAAMLEQLFPRASLVTPNGPELTQLGGNPDETT-----SA 158
Cdd:PRK12412   82 GSVEIIEMVAETIEKHNFKNVVVDPVMVCKGADEALHPETNDCLRDVLVPKALVVTPNLFEAYQLSGVKINSLedmkeAA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012 159 KTLLEYGCGAVLATGGHGTG-EFIENRLFTSDGGDrTWQQPRIGGEY-HGSGCTLAAGISAGMARGQALEAAIETGQEFV 236
Cdd:PRK12412  162 KKIHALGAKYVLIKGGSKLGtETAIDVLYDGETFD-LLESEKIDTTNtHGAGCTYSAAITAELAKGKPVKEAVKTAKEFI 240

                         250
                  ....*....|
gi 1596687012 237 AASIRSALRV 246
Cdd:PRK12412  241 TAAIRYSFKI 250
PRK12616 PRK12616
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
9-246 2.09e-30

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183624  Cd Length: 270  Bit Score: 114.37  E-value: 2.09e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012   9 LVLSGLDPSGGAGIQADIQAITALGCHPLPVLTCLTVQDTRNVYGAE--PVDADLIHRQLLHLEADTPIHAIKTGALGDE 86
Cdd:PRK12616    7 LTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAMDPENSWDHQvfPIDTDTIRAQLSTIVDGIGVDAMKTGMLPTV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  87 TVIQALTEFLDNREPIPYVLDPVIKAAGGGELADEKLIAAMLEQLFPRASLVTPNGPELTQLGGNPDETT------SAKT 160
Cdd:PRK12616   87 DIIELAADTIKEKQLKNVVIDPVMVCKGANEVLYPEHAEALREQLAPLATVITPNLFEAGQLSGMGEIKTveqmkeAAKK 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012 161 LLEYGCGAVLATGGhgtGEFIENR----LFTSDGGDRTwQQPRIGGEY-HGSGCTLAAGISAGMARGQALEAAIETGQEF 235
Cdd:PRK12616  167 IHELGAQYVVITGG---GKLKHEKavdvLYDGETAEVL-ESEMIDTPYtHGAGCTFSAAVTAELAKGSEVKEAIYAAKEF 242

                         250
                  ....*....|.
gi 1596687012 236 VAASIRSALRV 246
Cdd:PRK12616  243 ITAAIKESFPL 253
COG1992 COG1992
Predicted transcriptional regulator fused phosphomethylpyrimidine kinase (thiamin biosynthesis) ...
 17-254 1.10e-19

Predicted transcriptional regulator fused phosphomethylpyrimidine kinase (thiamin biosynthesis) [General function prediction only];


Pssm-ID: 441595 [Multi-domain]  Cd Length: 432  Bit Score: 87.50  E-value: 1.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  17 SGGAGIQADIQAITALGCHPLPVLTCLTVQDTRNVYGA--EPVDADLIHRQLLHLEADTPIHAIKTGALGDETVIQALTE 94
Cdd:COG1992     1 GGGGGGGADAKTAAALGAGGGGTTTAVTVTATTTVTGVgsDPPPPVEVQQQAVAADDDVDDAKTGMLMTATIVEVVAVVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  95 fldNREPIPYVLDPVIKAAGGGELADEKLIAAMLEQLFPRASLVTPNGPELTQLGGNPDETTSA------KTLLEYGCGA 168
Cdd:COG1992    81 ---KSRDKPLVVVVVPVAVAAAGLGLLLAEAELAKLLLPLLATVTPNEPEVEELLLPTIRSLLAearaarLALQEEGADA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012 169 VLATGGHGTGEFIENRLFtSDGGDRTWQQPRI-GGEYHGSGCTLAAGISAGMARGQALEAAIETGQEFVAASIRSALRVG 247
Cdd:COG1992   158 LGVKGGHVSGDAVVDVLE-DERDVETFRHPRLvTEATHGSGCTFSAAIAALLAKGLSLEEAVRGAKLFLLHAIRYGLLVG 236


                  ....*..
gi 1596687012 248 HGQPVPD 254
Cdd:COG1992   237 KGVGPVN 243
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 18-248 2.60e-19

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: 84.43  E-value: 2.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  18 GGAGIQADIQAITALGCHPLPVLTCL----------TVQDTrnvygaepvDADLIHRQLLHLEA-DTPIH--AIKTGALG 84
Cdd:COG2240    14 GHVGNSAAVPPLSALGVEVWPLPTVLlsnhtgygtfTGRDL---------PTDDIADILDGWKElGVLLEfdAVLSGYLG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  85 DETVIQALTEFLD---NREP-IPYVLDPVIKAAGGGELADEKLIAAMLEQLFPRASLVTPNGPELTQLGGNPDETTS--- 157
Cdd:COG2240    85 SAEQGDIIADFVArvkAANPdALYLCDPVMGDNGKGYYVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETLEeal 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012 158 --AKTLLEYGCGAVLATG---GHGTGEFIENRLFTsdgGDRTW--QQPRIGGEYHGSGCTLAAGISAGMARGQALEAAIE 230
Cdd:COG2240   165 aaARALLALGPKIVVVTSvplDDTPADKIGNLAVT---ADGAWlvETPLLPFSPNGTGDLFAALLLAHLLRGKSLEEALE 241

                         250
                  ....*....|....*...
gi 1596687012 231 TGQEFVAASIRSALRVGH 248
Cdd:COG2240   242 RAAAFVYEVLERTAAAGS 259
PTZ00493 PTZ00493
phosphomethylpyrimidine kinase; Provisional
 2-247 9.25e-18

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240440  Cd Length: 321  Bit Score: 81.19  E-value: 9.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012   2 LNEKPHVLVLSGLDPSGGAGIQADIQAITALGCHPLPVLTCLTVQDTRNVYGAEPVDADLIHRQLLHLEADTPIHAIKTG 81
Cdd:PTZ00493    1 MEGVSNILSIAGSDSCGGAGMQADIKTAMGLGCHCCTALVVLTAQNTKEVKRIVEIEEKFIVEQLDSIFADVTIDVVKLG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  82 ALGDETVIQALTEFLDN-----REPIPYVLDPVIKAAGGGELADE-KLIAAMLEQLFPRASLVTPNGPE----LTQLGGN 151
Cdd:PTZ00493   81 VLYSKKIISLVHNYITNmnkkrGKKLLVVFDPVFVSSSGCLLVENlEYIKFALDLICPISCIITPNFYEckviLEALDCQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012 152 PDETTSAKTLLeygCGAV----------LATGGHGTGEFIENRLFTSD-----------GGD------------------ 192
Cdd:PTZ00493  161 MDLSKANMTEL---CKLVteklninaclFKSCNVGENSAEENEVYAVDhlcirnvgsypTGEkqqidaggvtylydvykl 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1596687012 193 RTWQQPriGGEYHGSGCTLAAGISAGMARG-QALEAAIETgQEFVAASIRSALRVG 247
Cdd:PTZ00493  238 RSKRKP--GKDIHGTGCTLSTAIACYLAKKhNILQSCIES-KKYIYNCIRYAYPFG 290
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 18-241 6.85e-16

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: 74.93  E-value: 6.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  18 GGAGIQADIQAITALGCHPLPVLTCLTVQDTRnvYGAEP---VDADLIHRQLLHLEA-DTPIH--AIKTGALGDETVIQA 91
Cdd:cd01173    12 GYVGNSAAVFPLQRLGWDVDALPTVQFSNHTG--YGTWTgfvLSAEELEDLLEGLEAlGLLLEydAVLTGYLGSAEQVEA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  92 LTEFLD----NREPIPYVLDPVIKAAGGGELADEKLIAAMLEQLFPRASLVTPNGPELTQLGGNPDETTS-----AKTLL 162
Cdd:cd01173    90 VAEIVKrlkeKNPNLLYVCDPVMGDNGKLYVVAEEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLEdakaaARALH 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012 163 EYGCGAVLATGGH-GTGEFIENRLFTSDGGDRtWQQPRIGGEYH--GSGCTLAAGISAGMARGQALEAAIETGQEFVAAS 239
Cdd:cd01173   170 AKGPKTVVVTSVElADDDRIEMLGSTATEAWL-VQRPKIPFPAYfnGTGDLFAALLLARLLKGKSLAEALEKALNFVHEV 248


                  ..
gi 1596687012 240 IR 241
Cdd:cd01173   249 LE 250
pdxK PRK08176
pyridoxine/pyridoxal/pyridoxamine kinase;
77-241 1.55e-10

pyridoxine/pyridoxal/pyridoxamine kinase;


Pssm-ID: 181269 [Multi-domain]  Cd Length: 281  Bit Score: 60.05  E-value: 1.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  77 AIKTGALGDETVIQALTEFLDN-REPIPYVL---DPVIKAAGGGELADEKLIAAMLEQLFPRASLVTPNGPELTQLGGNP 152
Cdd:PRK08176   91 AVTTGYMGSASQIKILAEWLTAlRADHPDLLimvDPVIGDIDSGIYVKPDLPEAYRQHLLPLAQGLTPNIFELEILTGKP 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012 153 ----DET-TSAKTLLEYGCGAVLATG--GHGTGEFIENRLFTSDGGDRTwQQPRIGGEYHGSGCTLAAGISAGMARGQAL 225
Cdd:PRK08176  171 crtlDSAiAAAKSLLSDTLKWVVITSaaGNEENQEMQVVVVTADSVNVI-SHPRVDTDLKGTGDLFCAELVSGLLKGKAL 249

                         170
                  ....*....|....*.
gi 1596687012 226 EAAIETGQEFVAASIR 241
Cdd:PRK08176  250 TDAAHRAGLRVLEVMR 265
PRK07105 PRK07105
pyridoxamine kinase; Validated
 76-251 4.18e-10

pyridoxamine kinase; Validated


Pssm-ID: 180840 [Multi-domain]  Cd Length: 284  Bit Score: 58.77  E-value: 4.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  76 HAIKTGALGDETVIQALTEFLD--NREPIPYVLDPVIkaAGGGEL---ADEKLIAAMlEQLFPRASLVTPNGPELTQLGG 150
Cdd:PRK07105   77 DAIYSGYLGSPRQIQIVSDFIKyfKKKDLLVVVDPVM--GDNGKLyqgFDQEMVEEM-RKLIQKADVITPNLTEACLLLD 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012 151 NP--DETTSAKTLLEY-------GCGAVLATG----GHGTGEFIENRlftsdGGDRTWQ--QPRIGGEYHGSGCTLAAGI 215
Cdd:PRK07105  154 KPylEKSYSEEEIKQLlrkladlGPKIVIITSvpfeDGKIGVAYYDR-----ATDRFWKvfCKYIPAHYPGTGDIFTSVI 228

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1596687012 216 SAGMARGQALEAAIETGQEFVAASIRSALrvGHGQP 251
Cdd:PRK07105  229 TGSLLQGDSLPIALDRAVQFIEKGIRATL--GLKYD 262
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 54-256 2.82e-06

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: 47.57  E-value: 2.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  54 AEPVDADLIHR-QLLHLEADTPIHAIktgalGDETVIQALTEFLDNRepIPYVLDPVIKAAGGGELADEkliaamLEQLF 132
Cdd:COG0524   117 PEDLDEALLAGaDILHLGGITLASEP-----PREALLAALEAARAAG--VPVSLDPNYRPALWEPAREL------LRELL 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012 133 PRASLVTPNGPELTQLGGNPDETTSAKTLLEYGCGAVLAT-GGHG-----TGEFIENRLFTSDGGDRTwqqpriggeyhG 206
Cdd:COG0524   184 ALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVTlGAEGallytGGEVVHVPAFPVEVVDTT-----------G 252

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1596687012 207 SGCTLAAGISAGMARGQALEAAIETGqefVAASIRSALRVGHGQPVPDRS 256
Cdd:COG0524   253 AGDAFAAGFLAGLLEGLDLEEALRFA---NAAAALVVTRPGAQPALPTRE 299
PRK05756 PRK05756
pyridoxal kinase PdxY;
104-240 2.86e-06

pyridoxal kinase PdxY;


Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 47.56  E-value: 2.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012 104 YVLDPVIKAAGGGELADEKLIAAMLEQLFPRASLVTPNGPELTQLGGNPDET-----TSAKTLLEYGCGAVLAT----GG 174
Cdd:PRK05756  108 YFCDPVMGDPEKGCIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETledavAAARALIARGPKIVLVTslarAG 187

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012 175 HGTGEFiENRLFTsdgGDRTW--QQPRI--GGEYHGSGCTLAAGISAGMARGQALEAAIetgqEFVAASI 240
Cdd:PRK05756  188 YPADRF-EMLLVT---ADGAWhiSRPLVdfMRQPVGVGDLTSALFLARLLQGGSLEEAL----EHTTAAV 249
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
 68-243 6.95e-06

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 46.23  E-value: 6.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  68 HLEADtpIHAIKTGALGDETVIQAL----TEFLDNREPIPYVLDPVIKAAGggEL-ADEKLIAAMLEqLFPRASLVTPNG 142
Cdd:PTZ00344   73 NLLSD--YTYVLTGYINSADILREVlatvKEIKELRPKLIFLCDPVMGDDG--KLyVKEEVVDAYRE-LIPYADVITPNQ 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012 143 PELTQLGG----NPDETTSAKTLL-EYGCGAVLATGGHGTGEFIENRLFTS----DGGDRTWQQ---PRIGGEYHGSGCT 210
Cdd:PTZ00344  148 FEASLLSGvevkDLSDALEAIDWFhEQGIPVVVITSFREDEDPTHLRFLLScrdkDTKNNKRFTgkvPYIEGRYTGTGDL 227

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1596687012 211 LAAGISAGMARG---QALEAAIETGQEFVAASIRSA 243
Cdd:PTZ00344  228 FAALLLAFSHQHpmdLAVGKAMGVLQDIIKATRESG 263
pyridox_kin TIGR00687
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ...
 77-257 4.70e-05

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: 43.67  E-value: 4.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  77 AIKTGALGD----ETVIQALTEFLDNREPIPYVLDPVIKAAGGGELADEKLIAAMLEQLFPRASLVTPNGPELTQLGGNP 152
Cdd:TIGR00687  77 AVLSGYLGSaeqvAMVVGIVRQVKQANPQALYVCDPVMGDPWKGCYVAPDLLEVYREKAIPVADIITPNQFELELLTGRR 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012 153 DET-----TSAKTLLEYGCGAVLAT----GGHGTGEFIENRLFTSDGgdrTWQQPR----IGGEYHGSGCTLAAGISAGM 219
Cdd:TIGR00687 157 INTeeealAAADALIAMGPDIVLVThlirAGSQRDRSFEGLVATQEG---RWHISRplavFDPPPVGTGDLIAALLLATL 233

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1596687012 220 ARGQALEAAIETGQEFVAASIRSALRVGHG--QPVPDRSR 257
Cdd:TIGR00687 234 LHGNSLKEALEKTVSAVYHVLRTTIQLGKYelQPVAAQLE 273
PLN02978 PLN02978
pyridoxal kinase
 80-247 1.23e-03

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 39.34  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  80 TGALGDETVIQALTEFLDN-REPIP---YVLDPVIKAAGGGELADEkLIAAMLEQLFPRASLVTPNGPELTQLGGNPDET 155
Cdd:PLN02978   92 TGYIGSVSFLRTVLRVVKKlRSVNPnltYVCDPVLGDEGKLYVPPE-LVPVYREKVVPLATMLTPNQFEAEQLTGIRIVT 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012 156 TsaKTLLEyGCGAVLATGGHG---TGEFIENRLF----TSDGGDRTWQQ-----PRIGGEYHGSGCTLAAGISAGMAR-- 221
Cdd:PLN02978  171 E--EDARE-ACAILHAAGPSKvviTSIDIDGKLLlvgsHRKEKGARPEQfkiviPKIPAYFTGTGDLMAALLLGWSHKyp 247

                         170       180
                  ....*....|....*....|....*....
gi 1596687012 222 ---GQALEAAIETGQEFVAASIRSALRVG 247
Cdd:PLN02978  248 dnlDKAAELAVSSLQAVLRRTLADYKRAG 276
KdgK cd01166
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ...
 54-247 7.24e-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: 37.17  E-value: 7.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012  54 AEPVDADLIHR-QLLHLEADTPihaiktgALGD---ETVIQALTEFLDNREPIpyVLDPVIKAAgggeLADEKLIAAMLE 129
Cdd:cd01166   114 PEDLDEAALAGaDHLHLSGITL-------ALSEsarEALLEALEAAKARGVTV--SFDLNYRPK----LWSAEEAREALE 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1596687012 130 QLFPRASLVTPNGPELTQLGGNPDETTSAKTLLEYGCGAVLAT---GGHGTgefienrlFTSDGGDRTWQQPRIGGEYH- 205
Cdd:cd01166   181 ELLPYVDIVLPSEEEAEALLGDEDPTDAAERALALALGVKAVVvklGAEGA--------LVYTGGGRVFVPAYPVEVVDt 252

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1596687012 206 -GSGCTLAAGISAGMARGQALEAAIETGqefVAASIRSALRVG 247
Cdd:cd01166   253 tGAGDAFAAGFLAGLLEGWDLEEALRFA---NAAAALVVTRPG 292
 
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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