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Conserved domains on  [gi|446790135|ref|WP_000867391|]
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MULTISPECIES: bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase [Bacillus]

Protein Classification

hydroxymethylpyrimidine/phosphomethylpyrimidine kinase( domain architecture ID 10792784)

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

EC:  2.7.4.7|2.7.1.49
Gene Ontology:  GO:0008902|GO:0008972|GO:0009228|GO:0005829
PubMed:  11839308

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 1-263 3.59e-149

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


:

Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 417.60  E-value: 3.59e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135   1 MKVNKALTIAGSDSGGGAGIQADLKTFQELGVYGMTAITAITAQNTLGVQGVYPVPLEGVTEQLNSIGTDLTPDAVKLGM 80
Cdd:PRK06427   2 MKRPIALTIAGSDSGGGAGIQADLKTFQALGVYGMSAITALTAQNTLGVQRVHPIPPEFVAAQLDAVFSDIRIDAVKIGM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  81 LFSSEIIQIVAEQIKKFGWNNIVLDPVMIAKGGASLLQQEAVQALKEYLLPVATVITPNVPEAEVLTGMEIHNVEDS-KE 159
Cdd:PRK06427  82 LASAEIIETVAEALKRYPIPPVVLDPVMIAKSGDPLLADDAVAALRERLLPLATLITPNLPEAEALTGLPIADTEDEmKA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 160 AAKVLHELGAKYVLMKGGHaEYQGNEVIDFLFDGEKFIEFRSERIPSKQTHGSGCTFASAVTAGLAKGYSIEDAVQEAKR 239
Cdd:PRK06427 162 AARALHALGCKAVLIKGGH-LLDGEESVDWLFDGEGEERFSAPRIPTKNTHGTGCTLSAAIAAELAKGASLLDAVQTAKD 240

                        250       260
                 ....*....|....*....|....
gi 446790135 240 FISIAIEEPLNIGSGHGPTNHFAY 263
Cdd:PRK06427 241 YVTRAIRHALEIGQGHGPVNHFAY 264
 
Name Accession Description Interval E-value
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 1-263 3.59e-149

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 417.60  E-value: 3.59e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135   1 MKVNKALTIAGSDSGGGAGIQADLKTFQELGVYGMTAITAITAQNTLGVQGVYPVPLEGVTEQLNSIGTDLTPDAVKLGM 80
Cdd:PRK06427   2 MKRPIALTIAGSDSGGGAGIQADLKTFQALGVYGMSAITALTAQNTLGVQRVHPIPPEFVAAQLDAVFSDIRIDAVKIGM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  81 LFSSEIIQIVAEQIKKFGWNNIVLDPVMIAKGGASLLQQEAVQALKEYLLPVATVITPNVPEAEVLTGMEIHNVEDS-KE 159
Cdd:PRK06427  82 LASAEIIETVAEALKRYPIPPVVLDPVMIAKSGDPLLADDAVAALRERLLPLATLITPNLPEAEALTGLPIADTEDEmKA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 160 AAKVLHELGAKYVLMKGGHaEYQGNEVIDFLFDGEKFIEFRSERIPSKQTHGSGCTFASAVTAGLAKGYSIEDAVQEAKR 239
Cdd:PRK06427 162 AARALHALGCKAVLIKGGH-LLDGEESVDWLFDGEGEERFSAPRIPTKNTHGTGCTLSAAIAAELAKGASLLDAVQTAKD 240

                        250       260
                 ....*....|....*....|....
gi 446790135 240 FISIAIEEPLNIGSGHGPTNHFAY 263
Cdd:PRK06427 241 YVTRAIRHALEIGQGHGPVNHFAY 264
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 20-262 3.36e-140

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: 394.41  E-value: 3.36e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  20 IQADLKTFQELGVYGMTAITAITAQNTLGVQGVYPVPLEGVTEQLNSIGTDLTPDAVKLGMLFSSEIIQIVAEQIKKFGW 99
Cdd:COG0351   14 IQADLKTFAALGVYGMSVITALTAQNTLGVTGVHPVPPEFVAAQLRAVLEDIPVDAIKIGMLGSAEIIEAVAEILADYPL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 100 NNIVLDPVMIAKGGASLLQQEAVQALKEYLLPVATVITPNVPEAEVLTGMEIHNVEDSKEAAKVLHELGAKYVLMKGGHA 179
Cdd:COG0351   94 VPVVLDPVMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALLGIEITTLDDMREAAKALLELGAKAVLVKGGHL 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 180 EyqGNEVIDFLFDGEKFIEFRSERIPSKQTHGSGCTFASAVTAGLAKGYSIEDAVQEAKRFISIAIEEPLNIGSGHGPTN 259
Cdd:COG0351  174 P--GDEAVDVLYDGDGVREFSAPRIDTGNTHGTGCTLSSAIAALLAKGLDLEEAVREAKEYVTQAIRAALRLGMGHGPVN 251


                 ...
gi 446790135 260 HFA 262
Cdd:COG0351  252 HFA 254
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 20-259 2.70e-138

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: 389.15  E-value: 2.70e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135   20 IQADLKTFQELGVYGMTAITAITAQNTLGVQGVYPVPLEGVTEQLNSIGTDLTPDAVKLGMLFSSEIIQIVAEQIKKFGW 99
Cdd:pfam08543   8 IQADLKTFSALGVYGMSVITALTAQNTLGVQGVHPLPPEFVAAQLDAVLEDIPVDAVKTGMLGSAEIIEAVAEKLDKYGV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  100 NnIVLDPVMIAKGGASLLQQEAVQALKEYLLPVATVITPNVPEAEVLTGMEIHNVEDSKEAAKVLHELGAKYVLMKGGHA 179
Cdd:pfam08543  88 P-VVLDPVMVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKGGHL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  180 EYQGNEVIDFLFDGEKFIEFRSERIPSKQTHGSGCTFASAVTAGLAKGYSIEDAVQEAKRFISIAIEEPLNIGSGHGPTN 259
Cdd:pfam08543 167 EGEEAVVTDVLYDGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKEYVTEAIRDALNLGKGHGPVN 246
HMP-P_kinase TIGR00097
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ...
 6-261 1.51e-125

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: 357.37  E-value: 1.51e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135    6 ALTIAGSDSGGGAGIQADLKTFQELGVYGMTAITAITAQNTLGVQGVYPVPLEGVTEQLNSIGTDLTPDAVKLGMLFSSE 85
Cdd:TIGR00097   1 ALTIAGSDSGGGAGIQADLKTFSALGVFGTSVITALTAQNTRGVTGVYPIPPDFVEAQLDAVFSDIPVDAAKTGMLASAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135   86 IIQIVAEQIKKFGWNNIVLDPVMIAKGGASLLQQEAVQALKEYLLPVATVITPNVPEAEVLTGMEIHNVEDSKEAAKVLH 165
Cdd:TIGR00097  81 IVEAVARKLREYPVRPLVVDPVMVAKSGAPLLEEEAIEALRKRLLPLATLITPNLPEAEALLGTKIRTEQDMIKAAKKLR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  166 ELGAKYVLMKGGHAEyqGNEVIDFLFDGEKFIEFRSERIPSKQTHGSGCTFASAVTAGLAKGYSIEDAVQEAKRFISIAI 245
Cdd:TIGR00097 161 ELGPKAVLIKGGHLE--GDQAVDVLFDGGEIHILKAPRIETKNTHGTGCTLSAAIAANLAKGLSLKEAVKEAKEFVTGAI 238

                         250
                  ....*....|....*.
gi 446790135  246 EEPLNIGSGHGPTNHF 261
Cdd:TIGR00097 239 RYGLNIGHGHGPLNHF 254
HMPP_kinase cd01169
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ...
 20-247 2.06e-124

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: 353.73  E-value: 2.06e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  20 IQADLKTFQELGVYGMTAITAITAQNTLGVQGVYPVPLEGVTEQLNSIGTDLTPDAVKLGMLFSSEIIQIVAEQIKKFGW 99
Cdd:cd01169   16 IQADLKTFAALGVYGMSVITALTAQNTLGVFGVHPVPPEFVAAQLDAVLEDIPVDAIKIGMLGSAEIIEAVAEALKDYPD 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 100 NNIVLDPVMIAKGGASLLQQEAVQALKEYLLPVATVITPNVPEAEVLTGMEIHNVEDSKEAAKVLHELGAKYVLMKGGHA 179
Cdd:cd01169   96 IPVVLDPVMVAKSGDSLLDDDAIEALRELLLPLATLITPNLPEAELLTGLEIATEEDMMKAAKALLALGAKAVLIKGGHL 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446790135 180 EyqGNEVIDFLFDGEKFIEFRSERIPSKQTHGSGCTFASAVTAGLAKGYSIEDAVQEAKRFISIAIEE 247
Cdd:cd01169  176 P--GDEAVDVLYDGGGFFEFESPRIDTKNTHGTGCTLSSAIAANLAKGLSLEEAVREAKEYVTQAIRN 241
 
Name Accession Description Interval E-value
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 1-263 3.59e-149

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 417.60  E-value: 3.59e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135   1 MKVNKALTIAGSDSGGGAGIQADLKTFQELGVYGMTAITAITAQNTLGVQGVYPVPLEGVTEQLNSIGTDLTPDAVKLGM 80
Cdd:PRK06427   2 MKRPIALTIAGSDSGGGAGIQADLKTFQALGVYGMSAITALTAQNTLGVQRVHPIPPEFVAAQLDAVFSDIRIDAVKIGM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  81 LFSSEIIQIVAEQIKKFGWNNIVLDPVMIAKGGASLLQQEAVQALKEYLLPVATVITPNVPEAEVLTGMEIHNVEDS-KE 159
Cdd:PRK06427  82 LASAEIIETVAEALKRYPIPPVVLDPVMIAKSGDPLLADDAVAALRERLLPLATLITPNLPEAEALTGLPIADTEDEmKA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 160 AAKVLHELGAKYVLMKGGHaEYQGNEVIDFLFDGEKFIEFRSERIPSKQTHGSGCTFASAVTAGLAKGYSIEDAVQEAKR 239
Cdd:PRK06427 162 AARALHALGCKAVLIKGGH-LLDGEESVDWLFDGEGEERFSAPRIPTKNTHGTGCTLSAAIAAELAKGASLLDAVQTAKD 240

                        250       260
                 ....*....|....*....|....
gi 446790135 240 FISIAIEEPLNIGSGHGPTNHFAY 263
Cdd:PRK06427 241 YVTRAIRHALEIGQGHGPVNHFAY 264
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 20-262 3.36e-140

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: 394.41  E-value: 3.36e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  20 IQADLKTFQELGVYGMTAITAITAQNTLGVQGVYPVPLEGVTEQLNSIGTDLTPDAVKLGMLFSSEIIQIVAEQIKKFGW 99
Cdd:COG0351   14 IQADLKTFAALGVYGMSVITALTAQNTLGVTGVHPVPPEFVAAQLRAVLEDIPVDAIKIGMLGSAEIIEAVAEILADYPL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 100 NNIVLDPVMIAKGGASLLQQEAVQALKEYLLPVATVITPNVPEAEVLTGMEIHNVEDSKEAAKVLHELGAKYVLMKGGHA 179
Cdd:COG0351   94 VPVVLDPVMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALLGIEITTLDDMREAAKALLELGAKAVLVKGGHL 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 180 EyqGNEVIDFLFDGEKFIEFRSERIPSKQTHGSGCTFASAVTAGLAKGYSIEDAVQEAKRFISIAIEEPLNIGSGHGPTN 259
Cdd:COG0351  174 P--GDEAVDVLYDGDGVREFSAPRIDTGNTHGTGCTLSSAIAALLAKGLDLEEAVREAKEYVTQAIRAALRLGMGHGPVN 251


                 ...
gi 446790135 260 HFA 262
Cdd:COG0351  252 HFA 254
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 20-259 2.70e-138

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: 389.15  E-value: 2.70e-138
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135   20 IQADLKTFQELGVYGMTAITAITAQNTLGVQGVYPVPLEGVTEQLNSIGTDLTPDAVKLGMLFSSEIIQIVAEQIKKFGW 99
Cdd:pfam08543   8 IQADLKTFSALGVYGMSVITALTAQNTLGVQGVHPLPPEFVAAQLDAVLEDIPVDAVKTGMLGSAEIIEAVAEKLDKYGV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  100 NnIVLDPVMIAKGGASLLQQEAVQALKEYLLPVATVITPNVPEAEVLTGMEIHNVEDSKEAAKVLHELGAKYVLMKGGHA 179
Cdd:pfam08543  88 P-VVLDPVMVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKGGHL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  180 EYQGNEVIDFLFDGEKFIEFRSERIPSKQTHGSGCTFASAVTAGLAKGYSIEDAVQEAKRFISIAIEEPLNIGSGHGPTN 259
Cdd:pfam08543 167 EGEEAVVTDVLYDGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKEYVTEAIRDALNLGKGHGPVN 246
HMP-P_kinase TIGR00097
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ...
 6-261 1.51e-125

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: 357.37  E-value: 1.51e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135    6 ALTIAGSDSGGGAGIQADLKTFQELGVYGMTAITAITAQNTLGVQGVYPVPLEGVTEQLNSIGTDLTPDAVKLGMLFSSE 85
Cdd:TIGR00097   1 ALTIAGSDSGGGAGIQADLKTFSALGVFGTSVITALTAQNTRGVTGVYPIPPDFVEAQLDAVFSDIPVDAAKTGMLASAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135   86 IIQIVAEQIKKFGWNNIVLDPVMIAKGGASLLQQEAVQALKEYLLPVATVITPNVPEAEVLTGMEIHNVEDSKEAAKVLH 165
Cdd:TIGR00097  81 IVEAVARKLREYPVRPLVVDPVMVAKSGAPLLEEEAIEALRKRLLPLATLITPNLPEAEALLGTKIRTEQDMIKAAKKLR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  166 ELGAKYVLMKGGHAEyqGNEVIDFLFDGEKFIEFRSERIPSKQTHGSGCTFASAVTAGLAKGYSIEDAVQEAKRFISIAI 245
Cdd:TIGR00097 161 ELGPKAVLIKGGHLE--GDQAVDVLFDGGEIHILKAPRIETKNTHGTGCTLSAAIAANLAKGLSLKEAVKEAKEFVTGAI 238

                         250
                  ....*....|....*.
gi 446790135  246 EEPLNIGSGHGPTNHF 261
Cdd:TIGR00097 239 RYGLNIGHGHGPLNHF 254
HMPP_kinase cd01169
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ...
 20-247 2.06e-124

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: 353.73  E-value: 2.06e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  20 IQADLKTFQELGVYGMTAITAITAQNTLGVQGVYPVPLEGVTEQLNSIGTDLTPDAVKLGMLFSSEIIQIVAEQIKKFGW 99
Cdd:cd01169   16 IQADLKTFAALGVYGMSVITALTAQNTLGVFGVHPVPPEFVAAQLDAVLEDIPVDAIKIGMLGSAEIIEAVAEALKDYPD 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 100 NNIVLDPVMIAKGGASLLQQEAVQALKEYLLPVATVITPNVPEAEVLTGMEIHNVEDSKEAAKVLHELGAKYVLMKGGHA 179
Cdd:cd01169   96 IPVVLDPVMVAKSGDSLLDDDAIEALRELLLPLATLITPNLPEAELLTGLEIATEEDMMKAAKALLALGAKAVLIKGGHL 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446790135 180 EyqGNEVIDFLFDGEKFIEFRSERIPSKQTHGSGCTFASAVTAGLAKGYSIEDAVQEAKRFISIAIEE 247
Cdd:cd01169  176 P--GDEAVDVLYDGGGFFEFESPRIDTKNTHGTGCTLSSAIAANLAKGLSLEEAVREAKEYVTQAIRN 241
PRK08573 PRK08573
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
3-263 1.24e-102

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 236297 [Multi-domain]  Cd Length: 448  Bit Score: 305.88  E-value: 1.24e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135   3 VNKALTIAGSDSGGGAGIQADLKTFQELGVYGMTAITAITAQNTLGVQGVYPVPLEGVTEQLNSIGTDLTPDAVKLGMLF 82
Cdd:PRK08573   2 IPVALTIAGSDSGGGAGIEADLKTFAALGVHGAVAITSVTAQNTYEVRAIHDLPPEVVAAQIEAVWEDMGIDAAKTGMLS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  83 SSEIIQIVAEQIKKFGWnNIVLDPVMIAKGGASLLQQEAVQALKEYLLPVATVITPNVPEAEVLTGMEIHNVEDSKEAAK 162
Cdd:PRK08573  82 NREIIEAVAKTVSKYGF-PLVVDPVMIAKSGAPLLREDAVDALIKRLLPLATVVTPNRPEAEKLTGMKIRSVEDARKAAK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 163 VLH-ELGAKYVLMKGGHAEyqGNEVIDFLFDGEKFIEFRSERIPSKQTHGSGCTFASAVTAGLAKGYSIEDAVQEAKRFI 241
Cdd:PRK08573 161 YIVeELGAEAVVVKGGHLE--GEEAVDVLYHNGTFREFRAPRVESGCTHGTGCSFSAAIAAGLAKGLDPEEAIKTAKKFI 238

                        250       260
                 ....*....|....*....|..
gi 446790135 242 SIAIEEPLNIGSGHGPTNHFAY 263
Cdd:PRK08573 239 TMAIKYGVKIGKGHCPVNPMAW 260
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
 1-261 4.62e-102

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 306.31  E-value: 4.62e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135   1 MKVNKALTIAGSDSGGGAGIQADLKTFQELGVYGMTAITAITAQNTLGVQGVYPVPLEGVTEQLNSIGTDLTPDAVKLGM 80
Cdd:PLN02898   7 MKVPHVLTVAGSDSGAGAGIQADIKACAARGVYCTTAITAVTAQNTVGVQGVHAVPLDFVAEQLKSVLSDMPVDVVKTGM 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  81 LFSSEIIQIVAEQIKKFGWNNIVLDPVMIAKGGASLLQQEAVQALKEYLLPVATVITPNVPEAEVLTGM-EIHNVEDSKE 159
Cdd:PLN02898  87 LPSAEIVKVLCQALKEFPVKALVVDPVMVSTSGDVLAGPSILSALREELLPLATIVTPNVKEASALLGGdPLETVADMRS 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 160 AAKVLHELGAKYVLMKGGHAEyQGNEVIDFLFDGEKFIEFRSERIPSKQTHGSGCTFASAVTAGLAKGYSIEDAVQEAKR 239
Cdd:PLN02898 167 AAKELHKLGPRYVLVKGGHLP-DSLDAVDVLYDGTEFHELRSSRIKTRNTHGTGCTLASCIAAELAKGSDMLSAVKVAKR 245

                        250       260
                 ....*....|....*....|....*
gi 446790135 240 FISIAIEEPLNIGSG---HGPTNHF 261
Cdd:PLN02898 246 YVETALEYSKDIGIGngaQGPFNHL 270
PRK12412 PRK12412
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
3-267 2.87e-82

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183512 [Multi-domain]  Cd Length: 268  Bit Score: 247.96  E-value: 2.87e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135   3 VNKALTIAGSDSGGGAGIQADLKTFQELGVYGMTAITAITAQNTLG--VQGVYPVPLEGVTEQLNSIGTDLTPDAVKLGM 80
Cdd:PRK12412   1 LNKALTIAGSDTSGGAGIQADLKTFQELGVYGMTSLTTIVTMDPHNgwAHNVFPIPASTLKPQLETTIEGVGVDALKTGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  81 LFSSEIIQIVAEQIKKFGWNNIVLDPVMIAKGGASLLQQEAVQALKEYLLPVATVITPNVPEAEVLTGMEIHNVEDSKEA 160
Cdd:PRK12412  81 LGSVEIIEMVAETIEKHNFKNVVVDPVMVCKGADEALHPETNDCLRDVLVPKALVVTPNLFEAYQLSGVKINSLEDMKEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 161 AKVLHELGAKYVLMKGGhAEYQGNEVIDFLFDGEKFIEFRSERIPSKQTHGSGCTFASAVTAGLAKGYSIEDAVQEAKRF 240
Cdd:PRK12412 161 AKKIHALGAKYVLIKGG-SKLGTETAIDVLYDGETFDLLESEKIDTTNTHGAGCTYSAAITAELAKGKPVKEAVKTAKEF 239

                        250       260
                 ....*....|....*....|....*..
gi 446790135 241 ISIAIEEPLNIGSGHGPTNHFAYKLNK 267
Cdd:PRK12412 240 ITAAIRYSFKINEYVGPTHHGAYRKFV 266
PRK12616 PRK12616
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
1-267 1.17e-79

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183624  Cd Length: 270  Bit Score: 241.49  E-value: 1.17e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135   1 MKVNKALTIAGSDSGGGAGIQADLKTFQELGVYGMTAITAITA---QNTLGVQgVYPVPLEGVTEQLNSIGTDLTPDAVK 77
Cdd:PRK12616   1 MSMHKALTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAmdpENSWDHQ-VFPIDTDTIRAQLSTIVDGIGVDAMK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  78 LGMLFSSEIIQIVAEQIKKFGWNNIVLDPVMIAKGGASLLQQEAVQALKEYLLPVATVITPNVPEAEVLTGM-EIHNVED 156
Cdd:PRK12616  80 TGMLPTVDIIELAADTIKEKQLKNVVIDPVMVCKGANEVLYPEHAEALREQLAPLATVITPNLFEAGQLSGMgEIKTVEQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 157 SKEAAKVLHELGAKYVLMKGGhAEYQGNEVIDFLFDGEKFIEFRSERIPSKQTHGSGCTFASAVTAGLAKGYSIEDAVQE 236
Cdd:PRK12616 160 MKEAAKKIHELGAQYVVITGG-GKLKHEKAVDVLYDGETAEVLESEMIDTPYTHGAGCTFSAAVTAELAKGSEVKEAIYA 238

                        250       260       270
                 ....*....|....*....|....*....|.
gi 446790135 237 AKRFISIAIEEPLNIGSGHGPTNHFAYKLNK 267
Cdd:PRK12616 239 AKEFITAAIKESFPLNQYVGPTKHSALRLSG 269
PTZ00347 PTZ00347
phosphomethylpyrimidine kinase; Provisional
 1-260 1.71e-77

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240375 [Multi-domain]  Cd Length: 504  Bit Score: 243.33  E-value: 1.71e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135   1 MKVNKALTIAGSDSGGGAGIQADLKTFQELGVYGMTAITAITAQNTLGVQGVYPVPLEGVTEQLNSIGTDLTPDAVKLGM 80
Cdd:PTZ00347 228 MKIPTVLTVSGSDSGGGAGHQADLKTLEALGVYSTSALTSLTAQNTKGVQQIQVVNEDFFAAQIDSVMSDFNISVVKLGL 307

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  81 LFSSEIIQIVAEQIKKFgwnNIVLDPVMIAKGGASLLQQEAVQAL----KEYLLPVATVITPNVPEAEVLTGM-EIHNVE 155
Cdd:PTZ00347 308 VPTARQLEIVIEKLKNL---PMVVDPVLVATSGDDLVAQKNADDVlamyKERIFPMATIITPNIPEAERILGRkEITGVY 384

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 156 DSKEAAKVLHELGAKYVLMKGGHAEYQGNEVIDFLFDGEK--FIEFRSERIPSKQTHGSGCTFASAVTAGLAKGYSIEDA 233
Cdd:PTZ00347 385 EARAAAQALAQYGSRYVLVKGGHDLIDPEACRDVLYDREKdrFYEFTANRIATINTHGTGCTLASAISSFLARGYTVPDA 464

                        250       260       270
                 ....*....|....*....|....*....|.
gi 446790135 234 VQEAKRFISIAIEE----PLNIGsGHGPTNH 260
Cdd:PTZ00347 465 VERAIGYVHEAIVRscgvPLGQG-TNRPLVH 494
PRK14713 PRK14713
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
20-262 8.99e-67

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 237797 [Multi-domain]  Cd Length: 530  Bit Score: 216.19  E-value: 8.99e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  20 IQADLKTFQELGVYGMTAITAITAQNTLGVQGVYPVPLEGVTEQLNSIGTDLTPDAVKLGMLFSSEIIQIVAEQIKKFGW 99
Cdd:PRK14713  46 IQADLKSIAAAGGYGMAVITALVAQNTRGVRAVHVPPADFLRAQLDAVSDDVTVDAVKIGMLGDAEVIDAVRTWLAEHRP 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 100 NNIVLDPVMIAKGGASLLQQEAVQALKEyLLPVATVITPNVPEAEVLTGMEIHNVEDS--KEAAKVLHELGAKyVLMKGG 177
Cdd:PRK14713 126 PVVVLDPVMVATSGDRLLEEDAEAALRE-LVPRADLITPNLPELAVLLGEPPATTWEEalAQARRLAAETGTT-VLVKGG 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 178 HaeYQGNEVIDFLFDGE-KFIEFRSERIPSKQTHGSGCTFASAVTAGLAKGYSIEDAVQEAKRFISIAIE--EPLNIGSG 254
Cdd:PRK14713 204 H--LDGQRAPDALVGPDgAVTEVPGPRVDTRNTHGTGCSLSSALATRLGRGGDWAAALRWATAWLHGAIAagAALQVGTG 281


                 ....*...
gi 446790135 255 HGPTNHFA 262
Cdd:PRK14713 282 NGPVDHFH 289
PRK12413 PRK12413
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
1-246 4.54e-59

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183513 [Multi-domain]  Cd Length: 253  Bit Score: 188.35  E-value: 4.54e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135   1 MKVNKALTIAGSDSGGGAGIQADLKTFQELGVYGMTAITAITAQNTLGVQgVYPVPLEGVTEQLNSIgTDLTPDAVKLGM 80
Cdd:PRK12413   1 MKTNYILAISGNDIFSGGGLHADLATYTRNGLHGFVAVTCLTAMTEKGFE-VFPVDKEIFQQQLDSL-KDVPFSAIKIGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  81 LFSSEIIQIVAEQIKKFGWNNIVLDPVMIAKGGA----SLLQQEAVQalkeyLLPVATVITPNVPEAEVLTGMEIHNVED 156
Cdd:PRK12413  79 LPNVEIAEQALDFIKGHPGIPVVLDPVLVCKETHdvevSELRQELIQ-----FFPYVTVITPNLVEAELLSGKEIKTLED 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 157 SKEAAKVLHELGAKYVLMKGGHaEYQGNEVIDFLFDGEKFIEFRSERIpSKQTHGSGCTFASAVTAGLAKGYSIEDAVQE 236
Cdd:PRK12413 154 MKEAAKKLYDLGAKAVVIKGGN-RLSQKKAIDLFYDGKEFVILESPVL-EKNNIGAGCTFASSIASQLVKGKSPLEAVKN 231

                        250
                 ....*....|
gi 446790135 237 AKRFISIAIE 246
Cdd:PRK12413 232 SKDFVYQAIQ 241
PRK09517 PRK09517
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ...
 3-270 5.51e-48

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


Pssm-ID: 169939 [Multi-domain]  Cd Length: 755  Bit Score: 169.77  E-value: 5.51e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135   3 VNKALTIAGSDSGGGAGIQADLKTFQELGVYGMTAITAITAQNTLGVQGVYPVPLEGVTEQLNSIGTDLTPDAVKLGMLF 82
Cdd:PRK09517 241 APRVLSIAGTDPTGGAGIQADLKSIAAGGGYGMCVVTALVAQNTHGVNTIHTPPLTFLEEQLEAVFSDVTVDAVKLGMLG 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  83 SSEIIQIVAEQIKKFGWNNIVLDPVMIAKGGASLLQQEAVQALKEyLLPVATVITPNVPEAEVLTG-MEIHNVEDSKEAA 161
Cdd:PRK09517 321 SADTVDLVASWLGSHEHGPVVLDPVMVATSGDRLLDADATEALRR-LAVHVDVVTPNIPELAVLCGeAPAITMDEAIAQA 399

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 162 KVLHELGAKYVLMKGGHaeYQGNEVIDFLF--DGEKFIeFRSERIPSKQTHGSGCTFASAVTAGLAKGYSIEDAVQEAKR 239
Cdd:PRK09517 400 RGFARTHGTIVIVKGGH--LTGDLADNAVVrpDGSVHQ-VENPRVNTTNSHGTGCSLSAALATLIAAGESVEKALEWATR 476

                        250       260       270
                 ....*....|....*....|....*....|...
gi 446790135 240 FI--SIAIEEPLNIGSGHGPTNHFAYKLNKTRA 270
Cdd:PRK09517 477 WLneALRHADHLAVGSGNGPVDHGHLARRLTHA 509
COG1992 COG1992
Predicted transcriptional regulator fused phosphomethylpyrimidine kinase (thiamin biosynthesis) ...
 20-267 2.25e-46

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


Pssm-ID: 441595 [Multi-domain]  Cd Length: 432  Bit Score: 160.31  E-value: 2.25e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  20 IQADLKTFQELGVYGMTAITAITAQNTLGVQGVYPVPLEGVTEQLNSIGTDLTPDAVKLGMLFSSEIIQIVAEQIKKFGW 99
Cdd:COG1992    6 GGADAKTAAALGAGGGGTTTAVTVTATTTVTGVGSDPPPPVEVQQQAVAADDDVDDAKTGMLMTATIVEVVAVVVKSRDK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 100 NnIVLDPVMIAKGGASLLQQEAVQALKEYLLPVATVITPNVPEAEVLTGMEIHNVEDSKEAAKvLHELGAKYVLMKGGHA 179
Cdd:COG1992   86 P-LVVVVVPVAVAAAGLGLLLAEAELAKLLLPLLATVTPNEPEVEELLLPTIRSLLAEARAAR-LALQEEGADALGVKGG 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 180 EYQGNEVIDFLFDGEKFIEFRSERIPSKQTHGSGCTFASAVTAGLAKGYSIEDAVQEAKRFISIAIEEPLNIGSGHGPTN 259
Cdd:COG1992  164 HVSGDAVVDVLEDERDVETFRHPRLVTEATHGSGCTFSAAIAALLAKGLSLEEAVRGAKLFLLHAIRYGLLVGKGVGPVN 243


                 ....*...
gi 446790135 260 HFAYKLNK 267
Cdd:COG1992  244 HLADLRLE 251
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 34-247 9.42e-37

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: 131.04  E-value: 9.42e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  34 GMTAitAITAQNTLGVQgVYPVP----------------------LEGVTEQLNSIGTDLTPDAVKLGMLFSSEIIQIVA 91
Cdd:COG2240   17 GNSA--AVPPLSALGVE-VWPLPtvllsnhtgygtftgrdlptddIADILDGWKELGVLLEFDAVLSGYLGSAEQGDIIA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  92 EQIKKFGWNN----IVLDPVM-IAKGGASLLQQEAVQALKEyLLPVATVITPNVPEAEVLTGMEIHNVEDSKEAAKVLHE 166
Cdd:COG2240   94 DFVARVKAANpdalYLCDPVMgDNGKGYYVFPGIAEFIMRR-LVPLADIITPNLTELALLTGRPYETLEEALAAARALLA 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 167 LGAKYVLMKG-GHAEYQGNEVIDFLFDGEKFIEFRSERIPsKQTHGSGCTFASAVTAGLAKGYSIEDAVQEAKRFISIAI 245
Cdd:COG2240  173 LGPKIVVVTSvPLDDTPADKIGNLAVTADGAWLVETPLLP-FSPNGTGDLFAALLLAHLLRGKSLEEALERAAAFVYEVL 251


                 ..
gi 446790135 246 EE 247
Cdd:COG2240  252 ER 253
PTZ00493 PTZ00493
phosphomethylpyrimidine kinase; Provisional
 3-261 9.26e-32

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240440  Cd Length: 321  Bit Score: 119.33  E-value: 9.26e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135   3 VNKALTIAGSDSGGGAGIQADLKTFQELGVYGMTAITAITAQNTLGVQGVYPVPLEGVTEQLNSIGTDLTPDAVKLGMLF 82
Cdd:PTZ00493   4 VSNILSIAGSDSCGGAGMQADIKTAMGLGCHCCTALVVLTAQNTKEVKRIVEIEEKFIVEQLDSIFADVTIDVVKLGVLY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  83 SSEIIQIVAEQI----KKFGWN-NIVLDPVMIAKGGASLLQQ-EAVQALKEYLLPVATVITPNVPEAEVLT-----GMEI 151
Cdd:PTZ00493  84 SKKIISLVHNYItnmnKKRGKKlLVVFDPVFVSSSGCLLVENlEYIKFALDLICPISCIITPNFYECKVILealdcQMDL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 152 HNVEDSKEAAKVLHELGAKYVLMKG---GHAEYQGNEV--------------------------IDFLFDGEKfieFRSE 202
Cdd:PTZ00493 164 SKANMTELCKLVTEKLNINACLFKScnvGENSAEENEVyavdhlcirnvgsyptgekqqidaggVTYLYDVYK---LRSK 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446790135 203 RIPSKQTHGSGCTFASAVTAGLAKGYSIEDAVQEAKRFISIAIEEPLNIGSGHGPTNHF 261
Cdd:PTZ00493 241 RKPGKDIHGTGCTLSTAIACYLAKKHNILQSCIESKKYIYNCIRYAYPFGSKSQGLNHL 299
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 57-237 6.22e-31

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: 115.37  E-value: 6.22e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  57 LEGVTEQLNSIGTDLTPDAVKLGMLFSSEIIQIVAEQIKKFGWNN----IVLDPVMIAKGGASLLQQEAVQALKEYLLPV 132
Cdd:cd01173   57 LEDLLEGLEALGLLLEYDAVLTGYLGSAEQVEAVAEIVKRLKEKNpnllYVCDPVMGDNGKLYVVAEEIVPVYRDLLVPL 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 133 ATVITPNVPEAEVLTGMEIHNVEDSKEAAKVLHELGAKYVLMKggHAEYQGNEVID-FLFDGEKFIEFRSERIPSKQT-H 210
Cdd:cd01173  137 ADIITPNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVT--SVELADDDRIEmLGSTATEAWLVQRPKIPFPAYfN 214

                        170       180
                 ....*....|....*....|....*..
gi 446790135 211 GSGCTFASAVTAGLAKGYSIEDAVQEA 237
Cdd:cd01173  215 GTGDLFAALLLARLLKGKSLAEALEKA 241
PRK07105 PRK07105
pyridoxamine kinase; Validated
 39-246 5.80e-19

pyridoxamine kinase; Validated


Pssm-ID: 180840 [Multi-domain]  Cd Length: 284  Bit Score: 84.20  E-value: 5.80e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  39 TAITAQNTLGVQGVYPVPLegvTEQLNSIGT-----DLTPDAVKLGMLFSSEIIQIVAEQIKKFGWNN--IVLDPVMIAK 111
Cdd:PRK07105  40 TALLSSHTGGFQNPSIIDL---TDGMQAFLThwkslNLKFDAIYSGYLGSPRQIQIVSDFIKYFKKKDllVVVDPVMGDN 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 112 GgaSLLQ---QEAVQALKEyLLPVATVITPNVPEAEVLTGM----EIHNVEDSKEAAKVLHELGAKYVLMKGGHAEYQGN 184
Cdd:PRK07105 117 G--KLYQgfdQEMVEEMRK-LIQKADVITPNLTEACLLLDKpyleKSYSEEEIKQLLRKLADLGPKIVIITSVPFEDGKI 193

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446790135 185 EVIDFLFDGEKFIEFRSERIPSkQTHGSGCTFASAVTAGLAKGYSIEDAVQEAKRFISIAIE 246
Cdd:PRK07105 194 GVAYYDRATDRFWKVFCKYIPA-HYPGTGDIFTSVITGSLLQGDSLPIALDRAVQFIEKGIR 254
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 122-246 6.71e-17

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: 78.36  E-value: 6.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 122 VQALKEYLLPVATVITPNVPEAEVLTGMEIHNVEDSKEAAKVLHELGAKYVLMKGGHaeyQGneviDFLFDGEKFIEFRS 201
Cdd:cd01174  165 ARPLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGA---KG----ALLASGGEVEHVPA 237

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 446790135 202 ERIPSKQTHGSGCTFASAVTAGLAKGYSIEDAVQEAKRFISIAIE 246
Cdd:cd01174  238 FKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVT 282
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 85-248 4.01e-14

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 70.83  E-value: 4.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135   85 EIIQIVAEQIKKFgwNNIVLDPVMIAKggasllqqeavQALKEyLLPVATVITPNVPEAEVLTGMEIHNVEDSKEAAKVL 164
Cdd:pfam00294 147 EELIEAAKNGGTF--DPNLLDPLGAAR-----------EALLE-LLPLADLLKPNEEELEALTGAKLDDIEEALAALHKL 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  165 HELGAKYVLMKgghaeyQGNEVIDFlFDGEKFIEFrsERIPSKQ---THGSGCTFASAVTAGLAKGYSIEDAVQEAKRFI 241
Cdd:pfam00294 213 LAKGIKTVIVT------LGADGALV-VEGDGEVHV--PAVPKVKvvdTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAA 283


                  ....*..
gi 446790135  242 SIAIEEP 248
Cdd:pfam00294 284 ALVVQKS 290
pdxK PRK08176
pyridoxine/pyridoxal/pyridoxamine kinase;
75-246 5.68e-14

pyridoxine/pyridoxal/pyridoxamine kinase;


Pssm-ID: 181269 [Multi-domain]  Cd Length: 281  Bit Score: 70.07  E-value: 5.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  75 AVKLGMLFSSEIIQIVAEQIKKFGWNN----IVLDPVMIAKGGASLLQQEAVQALKEYLLPVATVITPNVPEAEVLTGME 150
Cdd:PRK08176  91 AVTTGYMGSASQIKILAEWLTALRADHpdllIMVDPVIGDIDSGIYVKPDLPEAYRQHLLPLAQGLTPNIFELEILTGKP 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 151 IHNVEDSKEAAKVLHELGAKYVLMKGGHAEYQGNEVIDFLFDGEKFIEFRSERIPSkQTHGSGCTFASAVTAGLAKGYSI 230
Cdd:PRK08176 171 CRTLDSAIAAAKSLLSDTLKWVVITSAAGNEENQEMQVVVVTADSVNVISHPRVDT-DLKGTGDLFCAELVSGLLKGKAL 249

                        170
                 ....*....|....*.
gi 446790135 231 EDAVQEAKRFISIAIE 246
Cdd:PRK08176 250 TDAAHRAGLRVLEVMR 265
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
 70-175 2.72e-13

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 68.18  E-value: 2.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  70 DLTPD--AVKLGMLFSSEIIQIVAEQIKKFGWNNIVL----DPVMiAKGGASLLQQEAVQALKEyLLPVATVITPNVPEA 143
Cdd:PTZ00344  73 NLLSDytYVLTGYINSADILREVLATVKEIKELRPKLiflcDPVM-GDDGKLYVKEEVVDAYRE-LIPYADVITPNQFEA 150

                         90       100       110
                 ....*....|....*....|....*....|..
gi 446790135 144 EVLTGMEIHNVEDSKEAAKVLHELGAKYVLMK 175
Cdd:PTZ00344 151 SLLSGVEVKDLSDALEAIDWFHEQGIPVVVIT 182
pyridox_kin TIGR00687
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ...
 54-235 6.02e-13

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: 67.16  E-value: 6.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135   54 PVPLEGVTEQLNSIGTDLTPDAVKLGMLFSSE----IIQIVaEQIKKFGWNNI-VLDPVMIAKGGASLLQQEAVQALKEY 128
Cdd:TIGR00687  56 PDELHELVEGLEAINKLNQCDAVLSGYLGSAEqvamVVGIV-RQVKQANPQALyVCDPVMGDPWKGCYVAPDLLEVYREK 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  129 LLPVATVITPNVPEAEVLTGMEIHNVEDSKEAAKVLHELGAKYVLMKG-GHAEYQGNEVIDFLF-DGEKFIEFRSERIP- 205
Cdd:TIGR00687 135 AIPVADIITPNQFELELLTGRRINTEEEALAAADALIAMGPDIVLVTHlIRAGSQRDRSFEGLVaTQEGRWHISRPLAVf 214

                         170       180       190
                  ....*....|....*....|....*....|
gi 446790135  206 SKQTHGSGCTFASAVTAGLAKGYSIEDAVQ 235
Cdd:TIGR00687 215 DPPPVGTGDLIAALLLATLLHGNSLKEALE 244
PRK05756 PRK05756
pyridoxal kinase PdxY;
74-237 8.12e-13

pyridoxal kinase PdxY;


Pssm-ID: 235592 [Multi-domain]  Cd Length: 286  Bit Score: 66.82  E-value: 8.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  74 DAVKLGMLFSSEIIQIVAEQIKKFGWNN----IVLDPVMIAKGGASLLQQEAVQALKEYLLPVATVITPNVPEAEVLTGM 149
Cdd:PRK05756  76 DAVLSGYLGSAEQGEAILDAVRRVKAANpqalYFCDPVMGDPEKGCIVAPGVAEFLRDRALPAADIITPNLFELEWLSGR 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 150 EIHNVEDSKEAAKVLHELGAKYVLMKggHAEYQG--NEVIDFLF-DGEKFIEFRSERIP-SKQTHGSGCTFASAVTAGLA 225
Cdd:PRK05756 156 PVETLEDAVAAARALIARGPKIVLVT--SLARAGypADRFEMLLvTADGAWHISRPLVDfMRQPVGVGDLTSALFLARLL 233

                        170
                 ....*....|..
gi 446790135 226 KGYSIEDAVQEA 237
Cdd:PRK05756 234 QGGSLEEALEHT 245
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 71-225 9.01e-13

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: 65.19  E-value: 9.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  71 LTPDAVKLGMLFSS-EIIQIVAEQIKKFGwNNIVLDPVMIAKggasllqqEAVQALKEYLLPVATVITPNVPEAEVLTGM 149
Cdd:cd00287   56 VGADAVVISGLSPApEAVLDALEEARRRG-VPVVLDPGPRAV--------RLDGEELEKLLPGVDILTPNEEEAEALTGR 126

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446790135 150 EIHNVEDSKEAAKVLHELGAKYVLMKGGHaeyQGneviDFLFDgEKFIEFRSERIPSKQ--THGSGCTFASAVTAGLA 225
Cdd:cd00287  127 RDLEVKEAAEAAALLLSKGPKVVIVTLGE---KG----AIVAT-RGGTEVHVPAFPVKVvdTTGAGDAFLAALAAGLA 196
PLN02978 PLN02978
pyridoxal kinase
 79-227 9.16e-13

pyridoxal kinase


Pssm-ID: 215529 [Multi-domain]  Cd Length: 308  Bit Score: 67.07  E-value: 9.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135  79 GMLFSSEIIQIVAEQIKKFGWNN----IVLDPVMIAKGGASLlQQEAVQALKEYLLPVATVITPNVPEAEVLTGMEIHNV 154
Cdd:PLN02978  93 GYIGSVSFLRTVLRVVKKLRSVNpnltYVCDPVLGDEGKLYV-PPELVPVYREKVVPLATMLTPNQFEAEQLTGIRIVTE 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 155 EDSKEAAKVLHELGAKYV-----------LMKGGHAEYQGNEVIDFLfdgekfieFRSERIPSKQThGSGCTFASAVTAG 223
Cdd:PLN02978 172 EDAREACAILHAAGPSKVvitsididgklLLVGSHRKEKGARPEQFK--------IVIPKIPAYFT-GTGDLMAALLLGW 242


                 ....
gi 446790135 224 LAKG 227
Cdd:PLN02978 243 SHKY 246
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
 128-246 2.66e-11

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: 62.33  E-value: 2.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 128 YLLPVATVITPNVPEAEVLTGMEIHNVEDSKEAAKVLHELGAKYVLMKGGhaeyqGNEVidFLFDGEKFIEFRSERIPSK 207
Cdd:cd01941  172 YLLHAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLG-----AKGV--LLSSREGGVETKLFPAPQP 244

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446790135 208 QT----HGSGCTFASAVTAGLAKGYSIEDAVQEAKRFISIAIE 246
Cdd:cd01941  245 ETvvnvTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALTLE 287
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 102-237 3.01e-11

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: 62.21  E-value: 3.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 102 IVLDPvmiakGGASLLQQEAVQALKEyLLPVATVITPNVPEAEVLTGMEihnveDSKEAAKVLHELGAKYVLMKGGHaey 181
Cdd:COG0524  161 VSLDP-----NYRPALWEPARELLRE-LLALVDILFPNEEEAELLTGET-----DPEEAAAALLARGVKLVVVTLGA--- 226

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446790135 182 QGneVIdfLFDGEKFIEFRSERIPSKQTHGSGCTFASAVTAGLAKGYSIEDAVQEA 237
Cdd:COG0524  227 EG--AL--LYTGGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFA 278
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
134-237 4.65e-11

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


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 61.69  E-value: 4.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 134 TVITPNVPEAEVLTGMEIHNVEDSKEAAKVLHELGAKYVL--MKGGHAeyqgnevidFLFDGEKFIEFRSERIPSKQTHG 211
Cdd:COG1105  179 DLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVvsLGADGA---------LLVTEDGVYRAKPPKVEVVSTVG 249

                         90       100
                 ....*....|....*....|....*.
gi 446790135 212 SGCTFASAVTAGLAKGYSIEDAVQEA 237
Cdd:COG1105  250 AGDSMVAGFLAGLARGLDLEEALRLA 275
PRK11142 PRK11142
ribokinase; Provisional
 123-245 2.51e-10

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 59.88  E-value: 2.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 123 QALKEYLLPVATVITPNVPEAEVLTGMEIHNVEDSKEAAKVLHELGAKYVLM----KGGHAEYQGNevidflfdGEKFIE 198
Cdd:PRK11142 169 RELPDELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLItlgsRGVWLSENGE--------GQRVPG 240

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446790135 199 FRSERIpskQTHGSGCTFASAVTAGLAKGYSIEDAVQEAKRFISIAI 245
Cdd:PRK11142 241 FRVQAV---DTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAV 284
KdgK cd01166
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ...
 118-237 1.42e-07

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: 51.42  E-value: 1.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 118 QQEAVQALKEyLLPVATVITPNVPEAEVLTGMEIHnvEDSKEAAKvLHELGAKYVLMKGGHAEYqgnevidFLFDGEKFI 197
Cdd:cd01166  172 AEEAREALEE-LLPYVDIVLPSEEEAEALLGDEDP--TDAAERAL-ALALGVKAVVVKLGAEGA-------LVYTGGGRV 240

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446790135 198 EFRSERIPSKQTHGSGCTFASAVTAGLAKGYSIEDAVQEA 237
Cdd:cd01166  241 FVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFA 280
RfaE_like cd01172
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ...
 133-235 3.51e-07

RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the lipopolysaccharide (LPS) core precursor ADP-L-glycero-D-manno-heptose. LPS plays an important role in maintaining the structural integrity of the bacterial outer membrane of gram-negative bacteria. RfaE consists of two domains, a sugar kinase domain, represented here, and a domain belonging to the cytidylyltransferase superfamily.


Pssm-ID: 238577 [Multi-domain]  Cd Length: 304  Bit Score: 50.25  E-value: 3.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 133 ATVITPNVPEAEVLTGMEIHNVEDSKEAA-KVLHELGAKYVLMKgghaeyQGNEVIdFLFDGEKfiefRSERIP--SKQ- 208
Cdd:cd01172  182 ATLLTPNEKEAREALGDEINDDDELEAAGeKLLELLNLEALLVT------LGEEGM-TLFERDG----EVQHIPalAKEv 250

                         90       100
                 ....*....|....*....|....*....
gi 446790135 209 --THGSGCTFASAVTAGLAKGYSIEDAVQ 235
Cdd:cd01172  251 ydVTGAGDTVIATLALALAAGADLEEAAF 279
YegV_kinase_like cd01944
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ...
 129-246 5.94e-04

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


Pssm-ID: 238919 [Multi-domain]  Cd Length: 289  Bit Score: 40.48  E-value: 5.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 129 LLPVATVITPNVPEAEVLTG-----MEIHNVED-SKEAAKVLHELGAK--YVLMKGGHAEYqgnevidflfdgekfIEfr 200
Cdd:cd01944  178 LMAKRPIWSCNREEAAIFAErgdpaAEASALRIyAKTAAPVVVRLGSNgaWIRLPDGNTHI---------------IP-- 240

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446790135 201 SERIPSKQTHGSGCTFASAVTAGLAKGYSIEDAVQEAKRFISIAIE 246
Cdd:cd01944  241 GFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVT 286
YXKO-related cd01171
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ...
 134-237 9.83e-04

B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of the ATP binding site, the substrate binding site and the Mg2+binding site and structural homology this group is a member of the ribokinase-like superfamily.


Pssm-ID: 238576  Cd Length: 254  Bit Score: 39.52  E-value: 9.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 134 TVITPNVPEAEVLTGMEIHNVE-DSKEAAKVLHELGAKYVLMKGGHaeyqgneviDFLFDGEKFIEFRSERIPSKQTHGS 212
Cdd:cd01171  130 VVLTPHPGEFARLLGALVEEIQaDRLAAAREAAAKLGATVVLKGAV---------TVIADPDGRVYVNPTGNPGLATGGS 200

                         90       100
                 ....*....|....*....|....*
gi 446790135 213 GCTFASAVTAGLAKGYSIEDAVQEA 237
Cdd:cd01171  201 GDVLAGIIAALLAQGLSPLEAAALA 225
PTZ00292 PTZ00292
ribokinase; Provisional
 122-248 1.24e-03

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 39.72  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 122 VQALKEYLLPVATVItPNVPEAEVLTGMEIHNVEDSKEAAKVLHELGAKYVLMKGGHAEYQgnevidFLFDGEKFIEFRS 201
Cdd:PTZ00292 189 VEIIKPFLKYVSLFC-VNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCL------IVEKENEPVHVPG 261

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446790135 202 ERIPSKQTHGSGCTFASAVTAGLAKGYSIEDAVQEAKRFISIAIEEP 248
Cdd:PTZ00292 262 KRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRH 308
Guanosine_kinase_like cd01947
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ...
 200-247 1.60e-03

Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like group is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.


Pssm-ID: 238922 [Multi-domain]  Cd Length: 265  Bit Score: 38.94  E-value: 1.60e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446790135 200 RSERIPSKQ-----THGSGCTFASAVTAGLAKGYSIEDAVQEAKRFISIAIEE 247
Cdd:cd01947  209 RYNHVPAKKakvpdSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSH 261
ribokinase_group_D cd01937
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ...
 126-246 1.82e-03

Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.


Pssm-ID: 238912 [Multi-domain]  Cd Length: 254  Bit Score: 38.92  E-value: 1.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446790135 126 KEYLLPVATVITPNVPEAEVLTgmeihnveDSKEAAKVLHELGAKYVLMKGGHAEYqgnevidFLFDGEKFIEFRSERIP 205
Cdd:cd01937  149 KCVILKLHDVLKLSRVEAEVIS--------TPTELARLIKETGVKEIIVTDGEEGG-------YIFDGNGKYTIPASKKD 213

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 446790135 206 SKQTHGSGCTFASAVTAGLAKGYSIEDAVQEAKRFISIAIE 246
Cdd:cd01937  214 VVDPTGAGDVFLAAFLYSRLSGKDIKEAAEFAAAAAAKFIE 254
 
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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