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Conserved domains on  [gi|556428804|ref|WP_023312429|]
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MULTISPECIES: bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase [Enterobacter]

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
 1-266 9.70e-163

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


:

Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 451.50  E-value: 9.70e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804   1 MKRINALTIAGTDPSGGAGIQADLKTFSALGAYGCSVITALVAQNTRGVQSVYRIEPDFVAAQLDSVFSDVRIDTTKIGM 80
Cdd:PRK06427   2 MKRPIALTIAGSDSGGGAGIQADLKTFQALGVYGMSAITALTAQNTLGVQRVHPIPPEFVAAQLDAVFSDIRIDAVKIGM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804  81 LAETDIVEAVAERLKRYQVQNVVLDTVMLAKSGDPLLSASAVETLRTKLLPQVALITPNLPEAAALLGTSHAQTEREMKA 160
Cdd:PRK06427  82 LASAEIIETVAEALKRYPIPPVVLDPVMIAKSGDPLLADDAVAALRERLLPLATLITPNLPEAEALTGLPIADTEDEMKA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804 161 QGNALLAMGCGAVLMKGGH-LDDAESPDWLFTRDGEVRFTAPRVQTKNTHGTGCTLSAALAALRPRHDGWADTVREAKTW 239
Cdd:PRK06427 162 AARALHALGCKAVLIKGGHlLDGEESVDWLFDGEGEERFSAPRIPTKNTHGTGCTLSAAIAAELAKGASLLDAVQTAKDY 241

                        250       260
                 ....*....|....*....|....*..
gi 556428804 240 LSAALakADTLEVGHGIGPVHHFHAWW 266
Cdd:PRK06427 242 VTRAI--RHALEIGQGHGPVNHFAYLW 266
 
Name Accession Description Interval E-value
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 1-266 9.70e-163

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 451.50  E-value: 9.70e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804   1 MKRINALTIAGTDPSGGAGIQADLKTFSALGAYGCSVITALVAQNTRGVQSVYRIEPDFVAAQLDSVFSDVRIDTTKIGM 80
Cdd:PRK06427   2 MKRPIALTIAGSDSGGGAGIQADLKTFQALGVYGMSAITALTAQNTLGVQRVHPIPPEFVAAQLDAVFSDIRIDAVKIGM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804  81 LAETDIVEAVAERLKRYQVQNVVLDTVMLAKSGDPLLSASAVETLRTKLLPQVALITPNLPEAAALLGTSHAQTEREMKA 160
Cdd:PRK06427  82 LASAEIIETVAEALKRYPIPPVVLDPVMIAKSGDPLLADDAVAALRERLLPLATLITPNLPEAEALTGLPIADTEDEMKA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804 161 QGNALLAMGCGAVLMKGGH-LDDAESPDWLFTRDGEVRFTAPRVQTKNTHGTGCTLSAALAALRPRHDGWADTVREAKTW 239
Cdd:PRK06427 162 AARALHALGCKAVLIKGGHlLDGEESVDWLFDGEGEERFSAPRIPTKNTHGTGCTLSAAIAAELAKGASLLDAVQTAKDY 241

                        250       260
                 ....*....|....*....|....*..
gi 556428804 240 LSAALakADTLEVGHGIGPVHHFHAWW 266
Cdd:PRK06427 242 VTRAI--RHALEIGQGHGPVNHFAYLW 266
HMP-P_kinase TIGR00097
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ...
 6-262 7.33e-143

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: 400.90  E-value: 7.33e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804    6 ALTIAGTDPSGGAGIQADLKTFSALGAYGCSVITALVAQNTRGVQSVYRIEPDFVAAQLDSVFSDVRIDTTKIGMLAETD 85
Cdd:TIGR00097   1 ALTIAGSDSGGGAGIQADLKTFSALGVFGTSVITALTAQNTRGVTGVYPIPPDFVEAQLDAVFSDIPVDAAKTGMLASAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804   86 IVEAVAERLKRYQVQNVVLDTVMLAKSGDPLLSASAVETLRTKLLPQVALITPNLPEAAALLGTsHAQTEREMKAQGNAL 165
Cdd:TIGR00097  81 IVEAVARKLREYPVRPLVVDPVMVAKSGAPLLEEEAIEALRKRLLPLATLITPNLPEAEALLGT-KIRTEQDMIKAAKKL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804  166 LAMGCGAVLMKGGHLDDAESPDWLFTRDGEVRFTAPRVQTKNTHGTGCTLSAALAALRPRHDGWADTVREAKTWLSAALA 245
Cdd:TIGR00097 160 RELGPKAVLIKGGHLEGDQAVDVLFDGGEIHILKAPRIETKNTHGTGCTLSAAIAANLAKGLSLKEAVKEAKEFVTGAIR 239

                         250
                  ....*....|....*..
gi 556428804  246 KAdtLEVGHGIGPVHHF 262
Cdd:TIGR00097 240 YG--LNIGHGHGPLNHF 254
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 7-263 5.75e-137

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: 385.93  E-value: 5.75e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804   7 LTIAGTDPSGGAGIQADLKTFSALGAYGCSVITALVAQNTRGVQSVYRIEPDFVAAQLDSVFSDVRIDTTKIGMLAETDI 86
Cdd:COG0351    1 LTIAGSDPSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVTGVHPVPPEFVAAQLRAVLEDIPVDAIKIGMLGSAEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804  87 VEAVAERLKRYQVQNVVLDTVMLAKSGDPLLSASAVETLRTKLLPQVALITPNLPEAAALLGTShAQTEREMKAQGNALL 166
Cdd:COG0351   81 IEAVAEILADYPLVPVVLDPVMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALLGIE-ITTLDDMREAAKALL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804 167 AMGCGAVLMKGGHLDDAESPDWLFTRDGEVRFTAPRVQTKNTHGTGCTLSAALAALRPRHDGWADTVREAKTWLSAALAK 246
Cdd:COG0351  160 ELGAKAVLVKGGHLPGDEAVDVLYDGDGVREFSAPRIDTGNTHGTGCTLSSAIAALLAKGLDLEEAVREAKEYVTQAIRA 239

                        250
                 ....*....|....*..
gi 556428804 247 AdtLEVGHGIGPVHHFH 263
Cdd:COG0351  240 A--LRLGMGHGPVNHFA 254
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 13-260 1.34e-126

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: 359.49  E-value: 1.34e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804   13 DPSGGAGIQADLKTFSALGAYGCSVITALVAQNTRGVQSVYRIEPDFVAAQLDSVFSDVRIDTTKIGMLAETDIVEAVAE 92
Cdd:pfam08543   1 DSSGGAGIQADLKTFSALGVYGMSVITALTAQNTLGVQGVHPLPPEFVAAQLDAVLEDIPVDAVKTGMLGSAEIIEAVAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804   93 RLKRYQVqNVVLDTVMLAKSGDPLLSASAVETLRTKLLPQVALITPNLPEAAALLGTsHAQTEREMKAQGNALLAMGCGA 172
Cdd:pfam08543  81 KLDKYGV-PVVLDPVMVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGR-KIKTLEDMKEAAKKLLALGAKA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804  173 VLMKGGHL--DDAESPDWLFTRDGEVRFTAPRVQTKNTHGTGCTLSAALAALRPRHDGWADTVREAKTWLSAALAKAdtL 250
Cdd:pfam08543 159 VLIKGGHLegEEAVVTDVLYDGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKEYVTEAIRDA--L 236

                         250
                  ....*....|
gi 556428804  251 EVGHGIGPVH 260
Cdd:pfam08543 237 NLGKGHGPVN 246
HMPP_kinase cd01169
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ...
 5-247 1.37e-120

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: 344.10  E-value: 1.37e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804   5 NALTIAGTDPSGGAGIQADLKTFSALGAYGCSVITALVAQNTRGVQSVYRIEPDFVAAQLDSVFSDVRIDTTKIGMLAET 84
Cdd:cd01169    1 VVLTIAGSDSSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVFGVHPVPPEFVAAQLDAVLEDIPVDAIKIGMLGSA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804  85 DIVEAVAERLKRYQVQNVVLDTVMLAKSGDPLLSASAVETLRTKLLPQVALITPNLPEAAALLGTSHAqTEREMKAQGNA 164
Cdd:cd01169   81 EIIEAVAEALKDYPDIPVVLDPVMVAKSGDSLLDDDAIEALRELLLPLATLITPNLPEAELLTGLEIA-TEEDMMKAAKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804 165 LLAMGCGAVLMKGGHLDDAESPDWLFTRDGEVRFTAPRVQTKNTHGTGCTLSAALAALRPRHDGWADTVREAKTWLSAAL 244
Cdd:cd01169  160 LLALGAKAVLIKGGHLPGDEAVDVLYDGGGFFEFESPRIDTKNTHGTGCTLSSAIAANLAKGLSLEEAVREAKEYVTQAI 239


                 ...
gi 556428804 245 AKA 247
Cdd:cd01169  240 RNA 242
 
Name Accession Description Interval E-value
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 1-266 9.70e-163

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


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 451.50  E-value: 9.70e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804   1 MKRINALTIAGTDPSGGAGIQADLKTFSALGAYGCSVITALVAQNTRGVQSVYRIEPDFVAAQLDSVFSDVRIDTTKIGM 80
Cdd:PRK06427   2 MKRPIALTIAGSDSGGGAGIQADLKTFQALGVYGMSAITALTAQNTLGVQRVHPIPPEFVAAQLDAVFSDIRIDAVKIGM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804  81 LAETDIVEAVAERLKRYQVQNVVLDTVMLAKSGDPLLSASAVETLRTKLLPQVALITPNLPEAAALLGTSHAQTEREMKA 160
Cdd:PRK06427  82 LASAEIIETVAEALKRYPIPPVVLDPVMIAKSGDPLLADDAVAALRERLLPLATLITPNLPEAEALTGLPIADTEDEMKA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804 161 QGNALLAMGCGAVLMKGGH-LDDAESPDWLFTRDGEVRFTAPRVQTKNTHGTGCTLSAALAALRPRHDGWADTVREAKTW 239
Cdd:PRK06427 162 AARALHALGCKAVLIKGGHlLDGEESVDWLFDGEGEERFSAPRIPTKNTHGTGCTLSAAIAAELAKGASLLDAVQTAKDY 241

                        250       260
                 ....*....|....*....|....*..
gi 556428804 240 LSAALakADTLEVGHGIGPVHHFHAWW 266
Cdd:PRK06427 242 VTRAI--RHALEIGQGHGPVNHFAYLW 266
HMP-P_kinase TIGR00097
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ...
 6-262 7.33e-143

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: 400.90  E-value: 7.33e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804    6 ALTIAGTDPSGGAGIQADLKTFSALGAYGCSVITALVAQNTRGVQSVYRIEPDFVAAQLDSVFSDVRIDTTKIGMLAETD 85
Cdd:TIGR00097   1 ALTIAGSDSGGGAGIQADLKTFSALGVFGTSVITALTAQNTRGVTGVYPIPPDFVEAQLDAVFSDIPVDAAKTGMLASAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804   86 IVEAVAERLKRYQVQNVVLDTVMLAKSGDPLLSASAVETLRTKLLPQVALITPNLPEAAALLGTsHAQTEREMKAQGNAL 165
Cdd:TIGR00097  81 IVEAVARKLREYPVRPLVVDPVMVAKSGAPLLEEEAIEALRKRLLPLATLITPNLPEAEALLGT-KIRTEQDMIKAAKKL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804  166 LAMGCGAVLMKGGHLDDAESPDWLFTRDGEVRFTAPRVQTKNTHGTGCTLSAALAALRPRHDGWADTVREAKTWLSAALA 245
Cdd:TIGR00097 160 RELGPKAVLIKGGHLEGDQAVDVLFDGGEIHILKAPRIETKNTHGTGCTLSAAIAANLAKGLSLKEAVKEAKEFVTGAIR 239

                         250
                  ....*....|....*..
gi 556428804  246 KAdtLEVGHGIGPVHHF 262
Cdd:TIGR00097 240 YG--LNIGHGHGPLNHF 254
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 7-263 5.75e-137

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: 385.93  E-value: 5.75e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804   7 LTIAGTDPSGGAGIQADLKTFSALGAYGCSVITALVAQNTRGVQSVYRIEPDFVAAQLDSVFSDVRIDTTKIGMLAETDI 86
Cdd:COG0351    1 LTIAGSDPSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVTGVHPVPPEFVAAQLRAVLEDIPVDAIKIGMLGSAEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804  87 VEAVAERLKRYQVQNVVLDTVMLAKSGDPLLSASAVETLRTKLLPQVALITPNLPEAAALLGTShAQTEREMKAQGNALL 166
Cdd:COG0351   81 IEAVAEILADYPLVPVVLDPVMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALLGIE-ITTLDDMREAAKALL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804 167 AMGCGAVLMKGGHLDDAESPDWLFTRDGEVRFTAPRVQTKNTHGTGCTLSAALAALRPRHDGWADTVREAKTWLSAALAK 246
Cdd:COG0351  160 ELGAKAVLVKGGHLPGDEAVDVLYDGDGVREFSAPRIDTGNTHGTGCTLSSAIAALLAKGLDLEEAVREAKEYVTQAIRA 239

                        250
                 ....*....|....*..
gi 556428804 247 AdtLEVGHGIGPVHHFH 263
Cdd:COG0351  240 A--LRLGMGHGPVNHFA 254
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 13-260 1.34e-126

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: 359.49  E-value: 1.34e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804   13 DPSGGAGIQADLKTFSALGAYGCSVITALVAQNTRGVQSVYRIEPDFVAAQLDSVFSDVRIDTTKIGMLAETDIVEAVAE 92
Cdd:pfam08543   1 DSSGGAGIQADLKTFSALGVYGMSVITALTAQNTLGVQGVHPLPPEFVAAQLDAVLEDIPVDAVKTGMLGSAEIIEAVAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804   93 RLKRYQVqNVVLDTVMLAKSGDPLLSASAVETLRTKLLPQVALITPNLPEAAALLGTsHAQTEREMKAQGNALLAMGCGA 172
Cdd:pfam08543  81 KLDKYGV-PVVLDPVMVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGR-KIKTLEDMKEAAKKLLALGAKA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804  173 VLMKGGHL--DDAESPDWLFTRDGEVRFTAPRVQTKNTHGTGCTLSAALAALRPRHDGWADTVREAKTWLSAALAKAdtL 250
Cdd:pfam08543 159 VLIKGGHLegEEAVVTDVLYDGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKEYVTEAIRDA--L 236

                         250
                  ....*....|
gi 556428804  251 EVGHGIGPVH 260
Cdd:pfam08543 237 NLGKGHGPVN 246
HMPP_kinase cd01169
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ...
 5-247 1.37e-120

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: 344.10  E-value: 1.37e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804   5 NALTIAGTDPSGGAGIQADLKTFSALGAYGCSVITALVAQNTRGVQSVYRIEPDFVAAQLDSVFSDVRIDTTKIGMLAET 84
Cdd:cd01169    1 VVLTIAGSDSSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVFGVHPVPPEFVAAQLDAVLEDIPVDAIKIGMLGSA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804  85 DIVEAVAERLKRYQVQNVVLDTVMLAKSGDPLLSASAVETLRTKLLPQVALITPNLPEAAALLGTSHAqTEREMKAQGNA 164
Cdd:cd01169   81 EIIEAVAEALKDYPDIPVVLDPVMVAKSGDSLLDDDAIEALRELLLPLATLITPNLPEAELLTGLEIA-TEEDMMKAAKA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804 165 LLAMGCGAVLMKGGHLDDAESPDWLFTRDGEVRFTAPRVQTKNTHGTGCTLSAALAALRPRHDGWADTVREAKTWLSAAL 244
Cdd:cd01169  160 LLALGAKAVLIKGGHLPGDEAVDVLYDGGGFFEFESPRIDTKNTHGTGCTLSSAIAANLAKGLSLEEAVREAKEYVTQAI 239


                 ...
gi 556428804 245 AKA 247
Cdd:cd01169  240 RNA 242
PRK14713 PRK14713
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
7-264 1.65e-100

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 237797 [Multi-domain]  Cd Length: 530  Bit Score: 303.25  E-value: 1.65e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804   7 LTIAGTDPSGGAGIQADLKTFSALGAYGCSVITALVAQNTRGVQSVYRIEPDFVAAQLDSVFSDVRIDTTKIGMLAETDI 86
Cdd:PRK14713  33 LSIAGTDPSGGAGIQADLKSIAAAGGYGMAVITALVAQNTRGVRAVHVPPADFLRAQLDAVSDDVTVDAVKIGMLGDAEV 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804  87 VEAVAERLKRYQVQNVVLDTVMLAKSGDPLLSASAVETLRtKLLPQVALITPNLPEAAALLGTSHAQTEREMKAQGNALL 166
Cdd:PRK14713 113 IDAVRTWLAEHRPPVVVLDPVMVATSGDRLLEEDAEAALR-ELVPRADLITPNLPELAVLLGEPPATTWEEALAQARRLA 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804 167 AMGCGAVLMKGGHLDDAESPDWLFTRDGEV-RFTAPRVQTKNTHGTGCTLSAALAALRPRHDGWADTVREAKTWLSAALA 245
Cdd:PRK14713 192 AETGTTVLVKGGHLDGQRAPDALVGPDGAVtEVPGPRVDTRNTHGTGCSLSSALATRLGRGGDWAAALRWATAWLHGAIA 271

                        250
                 ....*....|....*....
gi 556428804 246 KADTLEVGHGIGPVHHFHA 264
Cdd:PRK14713 272 AGAALQVGTGNGPVDHFHR 290
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
 1-262 8.46e-93

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 282.43  E-value: 8.46e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804   1 MKRINALTIAGTDPSGGAGIQADLKTFSALGAYGCSVITALVAQNTRGVQSVYRIEPDFVAAQLDSVFSDVRIDTTKIGM 80
Cdd:PLN02898   7 MKVPHVLTVAGSDSGAGAGIQADIKACAARGVYCTTAITAVTAQNTVGVQGVHAVPLDFVAEQLKSVLSDMPVDVVKTGM 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804  81 LAETDIVEAVAERLKRYQVQNVVLDTVMLAKSGDPLLSASAVETLRTKLLPQVALITPNLPEAAALLGTSHAQTEREMKA 160
Cdd:PLN02898  87 LPSAEIVKVLCQALKEFPVKALVVDPVMVSTSGDVLAGPSILSALREELLPLATIVTPNVKEASALLGGDPLETVADMRS 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804 161 QGNALLAMGCGAVLMKGGHL-DDAESPDWLFTRDGEVRFTAPRVQTKNTHGTGCTLSAALAALRPRHDGWADTVREAKTW 239
Cdd:PLN02898 167 AAKELHKLGPRYVLVKGGHLpDSLDAVDVLYDGTEFHELRSSRIKTRNTHGTGCTLASCIAAELAKGSDMLSAVKVAKRY 246

                        250       260
                 ....*....|....*....|....
gi 556428804 240 LSAALAKADTLEVGHGI-GPVHHF 262
Cdd:PLN02898 247 VETALEYSKDIGIGNGAqGPFNHL 270
PRK09517 PRK09517
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ...
 7-263 1.00e-77

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


Pssm-ID: 169939 [Multi-domain]  Cd Length: 755  Bit Score: 249.89  E-value: 1.00e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804   7 LTIAGTDPSGGAGIQADLKTFSALGAYGCSVITALVAQNTRGVQSVYRIEPDFVAAQLDSVFSDVRIDTTKIGMLAETDI 86
Cdd:PRK09517 245 LSIAGTDPTGGAGIQADLKSIAAGGGYGMCVVTALVAQNTHGVNTIHTPPLTFLEEQLEAVFSDVTVDAVKLGMLGSADT 324

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804  87 VEAVAERLKRYQVQNVVLDTVMLAKSGDPLLSASAVETLRtKLLPQVALITPNLPEAAALLGTSHAQTEREMKAQGNALL 166
Cdd:PRK09517 325 VDLVASWLGSHEHGPVVLDPVMVATSGDRLLDADATEALR-RLAVHVDVVTPNIPELAVLCGEAPAITMDEAIAQARGFA 403

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804 167 AMGCGAVLMKGGHLDDAESPDWLFTRDGEVRFTA-PRVQTKNTHGTGCTLSAALAALRPRHDGWADTVREAKTWLSAALA 245
Cdd:PRK09517 404 RTHGTIVIVKGGHLTGDLADNAVVRPDGSVHQVEnPRVNTTNSHGTGCSLSAALATLIAAGESVEKALEWATRWLNEALR 483

                        250
                 ....*....|....*...
gi 556428804 246 KADTLEVGHGIGPVHHFH 263
Cdd:PRK09517 484 HADHLAVGSGNGPVDHGH 501
PRK08573 PRK08573
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
6-265 2.77e-72

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 236297 [Multi-domain]  Cd Length: 448  Bit Score: 228.07  E-value: 2.77e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804   6 ALTIAGTDPSGGAGIQADLKTFSALGAYGCSVITALVAQNTRGVQSVYRIEPDFVAAQLDSVFSDVRIDTTKIGMLAETD 85
Cdd:PRK08573   5 ALTIAGSDSGGGAGIEADLKTFAALGVHGAVAITSVTAQNTYEVRAIHDLPPEVVAAQIEAVWEDMGIDAAKTGMLSNRE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804  86 IVEAVAERLKRYQVQNVVlDTVMLAKSGDPLLSASAVETLRTKLLPQVALITPNLPEAAALLGTSHAQTEREMKAQGNAL 165
Cdd:PRK08573  85 IIEAVAKTVSKYGFPLVV-DPVMIAKSGAPLLREDAVDALIKRLLPLATVVTPNRPEAEKLTGMKIRSVEDARKAAKYIV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804 166 LAMGCGAVLMKGGHLDDAESPDWLFTRDGEVRFTAPRVQTKNTHGTGCTLSAALAALRPRHDGWADTVREAKTWLSAALA 245
Cdd:PRK08573 164 EELGAEAVVVKGGHLEGEEAVDVLYHNGTFREFRAPRVESGCTHGTGCSFSAAIAAGLAKGLDPEEAIKTAKKFITMAIK 243

                        250       260
                 ....*....|....*....|
gi 556428804 246 KAdtLEVGHGIGPVHHFhAW 265
Cdd:PRK08573 244 YG--VKIGKGHCPVNPM-AW 260
PTZ00347 PTZ00347
phosphomethylpyrimidine kinase; Provisional
 1-265 1.19e-64

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240375 [Multi-domain]  Cd Length: 504  Bit Score: 209.82  E-value: 1.19e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804   1 MKRINALTIAGTDPSGGAGIQADLKTFSALGAYGCSVITALVAQNTRGVQSVYRIEPDFVAAQLDSVFSDVRIDTTKIGM 80
Cdd:PTZ00347 228 MKIPTVLTVSGSDSGGGAGHQADLKTLEALGVYSTSALTSLTAQNTKGVQQIQVVNEDFFAAQIDSVMSDFNISVVKLGL 307

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804  81 LAETDIVEAVAERLKRYQvqnVVLDTVMLAKSGDPLLSASAVETL----RTKLLPQVALITPNLPEAAALLGTSHAQTER 156
Cdd:PTZ00347 308 VPTARQLEIVIEKLKNLP---MVVDPVLVATSGDDLVAQKNADDVlamyKERIFPMATIITPNIPEAERILGRKEITGVY 384

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804 157 EMKAQGNALLAMGCGAVLMKGGH--LDDAESPDWLFTRDGE--VRFTAPRVQTKNTHGTGCTLSAALAALRPRHDGWADT 232
Cdd:PTZ00347 385 EARAAAQALAQYGSRYVLVKGGHdlIDPEACRDVLYDREKDrfYEFTANRIATINTHGTGCTLASAISSFLARGYTVPDA 464

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 556428804 233 VREAKTWLSAALAKADTLEVGHGI-GPVHH--FHAW 265
Cdd:PTZ00347 465 VERAIGYVHEAIVRSCGVPLGQGTnRPLVHslNSVW 500
PRK12412 PRK12412
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
6-261 2.54e-53

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183512 [Multi-domain]  Cd Length: 268  Bit Score: 174.00  E-value: 2.54e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804   6 ALTIAGTDPSGGAGIQADLKTFSALGAYGCSVITALVAQN--TRGVQSVYRIEPDFVAAQLDSVFSDVRIDTTKIGMLAE 83
Cdd:PRK12412   4 ALTIAGSDTSGGAGIQADLKTFQELGVYGMTSLTTIVTMDphNGWAHNVFPIPASTLKPQLETTIEGVGVDALKTGMLGS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804  84 TDIVEAVAERLKRYQVQNVVLDTVMLAKSGDPLLSASAVETLRTKLLPQVALITPNLPEAAALLGTShAQTEREMKAQGN 163
Cdd:PRK12412  84 VEIIEMVAETIEKHNFKNVVVDPVMVCKGADEALHPETNDCLRDVLVPKALVVTPNLFEAYQLSGVK-INSLEDMKEAAK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804 164 ALLAMGCGAVLMKGGH-LDDAESPDWLFtrDGEV--RFTAPRVQTKNTHGTGCTLSAALAALRPRHDGWADTVREAKTWL 240
Cdd:PRK12412 163 KIHALGAKYVLIKGGSkLGTETAIDVLY--DGETfdLLESEKIDTTNTHGAGCTYSAAITAELAKGKPVKEAVKTAKEFI 240

                        250       260
                 ....*....|....*....|.
gi 556428804 241 SAALAKadTLEVGHGIGPVHH 261
Cdd:PRK12412 241 TAAIRY--SFKINEYVGPTHH 259
PRK12616 PRK12616
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
1-261 6.46e-52

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183624  Cd Length: 270  Bit Score: 170.23  E-value: 6.46e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804   1 MKRINALTIAGTDPSGGAGIQADLKTFSALGAYGCSVITALVAQNTRGV--QSVYRIEPDFVAAQLDSVFSDVRIDTTKI 78
Cdd:PRK12616   1 MSMHKALTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAMDPENSwdHQVFPIDTDTIRAQLSTIVDGIGVDAMKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804  79 GMLAETDIVEAVAERLKRYQVQNVVLDTVMLAKSGDPLLSASAVETLRTKLLPQVALITPNLPEAAALLGTSHAQTEREM 158
Cdd:PRK12616  81 GMLPTVDIIELAADTIKEKQLKNVVIDPVMVCKGANEVLYPEHAEALREQLAPLATVITPNLFEAGQLSGMGEIKTVEQM 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804 159 KAQGNALLAMGCGAVLMK-GGHLDDAESPDWLFtrDGEV--RFTAPRVQTKNTHGTGCTLSAALAALRPRHDGWADTVRE 235
Cdd:PRK12616 161 KEAAKKIHELGAQYVVITgGGKLKHEKAVDVLY--DGETaeVLESEMIDTPYTHGAGCTFSAAVTAELAKGSEVKEAIYA 238

                        250       260
                 ....*....|....*....|....*.
gi 556428804 236 AKTWLSAALakADTLEVGHGIGPVHH 261
Cdd:PRK12616 239 AKEFITAAI--KESFPLNQYVGPTKH 262
PRK12413 PRK12413
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
1-248 5.07e-39

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183513 [Multi-domain]  Cd Length: 253  Bit Score: 136.35  E-value: 5.07e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804   1 MKRINALTIAGTDPSGGAGIQADLKTFSALGAYGCSVITALVAQNTRGVqSVYRIEPDFVAAQLDSvFSDVRIDTTKIGM 80
Cdd:PRK12413   1 MKTNYILAISGNDIFSGGGLHADLATYTRNGLHGFVAVTCLTAMTEKGF-EVFPVDKEIFQQQLDS-LKDVPFSAIKIGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804  81 LAETDIVEAVAERLKRYQVQNVVLDTVMLAKSGDPLlsasAVETLR---TKLLPQVALITPNLPEAAALLGTShAQTERE 157
Cdd:PRK12413  79 LPNVEIAEQALDFIKGHPGIPVVLDPVLVCKETHDV----EVSELRqelIQFFPYVTVITPNLVEAELLSGKE-IKTLED 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804 158 MKAQGNALLAMGCGAVLMKGGH-LDDAESPDWLFtrDGE--VRFTAPRVQTKNThGTGCTLSAALAALRPRHDGWADTVR 234
Cdd:PRK12413 154 MKEAAKKLYDLGAKAVVIKGGNrLSQKKAIDLFY--DGKefVILESPVLEKNNI-GAGCTFASSIASQLVKGKSPLEAVK 230

                        250
                 ....*....|....
gi 556428804 235 EAKTWLSAALAKAD 248
Cdd:PRK12413 231 NSKDFVYQAIQQSD 244
COG1992 COG1992
Predicted transcriptional regulator fused phosphomethylpyrimidine kinase (thiamin biosynthesis) ...
 15-261 1.05e-38

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


Pssm-ID: 441595 [Multi-domain]  Cd Length: 432  Bit Score: 139.89  E-value: 1.05e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804  15 SGGAGIQADLKTFSALGAYGCSVITALVAQNTRGVQSVYRIEPDFVAAQLDSVFSDVRIDTTKIGMLAETDIVEAVAERL 94
Cdd:COG1992    1 GGGGGGGADAKTAAALGAGGGGTTTAVTVTATTTVTGVGSDPPPPVEVQQQAVAADDDVDDAKTGMLMTATIVEVVAVVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804  95 KRYQVqNVVLDTVMLAKSGDPLLSASAVETLRTKLLPQVALITPNLPEAAALLGTSHAQTEREMKAQGNALLAMGCGAVL 174
Cdd:COG1992   81 KSRDK-PLVVVVVPVAVAAAGLGLLLAEAELAKLLLPLLATVTPNEPEVEELLLPTIRSLLAEARAARLALQEEGADALG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804 175 MKGGHLDDAESPDWLFTRDGEVRFTAPRVQTKNTHGTGCTLSAALAALRPRHDGWADTVREAKTWLSAALAKAdtLEVGH 254
Cdd:COG1992  160 VKGGHVSGDAVVDVLEDERDVETFRHPRLVTEATHGSGCTFSAAIAALLAKGLSLEEAVRGAKLFLLHAIRYG--LLVGK 237


                 ....*..
gi 556428804 255 GIGPVHH 261
Cdd:COG1992  238 GVGPVNH 244
PTZ00493 PTZ00493
phosphomethylpyrimidine kinase; Provisional
 5-227 6.64e-29

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240440  Cd Length: 321  Bit Score: 111.62  E-value: 6.64e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804   5 NALTIAGTDPSGGAGIQADLKTFSALGAYGCSVITALVAQNTRGVQSVYRIEPDFVAAQLDSVFSDVRIDTTKIGMLAET 84
Cdd:PTZ00493   6 NILSIAGSDSCGGAGMQADIKTAMGLGCHCCTALVVLTAQNTKEVKRIVEIEEKFIVEQLDSIFADVTIDVVKLGVLYSK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804  85 DIVEAVAERL-----KRYQVQNVVLDTVMLAKSGdpLLSASAVETLRTKL---LPQVALITPNLPEAAALLGTSHAQTER 156
Cdd:PTZ00493  86 KIISLVHNYItnmnkKRGKKLLVVFDPVFVSSSG--CLLVENLEYIKFALdliCPISCIITPNFYECKVILEALDCQMDL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804 157 EmKAQGNALLA-----MGCGAVLMKGGHLD-DAESPDWLFTRD------------GEV---------------RFTAPRV 203
Cdd:PTZ00493 164 S-KANMTELCKlvtekLNINACLFKSCNVGeNSAEENEVYAVDhlcirnvgsyptGEKqqidaggvtylydvyKLRSKRK 242

                        250       260
                 ....*....|....*....|....*
gi 556428804 204 QTKNTHGTGCTLSAALAA-LRPRHD 227
Cdd:PTZ00493 243 PGKDIHGTGCTLSTAIACyLAKKHN 267
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
84-249 1.47e-12

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


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 66.31  E-value: 1.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804  84 TDIVEAVAERLKRYQVQnVVLDTvmlakSGDPLLSAsavetLRTKllpqVALITPNLPEAAALLGTShAQTEREMKAQGN 163
Cdd:COG1105  144 PDFYAELIRLARARGAK-VVLDT-----SGEALKAA-----LEAG----PDLIKPNLEELEELLGRP-LETLEDIIAAAR 207

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804 164 ALLAMGCGAVLmkgghLDDAESPDWLFTRDGEVRFTAPRVQTKNTHGTGCTLSAALAALRPRHDGWADTVREAKTWLSAA 243
Cdd:COG1105  208 ELLERGAENVV-----VSLGADGALLVTEDGVYRAKPPKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAA 282


                 ....*.
gi 556428804 244 LAKADT 249
Cdd:COG1105  283 ALSPGT 288
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 79-221 3.51e-10

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: 57.88  E-value: 3.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804  79 GMLAETDIVEAVAERLKRYQVQnVVLDTVMLAKSGDPllsasaveTLRTKLLPQVALITPNLPEAAALLGTSHAQTErEM 158
Cdd:cd00287   65 GLSPAPEAVLDALEEARRRGVP-VVLDPGPRAVRLDG--------EELEKLLPGVDILTPNEEEAEALTGRRDLEVK-EA 134

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556428804 159 KAQGNALLAMGCGAVLMKGGHLDDaespdWLFTRDGEVRFT-APRVQTKNTHGTGCTLSAALAA 221
Cdd:cd00287  135 AEAAALLLSKGPKVVIVTLGEKGA-----IVATRGGTEVHVpAFPVKVVDTTGAGDAFLAALAA 193
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 79-246 6.56e-09

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: 54.90  E-value: 6.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804  79 GMLAETDIVEAVAERLKRYQVQN----VVLDTVMlaksGDP----LLSASAVETLRTKLLPQVALITPNLPEAAALLGTS 150
Cdd:cd01173   79 GYLGSAEQVEAVAEIVKRLKEKNpnllYVCDPVM----GDNgklyVVAEEIVPVYRDLLVPLADIITPNQFELELLTGKK 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804 151 hAQTEREMKAQGNALLAMGCGAVLMKGGHLDDAESPDWL-FTRDGEVRFTAPRVQTkNTH--GTGCTLSAALAALRPRHD 227
Cdd:cd01173  155 -INDLEDAKAAARALHAKGPKTVVVTSVELADDDRIEMLgSTATEAWLVQRPKIPF-PAYfnGTGDLFAALLLARLLKGK 232

                        170
                 ....*....|....*....
gi 556428804 228 GWADTVREAKTWLSAALAK 246
Cdd:cd01173  233 SLAEALEKALNFVHEVLEA 251
PRK07105 PRK07105
pyridoxamine kinase; Validated
 1-221 2.93e-08

pyridoxamine kinase; Validated


Pssm-ID: 180840 [Multi-domain]  Cd Length: 284  Bit Score: 53.38  E-value: 2.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804   1 MKRInaltIAGTDPS--GGAGIQADLKTFSALGAYGCSVITALVAQNTRGVQSVYRIE-----PDFVAaQLDSVfsDVRI 73
Cdd:PRK07105   4 VKRV----AAIHDLSgfGRVALTASIPIMSSMGLQVCPLPTALLSSHTGGFQNPSIIDltdgmQAFLT-HWKSL--NLKF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804  74 DTTKIGMLAETDIVEAVAERLKRYQVQN--VVLDTVMlaksGD-----PLLSASAVETLRtKLLPQVALITPNLPEAAAL 146
Cdd:PRK07105  77 DAIYSGYLGSPRQIQIVSDFIKYFKKKDllVVVDPVM----GDngklyQGFDQEMVEEMR-KLIQKADVITPNLTEACLL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804 147 LGTSHAQ---TEREMKAQGNALLAMGCGAVLMKGGHLDDAESPDWLFTRDGE--VRFTAPRVqtkNTH--GTGCTLSAAL 219
Cdd:PRK07105 152 LDKPYLEksySEEEIKQLLRKLADLGPKIVIITSVPFEDGKIGVAYYDRATDrfWKVFCKYI---PAHypGTGDIFTSVI 228


                 ..
gi 556428804 220 AA 221
Cdd:PRK07105 229 TG 230
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 85-245 2.67e-07

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


Pssm-ID: 440290 [Multi-domain]  Cd Length: 301  Bit Score: 50.65  E-value: 2.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804  85 DIVEAVAERLKRYQVQnVVLDTvmlakSGDPLLSASAVETLRtKLLPQVALITPNLPEAAALLGTShaqterEMKAQGNA 164
Cdd:COG0524  145 EALLAALEAARAAGVP-VSLDP-----NYRPALWEPARELLR-ELLALVDILFPNEEEAELLTGET------DPEEAAAA 211

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804 165 LLAMGCGAVLMKGGhlddaESPDWLFTRDGEVRFTAPRVQTKNTHGTGCTLSAALAALRPRHDGWADTVREAktWLSAAL 244
Cdd:COG0524  212 LLARGVKLVVVTLG-----AEGALLYTGGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFA--NAAAAL 284


                 .
gi 556428804 245 A 245
Cdd:COG0524  285 V 285
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 85-236 5.46e-07

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: 49.47  E-value: 5.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804  85 DIVEAVAERLKRYQVQnVVLDtvmlaksgdpllsASAVETLRTKLLPQVALITPNLPEAAALLGTsHAQTEREMKAQGNA 164
Cdd:cd01174  142 ETVLAALRAARRAGVT-VILN-------------PAPARPLPAELLALVDILVPNETEAALLTGI-EVTDEEDAEKAARL 206

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556428804 165 LLAMGCGAVLMKGGhlddaESPDWLFTRDGEVRFTAPRVQTKNTHGTGCTLSAALAALRPRHDGWADTVREA 236
Cdd:cd01174  207 LLAKGVKNVIVTLG-----AKGALLASGGEVEHVPAFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFA 273
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 84-234 3.61e-06

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 47.34  E-value: 3.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804   84 TDIVEAVAERLKryqvQNVVLDTVMLAKSGdpllsaSAVETLRtKLLPQVALITPNLPEAAALLGTSHAqTEREMKAQGN 163
Cdd:pfam00294 143 EATLEELIEAAK----NGGTFDPNLLDPLG------AAREALL-ELLPLADLLKPNEEELEALTGAKLD-DIEEALAALH 210

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556428804  164 ALLAMGCGAVLMKGGhlddaESPDWLFTRDGEVRFTA-PRVQTKNTHGTGCTLSAALAALRPRHDGWADTVR 234
Cdd:pfam00294 211 KLLAKGIKTVIVTLG-----ADGALVVEGDGEVHVPAvPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALR 277
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
 128-221 6.77e-03

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: 37.29  E-value: 6.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556428804 128 KLLPQVALITPNLPEAAALLGTSHAQTEREMKAQgNALLAMGCGAVLMKGGhlddaESPDWLFTRDGEVRFT---APRVQ 204
Cdd:cd01941  172 YLLHAIDLLTPNRAELEALAGALIENNEDENKAA-KILLLPGIKNVIVTLG-----AKGVLLSSREGGVETKlfpAPQPE 245

                         90
                 ....*....|....*...
gi 556428804 205 T-KNTHGTGCTLSAALAA 221
Cdd:cd01941  246 TvVNVTGAGDAFVAGLVA 263
 
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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