|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
4-265 |
3.83e-114 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 328.62 E-value: 3.83e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 4 PTSRPVVLCLSGHDPSGGAGLQADIEALLAQGCHAAPAVTALTVQDTVNVSDFRVLDREWVLAQANAVLADLPVAAVKLG 83
Cdd:PRK06427 1 MMKRPIALTIAGSDSGGGAGIQADLKTFQALGVYGMSAITALTAQNTLGVQRVHPIPPEFVAAQLDAVFSDIRIDAVKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 84 MLGSLEMVDTVAEILAAHPHLPVVCDPVLRAGGGGALGKGDVGFAMRERLLPRATIATPNLPEARLLADLPEGSADQC-- 161
Cdd:PRK06427 81 MLASAEIIETVAEALKRYPIPPVVLDPVMIAKSGDPLLADDAVAALRERLLPLATLITPNLPEAEALTGLPIADTEDEmk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 162 --AERLLE-HCEHLLITGGH-GDESEVHNRLYSRDGSrRTFTCQRLPG-SYHGSGCTLASALAGRIALGEALHGAVQSAL 236
Cdd:PRK06427 161 aaARALHAlGCKAVLIKGGHlLDGEESVDWLFDGEGE-ERFSAPRIPTkNTHGTGCTLSAAIAAELAKGASLLDAVQTAK 239
|
250 260
....*....|....*....|....*....
gi 15599170 237 DYTWRTLRDAesPGHGQYVPRRLPTDFCH 265
Cdd:PRK06427 240 DYVTRAIRHA--LEIGQGHGPVNHFAYLW 266
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
11-253 |
9.26e-97 |
|
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: 283.85 E-value: 9.26e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 11 LCLSGHDPSGGAGLQADIEALLAQGCHAAPAVTALTVQDTVNVSDFRVLDREWVLAQANAVLADLPVAAVKLGMLGSLEM 90
Cdd:COG0351 1 LTIAGSDPSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVTGVHPVPPEFVAAQLRAVLEDIPVDAIKIGMLGSAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 91 VDTVAEILAAHPHLPVVCDPVLRAGGGGALGKGDVGFAMRERLLPRATIATPNLPEARLLADLP---EGSADQCAERLLE 167
Cdd:COG0351 81 IEAVAEILADYPLVPVVLDPVMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALLGIEittLDDMREAAKALLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 168 H-CEHLLITGGHGDESEVHNRLYSRDGSRRtFTCQRLP-GSYHGSGCTLASALAGRIALGEALHGAVQSALDYTWRTLRD 245
Cdd:COG0351 161 LgAKAVLVKGGHLPGDEAVDVLYDGDGVRE-FSAPRIDtGNTHGTGCTLSSAIAALLAKGLDLEEAVREAKEYVTQAIRA 239
|
....*...
gi 15599170 246 AESPGHGQ 253
Cdd:COG0351 240 ALRLGMGH 247
|
|
| HMPP_kinase |
cd01169 |
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ... |
9-246 |
1.70e-93 |
|
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: 275.15 E-value: 1.70e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 9 VVLCLSGHDPSGGAGLQADIEALLAQGCHAAPAVTALTVQDTVNVSDFRVLDREWVLAQANAVLADLPVAAVKLGMLGSL 88
Cdd:cd01169 1 VVLTIAGSDSSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVFGVHPVPPEFVAAQLDAVLEDIPVDAIKIGMLGSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 89 EMVDTVAEILAAHPHLPVVCDPVLRAGGGGALGKGDVGFAMRERLLPRATIATPNLPEARLLADLPEGS---ADQCAERL 165
Cdd:cd01169 81 EIIEAVAEALKDYPDIPVVLDPVMVAKSGDSLLDDDAIEALRELLLPLATLITPNLPEAELLTGLEIATeedMMKAAKAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 166 LE-HCEHLLITGGHGDESEVHNRLYSRDGSRRTFTCQRLPGSYHGSGCTLASALAGRIALGEALHGAVQSALDYTWRTLR 244
Cdd:cd01169 161 LAlGAKAVLIKGGHLPGDEAVDVLYDGGGFFEFESPRIDTKNTHGTGCTLSSAIAANLAKGLSLEEAVREAKEYVTQAIR 240
|
..
gi 15599170 245 DA 246
Cdd:cd01169 241 NA 242
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
17-252 |
2.00e-91 |
|
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: 270.12 E-value: 2.00e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 17 DPSGGAGLQADIEALLAQGCHAAPAVTALTVQDTVNVSDFRVLDREWVLAQANAVLADLPVAAVKLGMLGSLEMVDTVAE 96
Cdd:pfam08543 1 DSSGGAGIQADLKTFSALGVYGMSVITALTAQNTLGVQGVHPLPPEFVAAQLDAVLEDIPVDAVKTGMLGSAEIIEAVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 97 ILaAHPHLPVVCDPVLRAGGGGALGKGDVGFAMRERLLPRATIATPNLPEARLLADLPEGS---ADQCAERLLEH-CEHL 172
Cdd:pfam08543 81 KL-DKYGVPVVLDPVMVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTledMKEAAKKLLALgAKAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 173 LITGGH--GDESEVHNRLYsRDGSRRTFTCQRLP-GSYHGSGCTLASALAGRIALGEALHGAVQSALDYTWRTLRDAESP 249
Cdd:pfam08543 160 LIKGGHleGEEAVVTDVLY-DGGGFYTLEAPRIPtKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKEYVTEAIRDALNL 238
|
...
gi 15599170 250 GHG 252
Cdd:pfam08543 239 GKG 241
|
|
| HMP-P_kinase |
TIGR00097 |
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ... |
10-253 |
4.35e-55 |
|
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: 177.87 E-value: 4.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 10 VLCLSGHDPSGGAGLQADIEALLAQGCHAAPAVTALTVQDTVNVSDFRVLDREWVLAQANAVLADLPVAAVKLGMLGSLE 89
Cdd:TIGR00097 1 ALTIAGSDSGGGAGIQADLKTFSALGVFGTSVITALTAQNTRGVTGVYPIPPDFVEAQLDAVFSDIPVDAAKTGMLASAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 90 MVDTVAEILAAHPHLPVVCDPVLRAGGGGALGKGDVGFAMRERLLPRATIATPNLPEARLLADLP---EGSADQCAERLL 166
Cdd:TIGR00097 81 IVEAVARKLREYPVRPLVVDPVMVAKSGAPLLEEEAIEALRKRLLPLATLITPNLPEAEALLGTKirtEQDMIKAAKKLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 167 EHCEH-LLITGGHGDESEVHNRLYSRDGSrrtftcQRLPGSY------HGSGCTLASALAGRIALGEALHGAVQSALDYT 239
Cdd:TIGR00097 161 ELGPKaVLIKGGHLEGDQAVDVLFDGGEI------HILKAPRietkntHGTGCTLSAAIAANLAKGLSLKEAVKEAKEFV 234
|
250
....*....|....
gi 15599170 240 WRTLRDAESPGHGQ 253
Cdd:TIGR00097 235 TGAIRYGLNIGHGH 248
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
4-265 |
3.83e-114 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 328.62 E-value: 3.83e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 4 PTSRPVVLCLSGHDPSGGAGLQADIEALLAQGCHAAPAVTALTVQDTVNVSDFRVLDREWVLAQANAVLADLPVAAVKLG 83
Cdd:PRK06427 1 MMKRPIALTIAGSDSGGGAGIQADLKTFQALGVYGMSAITALTAQNTLGVQRVHPIPPEFVAAQLDAVFSDIRIDAVKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 84 MLGSLEMVDTVAEILAAHPHLPVVCDPVLRAGGGGALGKGDVGFAMRERLLPRATIATPNLPEARLLADLPEGSADQC-- 161
Cdd:PRK06427 81 MLASAEIIETVAEALKRYPIPPVVLDPVMIAKSGDPLLADDAVAALRERLLPLATLITPNLPEAEALTGLPIADTEDEmk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 162 --AERLLE-HCEHLLITGGH-GDESEVHNRLYSRDGSrRTFTCQRLPG-SYHGSGCTLASALAGRIALGEALHGAVQSAL 236
Cdd:PRK06427 161 aaARALHAlGCKAVLIKGGHlLDGEESVDWLFDGEGE-ERFSAPRIPTkNTHGTGCTLSAAIAAELAKGASLLDAVQTAK 239
|
250 260
....*....|....*....|....*....
gi 15599170 237 DYTWRTLRDAesPGHGQYVPRRLPTDFCH 265
Cdd:PRK06427 240 DYVTRAIRHA--LEIGQGHGPVNHFAYLW 266
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
11-253 |
9.26e-97 |
|
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: 283.85 E-value: 9.26e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 11 LCLSGHDPSGGAGLQADIEALLAQGCHAAPAVTALTVQDTVNVSDFRVLDREWVLAQANAVLADLPVAAVKLGMLGSLEM 90
Cdd:COG0351 1 LTIAGSDPSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVTGVHPVPPEFVAAQLRAVLEDIPVDAIKIGMLGSAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 91 VDTVAEILAAHPHLPVVCDPVLRAGGGGALGKGDVGFAMRERLLPRATIATPNLPEARLLADLP---EGSADQCAERLLE 167
Cdd:COG0351 81 IEAVAEILADYPLVPVVLDPVMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALLGIEittLDDMREAAKALLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 168 H-CEHLLITGGHGDESEVHNRLYSRDGSRRtFTCQRLP-GSYHGSGCTLASALAGRIALGEALHGAVQSALDYTWRTLRD 245
Cdd:COG0351 161 LgAKAVLVKGGHLPGDEAVDVLYDGDGVRE-FSAPRIDtGNTHGTGCTLSSAIAALLAKGLDLEEAVREAKEYVTQAIRA 239
|
....*...
gi 15599170 246 AESPGHGQ 253
Cdd:COG0351 240 ALRLGMGH 247
|
|
| HMPP_kinase |
cd01169 |
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ... |
9-246 |
1.70e-93 |
|
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: 275.15 E-value: 1.70e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 9 VVLCLSGHDPSGGAGLQADIEALLAQGCHAAPAVTALTVQDTVNVSDFRVLDREWVLAQANAVLADLPVAAVKLGMLGSL 88
Cdd:cd01169 1 VVLTIAGSDSSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVFGVHPVPPEFVAAQLDAVLEDIPVDAIKIGMLGSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 89 EMVDTVAEILAAHPHLPVVCDPVLRAGGGGALGKGDVGFAMRERLLPRATIATPNLPEARLLADLPEGS---ADQCAERL 165
Cdd:cd01169 81 EIIEAVAEALKDYPDIPVVLDPVMVAKSGDSLLDDDAIEALRELLLPLATLITPNLPEAELLTGLEIATeedMMKAAKAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 166 LE-HCEHLLITGGHGDESEVHNRLYSRDGSRRTFTCQRLPGSYHGSGCTLASALAGRIALGEALHGAVQSALDYTWRTLR 244
Cdd:cd01169 161 LAlGAKAVLIKGGHLPGDEAVDVLYDGGGFFEFESPRIDTKNTHGTGCTLSSAIAANLAKGLSLEEAVREAKEYVTQAIR 240
|
..
gi 15599170 245 DA 246
Cdd:cd01169 241 NA 242
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
17-252 |
2.00e-91 |
|
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: 270.12 E-value: 2.00e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 17 DPSGGAGLQADIEALLAQGCHAAPAVTALTVQDTVNVSDFRVLDREWVLAQANAVLADLPVAAVKLGMLGSLEMVDTVAE 96
Cdd:pfam08543 1 DSSGGAGIQADLKTFSALGVYGMSVITALTAQNTLGVQGVHPLPPEFVAAQLDAVLEDIPVDAVKTGMLGSAEIIEAVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 97 ILaAHPHLPVVCDPVLRAGGGGALGKGDVGFAMRERLLPRATIATPNLPEARLLADLPEGS---ADQCAERLLEH-CEHL 172
Cdd:pfam08543 81 KL-DKYGVPVVLDPVMVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTledMKEAAKKLLALgAKAV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 173 LITGGH--GDESEVHNRLYsRDGSRRTFTCQRLP-GSYHGSGCTLASALAGRIALGEALHGAVQSALDYTWRTLRDAESP 249
Cdd:pfam08543 160 LIKGGHleGEEAVVTDVLY-DGGGFYTLEAPRIPtKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKEYVTEAIRDALNL 238
|
...
gi 15599170 250 GHG 252
Cdd:pfam08543 239 GKG 241
|
|
| HMP-P_kinase |
TIGR00097 |
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ... |
10-253 |
4.35e-55 |
|
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: 177.87 E-value: 4.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 10 VLCLSGHDPSGGAGLQADIEALLAQGCHAAPAVTALTVQDTVNVSDFRVLDREWVLAQANAVLADLPVAAVKLGMLGSLE 89
Cdd:TIGR00097 1 ALTIAGSDSGGGAGIQADLKTFSALGVFGTSVITALTAQNTRGVTGVYPIPPDFVEAQLDAVFSDIPVDAAKTGMLASAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 90 MVDTVAEILAAHPHLPVVCDPVLRAGGGGALGKGDVGFAMRERLLPRATIATPNLPEARLLADLP---EGSADQCAERLL 166
Cdd:TIGR00097 81 IVEAVARKLREYPVRPLVVDPVMVAKSGAPLLEEEAIEALRKRLLPLATLITPNLPEAEALLGTKirtEQDMIKAAKKLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 167 EHCEH-LLITGGHGDESEVHNRLYSRDGSrrtftcQRLPGSY------HGSGCTLASALAGRIALGEALHGAVQSALDYT 239
Cdd:TIGR00097 161 ELGPKaVLIKGGHLEGDQAVDVLFDGGEI------HILKAPRietkntHGTGCTLSAAIAANLAKGLSLKEAVKEAKEFV 234
|
250
....*....|....
gi 15599170 240 WRTLRDAESPGHGQ 253
Cdd:TIGR00097 235 TGAIRYGLNIGHGH 248
|
|
| PLN02898 |
PLN02898 |
HMP-P kinase/thiamin-monophosphate pyrophosphorylase |
4-252 |
4.76e-46 |
|
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
Pssm-ID: 215486 [Multi-domain] Cd Length: 502 Bit Score: 160.70 E-value: 4.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 4 PTSRPVVLCLSGHDPSGGAGLQADIEALLAQGCHAAPAVTALTVQDTVNVSDFRVLDREWVLAQANAVLADLPVAAVKLG 83
Cdd:PLN02898 6 PMKVPHVLTVAGSDSGAGAGIQADIKACAARGVYCTTAITAVTAQNTVGVQGVHAVPLDFVAEQLKSVLSDMPVDVVKTG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 84 MLGSLEMVDTVAEILAAHPHLPVVCDPVLRAGGGGALGKGDVGFAMRERLLPRATIATPNLPEARLLADLP--EGSADQC 161
Cdd:PLN02898 86 MLPSAEIVKVLCQALKEFPVKALVVDPVMVSTSGDVLAGPSILSALREELLPLATIVTPNVKEASALLGGDplETVADMR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 162 AERLLEH---CEHLLITGGH-GDESEVHNRLYSRDGSrRTFTCQRLPG-SYHGSGCTLASALAGRIALGEALHGAVQSAL 236
Cdd:PLN02898 166 SAAKELHklgPRYVLVKGGHlPDSLDAVDVLYDGTEF-HELRSSRIKTrNTHGTGCTLASCIAAELAKGSDMLSAVKVAK 244
|
250
....*....|....*.
gi 15599170 237 DYTWRTLRdaESPGHG 252
Cdd:PLN02898 245 RYVETALE--YSKDIG 258
|
|
| PTZ00347 |
PTZ00347 |
phosphomethylpyrimidine kinase; Provisional |
4-259 |
2.72e-41 |
|
phosphomethylpyrimidine kinase; Provisional
Pssm-ID: 240375 [Multi-domain] Cd Length: 504 Bit Score: 148.19 E-value: 2.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 4 PTSRPVVLCLSGHDPSGGAGLQADIEALLAQGCHAAPAVTALTVQDTVNVSDFRVLDREWVLAQANAVLADLPVAAVKLG 83
Cdd:PTZ00347 227 PMKIPTVLTVSGSDSGGGAGHQADLKTLEALGVYSTSALTSLTAQNTKGVQQIQVVNEDFFAAQIDSVMSDFNISVVKLG 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 84 MLGSLEMVDTVAEILAAhphLPVVCDPVLRAGG----GGALGKGDVGFAMRERLLPRATIATPNLPEARLLADLPEGS-- 157
Cdd:PTZ00347 307 LVPTARQLEIVIEKLKN---LPMVVDPVLVATSgddlVAQKNADDVLAMYKERIFPMATIITPNIPEAERILGRKEITgv 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 158 --ADQCAERLLEH-CEHLLITGGHG--DESEVHNRLYSRDGSR-RTFTCQRLPG-SYHGSGCTLASALAGRIALGEALHG 230
Cdd:PTZ00347 384 yeARAAAQALAQYgSRYVLVKGGHDliDPEACRDVLYDREKDRfYEFTANRIATiNTHGTGCTLASAISSFLARGYTVPD 463
|
250 260
....*....|....*....|....*....
gi 15599170 231 AVQSALDYTWRTLRDAESPGHGQYVPRRL 259
Cdd:PTZ00347 464 AVERAIGYVHEAIVRSCGVPLGQGTNRPL 492
|
|
| PRK14713 |
PRK14713 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
4-253 |
3.25e-41 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 237797 [Multi-domain] Cd Length: 530 Bit Score: 148.40 E-value: 3.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 4 PTSRPVVLCLSGHDPSGGAGLQADIEALLAQGCHAAPAVTALTVQDTVNVSDFRVLDREWVLAQANAVLADLPVAAVKLG 83
Cdd:PRK14713 26 AAATPRVLSIAGTDPSGGAGIQADLKSIAAAGGYGMAVITALVAQNTRGVRAVHVPPADFLRAQLDAVSDDVTVDAVKIG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 84 MLGSLEMVDTVAEILAAHPHLPVVCDPVLRAGGGGALGKGDVGFAMRErLLPRATIATPNLPEARLL-----ADLPEGSA 158
Cdd:PRK14713 106 MLGDAEVIDAVRTWLAEHRPPVVVLDPVMVATSGDRLLEEDAEAALRE-LVPRADLITPNLPELAVLlgeppATTWEEAL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 159 DQCAERLLEHCEHLLITGGHGDESEVHNRLYSRDGsrrtfTCQRLPG------SYHGSGCTLASALAGRIALGEALHGAV 232
Cdd:PRK14713 185 AQARRLAAETGTTVLVKGGHLDGQRAPDALVGPDG-----AVTEVPGprvdtrNTHGTGCSLSSALATRLGRGGDWAAAL 259
|
250 260
....*....|....*....|.
gi 15599170 233 QSALDYTWRTLRDAESPGHGQ 253
Cdd:PRK14713 260 RWATAWLHGAIAAGAALQVGT 280
|
|
| PRK08573 |
PRK08573 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
8-252 |
2.08e-37 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 236297 [Multi-domain] Cd Length: 448 Bit Score: 136.78 E-value: 2.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 8 PVVLCLSGHDPSGGAGLQADIEALLAQGCHAAPAVTALTVQDTVNVSDFRVLDREWVLAQANAVLADLPVAAVKLGMLGS 87
Cdd:PRK08573 3 PVALTIAGSDSGGGAGIEADLKTFAALGVHGAVAITSVTAQNTYEVRAIHDLPPEVVAAQIEAVWEDMGIDAAKTGMLSN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 88 LEMVDTVAEILAAHpHLPVVCDPVLRAGGGGALGKGDVGFAMRERLLPRATIATPNLPEARLLADLPEGS---ADQCAER 164
Cdd:PRK08573 83 REIIEAVAKTVSKY-GFPLVVDPVMIAKSGAPLLREDAVDALIKRLLPLATVVTPNRPEAEKLTGMKIRSvedARKAAKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 165 LLEH--CEHLLITGGHGDESEVHNRLYSRdGSRRTFTCQRL-PGSYHGSGCTLASALAGRIALGEALHGAVQSALDYTWR 241
Cdd:PRK08573 162 IVEElgAEAVVVKGGHLEGEEAVDVLYHN-GTFREFRAPRVeSGCTHGTGCSFSAAIAAGLAKGLDPEEAIKTAKKFITM 240
|
250
....*....|.
gi 15599170 242 TLRDAESPGHG 252
Cdd:PRK08573 241 AIKYGVKIGKG 251
|
|
| PRK09517 |
PRK09517 |
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ... |
6-252 |
2.65e-34 |
|
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; Provisional
Pssm-ID: 169939 [Multi-domain] Cd Length: 755 Bit Score: 130.86 E-value: 2.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 6 SRPVVLCLSGHDPSGGAGLQADIEALLAQGCHAAPAVTALTVQDTVNVSDFRVLDREWVLAQANAVLADLPVAAVKLGML 85
Cdd:PRK09517 240 SAPRVLSIAGTDPTGGAGIQADLKSIAAGGGYGMCVVTALVAQNTHGVNTIHTPPLTFLEEQLEAVFSDVTVDAVKLGML 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 86 GSLEMVDTVAEILAAHPHLPVVCDPVLRAGGGGALGKGDVGFAMReRLLPRATIATPNLPE-ARLLADLPEGSADQCAER 164
Cdd:PRK09517 320 GSADTVDLVASWLGSHEHGPVVLDPVMVATSGDRLLDADATEALR-RLAVHVDVVTPNIPElAVLCGEAPAITMDEAIAQ 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 165 ----LLEHCEHLLITGGHGDESEVHNRLYSRDGSRRTFTCQRL-PGSYHGSGCTLASALAGRIALGEALHGAVQSALDYT 239
Cdd:PRK09517 399 argfARTHGTIVIVKGGHLTGDLADNAVVRPDGSVHQVENPRVnTTNSHGTGCSLSAALATLIAAGESVEKALEWATRWL 478
|
250
....*....|...
gi 15599170 240 WRTLRDAESPGHG 252
Cdd:PRK09517 479 NEALRHADHLAVG 491
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
10-254 |
7.25e-34 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 122.86 E-value: 7.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 10 VLCLSGHDPSGGAGLQADIEALLAQGCHAAPAVTALTvqdTVNVSDFRV--LDREwVLAQANAVLADLPVAAVKLGMLGS 87
Cdd:PRK12413 6 ILAISGNDIFSGGGLHADLATYTRNGLHGFVAVTCLT---AMTEKGFEVfpVDKE-IFQQQLDSLKDVPFSAIKIGLLPN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 88 LEMVDTVAEILAAHPHLPVVCDPVLragggGALGKGDVGF-AMRE---RLLPRATIATPNLPEARLLADLPEGSADQC-- 161
Cdd:PRK12413 82 VEIAEQALDFIKGHPGIPVVLDPVL-----VCKETHDVEVsELRQeliQFFPYVTVITPNLVEAELLSGKEIKTLEDMke 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 162 AERLLEH--CEHLLITGGhgdesevhNRLYSR-------DGSR-RTFTCQRLPGSYHGSGCTLASALAGRIALGEALHGA 231
Cdd:PRK12413 157 AAKKLYDlgAKAVVIKGG--------NRLSQKkaidlfyDGKEfVILESPVLEKNNIGAGCTFASSIASQLVKGKSPLEA 228
|
250 260
....*....|....*....|...
gi 15599170 232 VQSALDYTWRTLRDAESPGHGQY 254
Cdd:PRK12413 229 VKNSKDFVYQAIQQSDQYGVVQY 251
|
|
| PRK12412 |
PRK12412 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
8-244 |
4.04e-28 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183512 [Multi-domain] Cd Length: 268 Bit Score: 108.52 E-value: 4.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 8 PVVLCLSGHDPSGGAGLQADIEALLAQGCHAAPAVTALTVQDTVNVSDFRV--LDREWVLAQANAVLADLPVAAVKLGML 85
Cdd:PRK12412 2 NKALTIAGSDTSGGAGIQADLKTFQELGVYGMTSLTTIVTMDPHNGWAHNVfpIPASTLKPQLETTIEGVGVDALKTGML 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 86 GSLEMVDTVAEILAAHPHLPVVCDPVLRAGGGGALGKGDVGFAMRERLLPRATIATPNLPEARLLADLPEGSAD---QCA 162
Cdd:PRK12412 82 GSVEIIEMVAETIEKHNFKNVVVDPVMVCKGADEALHPETNDCLRDVLVPKALVVTPNLFEAYQLSGVKINSLEdmkEAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 163 ERLLE-HCEHLLITGGH--GDESEVhNRLYsrDGsrRTF---TCQRLPGSY-HGSGCTLASALAGRIALGEALHGAVQSA 235
Cdd:PRK12412 162 KKIHAlGAKYVLIKGGSklGTETAI-DVLY--DG--ETFdllESEKIDTTNtHGAGCTYSAAITAELAKGKPVKEAVKTA 236
|
....*....
gi 15599170 236 LDYTWRTLR 244
Cdd:PRK12412 237 KEFITAAIR 245
|
|
| PRK12616 |
PRK12616 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
11-255 |
5.25e-26 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183624 Cd Length: 270 Bit Score: 102.82 E-value: 5.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 11 LCLSGHDPSGGAGLQADIEALLAQGCHAAPAVTALTVQDTVNVSDFRV--LDREWVLAQANAVLADLPVAAVKLGMLGSL 88
Cdd:PRK12616 7 LTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAMDPENSWDHQVfpIDTDTIRAQLSTIVDGIGVDAMKTGMLPTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 89 EMVDTVAEILAAHPHLPVVCDPVLRAGGGGALGKGDVGFAMRERLLPRATIATPNLPEARLLADLPE----GSADQCAER 164
Cdd:PRK12616 87 DIIELAADTIKEKQLKNVVIDPVMVCKGANEVLYPEHAEALREQLAPLATVITPNLFEAGQLSGMGEiktvEQMKEAAKK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 165 LLE-HCEHLLITGG----HGDESEVhnrLYsrDG-SRRTFTCQRLPGSY-HGSGCTLASALAGRIALGEALHGAVQSALD 237
Cdd:PRK12616 167 IHElGAQYVVITGGgklkHEKAVDV---LY--DGeTAEVLESEMIDTPYtHGAGCTFSAAVTAELAKGSEVKEAIYAAKE 241
|
250
....*....|....*...
gi 15599170 238 YTWRTLRdaESPGHGQYV 255
Cdd:PRK12616 242 FITAAIK--ESFPLNQYV 257
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
20-244 |
5.11e-25 |
|
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: 100.22 E-value: 5.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 20 GGAGLQADIEALLAQGCHAAPAVTAL----TVQDTVnvsDFRVLDREWVLA-----QANAVLADlpVAAVKLGMLGSLEM 90
Cdd:COG2240 14 GHVGNSAAVPPLSALGVEVWPLPTVLlsnhTGYGTF---TGRDLPTDDIADildgwKELGVLLE--FDAVLSGYLGSAEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 91 VDTVAEIL----AAHPHLPVVCDPVLraggggalgkGDVGF----------AMRERLLPRATIATPNLPEARLLADLP-- 154
Cdd:COG2240 89 GDIIADFVarvkAANPDALYLCDPVM----------GDNGKgyyvfpgiaeFIMRRLVPLADIITPNLTELALLTGRPye 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 155 -EGSADQCAERLLE-HCEHLLITG---GHGDESEVHNRLYSRDGSRRtFTCQRLPGSYHGSGCTLASALAGRIALGEALH 229
Cdd:COG2240 159 tLEEALAAARALLAlGPKIVVVTSvplDDTPADKIGNLAVTADGAWL-VETPLLPFSPNGTGDLFAALLLAHLLRGKSLE 237
|
250
....*....|....*
gi 15599170 230 GAVQSALDYTWRTLR 244
Cdd:COG2240 238 EALERAAAFVYEVLE 252
|
|
| PTZ00493 |
PTZ00493 |
phosphomethylpyrimidine kinase; Provisional |
8-246 |
3.55e-19 |
|
phosphomethylpyrimidine kinase; Provisional
Pssm-ID: 240440 Cd Length: 321 Bit Score: 85.05 E-value: 3.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 8 PVVLCLSGHDPSGGAGLQADIEALLAQGCHAAPAVTALTVQDTVNVSDFRVLDREWVLAQANAVLADLPVAAVKLGMLGS 87
Cdd:PTZ00493 5 SNILSIAGSDSCGGAGMQADIKTAMGLGCHCCTALVVLTAQNTKEVKRIVEIEEKFIVEQLDSIFADVTIDVVKLGVLYS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 88 LEMVDTVAEILAA-----HPHLPVVCDPVLRAGG--GGALGKGDVGFAMrERLLPRATIATPNLPEARLLADLPEGSADQ 160
Cdd:PTZ00493 85 KKIISLVHNYITNmnkkrGKKLLVVFDPVFVSSSgcLLVENLEYIKFAL-DLICPISCIITPNFYECKVILEALDCQMDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 161 CAERLLEHCEH----------LLITGGHGDESEVHNRLYS-------RDGSRRT-------------------FTCQRLP 204
Cdd:PTZ00493 164 SKANMTELCKLvteklninacLFKSCNVGENSAEENEVYAvdhlcirNVGSYPTgekqqidaggvtylydvykLRSKRKP 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 15599170 205 G-SYHGSGCTLASALAGRIAlgeALHGAVQSALD---YTWRTLRDA 246
Cdd:PTZ00493 244 GkDIHGTGCTLSTAIACYLA---KKHNILQSCIEskkYIYNCIRYA 286
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
79-237 |
7.39e-18 |
|
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: 80.32 E-value: 7.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 79 AVKLGMLGSLEMVDTVAEIL----AAHPHLPVVCDPVLRAGGGGALGKGDVGFAMRERLLPRATIATPNLPEARLLADLP 154
Cdd:cd01173 75 AVLTGYLGSAEQVEAVAEIVkrlkEKNPNLLYVCDPVMGDNGKLYVVAEEIVPVYRDLLVPLADIITPNQFELELLTGKK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 155 ---EGSADQCAERLLEHC-EHLLITGGH-GDESEVHNRLYSRDGSRRTFTC-QRLPGSYHGSGCTLASALAGRIALGEAL 228
Cdd:cd01173 155 indLEDAKAAARALHAKGpKTVVVTSVElADDDRIEMLGSTATEAWLVQRPkIPFPAYFNGTGDLFAALLLARLLKGKSL 234
|
....*....
gi 15599170 229 HGAVQSALD 237
Cdd:cd01173 235 AEALEKALN 243
|
|
| COG1992 |
COG1992 |
Predicted transcriptional regulator fused phosphomethylpyrimidine kinase (thiamin biosynthesis) ... |
19-256 |
3.25e-15 |
|
Predicted transcriptional regulator fused phosphomethylpyrimidine kinase (thiamin biosynthesis) [General function prediction only];
Pssm-ID: 441595 [Multi-domain] Cd Length: 432 Bit Score: 74.79 E-value: 3.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 19 SGGAGLQADIEALLAQGCHAAPAVTALTVQDTVNVSDFRVLDREWVLAQANAVLADLPVAAVKLGMLGSLEMVDTVAEIL 98
Cdd:COG1992 1 GGGGGGGADAKTAAALGAGGGGTTTAVTVTATTTVTGVGSDPPPPVEVQQQAVAADDDVDDAKTGMLMTATIVEVVAVVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 99 AAHP-HLPVVCDPVLRAGGGGALGKGDVgfAMRERLLPRATIATPNLPEARLLADLPEGS----ADQCAERLLEHCEHLL 173
Cdd:COG1992 81 KSRDkPLVVVVVPVAVAAAGLGLLLAEA--ELAKLLLPLLATVTPNEPEVEELLLPTIRSllaeARAARLALQEEGADAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 174 ITGGHGDESEVHNRLYSRDGSRRTFTCQRL-PGSYHGSGCTLASALAGRIALGEALHGAVQSALDYTWRTLRDAESPGHG 252
Cdd:COG1992 159 GVKGGHVSGDAVVDVLEDERDVETFRHPRLvTEATHGSGCTFSAAIAALLAKGLSLEEAVRGAKLFLLHAIRYGLLVGKG 238
|
....
gi 15599170 253 QYVP 256
Cdd:COG1992 239 VGPV 242
|
|
| pdxK |
PRK08176 |
pyridoxine/pyridoxal/pyridoxamine kinase; |
79-250 |
8.03e-13 |
|
pyridoxine/pyridoxal/pyridoxamine kinase;
Pssm-ID: 181269 [Multi-domain] Cd Length: 281 Bit Score: 66.60 E-value: 8.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 79 AVKLGMLGSLEMVDTVA----EILAAHPHLPVVCDPVLRAGGGGALGKGDVGFAMRERLLPRATIATPNLPEARLLADLP 154
Cdd:PRK08176 91 AVTTGYMGSASQIKILAewltALRADHPDLLIMVDPVIGDIDSGIYVKPDLPEAYRQHLLPLAQGLTPNIFELEILTGKP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 155 EGSADQ---CAERLL-EHCEHLLITG--GHGDESEVHNRLYSRDGsRRTFTCQRLPGSYHGSGCTLASALAGRIALGEAL 228
Cdd:PRK08176 171 CRTLDSaiaAAKSLLsDTLKWVVITSaaGNEENQEMQVVVVTADS-VNVISHPRVDTDLKGTGDLFCAELVSGLLKGKAL 249
|
170 180
....*....|....*....|..
gi 15599170 229 HGAVQSALDYTWRTLRDAESPG 250
Cdd:PRK08176 250 TDAAHRAGLRVLEVMRYTQQAG 271
|
|
| PRK07105 |
PRK07105 |
pyridoxamine kinase; Validated |
16-238 |
2.59e-10 |
|
pyridoxamine kinase; Validated
Pssm-ID: 180840 [Multi-domain] Cd Length: 284 Bit Score: 59.54 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 16 HDPS--GGAGLQADIEALLAQGCHAAPAVTALTVQDTVNVSDFRVLD---------REWvlaQAnavlADLPVAAVKLGM 84
Cdd:PRK07105 11 HDLSgfGRVALTASIPIMSSMGLQVCPLPTALLSSHTGGFQNPSIIDltdgmqaflTHW---KS----LNLKFDAIYSGY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 85 LGSLEMVDTVAEILAAH--PHLPVVCDPVLraggggalgkGDVG-----F------AMReRLLPRATIATPNLPEARLLA 151
Cdd:PRK07105 84 LGSPRQIQIVSDFIKYFkkKDLLVVVDPVM----------GDNGklyqgFdqemveEMR-KLIQKADVITPNLTEACLLL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 152 DLP--EGSADQCA-ERLLEHC-----EHLLITGGHGDESEVHNRLYSRDGSR-RTFTCQRLPGSYHGSGCTLASALAGRI 222
Cdd:PRK07105 153 DKPylEKSYSEEEiKQLLRKLadlgpKIVIITSVPFEDGKIGVAYYDRATDRfWKVFCKYIPAHYPGTGDIFTSVITGSL 232
|
250
....*....|....*.
gi 15599170 223 ALGEALHGAVQSALDY 238
Cdd:PRK07105 233 LQGDSLPIALDRAVQF 248
|
|
| PTZ00344 |
PTZ00344 |
pyridoxal kinase; Provisional |
67-218 |
2.18e-09 |
|
pyridoxal kinase; Provisional
Pssm-ID: 240372 [Multi-domain] Cd Length: 296 Bit Score: 57.01 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 67 QANAVLADlpVAAVKLGMLGSLEMV----DTVAEILAAHPHLPVVCDPVLrAGGGGALGKGDVGFAMRErLLPRATIATP 142
Cdd:PTZ00344 70 RANNLLSD--YTYVLTGYINSADILrevlATVKEIKELRPKLIFLCDPVM-GDDGKLYVKEEVVDAYRE-LIPYADVITP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 143 NLPEARLLAdlpeGSADQCAERLLEHCE--------HLLITGGHGDESEVHNRLY-----SRDGSRRTFTC--QRLPGSY 207
Cdd:PTZ00344 146 NQFEASLLS----GVEVKDLSDALEAIDwfheqgipVVVITSFREDEDPTHLRFLlscrdKDTKNNKRFTGkvPYIEGRY 221
|
170
....*....|.
gi 15599170 208 HGSGCTLASAL 218
Cdd:PTZ00344 222 TGTGDLFAALL 232
|
|
| PRK05756 |
PRK05756 |
pyridoxal kinase PdxY; |
60-176 |
5.90e-09 |
|
pyridoxal kinase PdxY;
Pssm-ID: 235592 [Multi-domain] Cd Length: 286 Bit Score: 55.65 E-value: 5.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 60 DREWvLAQANAVLAdlpvaavklGMLGSLEM----VDTVAEILAAHPHLPVVCDPVLRAGGGGALGKGDVGFAMRERLLP 135
Cdd:PRK05756 68 DIGW-LGECDAVLS---------GYLGSAEQgeaiLDAVRRVKAANPQALYFCDPVMGDPEKGCIVAPGVAEFLRDRALP 137
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 15599170 136 RATIATPNLPEARLLADLPEGSADQCaerlLEHCEHLLITG 176
Cdd:PRK05756 138 AADIITPNLFELEWLSGRPVETLEDA----VAAARALIARG 174
|
|
| pyridox_kin |
TIGR00687 |
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ... |
64-154 |
2.07e-07 |
|
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: 50.98 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 64 VLAQANAVLAdlpvaavklGMLGSLE----MVDTVAEILAAHPHLPVVCDPVLRAGGGGALGKGDVGFAMRERLLPRATI 139
Cdd:TIGR00687 71 KLNQCDAVLS---------GYLGSAEqvamVVGIVRQVKQANPQALYVCDPVMGDPWKGCYVAPDLLEVYREKAIPVADI 141
|
90
....*....|....*
gi 15599170 140 ATPNLPEARLLADLP 154
Cdd:TIGR00687 142 ITPNQFELELLTGRR 156
|
|
| PLN02978 |
PLN02978 |
pyridoxal kinase |
83-250 |
1.28e-06 |
|
pyridoxal kinase
Pssm-ID: 215529 [Multi-domain] Cd Length: 308 Bit Score: 48.58 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 83 GMLGSLEMVDTVAEILAA----HPHLPVVCDPVLRAGGGGALGKGDVGfAMRERLLPRATIATPNLPEARLLAdlpeGSA 158
Cdd:PLN02978 93 GYIGSVSFLRTVLRVVKKlrsvNPNLTYVCDPVLGDEGKLYVPPELVP-VYREKVVPLATMLTPNQFEAEQLT----GIR 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 159 DQCAERLLEHCEHL--------LITGGHGDESEV----HNRLYSRDGSRRTFTCQRLPGSYHGSGCTLASALAGRIA--- 223
Cdd:PLN02978 168 IVTEEDAREACAILhaagpskvVITSIDIDGKLLlvgsHRKEKGARPEQFKIVIPKIPAYFTGTGDLMAALLLGWSHkyp 247
|
170 180
....*....|....*....|....*....
gi 15599170 224 --LGEALHGAVQSALDYTWRTLRDAESPG 250
Cdd:PLN02978 248 dnLDKAAELAVSSLQAVLRRTLADYKRAG 276
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
77-223 |
2.14e-04 |
|
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: 41.31 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 77 VAAVKLGMLG-SLEMVDTVAEILAAHpHLPVVCDPVLRAGGGGALGkgdvgfamRERLLPRATIATPNLPEARLLA---- 151
Cdd:cd00287 58 ADAVVISGLSpAPEAVLDALEEARRR-GVPVVLDPGPRAVRLDGEE--------LEKLLPGVDILTPNEEEAEALTgrrd 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599170 152 DLPEGSADQCAERLLEHCEHLLITGGHGDesevhNRLYSRDGSR-RTFTCQRLPGSYHGSGCTLASALAGRIA 223
Cdd:cd00287 129 LEVKEAAEAAALLLSKGPKVVIVTLGEKG-----AIVATRGGTEvHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
87-179 |
5.57e-04 |
|
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: 40.64 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599170 87 SLEMVDTVAEILAAHpHLPVVCDPVLRAGGGGALGKGDvgfamrERLLPRATIATPNLPEARLLADlpEGSADQCAERLL 166
Cdd:COG0524 143 PREALLAALEAARAA-GVPVSLDPNYRPALWEPARELL------RELLALVDILFPNEEEAELLTG--ETDPEEAAAALL 213
|
90
....*....|....*
gi 15599170 167 EH-CEHLLIT-GGHG 179
Cdd:COG0524 214 ARgVKLVVVTlGAEG 228
|
|
| |
