|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05756 |
PRK05756 |
pyridoxal kinase PdxY; |
1-286 |
0e+00 |
|
pyridoxal kinase PdxY;
Pssm-ID: 235592 [Multi-domain] Cd Length: 286 Bit Score: 534.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 1 MKNILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPTHLTEIVKGIADIDKLQTCDAVLS 80
Cdd:PRK05756 1 MKNILSIQSHVVYGHVGNSAAVFPMQRLGVNVWPLNTVQFSNHTGYGKWTGCVMPPSHLTEIVQGIADIGWLGECDAVLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 81 GYLGSAEQGEHILGIVRQVKAANPRAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHAVHNV 160
Cdd:PRK05756 81 GYLGSAEQGEAILDAVRRVKAANPQALYFCDPVMGDPEKGCIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 161 TEAVMAARELIAQGPEIVLVKHLARAGISTDRFEMLLVTAEQAWHISRPLVDFGaRQPVGVGDVTSGLLLVKLLQGASLQ 240
Cdd:PRK05756 161 EDAVAAARALIARGPKIVLVTSLARAGYPADRFEMLLVTADGAWHISRPLVDFM-RQPVGVGDLTSALFLARLLQGGSLE 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 754952465 241 QALEHVTAAVYEVMIATKEMHEYELQVVAAQDRIAKPEHYFSATQL 286
Cdd:PRK05756 240 EALEHTTAAVYEVMARTKERGSYELQLVAAQDSIATPRAMFQARRL 285
|
|
| pyridox_kin |
TIGR00687 |
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ... |
1-286 |
6.17e-173 |
|
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: 479.33 E-value: 6.17e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 1 MKNILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPTHLTEIVKGIADIDKLQTCDAVLS 80
Cdd:TIGR00687 1 MKNVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLEAINKLNQCDAVLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 81 GYLGSAEQGEHILGIVRQVKAANPRAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHAVHNV 160
Cdd:TIGR00687 81 GYLGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKGCYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 161 TEAVMAARELIAQGPEIVLVKHLARAGISTDR-FEMLLVTAEQAWHISRPLVDFGaRQPVGVGDVTSGLLLVKLLQGASL 239
Cdd:TIGR00687 161 EEALAAADALIAMGPDIVLVTHLIRAGSQRDRsFEGLVATQEGRWHISRPLAVFD-PPPVGTGDLIAALLLATLLHGNSL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 754952465 240 QQALEHVTAAVYEVMIATKEMHEYELQVVAAQDRIAKPEHYFSATQL 286
Cdd:TIGR00687 240 KEALEKTVSAVYHVLRTTIQLGKYELQPVAAQLEIRMPQSKFDAEKV 286
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
1-275 |
1.85e-138 |
|
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: 391.43 E-value: 1.85e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 1 MKNILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPTHLTEIVKGIADIDKLQTCDAVLS 80
Cdd:COG2240 1 MKRVLSIQSHVVYGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWKELGVLLEFDAVLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 81 GYLGSAEQGEHILGIVRQVKAANPRAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHAVHNV 160
Cdd:COG2240 81 GYLGSAEQGDIIADFVARVKAANPDALYLCDPVMGDNGKGYYVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 161 TEAVMAARELIAQGPEIVLVKHLARAGISTDRFEMLLVTAEQAWHISRPLVDFgarQPVGVGDVTSGLLLVKLLQGASLQ 240
Cdd:COG2240 161 EEALAAARALLALGPKIVVVTSVPLDDTPADKIGNLAVTADGAWLVETPLLPF---SPNGTGDLFAALLLAHLLRGKSLE 237
|
250 260 270
....*....|....*....|....*....|....*
gi 754952465 241 QALEHVTAAVYEVMIATKEMHEYELQVVAAQDRIA 275
Cdd:COG2240 238 EALERAAAFVYEVLERTAAAGSDELLLEAALDELV 272
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
3-259 |
1.06e-112 |
|
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: 325.31 E-value: 1.06e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 3 NILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPTHLTEIVKGIADIDKLQTCDAVLSGY 82
Cdd:cd01173 1 RVLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLLLEYDAVLTGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 83 LGSAEQGEHILGIVRQVKAANPRAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHAVHNVTE 162
Cdd:cd01173 81 LGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGDNGKLYVVAEEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 163 AVMAARELIAQGPEIVLVKHLARAGisTDRFEMLLVTAEQAWHISRPLVDFGArQPVGVGDVTSGLLLVKLLQGASLQQA 242
Cdd:cd01173 161 AKAAARALHAKGPKTVVVTSVELAD--DDRIEMLGSTATEAWLVQRPKIPFPA-YFNGTGDLFAALLLARLLKGKSLAEA 237
|
250
....*....|....*..
gi 754952465 243 LEHVTAAVYEVMIATKE 259
Cdd:cd01173 238 LEKALNFVHEVLEATYE 254
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
53-250 |
3.50e-13 |
|
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: 67.51 E-value: 3.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 53 VMPPTHLTEIVKGI-ADIDklqtCDAVLSGYLGSAEqgehilgIVRQV--KAANPRAKYFCDPVM----GHPekgcIVAP 125
Cdd:pfam08543 42 PLPPEFVAAQLDAVlEDIP----VDAVKTGMLGSAE-------IIEAVaeKLDKYGVPVVLDPVMvaksGDS----LLDD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 126 GVAEFHVRHALPASDIIAPNLVELEILCEHAVHNVTEAVMAARELIAQGPEIVLVK--HLARAG-ISTDrfemLLVTAEQ 202
Cdd:pfam08543 107 EAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKggHLEGEEaVVTD----VLYDGGG 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 754952465 203 AWHISRPLVDfgARQPVGVGDVTSGLLLVKLLQGASLQQALEH----VTAAV 250
Cdd:pfam08543 183 FYTLEAPRIP--TKNTHGTGCTLSAAIAANLAKGLSLPEAVREakeyVTEAI 232
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05756 |
PRK05756 |
pyridoxal kinase PdxY; |
1-286 |
0e+00 |
|
pyridoxal kinase PdxY;
Pssm-ID: 235592 [Multi-domain] Cd Length: 286 Bit Score: 534.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 1 MKNILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPTHLTEIVKGIADIDKLQTCDAVLS 80
Cdd:PRK05756 1 MKNILSIQSHVVYGHVGNSAAVFPMQRLGVNVWPLNTVQFSNHTGYGKWTGCVMPPSHLTEIVQGIADIGWLGECDAVLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 81 GYLGSAEQGEHILGIVRQVKAANPRAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHAVHNV 160
Cdd:PRK05756 81 GYLGSAEQGEAILDAVRRVKAANPQALYFCDPVMGDPEKGCIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 161 TEAVMAARELIAQGPEIVLVKHLARAGISTDRFEMLLVTAEQAWHISRPLVDFGaRQPVGVGDVTSGLLLVKLLQGASLQ 240
Cdd:PRK05756 161 EDAVAAARALIARGPKIVLVTSLARAGYPADRFEMLLVTADGAWHISRPLVDFM-RQPVGVGDLTSALFLARLLQGGSLE 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 754952465 241 QALEHVTAAVYEVMIATKEMHEYELQVVAAQDRIAKPEHYFSATQL 286
Cdd:PRK05756 240 EALEHTTAAVYEVMARTKERGSYELQLVAAQDSIATPRAMFQARRL 285
|
|
| pyridox_kin |
TIGR00687 |
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ... |
1-286 |
6.17e-173 |
|
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: 479.33 E-value: 6.17e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 1 MKNILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPTHLTEIVKGIADIDKLQTCDAVLS 80
Cdd:TIGR00687 1 MKNVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLEAINKLNQCDAVLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 81 GYLGSAEQGEHILGIVRQVKAANPRAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHAVHNV 160
Cdd:TIGR00687 81 GYLGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKGCYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 161 TEAVMAARELIAQGPEIVLVKHLARAGISTDR-FEMLLVTAEQAWHISRPLVDFGaRQPVGVGDVTSGLLLVKLLQGASL 239
Cdd:TIGR00687 161 EEALAAADALIAMGPDIVLVTHLIRAGSQRDRsFEGLVATQEGRWHISRPLAVFD-PPPVGTGDLIAALLLATLLHGNSL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 754952465 240 QQALEHVTAAVYEVMIATKEMHEYELQVVAAQDRIAKPEHYFSATQL 286
Cdd:TIGR00687 240 KEALEKTVSAVYHVLRTTIQLGKYELQPVAAQLEIRMPQSKFDAEKV 286
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
1-275 |
1.85e-138 |
|
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: 391.43 E-value: 1.85e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 1 MKNILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPTHLTEIVKGIADIDKLQTCDAVLS 80
Cdd:COG2240 1 MKRVLSIQSHVVYGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWKELGVLLEFDAVLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 81 GYLGSAEQGEHILGIVRQVKAANPRAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHAVHNV 160
Cdd:COG2240 81 GYLGSAEQGDIIADFVARVKAANPDALYLCDPVMGDNGKGYYVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 161 TEAVMAARELIAQGPEIVLVKHLARAGISTDRFEMLLVTAEQAWHISRPLVDFgarQPVGVGDVTSGLLLVKLLQGASLQ 240
Cdd:COG2240 161 EEALAAARALLALGPKIVVVTSVPLDDTPADKIGNLAVTADGAWLVETPLLPF---SPNGTGDLFAALLLAHLLRGKSLE 237
|
250 260 270
....*....|....*....|....*....|....*
gi 754952465 241 QALEHVTAAVYEVMIATKEMHEYELQVVAAQDRIA 275
Cdd:COG2240 238 EALERAAAFVYEVLERTAAAGSDELLLEAALDELV 272
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
3-259 |
1.06e-112 |
|
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: 325.31 E-value: 1.06e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 3 NILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPTHLTEIVKGIADIDKLQTCDAVLSGY 82
Cdd:cd01173 1 RVLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLLLEYDAVLTGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 83 LGSAEQGEHILGIVRQVKAANPRAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHAVHNVTE 162
Cdd:cd01173 81 LGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGDNGKLYVVAEEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 163 AVMAARELIAQGPEIVLVKHLARAGisTDRFEMLLVTAEQAWHISRPLVDFGArQPVGVGDVTSGLLLVKLLQGASLQQA 242
Cdd:cd01173 161 AKAAARALHAKGPKTVVVTSVELAD--DDRIEMLGSTATEAWLVQRPKIPFPA-YFNGTGDLFAALLLARLLKGKSLAEA 237
|
250
....*....|....*..
gi 754952465 243 LEHVTAAVYEVMIATKE 259
Cdd:cd01173 238 LEKALNFVHEVLEATYE 254
|
|
| PTZ00344 |
PTZ00344 |
pyridoxal kinase; Provisional |
2-286 |
1.54e-52 |
|
pyridoxal kinase; Provisional
Pssm-ID: 240372 [Multi-domain] Cd Length: 296 Bit Score: 173.34 E-value: 1.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 2 KNILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPTHLTEIVKGIADIDKLQTCDAVLSG 81
Cdd:PTZ00344 5 KKVLSIQSHVTHGYVGNRAATFPLQLLGFDVDFVNTVQLSNHTGYPVIKGHRLDLNELITLMDGLRANNLLSDYTYVLTG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 82 YLGSAEQGEHILGIVRQVKAANPRAKYFCDPVMGHPEKGCIVAPGVAEFhvRHALPASDIIAPNLVELEILCEHAVHNVT 161
Cdd:PTZ00344 85 YINSADILREVLATVKEIKELRPKLIFLCDPVMGDDGKLYVKEEVVDAY--RELIPYADVITPNQFEASLLSGVEVKDLS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 162 EAVMAARELIAQGPEIVLVKHLARAGISTDRFEMLLVTAEQAWHISRplvdFGARQP------VGVGDVTSGLLLVKLLQ 235
Cdd:PTZ00344 163 DALEAIDWFHEQGIPVVVITSFREDEDPTHLRFLLSCRDKDTKNNKR----FTGKVPyiegryTGTGDLFAALLLAFSHQ 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 754952465 236 GaSLQQALEHVTAAVYEVMIATKEMH--------EYELQVVAAQDRIAKPEHYFSATQL 286
Cdd:PTZ00344 239 H-PMDLAVGKAMGVLQDIIKATRESGgsgssslmSRELRLIQSPRDLLNPETVFKVTPL 296
|
|
| PLN02978 |
PLN02978 |
pyridoxal kinase |
4-286 |
5.44e-43 |
|
pyridoxal kinase
Pssm-ID: 215529 [Multi-domain] Cd Length: 308 Bit Score: 149.12 E-value: 5.44e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 4 ILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPTHLTEIVKGIaDIDKLQTCDAVLSGYL 83
Cdd:PLN02978 17 VLSIQSHTVHGYVGNKSAVFPLQLLGFDVDPINSVQFSNHTGYPTFKGQVLDGEQLWALIEGL-EANGLLFYTHLLTGYI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 84 GSAEQGEHILGIVRQVKAANPRAKYFCDPVMGHPEKgCIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHAVHNVTEA 163
Cdd:PLN02978 96 GSVSFLRTVLRVVKKLRSVNPNLTYVCDPVLGDEGK-LYVPPELVPVYREKVVPLATMLTPNQFEAEQLTGIRIVTEEDA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 164 VMAARELIAQGPEIVLVKhlaragiSTDRFEMLLVTA---------EQAWHISRPLVdfgARQPVGVGDVTSGLLLV--- 231
Cdd:PLN02978 175 REACAILHAAGPSKVVIT-------SIDIDGKLLLVGshrkekgarPEQFKIVIPKI---PAYFTGTGDLMAALLLGwsh 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754952465 232 ----KLLQGASLQ----QALEHVTAAVYEVMIATKEMHEYELQVVAAQDRIAKPEHYFSATQL 286
Cdd:PLN02978 245 kypdNLDKAAELAvsslQAVLRRTLADYKRAGADPKSSSLELRLVQSQDDIRHPQVRFKAERY 307
|
|
| pdxK |
PRK08176 |
pyridoxine/pyridoxal/pyridoxamine kinase; |
3-266 |
1.07e-40 |
|
pyridoxine/pyridoxal/pyridoxamine kinase;
Pssm-ID: 181269 [Multi-domain] Cd Length: 281 Bit Score: 142.10 E-value: 1.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 3 NILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHTQYGKWTGCVMPPTHLTEIVKGIADIDKLQTCDAVLSGY 82
Cdd:PRK08176 17 DIVAVQSQVVYGSVGNSIAVPAIKANGLRVFAVPTVLLSNTPHYPTFYGGAIPDEWFSGYLRALQERDALRQLRAVTTGY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 83 LGSAEQGEHILGIVRQVKAANPRAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLVELEILCEHAVHNVTE 162
Cdd:PRK08176 97 MGSASQIKILAEWLTALRADHPDLLIMVDPVIGDIDSGIYVKPDLPEAYRQHLLPLAQGLTPNIFELEILTGKPCRTLDS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 163 AVMAARELIAQGPEIVLVKHlARAGISTDRFEMLLVTAEQAWHISRPLVDfgaRQPVGVGDVTSGLLLVKLLQGASLQQA 242
Cdd:PRK08176 177 AIAAAKSLLSDTLKWVVITS-AAGNEENQEMQVVVVTADSVNVISHPRVD---TDLKGTGDLFCAELVSGLLKGKALTDA 252
|
250 260
....*....|....*....|....
gi 754952465 243 LEHVTAAVYEVMIATKEMHEYELQ 266
Cdd:PRK08176 253 AHRAGLRVLEVMRYTQQAGSDELI 276
|
|
| PRK07105 |
PRK07105 |
pyridoxamine kinase; Validated |
1-265 |
2.81e-16 |
|
pyridoxamine kinase; Validated
Pssm-ID: 180840 [Multi-domain] Cd Length: 284 Bit Score: 76.88 E-value: 2.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 1 MKNILAIQSHVVFGHAGNSAAEFPMRRLGANVWPLNTVQFSNHT----QYGKWTgcvmppthLTEIVKGI------ADID 70
Cdd:PRK07105 4 VKRVAAIHDLSGFGRVALTASIPIMSSMGLQVCPLPTALLSSHTggfqNPSIID--------LTDGMQAFlthwksLNLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 71 klqtCDAVLSGYLGSAEQGEHILGIVRQVKaaNPRAKYFCDPVMGhpEKGCiVAPGVAEFHV---RHALPASDIIAPNLV 147
Cdd:PRK07105 76 ----FDAIYSGYLGSPRQIQIVSDFIKYFK--KKDLLVVVDPVMG--DNGK-LYQGFDQEMVeemRKLIQKADVITPNLT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 148 ELEILCEHA---VHNVTEAVMA-ARELIAQGPEIVLVkhlarAGISTDRFEMLLV----TAEQAWHISRPlvdfgaRQPV 219
Cdd:PRK07105 147 EACLLLDKPyleKSYSEEEIKQlLRKLADLGPKIVII-----TSVPFEDGKIGVAyydrATDRFWKVFCK------YIPA 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 754952465 220 ---GVGDVTSGLLLVKLLQGASLQQALEHVTAAVYEVMIATkEMHEYEL 265
Cdd:PRK07105 216 hypGTGDIFTSVITGSLLQGDSLPIALDRAVQFIEKGIRAT-LGLKYDL 263
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
133-249 |
1.58e-15 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 75.17 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 133 RHALPAS-DIIAPNLVELEILCEHAVHNVTEAVMAARELIAQGPEIVLVKhLARAGistdrfeMLLVTAEQAWHISRPLV 211
Cdd:COG1105 171 KAALEAGpDLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVS-LGADG-------ALLVTEDGVYRAKPPKV 242
|
90 100 110
....*....|....*....|....*....|....*...
gi 754952465 212 DfgARQPVGVGDVTSGLLLVKLLQGASLQQALEHVTAA 249
Cdd:COG1105 243 E--VVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAA 278
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
133-249 |
6.36e-15 |
|
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. FruK plays an important role in the predominant pathway for fructose utilisation.This group also contains tagatose-6-phophate kinase, an enzyme of the tagatose 6-phosphate pathway, which responsible for breakdown of the galactose moiety during lactose metabolism by bacteria such as L. lactis.
Pssm-ID: 238570 [Multi-domain] Cd Length: 289 Bit Score: 72.95 E-value: 6.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 133 RHALPAS-DIIAPNLVELEILCEHAVHNVTEAVMAARELIAQGPEIVLVKhLARAGistdrfeMLLVTAEQAWHISRPLV 211
Cdd:cd01164 171 LAALAAKpFLIKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVS-LGADG-------ALLVTKDGVYRASPPKV 242
|
90 100 110
....*....|....*....|....*....|....*...
gi 754952465 212 DfgARQPVGVGDVTSGLLLVKLLQGASLQQALEHVTAA 249
Cdd:cd01164 243 K--VVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAA 278
|
|
| HMPP_kinase |
cd01169 |
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ... |
75-250 |
1.25e-13 |
|
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: 68.68 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 75 CDAVLSGYLGSAEqgehILGIVRQVKAANPRAKYFCDPVM----GHPekgcIVAPGVAEFHVRHALPASDIIAPNLVELE 150
Cdd:cd01169 69 VDAIKIGMLGSAE----IIEAVAEALKDYPDIPVVLDPVMvaksGDS----LLDDDAIEALRELLLPLATLITPNLPEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 151 ILCEHAVHNVTEAVMAARELIAQGPEIVLVK--HLaRAGISTDrfemLLVTAEQAWHISRPLVDfgARQPVGVGDVTSGL 228
Cdd:cd01169 141 LLTGLEIATEEDMMKAAKALLALGAKAVLIKggHL-PGDEAVD----VLYDGGGFFEFESPRID--TKNTHGTGCTLSSA 213
|
170 180
....*....|....*....|....*.
gi 754952465 229 LLVKLLQGASL----QQALEHVTAAV 250
Cdd:cd01169 214 IAANLAKGLSLeeavREAKEYVTQAI 239
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
53-250 |
3.50e-13 |
|
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: 67.51 E-value: 3.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 53 VMPPTHLTEIVKGI-ADIDklqtCDAVLSGYLGSAEqgehilgIVRQV--KAANPRAKYFCDPVM----GHPekgcIVAP 125
Cdd:pfam08543 42 PLPPEFVAAQLDAVlEDIP----VDAVKTGMLGSAE-------IIEAVaeKLDKYGVPVVLDPVMvaksGDS----LLDD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 126 GVAEFHVRHALPASDIIAPNLVELEILCEHAVHNVTEAVMAARELIAQGPEIVLVK--HLARAG-ISTDrfemLLVTAEQ 202
Cdd:pfam08543 107 EAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKggHLEGEEaVVTD----VLYDGGG 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 754952465 203 AWHISRPLVDfgARQPVGVGDVTSGLLLVKLLQGASLQQALEH----VTAAV 250
Cdd:pfam08543 183 FYTLEAPRIP--TKNTHGTGCTLSAAIAANLAKGLSLPEAVREakeyVTEAI 232
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
140-249 |
9.98e-13 |
|
hexose kinase, 1-phosphofructokinase family; This family consists largely of 1-phosphofructokinases, but also includes tagatose-6-kinases and 6-phosphofructokinases.
Pssm-ID: 274464 [Multi-domain] Cd Length: 303 Bit Score: 66.83 E-value: 9.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 140 DIIAPNLVELEILCEHAVHNVTEAVMAARELIAQGPEIVLVKhLARAGistdrfeMLLVTAEQAWHISRPLVDfgARQPV 219
Cdd:TIGR03168 178 FLIKPNHEELEELFGRELKTLEEIIEAARELLDRGAENVLVS-LGADG-------ALLVTKEGALKATPPKVE--VVNTV 247
|
90 100 110
....*....|....*....|....*....|
gi 754952465 220 GVGDVTSGLLLVKLLQGASLQQALEHVTAA 249
Cdd:TIGR03168 248 GAGDSMVAGFLAGLARGLSLEEALRFAVAA 277
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
76-249 |
6.56e-11 |
|
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: 61.21 E-value: 6.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 76 DAVLSGYLGSAEQGEHILGIVRQVKAANprakYFCDPVM----GHPekgcIVAPGVAEFHVRHALPASDIIAPNLVELEI 151
Cdd:COG0351 68 DAIKIGMLGSAEIIEAVAEILADYPLVP----VVLDPVMvaksGDR----LLDEDAVEALRELLLPLATVVTPNLPEAEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 152 LCEHAVHNVTEAVMAARELIAQGPEIVLVK--HLArAGISTDrfemLLVTAEQAWHISRPLVDfgARQPVGVGDVTSGLL 229
Cdd:COG0351 140 LLGIEITTLDDMREAAKALLELGAKAVLVKggHLP-GDEAVD----VLYDGDGVREFSAPRID--TGNTHGTGCTLSSAI 212
|
170 180
....*....|....*....|....
gi 754952465 230 LVKLLQGASL----QQALEHVTAA 249
Cdd:COG0351 213 AALLAKGLDLeeavREAKEYVTQA 236
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
132-249 |
1.62e-10 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 60.43 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 132 VRHALPASDIIAPNLVELEILCEHAVHNVTEAVMAARELIAQGPEIVLVKhLARAGistdrfeMLLVTAEQAWHISRP-- 209
Cdd:pfam00294 174 LLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVT-LGADG-------ALVVEGDGEVHVPAVpk 245
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 754952465 210 --LVDfgarqPVGVGDVTSGLLLVKLLQGASLQQALEHVTAA 249
Cdd:pfam00294 246 vkVVD-----TTGAGDSFVGGFLAGLLAGKSLEEALRFANAA 282
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
68-249 |
8.30e-10 |
|
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: 58.36 E-value: 8.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 68 DIDKLQTCDAV-LSGYLGSAEQG-EHILGIVRQVKAANprAKYFCDPVMGHpekgCIVAPGVAEFhvRHALPASDIIAPN 145
Cdd:COG0524 121 DEALLAGADILhLGGITLASEPPrEALLAALEAARAAG--VPVSLDPNYRP----ALWEPARELL--RELLALVDILFPN 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 146 LVELEILCEHavhnvTEAVMAARELIAQGPEIVLVKhLARAGIstdrfemLLVTAEQAWHISRPLVDfgARQPVGVGDVT 225
Cdd:COG0524 193 EEEAELLTGE-----TDPEEAAAALLARGVKLVVVT-LGAEGA-------LLYTGGEVVHVPAFPVE--VVDTTGAGDAF 257
|
170 180
....*....|....*....|....
gi 754952465 226 SGLLLVKLLQGASLQQALEHVTAA 249
Cdd:COG0524 258 AAGFLAGLLEGLDLEEALRFANAA 281
|
|
| PRK14713 |
PRK14713 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
74-248 |
4.31e-08 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 237797 [Multi-domain] Cd Length: 530 Bit Score: 54.02 E-value: 4.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 74 TCDAVLSGYLGSAEqgehILGIVRQVKAANPRAKYFCDPVMGHPEKGCIVAPGvAEFHVRHALPASDIIAPNLVELEILC 153
Cdd:PRK14713 98 TVDAVKIGMLGDAE----VIDAVRTWLAEHRPPVVVLDPVMVATSGDRLLEED-AEAALRELVPRADLITPNLPELAVLL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 154 EHAVHNV-TEAVMAARELIAQGPEIVLVK--HLarAGISTDrfEMLLVTAEQAWHISRPLVDfgARQPVGVGDVTSGLLL 230
Cdd:PRK14713 173 GEPPATTwEEALAQARRLAAETGTTVLVKggHL--DGQRAP--DALVGPDGAVTEVPGPRVD--TRNTHGTGCSLSSALA 246
|
170
....*....|....*...
gi 754952465 231 VKLLQGASLQQALEHVTA 248
Cdd:PRK14713 247 TRLGRGGDWAAALRWATA 264
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
76-250 |
7.79e-08 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 52.05 E-value: 7.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 76 DAVLSGYLGSAEqgehILGIVRQVKAANPRAKYFCDPVM----GHPekgcIVAPGVAEFHVRHALPASDIIAPNLVELEI 151
Cdd:PRK06427 75 DAVKIGMLASAE----IIETVAEALKRYPIPPVVLDPVMiaksGDP----LLADDAVAALRERLLPLATLITPNLPEAEA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 152 LCEHAVHNvTEAVM--AARELIAQGPEIVLVK--HLARAGISTDRfemlLVTAEQAWHISRPLVDfgARQPVGVGDVTSG 227
Cdd:PRK06427 147 LTGLPIAD-TEDEMkaAARALHALGCKAVLIKggHLLDGEESVDW----LFDGEGEERFSAPRIP--TKNTHGTGCTLSA 219
|
170 180
....*....|....*....|....*..
gi 754952465 228 LLLVKLLQGASLQQALEH----VTAAV 250
Cdd:PRK06427 220 AIAAELAKGASLLDAVQTakdyVTRAI 246
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
77-234 |
1.46e-06 |
|
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: 47.86 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 77 AVLSGYLGSAEQGEHILGIVRQVKAAnprakYFCDPVMghpekgcivaPGVAEFH--VRHALPASDIIAPNLVELEILCE 154
Cdd:cd00287 61 VVISGLSPAPEAVLDALEEARRRGVP-----VVLDPGP----------RAVRLDGeeLEKLLPGVDILTPNEEEAEALTG 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 155 HAVHNVTEAVMAARELIAQGPEIVLVKHLARAGISTDRfemllvtaeQAWHISRPLVDFGARQPVGVGDVTSGLLLVKLL 234
Cdd:cd00287 126 RRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATR---------GGTEVHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| PRK09517 |
PRK09517 |
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ... |
74-248 |
7.20e-05 |
|
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; Provisional
Pssm-ID: 169939 [Multi-domain] Cd Length: 755 Bit Score: 44.19 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 74 TCDAVLSGYLGSAEqgehilgIVRQVKA---ANPRAKYFCDPVMGHPEKGCIVAPGVAEfHVRHALPASDIIAPNLVELE 150
Cdd:PRK09517 310 TVDAVKLGMLGSAD-------TVDLVASwlgSHEHGPVVLDPVMVATSGDRLLDADATE-ALRRLAVHVDVVTPNIPELA 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 151 ILC-EHAVHNVTEAVMAARELIAQGPEIVLVK--HLaragiSTDRFEMLLVTAEQAWH-ISRPLVDFGARQpvGVGDVTS 226
Cdd:PRK09517 382 VLCgEAPAITMDEAIAQARGFARTHGTIVIVKggHL-----TGDLADNAVVRPDGSVHqVENPRVNTTNSH--GTGCSLS 454
|
170 180
....*....|....*....|..
gi 754952465 227 GLLLVKLLQGASLQQALEHVTA 248
Cdd:PRK09517 455 AALATLIAAGESVEKALEWATR 476
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
117-243 |
3.71e-04 |
|
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: 41.15 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 117 PEKGCIVApgvaefHVRHALPASDIIAPNLVELEILCEHAVHNVTEAVMAARELIAQGPEIVLVKHLARAGISTDRFEML 196
Cdd:cd01941 161 PTSAPKLK------KLFYLLHAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSREGGV 234
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 754952465 197 LVTAEQAWHISRPLVDFGArqpvgvGDVTSGLLLVKLLQGASLQQAL 243
Cdd:cd01941 235 ETKLFPAPQPETVVNVTGA------GDAFVAGLVAGLLEGMSLDDSL 275
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
140-250 |
4.49e-04 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 41.01 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 140 DIIAPNLVELEILCEHAVHNVTEAVMAARELIAQGPEIVLVKHLAR-AGISTDRFEMLlvtaeqawhISRPLVDfgARQP 218
Cdd:PRK11142 180 DIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRgVWLSENGEGQR---------VPGFRVQ--AVDT 248
|
90 100 110
....*....|....*....|....*....|....
gi 754952465 219 VGVGDVTSGLLLVKLLQGASLQQALE--HVTAAV 250
Cdd:PRK11142 249 IAAGDTFNGALVTALLEGKPLPEAIRfaHAAAAI 282
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
141-248 |
5.74e-04 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 40.83 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 141 IIAPNLVELEILCEHAVHNVTEAVMAARELIAQGPEIVLvkhlaragISTDRFEMLLVTAEQAWHISRPLVDFGArqPVG 220
Cdd:PRK09513 183 LVKPNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVV--------ISLGAEGALWVNASGEWIAKPPACDVVS--TVG 252
|
90 100
....*....|....*....|....*...
gi 754952465 221 VGDVTSGLLLVKLLQGASLQQALEHVTA 248
Cdd:PRK09513 253 AGDSMVGGLIYGLLMRESSEHTLRLATA 280
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
136-181 |
1.23e-03 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 39.66 E-value: 1.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 754952465 136 LPASDIIAPNLVELEILCEHAVHNVTEAVMAARELIAQGPEIVLVK 181
Cdd:PRK12413 127 FPYVTVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAVVIK 172
|
|
| PLN02898 |
PLN02898 |
HMP-P kinase/thiamin-monophosphate pyrophosphorylase |
76-193 |
2.29e-03 |
|
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
Pssm-ID: 215486 [Multi-domain] Cd Length: 502 Bit Score: 39.37 E-value: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 76 DAVLSGYLGSAEqgehILGIVRQVKAANPRAKYFCDPVMGHPEKGCIVAPGVAEFHVRHALPASDIIAPNLVELE-ILCE 154
Cdd:PLN02898 80 DVVKTGMLPSAE----IVKVLCQALKEFPVKALVVDPVMVSTSGDVLAGPSILSALREELLPLATIVTPNVKEASaLLGG 155
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 754952465 155 HAVHNVTEAVMAARELIAQGPEIVLVK--HLARAGISTDRF 193
Cdd:PLN02898 156 DPLETVADMRSAAKELHKLGPRYVLVKggHLPDSLDAVDVL 196
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
140-249 |
7.40e-03 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 37.46 E-value: 7.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754952465 140 DIIAPNLVELEILCEHAVHNVTEAVMAARELIAQGPEIVLVKHLARAGistdrfeMLLVTAEQAWHISRPLVDfgARQPV 219
Cdd:PRK10294 182 ELVKPNQKELSALVNRDLTQPDDVRKAAQELVNSGKAKRVVVSLGPQG-------ALGVDSENCIQVVPPPVK--SQSTV 252
|
90 100 110
....*....|....*....|....*....|
gi 754952465 220 GVGDVTSGLLLVKLLQGASLQQALEHVTAA 249
Cdd:PRK10294 253 GAGDSMVGAMTLKLAENASLEEMVRFGVAA 282
|
|
|