|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02978 |
PLN02978 |
pyridoxal kinase |
1-311 |
0e+00 |
|
pyridoxal kinase
Pssm-ID: 215529 [Multi-domain] Cd Length: 308 Bit Score: 532.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 1 MNVSSSTGRALTIQSHVVSGYVGNKCAVFPLQLHGFDVDPILSVQFSNHTGYGCWKGEVMTGEQLQSLVEGLEQNGLLEg 80
Cdd:PLN02978 8 LALPSSTGRVLSIQSHTVHGYVGNKSAVFPLQLLGFDVDPINSVQFSNHTGYPTFKGQVLDGEQLWALIEGLEANGLLF- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 81 YTHLLTGYIGSASMLRTVARLVRKLRTYNPNLVYVCDPVLGDNGRLYVPAELTTIYREEIVPLATLLTPNQFEAELLTGM 160
Cdd:PLN02978 87 YTHLLTGYIGSVSFLRTVLRVVKKLRSVNPNLTYVCDPVLGDEGKLYVPPELVPVYREKVVPLATMLTPNQFEAEQLTGI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 161 TIGSEEDALAACASLHQAGPPSVVLTSLDLDHsassssTITLLGSTSQPQAERcGQRFRIVVPRIPSYFTGTGDLCAALL 240
Cdd:PLN02978 167 RIVTEEDAREACAILHAAGPSKVVITSIDIDG------KLLLVGSHRKEKGAR-PEQFKIVIPKIPAYFTGTGDLMAALL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255077080 241 LAWTAKMPDKLGRAAEMAVASLQGVLRRTAAAQAVAEAagKTGIGCRELRLVNSVDELLHPKITEEVTWLD 311
Cdd:PLN02978 240 LGWSHKYPDNLDKAAELAVSSLQAVLRRTLADYKRAGA--DPKSSSLELRLVQSQDDIRHPQVRFKAERYS 308
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
9-269 |
2.05e-110 |
|
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: 320.69 E-value: 2.05e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 9 RALTIQSHVVSGYVGNKCAVFPLQLHGFDVDPILSVQFSNHTGYGCWKGEVMTGEQLQSLVEGLEQNGLLEGYTHLLTGY 88
Cdd:cd01173 1 RVLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLLLEYDAVLTGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 89 IGSASMLRTVARLVRKLRTYNPNLVYVCDPVLGDNGRLYVPA-ELTTIYREEIVPLATLLTPNQFEAELLTGMTIGSEED 167
Cdd:cd01173 81 LGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGDNGKLYVVAeEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 168 ALAACASLHQAGPPSVVLTSLDLdhsaSSSSTITLLGSTsqpqaerCGQRFRIVVPRIP--SYFTGTGDLCAALLLAWTA 245
Cdd:cd01173 161 AKAAARALHAKGPKTVVVTSVEL----ADDDRIEMLGST-------ATEAWLVQRPKIPfpAYFNGTGDLFAALLLARLL 229
|
250 260
....*....|....*....|....
gi 255077080 246 KMPDkLGRAAEMAVASLQGVLRRT 269
Cdd:cd01173 230 KGKS-LAEALEKALNFVHEVLEAT 252
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
9-299 |
8.16e-88 |
|
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: 263.93 E-value: 8.16e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 9 RALTIQSHVVSGYVGNKCAVFPLQLHGFDVDPILSVQFSNHTGYGCWKGEVMTGEQLQSLVEGLEQNGLLEGYTHLLTGY 88
Cdd:COG2240 3 RVLSIQSHVVYGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWKELGVLLEFDAVLSGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 89 IGSASMLRTVARLVRKLRTYNPNLVYVCDPVLGDNGRLY-VPAELTTIYREEIVPLATLLTPNQFEAELLTGMTIGSEED 167
Cdd:COG2240 83 LGSAEQGDIIADFVARVKAANPDALYLCDPVMGDNGKGYyVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETLEE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 168 ALAACASLHQAGPPSVVLTSLDLDhsASSSSTITLLGSTSqpqaercGQRFRIVVPRIPSYFTGTGDLCAALLLAWTAKm 247
Cdd:COG2240 163 ALAAARALLALGPKIVVVTSVPLD--DTPADKIGNLAVTA-------DGAWLVETPLLPFSPNGTGDLFAALLLAHLLR- 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 255077080 248 PDKLGRAAEMAVASLQGVLRRTAAAqavaeaagktgiGCRELRLVNSVDELL 299
Cdd:COG2240 233 GKSLEEALERAAAFVYEVLERTAAA------------GSDELLLEAALDELV 272
|
|
| pyridox_kin |
TIGR00687 |
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ... |
9-302 |
1.10e-82 |
|
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: 251.29 E-value: 1.10e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 9 RALTIQSHVVSGYVGNKCAVFPLQLHGFDVDPILSVQFSNHTGYGCWKGEVMTGEQLQSLVEGLEQNGLLEGYTHLLTGY 88
Cdd:TIGR00687 3 NVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLEAINKLNQCDAVLSGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 89 IGSASMLRTVARLVRKLRTYNPNLVYVCDPVLGDNGR-LYVPAELTTIYREEIVPLATLLTPNQFEAELLTGMTIGSEED 167
Cdd:TIGR00687 83 LGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKgCYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTEEE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 168 ALAACASLHQAGPPSVVLTSLdLDHSASSSSTITLLGSTSQPQAERCGQRFRIVVPRIpsyftGTGDLCAALLLAwTAKM 247
Cdd:TIGR00687 163 ALAAADALIAMGPDIVLVTHL-IRAGSQRDRSFEGLVATQEGRWHISRPLAVFDPPPV-----GTGDLIAALLLA-TLLH 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 255077080 248 PDKLGRAAEMAVASLQGVLRRTAAaqavaeaagktgIGCRELRLVNSVDELLHPK 302
Cdd:TIGR00687 236 GNSLKEALEKTVSAVYHVLRTTIQ------------LGKYELQPVAAQLEIRMPQ 278
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
86-268 |
7.43e-21 |
|
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: 89.46 E-value: 7.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 86 TGYIGSASMLRTVARlvrKLRTYNPNLVyvCDPVL--GDNGRLyVPAELTTIYREEIVPLATLLTPNQFEAELLTGMTIG 163
Cdd:pfam08543 66 TGMLGSAEIIEAVAE---KLDKYGVPVV--LDPVMvaKSGDSL-LDDEAIEALKEELLPLATLITPNLPEAEALTGRKIK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 164 SEEDALAACASLHQAGPPSVVLTSldlDHSASSSSTIT-LLGSTsqpqaercGQRFRIVVPRIPSYFT-GTGD-LCAAL- 239
Cdd:pfam08543 140 TLEDMKEAAKKLLALGAKAVLIKG---GHLEGEEAVVTdVLYDG--------GGFYTLEAPRIPTKNThGTGCtLSAAIa 208
|
170 180 190
....*....|....*....|....*....|
gi 255077080 240 -LLAWTAKMPDklgrAAEMAVASLQGVLRR 268
Cdd:pfam08543 209 aNLAKGLSLPE----AVREAKEYVTEAIRD 234
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02978 |
PLN02978 |
pyridoxal kinase |
1-311 |
0e+00 |
|
pyridoxal kinase
Pssm-ID: 215529 [Multi-domain] Cd Length: 308 Bit Score: 532.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 1 MNVSSSTGRALTIQSHVVSGYVGNKCAVFPLQLHGFDVDPILSVQFSNHTGYGCWKGEVMTGEQLQSLVEGLEQNGLLEg 80
Cdd:PLN02978 8 LALPSSTGRVLSIQSHTVHGYVGNKSAVFPLQLLGFDVDPINSVQFSNHTGYPTFKGQVLDGEQLWALIEGLEANGLLF- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 81 YTHLLTGYIGSASMLRTVARLVRKLRTYNPNLVYVCDPVLGDNGRLYVPAELTTIYREEIVPLATLLTPNQFEAELLTGM 160
Cdd:PLN02978 87 YTHLLTGYIGSVSFLRTVLRVVKKLRSVNPNLTYVCDPVLGDEGKLYVPPELVPVYREKVVPLATMLTPNQFEAEQLTGI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 161 TIGSEEDALAACASLHQAGPPSVVLTSLDLDHsassssTITLLGSTSQPQAERcGQRFRIVVPRIPSYFTGTGDLCAALL 240
Cdd:PLN02978 167 RIVTEEDAREACAILHAAGPSKVVITSIDIDG------KLLLVGSHRKEKGAR-PEQFKIVIPKIPAYFTGTGDLMAALL 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255077080 241 LAWTAKMPDKLGRAAEMAVASLQGVLRRTAAAQAVAEAagKTGIGCRELRLVNSVDELLHPKITEEVTWLD 311
Cdd:PLN02978 240 LGWSHKYPDNLDKAAELAVSSLQAVLRRTLADYKRAGA--DPKSSSLELRLVQSQDDIRHPQVRFKAERYS 308
|
|
| PTZ00344 |
PTZ00344 |
pyridoxal kinase; Provisional |
4-310 |
2.35e-130 |
|
pyridoxal kinase; Provisional
Pssm-ID: 240372 [Multi-domain] Cd Length: 296 Bit Score: 372.88 E-value: 2.35e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 4 SSSTGRALTIQSHVVSGYVGNKCAVFPLQLHGFDVDPILSVQFSNHTGYGCWKGEVMTGEQLQSLVEGLEQNGLLEGYTH 83
Cdd:PTZ00344 1 MSMEKKVLSIQSHVTHGYVGNRAATFPLQLLGFDVDFVNTVQLSNHTGYPVIKGHRLDLNELITLMDGLRANNLLSDYTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 84 LLTGYIGSASMLRTVARLVRKLRTYNPNLVYVCDPVLGDNGRLYVPAELTTIYReEIVPLATLLTPNQFEAELLTGMTIG 163
Cdd:PTZ00344 81 VLTGYINSADILREVLATVKEIKELRPKLIFLCDPVMGDDGKLYVKEEVVDAYR-ELIPYADVITPNQFEASLLSGVEVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 164 SEEDALAACASLHQAGPPSVVLTSLDLDhsaSSSSTITLLGSTSQPQAERcGQRFRIVVPRIPSYFTGTGDLCAALLLAW 243
Cdd:PTZ00344 160 DLSDALEAIDWFHEQGIPVVVITSFRED---EDPTHLRFLLSCRDKDTKN-NKRFTGKVPYIEGRYTGTGDLFAALLLAF 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255077080 244 TAKMPDKLgrAAEMAVASLQGVLRRTaaaqAVAEAAGKTGIGCRELRLVNSVDELLHPKITEEVTWL 310
Cdd:PTZ00344 236 SHQHPMDL--AVGKAMGVLQDIIKAT----RESGGSGSSSLMSRELRLIQSPRDLLNPETVFKVTPL 296
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
9-269 |
2.05e-110 |
|
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: 320.69 E-value: 2.05e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 9 RALTIQSHVVSGYVGNKCAVFPLQLHGFDVDPILSVQFSNHTGYGCWKGEVMTGEQLQSLVEGLEQNGLLEGYTHLLTGY 88
Cdd:cd01173 1 RVLSIQSHVVHGYVGNSAAVFPLQRLGWDVDALPTVQFSNHTGYGTWTGFVLSAEELEDLLEGLEALGLLLEYDAVLTGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 89 IGSASMLRTVARLVRKLRTYNPNLVYVCDPVLGDNGRLYVPA-ELTTIYREEIVPLATLLTPNQFEAELLTGMTIGSEED 167
Cdd:cd01173 81 LGSAEQVEAVAEIVKRLKEKNPNLLYVCDPVMGDNGKLYVVAeEIVPVYRDLLVPLADIITPNQFELELLTGKKINDLED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 168 ALAACASLHQAGPPSVVLTSLDLdhsaSSSSTITLLGSTsqpqaerCGQRFRIVVPRIP--SYFTGTGDLCAALLLAWTA 245
Cdd:cd01173 161 AKAAARALHAKGPKTVVVTSVEL----ADDDRIEMLGST-------ATEAWLVQRPKIPfpAYFNGTGDLFAALLLARLL 229
|
250 260
....*....|....*....|....
gi 255077080 246 KMPDkLGRAAEMAVASLQGVLRRT 269
Cdd:cd01173 230 KGKS-LAEALEKALNFVHEVLEAT 252
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
9-299 |
8.16e-88 |
|
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: 263.93 E-value: 8.16e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 9 RALTIQSHVVSGYVGNKCAVFPLQLHGFDVDPILSVQFSNHTGYGCWKGEVMTGEQLQSLVEGLEQNGLLEGYTHLLTGY 88
Cdd:COG2240 3 RVLSIQSHVVYGHVGNSAAVPPLSALGVEVWPLPTVLLSNHTGYGTFTGRDLPTDDIADILDGWKELGVLLEFDAVLSGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 89 IGSASMLRTVARLVRKLRTYNPNLVYVCDPVLGDNGRLY-VPAELTTIYREEIVPLATLLTPNQFEAELLTGMTIGSEED 167
Cdd:COG2240 83 LGSAEQGDIIADFVARVKAANPDALYLCDPVMGDNGKGYyVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETLEE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 168 ALAACASLHQAGPPSVVLTSLDLDhsASSSSTITLLGSTSqpqaercGQRFRIVVPRIPSYFTGTGDLCAALLLAWTAKm 247
Cdd:COG2240 163 ALAAARALLALGPKIVVVTSVPLD--DTPADKIGNLAVTA-------DGAWLVETPLLPFSPNGTGDLFAALLLAHLLR- 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 255077080 248 PDKLGRAAEMAVASLQGVLRRTAAAqavaeaagktgiGCRELRLVNSVDELL 299
Cdd:COG2240 233 GKSLEEALERAAAFVYEVLERTAAA------------GSDELLLEAALDELV 272
|
|
| PRK05756 |
PRK05756 |
pyridoxal kinase PdxY; |
11-301 |
2.17e-83 |
|
pyridoxal kinase PdxY;
Pssm-ID: 235592 [Multi-domain] Cd Length: 286 Bit Score: 252.87 E-value: 2.17e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 11 LTIQSHVVSGYVGNKCAVFPLQLHGFDVDPILSVQFSNHTGYGCWKGEVMTGEQLQSLVEGLEQNGLLEGYTHLLTGYIG 90
Cdd:PRK05756 5 LSIQSHVVYGHVGNSAAVFPMQRLGVNVWPLNTVQFSNHTGYGKWTGCVMPPSHLTEIVQGIADIGWLGECDAVLSGYLG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 91 SASMLRTVARLVRKLRTYNPNLVYVCDPVLGDNGR-LYVPAELTTIYREEIVPLATLLTPNQFEAELLTGMTIGSEEDAL 169
Cdd:PRK05756 85 SAEQGEAILDAVRRVKAANPQALYFCDPVMGDPEKgCIVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETLEDAV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 170 AACASLHQAGPPSVVLTSldLDHSASSSSTITLLGSTSQpqaercgQRFRIVVPRIPSYF--TGTGDLCAALLLAWTAKM 247
Cdd:PRK05756 165 AAARALIARGPKIVLVTS--LARAGYPADRFEMLLVTAD-------GAWHISRPLVDFMRqpVGVGDLTSALFLARLLQG 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 255077080 248 PDkLGRAAEMAVASLQGVLRRTAAAqavaeaagktgiGCRELRLVNSVDELLHP 301
Cdd:PRK05756 236 GS-LEEALEHTTAAVYEVMARTKER------------GSYELQLVAAQDSIATP 276
|
|
| pyridox_kin |
TIGR00687 |
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ... |
9-302 |
1.10e-82 |
|
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: 251.29 E-value: 1.10e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 9 RALTIQSHVVSGYVGNKCAVFPLQLHGFDVDPILSVQFSNHTGYGCWKGEVMTGEQLQSLVEGLEQNGLLEGYTHLLTGY 88
Cdd:TIGR00687 3 NVLSIQSHVVYGHVGNRAATFPLQRLGFEVWAVNTVQFSNHTGYGKWTGQVLPPDELHELVEGLEAINKLNQCDAVLSGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 89 IGSASMLRTVARLVRKLRTYNPNLVYVCDPVLGDNGR-LYVPAELTTIYREEIVPLATLLTPNQFEAELLTGMTIGSEED 167
Cdd:TIGR00687 83 LGSAEQVAMVVGIVRQVKQANPQALYVCDPVMGDPWKgCYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTEEE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 168 ALAACASLHQAGPPSVVLTSLdLDHSASSSSTITLLGSTSQPQAERCGQRFRIVVPRIpsyftGTGDLCAALLLAwTAKM 247
Cdd:TIGR00687 163 ALAAADALIAMGPDIVLVTHL-IRAGSQRDRSFEGLVATQEGRWHISRPLAVFDPPPV-----GTGDLIAALLLA-TLLH 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 255077080 248 PDKLGRAAEMAVASLQGVLRRTAAaqavaeaagktgIGCRELRLVNSVDELLHPK 302
Cdd:TIGR00687 236 GNSLKEALEKTVSAVYHVLRTTIQ------------LGKYELQPVAAQLEIRMPQ 278
|
|
| pdxK |
PRK08176 |
pyridoxine/pyridoxal/pyridoxamine kinase; |
8-269 |
3.30e-41 |
|
pyridoxine/pyridoxal/pyridoxamine kinase;
Pssm-ID: 181269 [Multi-domain] Cd Length: 281 Bit Score: 144.41 E-value: 3.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 8 GRAL-----TIQSHVVSGYVGNKCAVFPLQLHGFDVDPILSVQFSNHTGYGCWKGEVMTGEQLQSLVEGLEQNGLLEGYT 82
Cdd:PRK08176 11 SRALqadivAVQSQVVYGSVGNSIAVPAIKANGLRVFAVPTVLLSNTPHYPTFYGGAIPDEWFSGYLRALQERDALRQLR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 83 HLLTGYIGSASMLRTVARLVRKLRTYNPNLVYVCDPVLGDNGR-LYVPAELTTIYREEIVPLATLLTPNQFEAELLTGMT 161
Cdd:PRK08176 91 AVTTGYMGSASQIKILAEWLTALRADHPDLLIMVDPVIGDIDSgIYVKPDLPEAYRQHLLPLAQGLTPNIFELEILTGKP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 162 IGSEEDALAACASLHQAGPPSVVLTSLDldhSASSSSTITLLGSTSQpqaercgQRFRIVVPRIPSYFTGTGDL-CAALL 240
Cdd:PRK08176 171 CRTLDSAIAAAKSLLSDTLKWVVITSAA---GNEENQEMQVVVVTAD-------SVNVISHPRVDTDLKGTGDLfCAELV 240
|
250 260
....*....|....*....|....*....
gi 255077080 241 LAWTAKMPdkLGRAAEMAVASLQGVLRRT 269
Cdd:PRK08176 241 SGLLKGKA--LTDAAHRAGLRVLEVMRYT 267
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
86-268 |
3.18e-22 |
|
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: 93.18 E-value: 3.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 86 TGYIGSASMLRTVARLVRKLRTYNpnlvYVCDPVL----GDngRLyVPAELTTIYREEIVPLATLLTPNQFEAELLTGMT 161
Cdd:COG0351 72 IGMLGSAEIIEAVAEILADYPLVP----VVLDPVMvaksGD--RL-LDEDAVEALRELLLPLATVVTPNLPEAEALLGIE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 162 IGSEEDALAACASLHQAGPPSVVLTSLdldHSASSSSTITLLGStsqpqaercGQRFRIVVPRIPS-YFTGTGD-LCAAL 239
Cdd:COG0351 145 ITTLDDMREAAKALLELGAKAVLVKGG---HLPGDEAVDVLYDG---------DGVREFSAPRIDTgNTHGTGCtLSSAI 212
|
170 180 190
....*....|....*....|....*....|.
gi 255077080 240 --LLAWTAKMPDklgrAAEMAVASLQGVLRR 268
Cdd:COG0351 213 aaLLAKGLDLEE----AVREAKEYVTQAIRA 239
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
86-268 |
7.43e-21 |
|
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: 89.46 E-value: 7.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 86 TGYIGSASMLRTVARlvrKLRTYNPNLVyvCDPVL--GDNGRLyVPAELTTIYREEIVPLATLLTPNQFEAELLTGMTIG 163
Cdd:pfam08543 66 TGMLGSAEIIEAVAE---KLDKYGVPVV--LDPVMvaKSGDSL-LDDEAIEALKEELLPLATLITPNLPEAEALTGRKIK 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 164 SEEDALAACASLHQAGPPSVVLTSldlDHSASSSSTIT-LLGSTsqpqaercGQRFRIVVPRIPSYFT-GTGD-LCAAL- 239
Cdd:pfam08543 140 TLEDMKEAAKKLLALGAKAVLIKG---GHLEGEEAVVTdVLYDG--------GGFYTLEAPRIPTKNThGTGCtLSAAIa 208
|
170 180 190
....*....|....*....|....*....|
gi 255077080 240 -LLAWTAKMPDklgrAAEMAVASLQGVLRR 268
Cdd:pfam08543 209 aNLAKGLSLPE----AVREAKEYVTEAIRD 234
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
86-267 |
7.44e-20 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 87.10 E-value: 7.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 86 TGYIGSASMLRTVARLVRKLrtynPNLVYVCDPVL----GDngRLyvpAELTTIY--REEIVPLATLLTPNQFEAELLTG 159
Cdd:PRK06427 79 IGMLASAEIIETVAEALKRY----PIPPVVLDPVMiaksGD--PL---LADDAVAalRERLLPLATLITPNLPEAEALTG 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 160 MTIGSEEDALAACA-SLHQAGPPSVVLTSldlDHSASSSSTITLL--GSTSqpqaercgQRFRivVPRIPSYFT-GTGD- 234
Cdd:PRK06427 150 LPIADTEDEMKAAArALHALGCKAVLIKG---GHLLDGEESVDWLfdGEGE--------ERFS--APRIPTKNThGTGCt 216
|
170 180 190
....*....|....*....|....*....|....*
gi 255077080 235 LCAAL--LLAWTAKMPDklgrAAEMAVASLQGVLR 267
Cdd:PRK06427 217 LSAAIaaELAKGASLLD----AVQTAKDYVTRAIR 247
|
|
| PRK07105 |
PRK07105 |
pyridoxamine kinase; Validated |
84-254 |
5.32e-14 |
|
pyridoxamine kinase; Validated
Pssm-ID: 180840 [Multi-domain] Cd Length: 284 Bit Score: 70.71 E-value: 5.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 84 LLTGYIGSASMLRTVARLVRKLRTynPNLVYVCDPVLGDNGRLYVPAELTTIYR-EEIVPLATLLTPNQFEAELLTGM-- 160
Cdd:PRK07105 79 IYSGYLGSPRQIQIVSDFIKYFKK--KDLLVVVDPVMGDNGKLYQGFDQEMVEEmRKLIQKADVITPNLTEACLLLDKpy 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 161 --TIGSEEDALAACASLHQAGPPSVVLTSLDLDHsasssstitllGSTSQPQAERCGQRFRIVV-PRIPSYFTGTGDLCA 237
Cdd:PRK07105 157 leKSYSEEEIKQLLRKLADLGPKIVIITSVPFED-----------GKIGVAYYDRATDRFWKVFcKYIPAHYPGTGDIFT 225
|
170 180
....*....|....*....|
gi 255077080 238 ALLLAWTAK---MPDKLGRA 254
Cdd:PRK07105 226 SVITGSLLQgdsLPIALDRA 245
|
|
| PRK08573 |
PRK08573 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
86-177 |
2.67e-11 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 236297 [Multi-domain] Cd Length: 448 Bit Score: 63.98 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 86 TGYIGSASMLRTVARLVRKLrtynpNLVYVCDPVL-GDNGRLYVPAELTTIYREEIVPLATLLTPNQFEAELLTGMTIGS 164
Cdd:PRK08573 77 TGMLSNREIIEAVAKTVSKY-----GFPLVVDPVMiAKSGAPLLREDAVDALIKRLLPLATVVTPNRPEAEKLTGMKIRS 151
|
90
....*....|...
gi 255077080 165 EEDALAACASLHQ 177
Cdd:PRK08573 152 VEDARKAAKYIVE 164
|
|
| PRK12412 |
PRK12412 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
9-185 |
2.77e-11 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183512 [Multi-domain] Cd Length: 268 Bit Score: 62.68 E-value: 2.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 9 RALTIQSHVVSGYVGNKCAVFPLQLHGF----DVDPILSVQFSNHTGYGCWKGEVMTGE-QLQSLVEGLeqnglleGYTH 83
Cdd:PRK12412 3 KALTIAGSDTSGGAGIQADLKTFQELGVygmtSLTTIVTMDPHNGWAHNVFPIPASTLKpQLETTIEGV-------GVDA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 84 LLTGYIGSASMLRTVARLVRKLRTYNpnlvYVCDPVL---GDNGRLYvpAELTTIYREEIVPLATLLTPNQFEAELLTGM 160
Cdd:PRK12412 76 LKTGMLGSVEIIEMVAETIEKHNFKN----VVVDPVMvckGADEALH--PETNDCLRDVLVPKALVVTPNLFEAYQLSGV 149
|
170 180
....*....|....*....|....*
gi 255077080 161 TIGSEEDALAACASLHQAGPPSVVL 185
Cdd:PRK12412 150 KINSLEDMKEAAKKIHALGAKYVLI 174
|
|
| PRK12616 |
PRK12616 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
64-186 |
6.54e-10 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183624 Cd Length: 270 Bit Score: 58.90 E-value: 6.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 64 QLQSLVEGLeqnglleGYTHLLTGYIGSASMLRTVARLVRKLRTYNpnlvYVCDPVL---GDNGRLYvpAELTTIYREEI 140
Cdd:PRK12616 65 QLSTIVDGI-------GVDAMKTGMLPTVDIIELAADTIKEKQLKN----VVIDPVMvckGANEVLY--PEHAEALREQL 131
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 255077080 141 VPLATLLTPNQFEAELLTGM-TIGSEEDALAACASLHQAGPPSVVLT 186
Cdd:PRK12616 132 APLATVITPNLFEAGQLSGMgEIKTVEQMKEAAKKIHELGAQYVVIT 178
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
130-186 |
1.43e-09 |
|
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: 57.95 E-value: 1.43e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 255077080 130 AELTTIY--------REEIVPLATLLTPNQFEAELLTGMTIGSEEDALAACASLHQAGPPSVVLT 186
Cdd:cd01174 154 AGVTVILnpaparplPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVT 218
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
138-262 |
1.60e-09 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 57.74 E-value: 1.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 138 EEIVPLATLLTPNQFEAELLTGMTIGSEEDALAACASLHQAGPPSVVLTsldldhsasssstitlLGSTSQPQAERCGQR 217
Cdd:pfam00294 175 LELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVT----------------LGADGALVVEGDGEV 238
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 255077080 218 FRIVVPRIPSY-FTGTGD-LCAALLLAWTAKMPDK-LGRAAeMAVASL 262
Cdd:pfam00294 239 HVPAVPKVKVVdTTGAGDsFVGGFLAGLLAGKSLEeALRFA-NAAAAL 285
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
98-185 |
2.15e-09 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 57.00 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 98 VARLVRKLRTYNPNLVYVCDPVL--GDNGRLYVpAELttiyREEIV---PLATLLTPNQFEAELLTGMTIGSEEDALAAC 172
Cdd:PRK12413 84 IAEQALDFIKGHPGIPVVLDPVLvcKETHDVEV-SEL----RQELIqffPYVTVITPNLVEAELLSGKEIKTLEDMKEAA 158
|
90
....*....|...
gi 255077080 173 ASLHQAGPPSVVL 185
Cdd:PRK12413 159 KKLYDLGAKAVVI 171
|
|
| PLN02898 |
PLN02898 |
HMP-P kinase/thiamin-monophosphate pyrophosphorylase |
86-196 |
6.16e-09 |
|
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
Pssm-ID: 215486 [Multi-domain] Cd Length: 502 Bit Score: 56.70 E-value: 6.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 86 TGYIGSASMLRTVARLVRKLRTYNpnlvYVCDPVL-GDNGRLYVPAELTTIYREEIVPLATLLTPNQFEAE-LLTGMTIG 163
Cdd:PLN02898 84 TGMLPSAEIVKVLCQALKEFPVKA----LVVDPVMvSTSGDVLAGPSILSALREELLPLATIVTPNVKEASaLLGGDPLE 159
|
90 100 110
....*....|....*....|....*....|...
gi 255077080 164 SEEDALAACASLHQAGPPSVVLTSLDLDHSASS 196
Cdd:PLN02898 160 TVADMRSAAKELHKLGPRYVLVKGGHLPDSLDA 192
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
98-245 |
8.27e-09 |
|
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: 54.41 E-value: 8.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 98 VARLVRKLRTYNpnLVYVCDPVlgdnGRLYVPAELTtiyREEIVPLATLLTPNQFEAELLTGMTIGSEEDALAACASLHQ 177
Cdd:cd00287 73 VLDALEEARRRG--VPVVLDPG----PRAVRLDGEE---LEKLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLS 143
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 255077080 178 AGPPSVVLTsldLDHSASSSSTitllgstsqpqaercGQRFRIVVPRIPSY---FTGTGDLCAALLLAWTA 245
Cdd:cd00287 144 KGPKVVIVT---LGEKGAIVAT---------------RGGTEVHVPAFPVKvvdTTGAGDAFLAALAAGLA 196
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
77-260 |
1.36e-08 |
|
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: 54.89 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 77 LLEGYTHLLTGYIGSAS--MLRTVARLVRKLRTYNpnLVYVCDPvlgdNGRLYVPAELTTIYREeIVPLATLLTPNQFEA 154
Cdd:COG0524 124 LLAGADILHLGGITLASepPREALLAALEAARAAG--VPVSLDP----NYRPALWEPARELLRE-LLALVDILFPNEEEA 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 155 ELLTGMTigseeDALAACASLHQAGPPSVVLTsldldhsasssstitlLGstsqpqAERC-----GQRFRIVVPRI---- 225
Cdd:COG0524 197 ELLTGET-----DPEEAAAALLARGVKLVVVT----------------LG------AEGAllytgGEVVHVPAFPVevvd 249
|
170 180 190
....*....|....*....|....*....|....*.
gi 255077080 226 PsyfTGTGD-LCAALLLAWTAKMPdkLGRAAEMAVA 260
Cdd:COG0524 250 T---TGAGDaFAAGFLAGLLEGLD--LEEALRFANA 280
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
138-186 |
2.58e-07 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 51.02 E-value: 2.58e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 255077080 138 EEIVPLATLLTPNQFEAELLTGMTIGSEEDALAACASLHQAGPPSVVLT 186
Cdd:PRK11142 173 DELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLIT 221
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
145-260 |
4.10e-07 |
|
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: 50.39 E-value: 4.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 145 TLLTPNQFEAELLTGMTIGSEEDALAACASLHQAGPPSVVLTsLDLDHSASSSStITLLGSTSQPQAercgQRFRIV-Vp 223
Cdd:cd01941 178 DLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVT-LGAKGVLLSSR-EGGVETKLFPAP----QPETVVnV- 250
|
90 100 110
....*....|....*....|....*....|....*...
gi 255077080 224 ripsyfTGTGD-LCAALLLAWTAKMPdkLGRAAEMAVA 260
Cdd:cd01941 251 ------TGAGDaFVAGLVAGLLEGMS--LDDSLRFAQA 280
|
|
| PTZ00347 |
PTZ00347 |
phosphomethylpyrimidine kinase; Provisional |
86-185 |
1.03e-05 |
|
phosphomethylpyrimidine kinase; Provisional
Pssm-ID: 240375 [Multi-domain] Cd Length: 504 Bit Score: 46.88 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 86 TGYIGSASMLRTVARlvrKLRtynpNLVYVCDPVL----GDNGRLYVPAE-LTTIYREEIVPLATLLTPNQFEAELLTGM 160
Cdd:PTZ00347 305 LGLVPTARQLEIVIE---KLK----NLPMVVDPVLvatsGDDLVAQKNADdVLAMYKERIFPMATIITPNIPEAERILGR 377
|
90 100
....*....|....*....|....*.
gi 255077080 161 T-IGSEEDALAACASLHQAGPPSVVL 185
Cdd:PTZ00347 378 KeITGVYEARAAAQALAQYGSRYVLV 403
|
|
| PRK14713 |
PRK14713 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
86-267 |
4.51e-05 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 237797 [Multi-domain] Cd Length: 530 Bit Score: 44.78 E-value: 4.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 86 TGYIGSASMLRTVARLVRKlrtyNPNLVYVCDPVL----GDngRLYVP-AELTTIyreEIVPLATLLTPNQFEAELLTGM 160
Cdd:PRK14713 104 IGMLGDAEVIDAVRTWLAE----HRPPVVVLDPVMvatsGD--RLLEEdAEAALR---ELVPRADLITPNLPELAVLLGE 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 161 TIGSE-EDALAACASLHQAGPPSVVLTSldlDHSASSSSTITLLGSTsqpqaercGQRFRIVVPRIPSYFT-GTGDLCAA 238
Cdd:PRK14713 175 PPATTwEEALAQARRLAAETGTTVLVKG---GHLDGQRAPDALVGPD--------GAVTEVPGPRVDTRNThGTGCSLSS 243
|
170 180
....*....|....*....|....*....
gi 255077080 239 LLLAWTAKMPDkLGRAAEMAVASLQGVLR 267
Cdd:PRK14713 244 ALATRLGRGGD-WAAALRWATAWLHGAIA 271
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
144-258 |
2.88e-04 |
|
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the lipopolysaccharide (LPS) core precursor ADP-L-glycero-D-manno-heptose. LPS plays an important role in maintaining the structural integrity of the bacterial outer membrane of gram-negative bacteria. RfaE consists of two domains, a sugar kinase domain, represented here, and a domain belonging to the cytidylyltransferase superfamily.
Pssm-ID: 238577 [Multi-domain] Cd Length: 304 Bit Score: 41.78 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255077080 144 ATLLTPNQFEAELLTGMTIGSEEDALAACASL-HQAGPPSVVLTsldldhsaSSSSTITLLGSTSQPQaercgqrfrivv 222
Cdd:cd01172 182 ATLLTPNEKEAREALGDEINDDDELEAAGEKLlELLNLEALLVT--------LGEEGMTLFERDGEVQ------------ 241
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 255077080 223 pRIPSY------FTGTGDL---CAALLLAWTAKMPDklgrAAEMA 258
Cdd:cd01172 242 -HIPALakevydVTGAGDTviaTLALALAAGADLEE----AAFLA 281
|
|
| |
