|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
1-266 |
7.19e-154 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 429.55 E-value: 7.19e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 1 MNKPKIALTIAGTDPTGGAGVMADLKSFHSCGVYGMASITSIVAQNTLGVQHIHNLETSWVKEQLESIFNDELPHAIKTG 80
Cdd:PRK06427 1 MMKRPIALTIAGSDSGGGAGIQADLKTFQALGVYGMSAITALTAQNTLGVQRVHPIPPEFVAAQLDAVFSDIRIDAVKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 81 MIATEDTMHLVQSYLQQYPEIPYVIDPVMLAKSGDSLMNDETKQKLQDTLLPLADVVTPNIPEAEEITGIKIDTEENIRK 160
Cdd:PRK06427 81 MLASAEIIETVAEALKRYPIPPVVLDPVMIAKSGDPLLADDAVAALRERLLPLATLITPNLPEAEALTGLPIADTEDEMK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 161 AGNIFINEIGSKGVVIKGGHSADLNNAKDFLFTQDGVYTFEDERFETKHTHGTGCTFSAVITAELAKGRSIYEAVEKAKK 240
Cdd:PRK06427 161 AAARALHALGCKAVLIKGGHLLDGEESVDWLFDGEGEERFSAPRIPTKNTHGTGCTLSAAIAAELAKGASLLDAVQTAKD 240
|
250 260
....*....|....*....|....*.
gi 516232796 241 FISLSIKYTPEIGKGRGPVNHFAYLK 266
Cdd:PRK06427 241 YVTRAIRHALEIGQGHGPVNHFAYLW 266
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
8-263 |
4.61e-129 |
|
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: 366.29 E-value: 4.61e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 8 LTIAGTDPTGGAGVMADLKSFHSCGVYGMASITSIVAQNTLGVQHIHNLETSWVKEQLESIFNDELPHAIKTGMIATEDT 87
Cdd:COG0351 1 LTIAGSDPSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVTGVHPVPPEFVAAQLRAVLEDIPVDAIKIGMLGSAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 88 MHLVQSYLQQYPEIPYVIDPVMLAKSGDSLMNDETKQKLQDTLLPLADVVTPNIPEAEEITGIKIDTEENIRKAGNIfIN 167
Cdd:COG0351 81 IEAVAEILADYPLVPVVLDPVMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALLGIEITTLDDMREAAKA-LL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 168 EIGSKGVVIKGGHSADlNNAKDFLFTQDGVYTFEDERFETKHTHGTGCTFSAVITAELAKGRSIYEAVEKAKKFISLSIK 247
Cdd:COG0351 160 ELGAKAVLVKGGHLPG-DEAVDVLYDGDGVREFSAPRIDTGNTHGTGCTLSSAIAALLAKGLDLEEAVREAKEYVTQAIR 238
|
250
....*....|....*.
gi 516232796 248 YTPEIGKGRGPVNHFA 263
Cdd:COG0351 239 AALRLGMGHGPVNHFA 254
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
14-260 |
6.36e-125 |
|
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: 355.25 E-value: 6.36e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 14 DPTGGAGVMADLKSFHSCGVYGMASITSIVAQNTLGVQHIHNLETSWVKEQLESIFNDELPHAIKTGMIATEDTMHLVQS 93
Cdd:pfam08543 1 DSSGGAGIQADLKTFSALGVYGMSVITALTAQNTLGVQGVHPLPPEFVAAQLDAVLEDIPVDAVKTGMLGSAEIIEAVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 94 YLQQYPeIPYVIDPVMLAKSGDSLMNDETKQKLQDTLLPLADVVTPNIPEAEEITGIKIDTEENIRKAGNIfINEIGSKG 173
Cdd:pfam08543 81 KLDKYG-VPVVLDPVMVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKK-LLALGAKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 174 VVIKGGHSADLN-NAKDFLFTQDGVYTFEDERFETKHTHGTGCTFSAVITAELAKGRSIYEAVEKAKKFISLSIKYTPEI 252
Cdd:pfam08543 159 VLIKGGHLEGEEaVVTDVLYDGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKEYVTEAIRDALNL 238
|
....*...
gi 516232796 253 GKGRGPVN 260
Cdd:pfam08543 239 GKGHGPVN 246
|
|
| HMPP_kinase |
cd01169 |
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ... |
6-248 |
5.53e-116 |
|
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: 332.55 E-value: 5.53e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 6 IALTIAGTDPTGGAGVMADLKSFHSCGVYGMASITSIVAQNTLGVQHIHNLETSWVKEQLESIFNDELPHAIKTGMIATE 85
Cdd:cd01169 1 VVLTIAGSDSSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVFGVHPVPPEFVAAQLDAVLEDIPVDAIKIGMLGSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 86 DTMHLVQSYLQQYPEIPYVIDPVMLAKSGDSLMNDETKQKLQDTLLPLADVVTPNIPEAEEITGIKIDTEENIRKAGNIf 165
Cdd:cd01169 81 EIIEAVAEALKDYPDIPVVLDPVMVAKSGDSLLDDDAIEALRELLLPLATLITPNLPEAELLTGLEIATEEDMMKAAKA- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 166 INEIGSKGVVIKGGHSADlNNAKDFLFTQDGVYTFEDERFETKHTHGTGCTFSAVITAELAKGRSIYEAVEKAKKFISLS 245
Cdd:cd01169 160 LLALGAKAVLIKGGHLPG-DEAVDVLYDGGGFFEFESPRIDTKNTHGTGCTLSSAIAANLAKGLSLEEAVREAKEYVTQA 238
|
...
gi 516232796 246 IKY 248
Cdd:cd01169 239 IRN 241
|
|
| HMP-P_kinase |
TIGR00097 |
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ... |
7-262 |
8.55e-110 |
|
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: 317.31 E-value: 8.55e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 7 ALTIAGTDPTGGAGVMADLKSFHSCGVYGMASITSIVAQNTLGVQHIHNLETSWVKEQLESIFNDELPHAIKTGMIATED 86
Cdd:TIGR00097 1 ALTIAGSDSGGGAGIQADLKTFSALGVFGTSVITALTAQNTRGVTGVYPIPPDFVEAQLDAVFSDIPVDAAKTGMLASAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 87 TMHLVQSYLQQYPEIPYVIDPVMLAKSGDSLMNDETKQKLQDTLLPLADVVTPNIPEAEEITGIKIDTEENIRKAGNIfI 166
Cdd:TIGR00097 81 IVEAVARKLREYPVRPLVVDPVMVAKSGAPLLEEEAIEALRKRLLPLATLITPNLPEAEALLGTKIRTEQDMIKAAKK-L 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 167 NEIGSKGVVIKGGHSADlNNAKDFLFTQDGVYTFEDERFETKHTHGTGCTFSAVITAELAKGRSIYEAVEKAKKFISLSI 246
Cdd:TIGR00097 160 RELGPKAVLIKGGHLEG-DQAVDVLFDGGEIHILKAPRIETKNTHGTGCTLSAAIAANLAKGLSLKEAVKEAKEFVTGAI 238
|
250
....*....|....*.
gi 516232796 247 KYTPEIGKGRGPVNHF 262
Cdd:TIGR00097 239 RYGLNIGHGHGPLNHF 254
|
|
| PRK08573 |
PRK08573 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
5-265 |
1.81e-91 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 236297 [Multi-domain] Cd Length: 448 Bit Score: 277.76 E-value: 1.81e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 5 KIALTIAGTDPTGGAGVMADLKSFHSCGVYGMASITSIVAQNTLGVQHIHNLETSWVKEQLESIFNDELPHAIKTGMIAT 84
Cdd:PRK08573 3 PVALTIAGSDSGGGAGIEADLKTFAALGVHGAVAITSVTAQNTYEVRAIHDLPPEVVAAQIEAVWEDMGIDAAKTGMLSN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 85 EDTMHLVQSYLQQYpEIPYVIDPVMLAKSGDSLMNDETKQKLQDTLLPLADVVTPNIPEAEEITGIKIDTEENIRKAGNI 164
Cdd:PRK08573 83 REIIEAVAKTVSKY-GFPLVVDPVMIAKSGAPLLREDAVDALIKRLLPLATVVTPNRPEAEKLTGMKIRSVEDARKAAKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 165 FINEIGSKGVVIKGGHsADLNNAKDFLFTQDGVYTFEDERFETKHTHGTGCTFSAVITAELAKGRSIYEAVEKAKKFISL 244
Cdd:PRK08573 162 IVEELGAEAVVVKGGH-LEGEEAVDVLYHNGTFREFRAPRVESGCTHGTGCSFSAAIAAGLAKGLDPEEAIKTAKKFITM 240
|
250 260
....*....|....*....|.
gi 516232796 245 SIKYTPEIGKGRGPVNHFAYL 265
Cdd:PRK08573 241 AIKYGVKIGKGHCPVNPMAWI 261
|
|
| PLN02898 |
PLN02898 |
HMP-P kinase/thiamin-monophosphate pyrophosphorylase |
1-267 |
3.96e-81 |
|
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
Pssm-ID: 215486 [Multi-domain] Cd Length: 502 Bit Score: 252.77 E-value: 3.96e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 1 MNKPKIaLTIAGTDPTGGAGVMADLKSFHSCGVYGMASITSIVAQNTLGVQHIHNLETSWVKEQLESIFNDELPHAIKTG 80
Cdd:PLN02898 7 MKVPHV-LTVAGSDSGAGAGIQADIKACAARGVYCTTAITAVTAQNTVGVQGVHAVPLDFVAEQLKSVLSDMPVDVVKTG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 81 MIATEDTMHLVQSYLQQYPEIPYVIDPVMLAKSGDSLMNDETKQKLQDTLLPLADVVTPNIPEAEEITG-IKIDTEENIR 159
Cdd:PLN02898 86 MLPSAEIVKVLCQALKEFPVKALVVDPVMVSTSGDVLAGPSILSALREELLPLATIVTPNVKEASALLGgDPLETVADMR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 160 KAGNIfINEIGSKGVVIKGGHSADLNNAKDFLFTQDGVYTFEDERFETKHTHGTGCTFSAVITAELAKGRSIYEAVEKAK 239
Cdd:PLN02898 166 SAAKE-LHKLGPRYVLVKGGHLPDSLDAVDVLYDGTEFHELRSSRIKTRNTHGTGCTLASCIAAELAKGSDMLSAVKVAK 244
|
250 260 270
....*....|....*....|....*....|.
gi 516232796 240 KFISLSIKYTPEIGKG---RGPVNHFAYLKK 267
Cdd:PLN02898 245 RYVETALEYSKDIGIGngaQGPFNHLFFLKS 275
|
|
| PRK12412 |
PRK12412 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
1-266 |
3.20e-69 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183512 [Multi-domain] Cd Length: 268 Bit Score: 214.83 E-value: 3.20e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 1 MNKpkiALTIAGTDPTGGAGVMADLKSFHSCGVYGMASITSIVAQNTLGvQHIHNL---ETSWVKEQLESIFNDELPHAI 77
Cdd:PRK12412 1 LNK---ALTIAGSDTSGGAGIQADLKTFQELGVYGMTSLTTIVTMDPHN-GWAHNVfpiPASTLKPQLETTIEGVGVDAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 78 KTGMIATEDTMHLVQSYLQQYPEIPYVIDPVMLAKSGDSLMNDETKQKLQDTLLPLADVVTPNIPEAEEITGIKIDTEEN 157
Cdd:PRK12412 77 KTGMLGSVEIIEMVAETIEKHNFKNVVVDPVMVCKGADEALHPETNDCLRDVLVPKALVVTPNLFEAYQLSGVKINSLED 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 158 IRKAGnIFINEIGSKGVVIKGGHSADLNNAKDFLFTQDGVYTFEDERFETKHTHGTGCTFSAVITAELAKGRSIYEAVEK 237
Cdd:PRK12412 157 MKEAA-KKIHALGAKYVLIKGGSKLGTETAIDVLYDGETFDLLESEKIDTTNTHGAGCTYSAAITAELAKGKPVKEAVKT 235
|
250 260
....*....|....*....|....*....
gi 516232796 238 AKKFISLSIKYTPEIGKGRGPVNHFAYLK 266
Cdd:PRK12412 236 AKEFITAAIRYSFKINEYVGPTHHGAYRK 264
|
|
| PRK14713 |
PRK14713 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
8-271 |
2.40e-67 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 237797 [Multi-domain] Cd Length: 530 Bit Score: 217.73 E-value: 2.40e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 8 LTIAGTDPTGGAGVMADLKSFHSCGVYGMASITSIVAQNTLGVQHIHNLETSWVKEQLESIFNDELPHAIKTGMIATEDT 87
Cdd:PRK14713 33 LSIAGTDPSGGAGIQADLKSIAAAGGYGMAVITALVAQNTRGVRAVHVPPADFLRAQLDAVSDDVTVDAVKIGMLGDAEV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 88 MHLVQSYLQQYPEIPYVIDPVMLAKSGDSLMNDETKQKLQDtLLPLADVVTPNIPEAEEITG--IKIDTEENIRKAGNIf 165
Cdd:PRK14713 113 IDAVRTWLAEHRPPVVVLDPVMVATSGDRLLEEDAEAALRE-LVPRADLITPNLPELAVLLGepPATTWEEALAQARRL- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 166 INEIGSKgVVIKGGHSADlNNAKDFLFTQDG-VYTFEDERFETKHTHGTGCTFSAVITAELAKGRSIYEAVEKAKKFISL 244
Cdd:PRK14713 191 AAETGTT-VLVKGGHLDG-QRAPDALVGPDGaVTEVPGPRVDTRNTHGTGCSLSSALATRLGRGGDWAAALRWATAWLHG 268
|
250 260
....*....|....*....|....*....
gi 516232796 245 SIKY--TPEIGKGRGPVNHFAYLKKEGLD 271
Cdd:PRK14713 269 AIAAgaALQVGTGNGPVDHFHRARRLAAD 297
|
|
| PRK09517 |
PRK09517 |
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ... |
4-267 |
1.14e-64 |
|
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; Provisional
Pssm-ID: 169939 [Multi-domain] Cd Length: 755 Bit Score: 215.22 E-value: 1.14e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 4 PKIaLTIAGTDPTGGAGVMADLKSFHSCGVYGMASITSIVAQNTLGVQHIHNLETSWVKEQLESIFNDELPHAIKTGMIA 83
Cdd:PRK09517 242 PRV-LSIAGTDPTGGAGIQADLKSIAAGGGYGMCVVTALVAQNTHGVNTIHTPPLTFLEEQLEAVFSDVTVDAVKLGMLG 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 84 TEDTMHLVQSYLQQYPEIPYVIDPVMLAKSGDSLMNDETKQKLQDtLLPLADVVTPNIPEAEEITGIK-IDTEENIRKAG 162
Cdd:PRK09517 321 SADTVDLVASWLGSHEHGPVVLDPVMVATSGDRLLDADATEALRR-LAVHVDVVTPNIPELAVLCGEApAITMDEAIAQA 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 163 NIFINEIGSKgVVIKGGH--SADLNNAkdfLFTQDG-VYTFEDERFETKHTHGTGCTFSAVITAELAKGRSIYEAVEKAK 239
Cdd:PRK09517 400 RGFARTHGTI-VIVKGGHltGDLADNA---VVRPDGsVHQVENPRVNTTNSHGTGCSLSAALATLIAAGESVEKALEWAT 475
|
250 260 270
....*....|....*....|....*....|
gi 516232796 240 KFISLSIKYTP--EIGKGRGPVNHFAYLKK 267
Cdd:PRK09517 476 RWLNEALRHADhlAVGSGNGPVDHGHLARR 505
|
|
| PTZ00347 |
PTZ00347 |
phosphomethylpyrimidine kinase; Provisional |
3-261 |
4.24e-60 |
|
phosphomethylpyrimidine kinase; Provisional
Pssm-ID: 240375 [Multi-domain] Cd Length: 504 Bit Score: 198.26 E-value: 4.24e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 3 KPKIALTIAGTDPTGGAGVMADLKSFHSCGVYGMASITSIVAQNTLGVQHIHNLETSWVKEQLESIFNDELPHAIKTGMI 82
Cdd:PTZ00347 229 KIPTVLTVSGSDSGGGAGHQADLKTLEALGVYSTSALTSLTAQNTKGVQQIQVVNEDFFAAQIDSVMSDFNISVVKLGLV 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 83 ATEDTMHLVqsyLQQYPEIPYVIDPVMLAKSGDSLMNDETKQKL----QDTLLPLADVVTPNIPEAEEITGIK-IDTEEN 157
Cdd:PTZ00347 309 PTARQLEIV---IEKLKNLPMVVDPVLVATSGDDLVAQKNADDVlamyKERIFPMATIITPNIPEAERILGRKeITGVYE 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 158 IRKAGNIfINEIGSKGVVIKGGHS-ADLNNAKDFLF--TQDGVYTFEDERFETKHTHGTGCTFSAVITAELAKGRSIYEA 234
Cdd:PTZ00347 386 ARAAAQA-LAQYGSRYVLVKGGHDlIDPEACRDVLYdrEKDRFYEFTANRIATINTHGTGCTLASAISSFLARGYTVPDA 464
|
250 260 270
....*....|....*....|....*....|
gi 516232796 235 VEKAKKFISLSI--KYTPEIGKG-RGPVNH 261
Cdd:PTZ00347 465 VERAIGYVHEAIvrSCGVPLGQGtNRPLVH 494
|
|
| PRK12616 |
PRK12616 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
1-263 |
4.59e-59 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183624 Cd Length: 270 Bit Score: 189.10 E-value: 4.59e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 1 MNKpkiALTIAGTDPTGGAGVMADLKSFHSCGVYGMASITSIVA---QNTLGVQhIHNLETSWVKEQLESIFNDELPHAI 77
Cdd:PRK12616 3 MHK---ALTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAmdpENSWDHQ-VFPIDTDTIRAQLSTIVDGIGVDAM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 78 KTGMIATEDTMHLVQSYLQQYPEIPYVIDPVMLAKSGDSLMNDETKQKLQDTLLPLADVVTPNIPEAEEITGI-KIDTEE 156
Cdd:PRK12616 79 KTGMLPTVDIIELAADTIKEKQLKNVVIDPVMVCKGANEVLYPEHAEALREQLAPLATVITPNLFEAGQLSGMgEIKTVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 157 NIRKAGNIfINEIGSKGVVIKGGHSADLNNAKDFLFTQDGVYTFEDERFETKHTHGTGCTFSAVITAELAKGRSIYEAVE 236
Cdd:PRK12616 159 QMKEAAKK-IHELGAQYVVITGGGKLKHEKAVDVLYDGETAEVLESEMIDTPYTHGAGCTFSAAVTAELAKGSEVKEAIY 237
|
250 260
....*....|....*....|....*..
gi 516232796 237 KAKKFISLSIKYTPEIGKGRGPVNHFA 263
Cdd:PRK12616 238 AAKEFITAAIKESFPLNQYVGPTKHSA 264
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
2-253 |
6.40e-47 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 157.15 E-value: 6.40e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 2 NKPKIALTIAGTDPTGGAGVMADLKSFHSCGVYGMASITSIVAQNTLGVQhIHNLETSWVKEQLESIFNDELpHAIKTGM 81
Cdd:PRK12413 1 MKTNYILAISGNDIFSGGGLHADLATYTRNGLHGFVAVTCLTAMTEKGFE-VFPVDKEIFQQQLDSLKDVPF-SAIKIGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 82 IATEDTMHLVQSYLQQYPEIPYVIDPVMLAKSGDSLMNDETKQKLQdTLLPLADVVTPNIPEAEEITGIKIDTEENIRKA 161
Cdd:PRK12413 79 LPNVEIAEQALDFIKGHPGIPVVLDPVLVCKETHDVEVSELRQELI-QFFPYVTVITPNLVEAELLSGKEIKTLEDMKEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 162 GNIFiNEIGSKGVVIKGGHSADLNNAKDFLFTQDGVYTFEDERFETKHThGTGCTFSAVITAELAKGRSIYEAVEKAKKF 241
Cdd:PRK12413 158 AKKL-YDLGAKAVVIKGGNRLSQKKAIDLFYDGKEFVILESPVLEKNNI-GAGCTFASSIASQLVKGKSPLEAVKNSKDF 235
|
250
....*....|..
gi 516232796 242 ISLSIKYTPEIG 253
Cdd:PRK12413 236 VYQAIQQSDQYG 247
|
|
| COG1992 |
COG1992 |
Predicted transcriptional regulator fused phosphomethylpyrimidine kinase (thiamin biosynthesis) ... |
17-268 |
1.22e-38 |
|
Predicted transcriptional regulator fused phosphomethylpyrimidine kinase (thiamin biosynthesis) [General function prediction only];
Pssm-ID: 441595 [Multi-domain] Cd Length: 432 Bit Score: 139.89 E-value: 1.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 17 GGAGVMADLKSFHSCGVYGMASITSIVAQNTLGVQHIHNLETSWVKEQLESIFNDELPHAIKTGMIATEdTMHLVQSYLQ 96
Cdd:COG1992 2 GGGGGGADAKTAAALGAGGGGTTTAVTVTATTTVTGVGSDPPPPVEVQQQAVAADDDVDDAKTGMLMTA-TIVEVVAVVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 97 QYPEIPYVIDPVMLAKSGDSLMNDETKQKLQDTLLPLADVVTPNIPEAEEITGIKIDTEENIRKAGNIFINEIGSKGVVI 176
Cdd:COG1992 81 KSRDKPLVVVVVPVAVAAAGLGLLLAEAELAKLLLPLLATVTPNEPEVEELLLPTIRSLLAEARAARLALQEEGADALGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 177 KGGHSaDLNNAKDFLFTQDGVYTFEDERFETKHTHGTGCTFSAVITAELAKGRSIYEAVEKAKKFISLSIKYTPEIGKGR 256
Cdd:COG1992 161 KGGHV-SGDAVVDVLEDERDVETFRHPRLVTEATHGSGCTFSAAIAALLAKGLSLEEAVRGAKLFLLHAIRYGLLVGKGV 239
|
250
....*....|..
gi 516232796 257 GPVNHFAYLKKE 268
Cdd:COG1992 240 GPVNHLADLRLE 251
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
27-253 |
1.47e-32 |
|
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: 120.25 E-value: 1.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 27 SFHSCGVYGMASITSIV-AQNTLGVQ------------------HIHNLETSWVKEQLESIFN-DELPH--AIKTGMIAT 84
Cdd:COG2240 6 SIQSHVVYGHVGNSAAVpPLSALGVEvwplptvllsnhtgygtfTGRDLPTDDIADILDGWKElGVLLEfdAVLSGYLGS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 85 EDTMHLVQSYLQQY----PEIPYVIDPVMlaksGD--SLMN--DETKQKLQDTLLPLADVVTPNIPEAEEITGIKIDTEE 156
Cdd:COG2240 86 AEQGDIIADFVARVkaanPDALYLCDPVM----GDngKGYYvfPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETLE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 157 NIRKAGNIFINeIGSKGVVIKGGHSADLNNAK--DFLFTQDGVYTFEDERFEtKHTHGTGCTFSAVITAELAKGRSIYEA 234
Cdd:COG2240 162 EALAAARALLA-LGPKIVVVTSVPLDDTPADKigNLAVTADGAWLVETPLLP-FSPNGTGDLFAALLLAHLLRGKSLEEA 239
|
250
....*....|....*....
gi 516232796 235 VEKAKKFISLSIKYTPEIG 253
Cdd:COG2240 240 LERAAAFVYEVLERTAAAG 258
|
|
| PTZ00493 |
PTZ00493 |
phosphomethylpyrimidine kinase; Provisional |
4-262 |
1.13e-27 |
|
phosphomethylpyrimidine kinase; Provisional
Pssm-ID: 240440 Cd Length: 321 Bit Score: 108.54 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 4 PKIaLTIAGTDPTGGAGVMADLKSFHSCGVYGMASITSIVAQNTLGVQHIHNLETSWVKEQLESIFNDELPHAIKTGMIA 83
Cdd:PTZ00493 5 SNI-LSIAGSDSCGGAGMQADIKTAMGLGCHCCTALVVLTAQNTKEVKRIVEIEEKFIVEQLDSIFADVTIDVVKLGVLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 84 TEDTMHLVQSYLQQY-----PEIPYVIDPVMLAKSGDSLM-NDETKQKLQDTLLPLADVVTPNIPEAEEI---------- 147
Cdd:PTZ00493 84 SKKIISLVHNYITNMnkkrgKKLLVVFDPVFVSSSGCLLVeNLEYIKFALDLICPISCIITPNFYECKVIlealdcqmdl 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 148 ---------------------------TGIKIDTEENIRKAGNIFINEIGSkgvvIKGGHSADLnNAKDFLFTQDgVYTF 200
Cdd:PTZ00493 164 skanmtelcklvteklninaclfkscnVGENSAEENEVYAVDHLCIRNVGS----YPTGEKQQI-DAGGVTYLYD-VYKL 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 516232796 201 EDERFETKHTHGTGCTFSAVITAELAKGRSIYEAVEKAKKFISLSIKYTPEIGKGRGPVNHF 262
Cdd:PTZ00493 238 RSKRKPGKDIHGTGCTLSTAIACYLAKKHNILQSCIESKKYIYNCIRYAYPFGSKSQGLNHL 299
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
63-249 |
1.15e-24 |
|
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: 98.81 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 63 EQLESIFND-----ELPH--AIKTGMIATEDTMHLVQSYLQQY----PEIPYVIDPVMlaksGDS----LMNDETKQKLQ 127
Cdd:cd01173 55 EELEDLLEGlealgLLLEydAVLTGYLGSAEQVEAVAEIVKRLkeknPNLLYVCDPVM----GDNgklyVVAEEIVPVYR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 128 DTLLPLADVVTPNIPEAEEITGIKIDTEENIRKAGNIFINEiGSKGVVIKGGHSADLNNAKDFLFTQDGVYTFEDERFET 207
Cdd:cd01173 131 DLLVPLADIITPNQFELELLTGKKINDLEDAKAAARALHAK-GPKTVVVTSVELADDDRIEMLGSTATEAWLVQRPKIPF 209
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 516232796 208 K-HTHGTGCTFSAVITAELAKGRSIYEAVEKAKKFISLSIKYT 249
Cdd:cd01173 210 PaYFNGTGDLFAALLLARLLKGKSLAEALEKALNFVHEVLEAT 252
|
|
| PRK07105 |
PRK07105 |
pyridoxamine kinase; Validated |
75-249 |
4.88e-14 |
|
pyridoxamine kinase; Validated
Pssm-ID: 180840 [Multi-domain] Cd Length: 284 Bit Score: 70.33 E-value: 4.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 75 HAIKTGMIATEDTMHLVQSYLQQY--PEIPYVIDPVMlaksGD-----SLMNDETKQKLQDtLLPLADVVTPNIPEA--- 144
Cdd:PRK07105 77 DAIYSGYLGSPRQIQIVSDFIKYFkkKDLLVVVDPVM----GDngklyQGFDQEMVEEMRK-LIQKADVITPNLTEAcll 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 145 --EEITGIKIDTEE---NIRKagnifINEIGSKGVVIKGGHSADlnnakdflfTQDGVYTF--EDERFeTKHTH------ 211
Cdd:PRK07105 152 ldKPYLEKSYSEEEikqLLRK-----LADLGPKIVIITSVPFED---------GKIGVAYYdrATDRF-WKVFCkyipah 216
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 516232796 212 --GTGCTFSAVITAELAKGRSIYEAVEKAKKFISLSIKYT 249
Cdd:PRK07105 217 ypGTGDIFTSVITGSLLQGDSLPIALDRAVQFIEKGIRAT 256
|
|
| pdxK |
PRK08176 |
pyridoxine/pyridoxal/pyridoxamine kinase; |
76-253 |
1.73e-12 |
|
pyridoxine/pyridoxal/pyridoxamine kinase;
Pssm-ID: 181269 [Multi-domain] Cd Length: 281 Bit Score: 65.83 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 76 AIKTGMIATEDTMHLVQSYLQ----QYPEIPYVIDPVMlaksGD--SLM--NDETKQKLQDTLLPLADVVTPNIPEAEEI 147
Cdd:PRK08176 91 AVTTGYMGSASQIKILAEWLTalraDHPDLLIMVDPVI----GDidSGIyvKPDLPEAYRQHLLPLAQGLTPNIFELEIL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 148 TGIKIDT-EENIRKAGNIFINeiGSKGVVIKGGHSADLN-NAKDFLFTQDGVYTFEDERFETKhTHGTGCTFSAVITAEL 225
Cdd:PRK08176 167 TGKPCRTlDSAIAAAKSLLSD--TLKWVVITSAAGNEENqEMQVVVVTADSVNVISHPRVDTD-LKGTGDLFCAELVSGL 243
|
170 180
....*....|....*....|....*...
gi 516232796 226 AKGRSIYEAVEKAKKFISLSIKYTPEIG 253
Cdd:PRK08176 244 LKGKALTDAAHRAGLRVLEVMRYTQQAG 271
|
|
| PTZ00344 |
PTZ00344 |
pyridoxal kinase; Provisional |
79-254 |
2.44e-12 |
|
pyridoxal kinase; Provisional
Pssm-ID: 240372 [Multi-domain] Cd Length: 296 Bit Score: 65.49 E-value: 2.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 79 TGMIATEDTMH----LVQSYLQQYPEIPYVIDPVMlaksGDslmNDE--TKQKLQDT---LLPLADVVTPNIPEAEEITG 149
Cdd:PTZ00344 83 TGYINSADILRevlaTVKEIKELRPKLIFLCDPVM----GD---DGKlyVKEEVVDAyreLIPYADVITPNQFEASLLSG 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 150 IKIDTEENIRKAGNIFiNEIGSKGVVIKgghSADLNNAKDFL-------FTQDGV---YTFEDERFETKHThGTGCTFSA 219
Cdd:PTZ00344 156 VEVKDLSDALEAIDWF-HEQGIPVVVIT---SFREDEDPTHLrfllscrDKDTKNnkrFTGKVPYIEGRYT-GTGDLFAA 230
|
170 180 190
....*....|....*....|....*....|....*
gi 516232796 220 VITAELAKGrSIYEAVEKAKKFISLSIKYTPEIGK 254
Cdd:PTZ00344 231 LLLAFSHQH-PMDLAVGKAMGVLQDIIKATRESGG 264
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
106-249 |
4.40e-12 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 64.67 E-value: 4.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 106 DPVMLAKSGdslmndETKQKLQDtLLPLADVVTPNIPEAEEITGIKIDTEENIRKAGNIFInEIGSKGVVIK-GGHSADL 184
Cdd:pfam00294 160 DPNLLDPLG------AAREALLE-LLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLL-AKGIKTVIVTlGADGALV 231
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516232796 185 NNAKDFLFtqdgVYTFEDErfETKHTHGTGCTFSAVITAELAKGRSIYEAVEKAKKFISLSIKYT 249
Cdd:pfam00294 232 VEGDGEVH----VPAVPKV--KVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKS 290
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
124-246 |
7.98e-11 |
|
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: 61.03 E-value: 7.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 124 QKLQDTLLPLADVVTPNIPEAEEITGIKIDTEENIRKAGNIFiNEIGSKGVVIK-GGHSAdlnnakdFLFTQDGVYTFED 202
Cdd:cd01174 166 RPLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLL-LAKGVKNVIVTlGAKGA-------LLASGGEVEHVPA 237
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 516232796 203 ERFETKHTHGTGCTFSAVITAELAKGRSIYEAVEKAKKFISLSI 246
Cdd:cd01174 238 FKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSV 281
|
|
| PLN02978 |
PLN02978 |
pyridoxal kinase |
63-238 |
2.32e-10 |
|
pyridoxal kinase
Pssm-ID: 215529 [Multi-domain] Cd Length: 308 Bit Score: 59.75 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 63 EQLESIF-----NDELPHA-IKTGMIATE---DTMHLVQSYLQQY-PEIPYVIDPVMlAKSGDSLMNDETKQKLQDTLLP 132
Cdd:PLN02978 70 EQLWALIegleaNGLLFYThLLTGYIGSVsflRTVLRVVKKLRSVnPNLTYVCDPVL-GDEGKLYVPPELVPVYREKVVP 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 133 LADVVTPNIPEAEEITGIKIDTEENIRKAGNIfINEIGSKGVVIKgghSADLNNAKDFLFTQDGVYTFEDERFETK---- 208
Cdd:PLN02978 149 LATMLTPNQFEAEQLTGIRIVTEEDAREACAI-LHAAGPSKVVIT---SIDIDGKLLLVGSHRKEKGARPEQFKIVipki 224
|
170 180 190
....*....|....*....|....*....|...
gi 516232796 209 --HTHGTGCTFSAVITAELAKG-RSIYEAVEKA 238
Cdd:PLN02978 225 paYFTGTGDLMAALLLGWSHKYpDNLDKAAELA 257
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
102-226 |
2.55e-10 |
|
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).
Pssm-ID: 238177 [Multi-domain] Cd Length: 196 Bit Score: 58.65 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 102 PYVIDPVMLAKSGDslmnDETKQKLqdtlLPLADVVTPNIPEAEEITGIKIDTEENIRKAgNIFINEIGSKGVVIKGGHS 181
Cdd:cd00287 86 PVVLDPGPRAVRLD----GEELEKL----LPGVDILTPNEEEAEALTGRRDLEVKEAAEA-AALLLSKGPKVVIVTLGEK 156
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 516232796 182 ADLnnakdfLFTQDGVY-TFEDERFETKHTHGTGCTFSAVITAELA 226
Cdd:cd00287 157 GAI------VATRGGTEvHVPAFPVKVVDTTGAGDAFLAALAAGLA 196
|
|
| PRK05756 |
PRK05756 |
pyridoxal kinase PdxY; |
99-238 |
7.74e-09 |
|
pyridoxal kinase PdxY;
Pssm-ID: 235592 [Multi-domain] Cd Length: 286 Bit Score: 55.26 E-value: 7.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 99 PEIPYVIDPVMlaksGDSL----MNDETKQKLQDTLLPLADVVTPNIPEAEEITGIKIDTEENIRKAGNIFInEIGSKGV 174
Cdd:PRK05756 104 PQALYFCDPVM----GDPEkgciVAPGVAEFLRDRALPAADIITPNLFELEWLSGRPVETLEDAVAAARALI-ARGPKIV 178
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 516232796 175 VIKGGHSADLNNAK--DFLFTQDGVYTFEDERFETKH-THGTGCTFSAVITAELAKGRSIYEAVEKA 238
Cdd:PRK05756 179 LVTSLARAGYPADRfeMLLVTADGAWHISRPLVDFMRqPVGVGDLTSALFLARLLQGGSLEEALEHT 245
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
101-238 |
9.59e-09 |
|
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: 9.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 101 IPYVIDPvmlakSGDSLMNDETKQKLQDtLLPLADVVTPNIPEAEEITGIKiDTEENIRKagnifINEIGSKGVVIK-GG 179
Cdd:COG0524 159 VPVSLDP-----NYRPALWEPARELLRE-LLALVDILFPNEEEAELLTGET-DPEEAAAA-----LLARGVKLVVVTlGA 226
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 516232796 180 HSAdlnnakdFLFTQDGVYTFEDERFETKHTHGTGCTFSAVITAELAKGRSIYEAVEKA 238
Cdd:COG0524 227 EGA-------LLYTGGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFA 278
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
134-236 |
1.11e-07 |
|
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the lipopolysaccharide (LPS) core precursor ADP-L-glycero-D-manno-heptose. LPS plays an important role in maintaining the structural integrity of the bacterial outer membrane of gram-negative bacteria. RfaE consists of two domains, a sugar kinase domain, represented here, and a domain belonging to the cytidylyltransferase superfamily.
Pssm-ID: 238577 [Multi-domain] Cd Length: 304 Bit Score: 51.79 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 134 ADVVTPNIPEAEEITGIKIDTEENIRKAGNIFINEIGSKGVVIKGGhsadlnnakdflftQDGVYTFEDE----RFETKH 209
Cdd:cd01172 182 ATLLTPNEKEAREALGDEINDDDELEAAGEKLLELLNLEALLVTLG--------------EEGMTLFERDgevqHIPALA 247
|
90 100 110
....*....|....*....|....*....|..
gi 516232796 210 TH-----GTGCTFSAVITAELAKGRSIYEAVE 236
Cdd:cd01172 248 KEvydvtGAGDTVIATLALALAAGADLEEAAF 279
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
124-174 |
2.63e-07 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 50.64 E-value: 2.63e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 516232796 124 QKLQDTLLPLADVVTPNIPEAEEITGIKIDTEENIRKAGNIF--------INEIGSKGV 174
Cdd:PRK11142 169 RELPDELLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLhqkgietvLITLGSRGV 227
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
125-238 |
3.16e-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: 41.53 E-value: 3.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 125 KLQDTLLPLA--DVVTPNIPEAEEITGIKIDTEENIRKAGNIFInEIGSKGVVIKGGhsadlnnakdflftQDGVYTFED 202
Cdd:cd01941 166 KLKKLFYLLHaiDLLTPNRAELEALAGALIENNEDENKAAKILL-LPGIKNVIVTLG--------------AKGVLLSSR 230
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 516232796 203 ERFETKHTH------------GTGCTFSAVITAELAKGRSIYEAVEKA 238
Cdd:cd01941 231 EGGVETKLFpapqpetvvnvtGAGDAFVAGLVAGLLEGMSLDDSLRFA 278
|
|
| Carb_kinase |
pfam01256 |
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ... |
7-235 |
1.17e-03 |
|
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also is a carbohydrate kinase. (personal obs Yeats C).
Pssm-ID: 396007 Cd Length: 242 Bit Score: 39.27 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 7 ALTIAGTDPTGGAGVMADLKSFHScGVyGMASITSIVAQNTLGVQHIHNLETSWVKEQLESIFNDELPHA--IKTGMIAT 84
Cdd:pfam01256 1 VLVIGGSKDYTGAPLLAALAALRS-GA-GLVSVATDSEAIAVLKSPLPEVMVHPLPETSSILEKLSRYDAvvIGPGLGRD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 85 EDTMHLVQSYLQQYpeIPYVIDpvmlaksGDSLmndetKQKLQDTLLPL---ADVVTPNIPEAEEITGIKIDTEENIRKA 161
Cdd:pfam01256 79 EKGKAALEEVLAKD--CPLVID-------ADAL-----NLLAINNEKPAregPTVLTPHPGEFERLCGLAGILGDDRLEA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 516232796 162 GNIFINEIGSKgVVIKGGHsadlnnakDFLFTQDG-VYTFEDERfETKHTHGTGCTFSAVITAELAKGRSIYEAV 235
Cdd:pfam01256 145 ARELAQKLNGT-ILLKGNV--------TVIAAPGGeVWINSTGN-SALAKGGSGDVLAGLIGGLLAQNEDPYDAA 209
|
|
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
10-238 |
1.93e-03 |
|
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of the ATP binding site, the substrate binding site and the Mg2+binding site and structural homology this group is a member of the ribokinase-like superfamily.
Pssm-ID: 238576 Cd Length: 254 Bit Score: 38.75 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 10 IAGTDPTGGAGVMAdLKSFHSCGVyGMASI-------TSIVAQNT-LGVQHIHNLETSWVKEQLESIfndelpHA--IKT 79
Cdd:cd01171 14 IGGSRGYTGAAYLA-ALAALRAGA-GLVTVatppeaaAVIKSYSPeLMVHPLLETDIEELLELLERA------DAvvIGP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 80 GMIATEDTMHLVQSYLQQypEIPYVIDpvmlaksGDSLMNDETKQKLQdtLLPLADVVTPNIPEAEEITGIKIDTEENIR 159
Cdd:cd01171 86 GLGRDEEAAEILEKALAK--DKPLVLD-------ADALNLLADEPSLI--KRYGPVVLTPHPGEFARLLGALVEEIQADR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 516232796 160 KAGNIFINEIGSKGVVIKGghsadlnnAKDFLFTQDGVYTFEDERFETKHTHGTGCTFSAVITAELAKGRSIYEAVEKA 238
Cdd:cd01171 155 LAAAREAAAKLGATVVLKG--------AVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALA 225
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
130-246 |
6.02e-03 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 37.41 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 516232796 130 LLPLADVVTPNIPEAEEITGIKIDTEENIRKAGNIFINeIGSKGVVIKGGhsadlnnAKDFLFTQDG---VYTfEDERFE 206
Cdd:PTZ00292 195 FLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQ-LGVENVIITLG-------ANGCLIVEKEnepVHV-PGKRVK 265
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 516232796 207 TKHTHGTGCTFSAVITAELAKGRSIYEAVEKAKKFISLSI 246
Cdd:PTZ00292 266 AVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISV 305
|
|
| |
