|
Name |
Accession |
Description |
Interval |
E-value |
| HMPP_kinase |
cd01169 |
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ... |
6-245 |
2.14e-93 |
|
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two consecutive phosphorylation steps in the thiamine phosphate biosynthesis pathway, leading to the synthesis of vitamin B1. The first step is the phosphorylation of the hydroxyl group of HMP to form 4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate (HMP-P) and then the phophorylation of HMP-P to form 4-amino-5-hydroxymethyl-2-methyl-pyrimidine pyrophosphate (HMP-PP), which is the substrate for the thiamine synthase coupling reaction.
Pssm-ID: 238574 [Multi-domain] Cd Length: 242 Bit Score: 282.86 E-value: 2.14e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 6 IVWSIGGSDCSGGAGCQADILTCRDFNVHAASIITTITAQNAEQVLKINYCDSDLIQKQIQALKETLPPTVIKLGLLGTK 85
Cdd:cd01169 1 VVLTIAGSDSSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVFGVHPVPPEFVAAQLDAVLEDIPVDAIKIGMLGSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 86 EIVTAVASYLKNYS-GKVVCDPVLNSTSGVLLHASDYLDLLKKLLFPHVDLLTPNIPEAEILIQNKIHTFSDIISAAHQL 164
Cdd:cd01169 81 EIIEAVAEALKDYPdIPVVLDPVMVAKSGDSLLDDDAIEALRELLLPLATLITPNLPEAELLTGLEIATEEDMMKAAKAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 165 LKCGVSAVLLKGGHLIGSKARDFFTDGKCEFWLAHTKIPKTRVRGTGCALSSAISSAIALGYSLKDAIVVAKMYVQQGIR 244
Cdd:cd01169 161 LALGAKAVLIKGGHLPGDEAVDVLYDGGGFFEFESPRIDTKNTHGTGCTLSSAIAANLAKGLSLEEAVREAKEYVTQAIR 240
|
.
gi 500791842 245 Q 245
Cdd:cd01169 241 N 241
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
8-250 |
1.17e-89 |
|
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: 273.84 E-value: 1.17e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 8 WSIGGSDCSGGAGCQADILTCRDFNVHAASIITTITAQNAEQVLKINYCDSDLIQKQIQALKETLPPTVIKLGLLGTKEI 87
Cdd:COG0351 1 LTIAGSDPSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVTGVHPVPPEFVAAQLRAVLEDIPVDAIKIGMLGSAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 88 VTAVASYLKNYSGK-VVCDPVLNSTSGVLLHASDYLDLLKKLLFPHVDLLTPNIPEAEILIQNKIHTFSDIISAAHQLLK 166
Cdd:COG0351 81 IEAVAEILADYPLVpVVLDPVMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALLGIEITTLDDMREAAKALLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 167 CGVSAVLLKGGHLIGSKARDFFTDGKCEFWLAHTKIPKTRVRGTGCALSSAISSAIALGYSLKDAIVVAKMYVQQGIRQN 246
Cdd:COG0351 161 LGAKAVLVKGGHLPGDEAVDVLYDGDGVREFSAPRIDTGNTHGTGCTLSSAIAALLAKGLDLEEAVREAKEYVTQAIRAA 240
|
....
gi 500791842 247 FKVN 250
Cdd:COG0351 241 LRLG 244
|
|
| PRK03512 |
PRK03512 |
thiamine phosphate synthase; |
288-479 |
2.32e-87 |
|
thiamine phosphate synthase;
Pssm-ID: 179586 Cd Length: 211 Bit Score: 266.53 E-value: 2.32e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 288 GFYPIVDSVEWVERLLSYGVRTIQLRIKNASPQKIKKAVIESVALARHYQAKLFINDYWKLAIEAGAYGVHLGQEDLETA 367
Cdd:PRK03512 14 GLYPVVDSVQWIERLLDAGVRTLQLRIKDRRDEEVEADVVAAIALGRRYQARLFINDYWRLAIKHQAYGVHLGQEDLETA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 368 DLSAIRAANLRLGISTHTLYELSRAHAIQPSYVAFGPIYETYSKPMPYSARGLEWLRYWCEISP-YPVVAIGGINLNRLE 446
Cdd:PRK03512 94 DLNAIRAAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLAQLARHVERLAdYPTVAIGGISLERAP 173
|
170 180 190
....*....|....*....|....*....|...
gi 500791842 447 SVLNAGAVNVAVISAVTKSKTPQKTVRAFLNRI 479
Cdd:PRK03512 174 AVLATGVGSIAVVSAITQAADWRAATAQLLELA 206
|
|
| PLN02898 |
PLN02898 |
HMP-P kinase/thiamin-monophosphate pyrophosphorylase |
7-476 |
2.25e-81 |
|
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
Pssm-ID: 215486 [Multi-domain] Cd Length: 502 Bit Score: 260.86 E-value: 2.25e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 7 VWSIGGSDCSGGAGCQADILTCRDFNVHAASIITTITAQNAEQVLKINYCDSDLIQKQIQALKETLPPTVIKLGLLGTKE 86
Cdd:PLN02898 12 VLTVAGSDSGAGAGIQADIKACAARGVYCTTAITAVTAQNTVGVQGVHAVPLDFVAEQLKSVLSDMPVDVVKTGMLPSAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 87 IVTAVASYLKNYSGK-VVCDPVLNSTSGVLLHASDYLDLLKKLLFPHVDLLTPNIPEAEILIQNK-IHTFSDIISAAHQL 164
Cdd:PLN02898 92 IVKVLCQALKEFPVKaLVVDPVMVSTSGDVLAGPSILSALREELLPLATIVTPNVKEASALLGGDpLETVADMRSAAKEL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 165 LKCGVSAVLLKGGHLIGS-KARDFFTDGKCEFWLAHTKIpKTR-VRGTGCALSSAISSAIALGYSLKDAIVVAKMYVQQG 242
Cdd:PLN02898 172 HKLGPRYVLVKGGHLPDSlDAVDVLYDGTEFHELRSSRI-KTRnTHGTGCTLASCIAAELAKGSDMLSAVKVAKRYVETA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 243 IRQN--FKVNTqelmGRQG----FPRRSIDLPWVTKNANFKRKSFPLcnsfgfYPIVDS----------VEWVERLLSYG 306
Cdd:PLN02898 251 LEYSkdIGIGN----GAQGpfnhLFFLKSWAKKSSRQSRFNPRNLFL------YAVTDSgmnkkwgrstVDAVRAAIEGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 307 VRTIQLRIKNASPQKIKKAVIESVALARHYQAKLFINDYWKLAIEAGAYGVHLGQEDLETADLSAIRAANLRLGISTHTL 386
Cdd:PLN02898 321 ATIVQLREKEAETREFIEEAKACLAICRSYGVPLLINDRVDVALACDADGVHLGQSDMPVRLARSLLGPGKIIGVSCKTP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 387 YELSRAHAIQPSYVAFGPIYETYSKPmPYSARGLEWLRYWCEISPYPVVAIGGINLNRLESVLNAGAVN---VAVISAVT 463
Cdd:PLN02898 401 EQAEQAWKDGADYIGCGGVFPTNTKA-NNKTIGLDGLREVCEASKLPVVAIGGISASNAASVMESGAPNlkgVAVVSALF 479
|
490
....*....|...
gi 500791842 464 KSKTPQKTVRAFL 476
Cdd:PLN02898 480 DQEDVLKATRKLH 492
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
14-250 |
2.04e-79 |
|
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: 247.39 E-value: 2.04e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 14 DCSGGAGCQADILTCRDFNVHAASIITTITAQNAEQVLKINYCDSDLIQKQIQALKETLPPTVIKLGLLGTKEIVTAVAS 93
Cdd:pfam08543 1 DSSGGAGIQADLKTFSALGVYGMSVITALTAQNTLGVQGVHPLPPEFVAAQLDAVLEDIPVDAVKTGMLGSAEIIEAVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 94 YLKNYSGKVVCDPVLNSTSGVLLHASDYLDLLKKLLFPHVDLLTPNIPEAEILIQNKIHTFSDIISAAHQLLKCGVSAVL 173
Cdd:pfam08543 81 KLDKYGVPVVLDPVMVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500791842 174 LKGGHLIG--SKARDFFTDGKCEFWLAHTKIPKTRVRGTGCALSSAISSAIALGYSLKDAIVVAKMYVQQGIRQNFKVN 250
Cdd:pfam08543 161 IKGGHLEGeeAVVTDVLYDGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKEYVTEAIRDALNLG 239
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
289-476 |
8.13e-78 |
|
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole phosphate to yield thiamine phosphate. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions.
Pssm-ID: 238317 [Multi-domain] Cd Length: 196 Bit Score: 241.27 E-value: 8.13e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 289 FYPIVDS-------VEWVERLLSYGVRTIQLRIKNASPQKIKKAVIESVALARHYQAKLFINDYWKLAIEAGAYGVHLGQ 361
Cdd:cd00564 1 LYLITDRrldgedlLEVVEAALKGGVTLVQLREKDLSARELLELARALRELCRKYGVPLIINDRVDLALAVGADGVHLGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 362 EDLETADLSAIRAANLRLGISTHTLYELSRAHAIQPSYVAFGPIYETYSKPMPYSARGLEWLRYWCEISPYPVVAIGGIN 441
Cdd:cd00564 81 DDLPVAEARALLGPDLIIGVSTHSLEEALRAEELGADYVGFGPVFPTPTKPGAGPPLGLELLREIAELVEIPVVAIGGIT 160
|
170 180 190
....*....|....*....|....*....|....*
gi 500791842 442 LNRLESVLNAGAVNVAVISAVTKSKTPQKTVRAFL 476
Cdd:cd00564 161 PENAAEVLAAGADGVAVISAITGADDPAAAARELL 195
|
|
| ThiE |
COG0352 |
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
285-479 |
9.93e-78 |
|
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate synthase is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 440121 [Multi-domain] Cd Length: 206 Bit Score: 241.24 E-value: 9.93e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 285 NSFGFYPIVDS-------VEWVERLLSYGVRTIQLRIKNASPQKIKKAVIESVALARHYQAKLFINDYWKLAIEAGAYGV 357
Cdd:COG0352 2 TLPRLYLITDPdlcgrdlLEVLEAALAGGVDLVQLREKDLDERELLALARALRALCRAYGVPLIINDRVDLALALGADGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 358 HLGQEDLETADLSAIRAANLRLGISTHTLYELSRAHAIQPSYVAFGPIYETYSKPMPYSARGLEWLRYWCEISPYPVVAI 437
Cdd:COG0352 82 HLGQEDLPVAEARALLGPDLIIGVSCHSLEEALRAEEAGADYVGFGPVFPTPTKPGAPPPLGLEGLAWWAELVEIPVVAI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 500791842 438 GGINLNRLESVLNAGAVNVAVISAVTKSKTPQKTVRAFLNRI 479
Cdd:COG0352 162 GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAAL 203
|
|
| TMP-TENI |
pfam02581 |
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ... |
289-462 |
4.55e-69 |
|
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl)thiazole phosphate to yield thiamine phosphate. This Pfam family also includes the regulatory protein TENI, a protein from Bacillus subtilis that regulates the production of several extracellular enzymes by reducing alkaline protease production. While TenI shows high sequence similarity with thiamin phosphate synthase, the purified protein has no thiamin phosphate synthase activity. Instead, it is a thiazole tautomerase.
Pssm-ID: 426849 [Multi-domain] Cd Length: 180 Bit Score: 218.19 E-value: 4.55e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 289 FYPIVDS-------VEWVERLLSYGVRTIQLRIKNASPQKIKKAVIESVALARHYQAKLFINDYWKLAIEAGAYGVHLGQ 361
Cdd:pfam02581 1 LYLVTDPgldgedlLEVVEEALKGGVTIVQLREKELDDREFLELAKELRALCRKYGVPLIINDRVDLALAVGADGVHLGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 362 EDLETADLSAIRAANLRLGISTHTLYELSRAHAIQPSYVAFGPIYETYSKPMPySARGLEWLRYWCEISPYPVVAIGGIN 441
Cdd:pfam02581 81 DDLPVAEARELLGPDLIIGVSTHTLEEALEAEALGADYIGFGPIFPTPTKPDA-PPLGLEGLKAIAEAVEIPVVAIGGIT 159
|
170 180
....*....|....*....|.
gi 500791842 442 LNRLESVLNAGAVNVAVISAV 462
Cdd:pfam02581 160 PENVPEVIEAGADGVAVVSAI 180
|
|
| HMP-P_kinase |
TIGR00097 |
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ... |
7-249 |
7.66e-66 |
|
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: 212.54 E-value: 7.66e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 7 VWSIGGSDCSGGAGCQADILTCRDFNVHAASIITTITAQNAEQVLKINYCDSDLIQKQIQALKETLPPTVIKLGLLGTKE 86
Cdd:TIGR00097 1 ALTIAGSDSGGGAGIQADLKTFSALGVFGTSVITALTAQNTRGVTGVYPIPPDFVEAQLDAVFSDIPVDAAKTGMLASAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 87 IVTAVASYLKNYS-GKVVCDPVLNSTSGVLLHASDYLDLLKKLLFPHVDLLTPNIPEAEILIQNKIHTFSDIISAAHQLL 165
Cdd:TIGR00097 81 IVEAVARKLREYPvRPLVVDPVMVAKSGAPLLEEEAIEALRKRLLPLATLITPNLPEAEALLGTKIRTEQDMIKAAKKLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 166 KCGVSAVLLKGGHLIGSKARDFFTDGKCEFWLAHTKIPKTRVRGTGCALSSAISSAIALGYSLKDAIVVAKMYVQQGIRQ 245
Cdd:TIGR00097 161 ELGPKAVLIKGGHLEGDQAVDVLFDGGEIHILKAPRIETKNTHGTGCTLSAAIAANLAKGLSLKEAVKEAKEFVTGAIRY 240
|
....
gi 500791842 246 NFKV 249
Cdd:TIGR00097 241 GLNI 244
|
|
| thiE |
TIGR00693 |
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ... |
288-475 |
9.49e-61 |
|
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate pyrophosphorylase, ThiE, of a number of bacteria, and N-terminal domains of bifunctional thiamine proteins of Saccharomyces cerevisiae and Schizosaccharomyces pombe, in which the C-terminal domain corresponds to the bacterial hydroxyethylthiazole kinase (EC 2.7.1.50), ThiM. This model includes ThiE from Bacillus subtilis but excludes its paralog, the regulatory protein TenI (SP:P25053), and neighbors of TenI. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
Pssm-ID: 273222 [Multi-domain] Cd Length: 196 Bit Score: 197.09 E-value: 9.49e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 288 GFYPIVDS-------VEWVERLLSYGVRTIQLRIKNASPQKIKKAVIESVALARHYQAKLFINDYWKLAIEAGAYGVHLG 360
Cdd:TIGR00693 1 GLYLITDPqdgpadlLNRVEAALKGGVTLVQLRDKGSNTRERLALAEKLQELCRRYGVPFIVNDRVDLALALGADGVHLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 361 QEDLETADLSAIRAANLRLGISTHTLYELSRAHAIQPSYVAFGPIYETYSKPMPYSARGLEWLRYWCEISP-YPVVAIGG 439
Cdd:TIGR00693 81 QDDLPASEARALLGPDKIIGVSTHNLEELAEAEAEGADYIGFGPIFPTPTKKDPAPPAGVELLREIAATLIdIPIVAIGG 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 500791842 440 INLNRLESVLNAGAVNVAVISAVTKSKTPQKTVRAF 475
Cdd:TIGR00693 161 ITLENAAEVLAAGADGVAVVSAIMQAADPKAAAKRL 196
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HMPP_kinase |
cd01169 |
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ... |
6-245 |
2.14e-93 |
|
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two consecutive phosphorylation steps in the thiamine phosphate biosynthesis pathway, leading to the synthesis of vitamin B1. The first step is the phosphorylation of the hydroxyl group of HMP to form 4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate (HMP-P) and then the phophorylation of HMP-P to form 4-amino-5-hydroxymethyl-2-methyl-pyrimidine pyrophosphate (HMP-PP), which is the substrate for the thiamine synthase coupling reaction.
Pssm-ID: 238574 [Multi-domain] Cd Length: 242 Bit Score: 282.86 E-value: 2.14e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 6 IVWSIGGSDCSGGAGCQADILTCRDFNVHAASIITTITAQNAEQVLKINYCDSDLIQKQIQALKETLPPTVIKLGLLGTK 85
Cdd:cd01169 1 VVLTIAGSDSSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVFGVHPVPPEFVAAQLDAVLEDIPVDAIKIGMLGSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 86 EIVTAVASYLKNYS-GKVVCDPVLNSTSGVLLHASDYLDLLKKLLFPHVDLLTPNIPEAEILIQNKIHTFSDIISAAHQL 164
Cdd:cd01169 81 EIIEAVAEALKDYPdIPVVLDPVMVAKSGDSLLDDDAIEALRELLLPLATLITPNLPEAELLTGLEIATEEDMMKAAKAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 165 LKCGVSAVLLKGGHLIGSKARDFFTDGKCEFWLAHTKIPKTRVRGTGCALSSAISSAIALGYSLKDAIVVAKMYVQQGIR 244
Cdd:cd01169 161 LALGAKAVLIKGGHLPGDEAVDVLYDGGGFFEFESPRIDTKNTHGTGCTLSSAIAANLAKGLSLEEAVREAKEYVTQAIR 240
|
.
gi 500791842 245 Q 245
Cdd:cd01169 241 N 241
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
8-250 |
1.17e-89 |
|
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: 273.84 E-value: 1.17e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 8 WSIGGSDCSGGAGCQADILTCRDFNVHAASIITTITAQNAEQVLKINYCDSDLIQKQIQALKETLPPTVIKLGLLGTKEI 87
Cdd:COG0351 1 LTIAGSDPSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVTGVHPVPPEFVAAQLRAVLEDIPVDAIKIGMLGSAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 88 VTAVASYLKNYSGK-VVCDPVLNSTSGVLLHASDYLDLLKKLLFPHVDLLTPNIPEAEILIQNKIHTFSDIISAAHQLLK 166
Cdd:COG0351 81 IEAVAEILADYPLVpVVLDPVMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALLGIEITTLDDMREAAKALLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 167 CGVSAVLLKGGHLIGSKARDFFTDGKCEFWLAHTKIPKTRVRGTGCALSSAISSAIALGYSLKDAIVVAKMYVQQGIRQN 246
Cdd:COG0351 161 LGAKAVLVKGGHLPGDEAVDVLYDGDGVREFSAPRIDTGNTHGTGCTLSSAIAALLAKGLDLEEAVREAKEYVTQAIRAA 240
|
....
gi 500791842 247 FKVN 250
Cdd:COG0351 241 LRLG 244
|
|
| PRK03512 |
PRK03512 |
thiamine phosphate synthase; |
288-479 |
2.32e-87 |
|
thiamine phosphate synthase;
Pssm-ID: 179586 Cd Length: 211 Bit Score: 266.53 E-value: 2.32e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 288 GFYPIVDSVEWVERLLSYGVRTIQLRIKNASPQKIKKAVIESVALARHYQAKLFINDYWKLAIEAGAYGVHLGQEDLETA 367
Cdd:PRK03512 14 GLYPVVDSVQWIERLLDAGVRTLQLRIKDRRDEEVEADVVAAIALGRRYQARLFINDYWRLAIKHQAYGVHLGQEDLETA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 368 DLSAIRAANLRLGISTHTLYELSRAHAIQPSYVAFGPIYETYSKPMPYSARGLEWLRYWCEISP-YPVVAIGGINLNRLE 446
Cdd:PRK03512 94 DLNAIRAAGLRLGVSTHDDMEIDVALAARPSYIALGHVFPTQTKQMPSAPQGLAQLARHVERLAdYPTVAIGGISLERAP 173
|
170 180 190
....*....|....*....|....*....|...
gi 500791842 447 SVLNAGAVNVAVISAVTKSKTPQKTVRAFLNRI 479
Cdd:PRK03512 174 AVLATGVGSIAVVSAITQAADWRAATAQLLELA 206
|
|
| PLN02898 |
PLN02898 |
HMP-P kinase/thiamin-monophosphate pyrophosphorylase |
7-476 |
2.25e-81 |
|
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
Pssm-ID: 215486 [Multi-domain] Cd Length: 502 Bit Score: 260.86 E-value: 2.25e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 7 VWSIGGSDCSGGAGCQADILTCRDFNVHAASIITTITAQNAEQVLKINYCDSDLIQKQIQALKETLPPTVIKLGLLGTKE 86
Cdd:PLN02898 12 VLTVAGSDSGAGAGIQADIKACAARGVYCTTAITAVTAQNTVGVQGVHAVPLDFVAEQLKSVLSDMPVDVVKTGMLPSAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 87 IVTAVASYLKNYSGK-VVCDPVLNSTSGVLLHASDYLDLLKKLLFPHVDLLTPNIPEAEILIQNK-IHTFSDIISAAHQL 164
Cdd:PLN02898 92 IVKVLCQALKEFPVKaLVVDPVMVSTSGDVLAGPSILSALREELLPLATIVTPNVKEASALLGGDpLETVADMRSAAKEL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 165 LKCGVSAVLLKGGHLIGS-KARDFFTDGKCEFWLAHTKIpKTR-VRGTGCALSSAISSAIALGYSLKDAIVVAKMYVQQG 242
Cdd:PLN02898 172 HKLGPRYVLVKGGHLPDSlDAVDVLYDGTEFHELRSSRI-KTRnTHGTGCTLASCIAAELAKGSDMLSAVKVAKRYVETA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 243 IRQN--FKVNTqelmGRQG----FPRRSIDLPWVTKNANFKRKSFPLcnsfgfYPIVDS----------VEWVERLLSYG 306
Cdd:PLN02898 251 LEYSkdIGIGN----GAQGpfnhLFFLKSWAKKSSRQSRFNPRNLFL------YAVTDSgmnkkwgrstVDAVRAAIEGG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 307 VRTIQLRIKNASPQKIKKAVIESVALARHYQAKLFINDYWKLAIEAGAYGVHLGQEDLETADLSAIRAANLRLGISTHTL 386
Cdd:PLN02898 321 ATIVQLREKEAETREFIEEAKACLAICRSYGVPLLINDRVDVALACDADGVHLGQSDMPVRLARSLLGPGKIIGVSCKTP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 387 YELSRAHAIQPSYVAFGPIYETYSKPmPYSARGLEWLRYWCEISPYPVVAIGGINLNRLESVLNAGAVN---VAVISAVT 463
Cdd:PLN02898 401 EQAEQAWKDGADYIGCGGVFPTNTKA-NNKTIGLDGLREVCEASKLPVVAIGGISASNAASVMESGAPNlkgVAVVSALF 479
|
490
....*....|...
gi 500791842 464 KSKTPQKTVRAFL 476
Cdd:PLN02898 480 DQEDVLKATRKLH 492
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
14-250 |
2.04e-79 |
|
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: 247.39 E-value: 2.04e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 14 DCSGGAGCQADILTCRDFNVHAASIITTITAQNAEQVLKINYCDSDLIQKQIQALKETLPPTVIKLGLLGTKEIVTAVAS 93
Cdd:pfam08543 1 DSSGGAGIQADLKTFSALGVYGMSVITALTAQNTLGVQGVHPLPPEFVAAQLDAVLEDIPVDAVKTGMLGSAEIIEAVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 94 YLKNYSGKVVCDPVLNSTSGVLLHASDYLDLLKKLLFPHVDLLTPNIPEAEILIQNKIHTFSDIISAAHQLLKCGVSAVL 173
Cdd:pfam08543 81 KLDKYGVPVVLDPVMVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 500791842 174 LKGGHLIG--SKARDFFTDGKCEFWLAHTKIPKTRVRGTGCALSSAISSAIALGYSLKDAIVVAKMYVQQGIRQNFKVN 250
Cdd:pfam08543 161 IKGGHLEGeeAVVTDVLYDGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKEYVTEAIRDALNLG 239
|
|
| TMP_TenI |
cd00564 |
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ... |
289-476 |
8.13e-78 |
|
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole phosphate to yield thiamine phosphate. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions.
Pssm-ID: 238317 [Multi-domain] Cd Length: 196 Bit Score: 241.27 E-value: 8.13e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 289 FYPIVDS-------VEWVERLLSYGVRTIQLRIKNASPQKIKKAVIESVALARHYQAKLFINDYWKLAIEAGAYGVHLGQ 361
Cdd:cd00564 1 LYLITDRrldgedlLEVVEAALKGGVTLVQLREKDLSARELLELARALRELCRKYGVPLIINDRVDLALAVGADGVHLGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 362 EDLETADLSAIRAANLRLGISTHTLYELSRAHAIQPSYVAFGPIYETYSKPMPYSARGLEWLRYWCEISPYPVVAIGGIN 441
Cdd:cd00564 81 DDLPVAEARALLGPDLIIGVSTHSLEEALRAEELGADYVGFGPVFPTPTKPGAGPPLGLELLREIAELVEIPVVAIGGIT 160
|
170 180 190
....*....|....*....|....*....|....*
gi 500791842 442 LNRLESVLNAGAVNVAVISAVTKSKTPQKTVRAFL 476
Cdd:cd00564 161 PENAAEVLAAGADGVAVISAITGADDPAAAARELL 195
|
|
| ThiE |
COG0352 |
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ... |
285-479 |
9.93e-78 |
|
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate synthase is part of the Pathway/BioSystem: Thiamine biosynthesis
Pssm-ID: 440121 [Multi-domain] Cd Length: 206 Bit Score: 241.24 E-value: 9.93e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 285 NSFGFYPIVDS-------VEWVERLLSYGVRTIQLRIKNASPQKIKKAVIESVALARHYQAKLFINDYWKLAIEAGAYGV 357
Cdd:COG0352 2 TLPRLYLITDPdlcgrdlLEVLEAALAGGVDLVQLREKDLDERELLALARALRALCRAYGVPLIINDRVDLALALGADGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 358 HLGQEDLETADLSAIRAANLRLGISTHTLYELSRAHAIQPSYVAFGPIYETYSKPMPYSARGLEWLRYWCEISPYPVVAI 437
Cdd:COG0352 82 HLGQEDLPVAEARALLGPDLIIGVSCHSLEEALRAEEAGADYVGFGPVFPTPTKPGAPPPLGLEGLAWWAELVEIPVVAI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 500791842 438 GGINLNRLESVLNAGAVNVAVISAVTKSKTPQKTVRAFLNRI 479
Cdd:COG0352 162 GGITPENAAEVLAAGADGVAVISAIWGAPDPAAAARELRAAL 203
|
|
| thiE |
PRK12290 |
thiamine phosphate synthase; |
220-475 |
2.05e-74 |
|
thiamine phosphate synthase;
Pssm-ID: 237041 [Multi-domain] Cd Length: 437 Bit Score: 240.85 E-value: 2.05e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 220 SAIALGYSLKDAIVVAKMYVQQGirQNFKVNTQElMGRQGFPR-----RSID-LPWVTKNAnfKRKSFPLCN--SFGFYP 291
Cdd:PRK12290 141 TLLALDFPIEDALTLARAMLTQG--DNVSRETWP-TQFELFPTpvlndRRLDiQVGWSKEG--ATRAFPTLDkqSLGLYP 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 292 IVDSVEWVERLLSYGVRTIQLRIKNASPQKIKKAVIESVALARHYQAKLFINDYWKLAIEAGAYGVHLGQEDLETADLSA 371
Cdd:PRK12290 216 VVDDVEWIERLLPLGINTVQLRIKDPQQADLEQQIIRAIALGREYNAQVFINDYWQLAIKHQAYGVHLGQEDLEEANLAQ 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 372 IRAANLRLGISTHTLYELSRAHAIQPSYVAFGPIYETYSKPMPYSARGLEWLRYW---------CEISPYPVVAIGGINL 442
Cdd:PRK12290 296 LTDAGIRLGLSTHGYYELLRIVQIQPSYIALGHIFPTTTKQMPSKPQGLVRLALYqklidtipyQGQTGFPTVAIGGIDQ 375
|
250 260 270
....*....|....*....|....*....|...
gi 500791842 443 NRLESVLNAGAVNVAVISAVTKSKTPQKTVRAF 475
Cdd:PRK12290 376 SNAEQVWQCGVSSLAVVRAITLAEDPQLVIEFF 408
|
|
| TMP-TENI |
pfam02581 |
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ... |
289-462 |
4.55e-69 |
|
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl)thiazole phosphate to yield thiamine phosphate. This Pfam family also includes the regulatory protein TENI, a protein from Bacillus subtilis that regulates the production of several extracellular enzymes by reducing alkaline protease production. While TenI shows high sequence similarity with thiamin phosphate synthase, the purified protein has no thiamin phosphate synthase activity. Instead, it is a thiazole tautomerase.
Pssm-ID: 426849 [Multi-domain] Cd Length: 180 Bit Score: 218.19 E-value: 4.55e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 289 FYPIVDS-------VEWVERLLSYGVRTIQLRIKNASPQKIKKAVIESVALARHYQAKLFINDYWKLAIEAGAYGVHLGQ 361
Cdd:pfam02581 1 LYLVTDPgldgedlLEVVEEALKGGVTIVQLREKELDDREFLELAKELRALCRKYGVPLIINDRVDLALAVGADGVHLGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 362 EDLETADLSAIRAANLRLGISTHTLYELSRAHAIQPSYVAFGPIYETYSKPMPySARGLEWLRYWCEISPYPVVAIGGIN 441
Cdd:pfam02581 81 DDLPVAEARELLGPDLIIGVSTHTLEEALEAEALGADYIGFGPIFPTPTKPDA-PPLGLEGLKAIAEAVEIPVVAIGGIT 159
|
170 180
....*....|....*....|.
gi 500791842 442 LNRLESVLNAGAVNVAVISAV 462
Cdd:pfam02581 160 PENVPEVIEAGADGVAVVSAI 180
|
|
| HMP-P_kinase |
TIGR00097 |
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ... |
7-249 |
7.66e-66 |
|
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: 212.54 E-value: 7.66e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 7 VWSIGGSDCSGGAGCQADILTCRDFNVHAASIITTITAQNAEQVLKINYCDSDLIQKQIQALKETLPPTVIKLGLLGTKE 86
Cdd:TIGR00097 1 ALTIAGSDSGGGAGIQADLKTFSALGVFGTSVITALTAQNTRGVTGVYPIPPDFVEAQLDAVFSDIPVDAAKTGMLASAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 87 IVTAVASYLKNYS-GKVVCDPVLNSTSGVLLHASDYLDLLKKLLFPHVDLLTPNIPEAEILIQNKIHTFSDIISAAHQLL 165
Cdd:TIGR00097 81 IVEAVARKLREYPvRPLVVDPVMVAKSGAPLLEEEAIEALRKRLLPLATLITPNLPEAEALLGTKIRTEQDMIKAAKKLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 166 KCGVSAVLLKGGHLIGSKARDFFTDGKCEFWLAHTKIPKTRVRGTGCALSSAISSAIALGYSLKDAIVVAKMYVQQGIRQ 245
Cdd:TIGR00097 161 ELGPKAVLIKGGHLEGDQAVDVLFDGGEIHILKAPRIETKNTHGTGCTLSAAIAANLAKGLSLKEAVKEAKEFVTGAIRY 240
|
....
gi 500791842 246 NFKV 249
Cdd:TIGR00097 241 GLNI 244
|
|
| thiE |
PRK00043 |
thiamine phosphate synthase; |
288-479 |
4.19e-65 |
|
thiamine phosphate synthase;
Pssm-ID: 234590 [Multi-domain] Cd Length: 212 Bit Score: 208.88 E-value: 4.19e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 288 GFYPIVDS--------VEWVERLLSYGVRTIQLRIKNASPQKIKKAVIESVALARHYQAKLFINDYWKLAIEAGAYGVHL 359
Cdd:PRK00043 8 RLYLITDSrddsgrdlLEVVEAALEGGVTLVQLREKGLDTRERLELARALKELCRRYGVPLIVNDRVDLALAVGADGVHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 360 GQEDLETADLSAIRAANLRLGISTHTLYELSRAHAIQPSYVAFGPIYETYSKPMPYSARGLEWLRYWCEISPY-PVVAIG 438
Cdd:PRK00043 88 GQDDLPVADARALLGPDAIIGLSTHTLEEAAAALAAGADYVGVGPIFPTPTKKDAKAPQGLEGLREIRAAVGDiPIVAIG 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 500791842 439 GINLNRLESVLNAGAVNVAVISAVTKSKTPQKTVRAFLNRI 479
Cdd:PRK00043 168 GITPENAPEVLEAGADGVAVVSAITGAEDPEAAARALLAAF 208
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
6-245 |
9.19e-64 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 207.29 E-value: 9.19e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 6 IVWSIGGSDCSGGAGCQADILTcrdFN---VHAASIITTITAQNAEQVLKINYCDSDLIQKQIQALKETLPPTVIKLGLL 82
Cdd:PRK06427 6 IALTIAGSDSGGGAGIQADLKT---FQalgVYGMSAITALTAQNTLGVQRVHPIPPEFVAAQLDAVFSDIRIDAVKIGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 83 GTKEIVTAVASYLKNYSGK-VVCDPVLNSTSGVLLHASDYLDLLKKLLFPHVDLLTPNIPEAEILIQNKIHTFSDII-SA 160
Cdd:PRK06427 83 ASAEIIETVAEALKRYPIPpVVLDPVMIAKSGDPLLADDAVAALRERLLPLATLITPNLPEAEALTGLPIADTEDEMkAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 161 AHQLLKCGVSAVLLKGGH-LIGSKARDFFTDGKCEFWLAHTKIPKTRVRGTGCALSSAISSAIALGYSLKDAIVVAKMYV 239
Cdd:PRK06427 163 ARALHALGCKAVLIKGGHlLDGEESVDWLFDGEGEERFSAPRIPTKNTHGTGCTLSAAIAAELAKGASLLDAVQTAKDYV 242
|
....*.
gi 500791842 240 QQGIRQ 245
Cdd:PRK06427 243 TRAIRH 248
|
|
| thiE |
TIGR00693 |
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ... |
288-475 |
9.49e-61 |
|
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate pyrophosphorylase, ThiE, of a number of bacteria, and N-terminal domains of bifunctional thiamine proteins of Saccharomyces cerevisiae and Schizosaccharomyces pombe, in which the C-terminal domain corresponds to the bacterial hydroxyethylthiazole kinase (EC 2.7.1.50), ThiM. This model includes ThiE from Bacillus subtilis but excludes its paralog, the regulatory protein TenI (SP:P25053), and neighbors of TenI. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]
Pssm-ID: 273222 [Multi-domain] Cd Length: 196 Bit Score: 197.09 E-value: 9.49e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 288 GFYPIVDS-------VEWVERLLSYGVRTIQLRIKNASPQKIKKAVIESVALARHYQAKLFINDYWKLAIEAGAYGVHLG 360
Cdd:TIGR00693 1 GLYLITDPqdgpadlLNRVEAALKGGVTLVQLRDKGSNTRERLALAEKLQELCRRYGVPFIVNDRVDLALALGADGVHLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 361 QEDLETADLSAIRAANLRLGISTHTLYELSRAHAIQPSYVAFGPIYETYSKPMPYSARGLEWLRYWCEISP-YPVVAIGG 439
Cdd:TIGR00693 81 QDDLPASEARALLGPDKIIGVSTHNLEELAEAEAEGADYIGFGPIFPTPTKKDPAPPAGVELLREIAATLIdIPIVAIGG 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 500791842 440 INLNRLESVLNAGAVNVAVISAVTKSKTPQKTVRAF 475
Cdd:TIGR00693 161 ITLENAAEVLAAGADGVAVVSAIMQAADPKAAAKRL 196
|
|
| PTZ00347 |
PTZ00347 |
phosphomethylpyrimidine kinase; Provisional |
7-249 |
2.29e-43 |
|
phosphomethylpyrimidine kinase; Provisional
Pssm-ID: 240375 [Multi-domain] Cd Length: 504 Bit Score: 160.13 E-value: 2.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 7 VWSIGGSDCSGGAGCQADILTCRDFNVHAASIITTITAQNAEQVLKINYCDSDLIQKQIQALKETLPPTVIKLGLLGTKE 86
Cdd:PTZ00347 233 VLTVSGSDSGGGAGHQADLKTLEALGVYSTSALTSLTAQNTKGVQQIQVVNEDFFAAQIDSVMSDFNISVVKLGLVPTAR 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 87 IVTAVASYLKNYsgKVVCDPVLNSTSGVLL----HASDYLDLLKKLLFPHVDLLTPNIPEAE-ILIQNKIHTFSDIISAA 161
Cdd:PTZ00347 313 QLEIVIEKLKNL--PMVVDPVLVATSGDDLvaqkNADDVLAMYKERIFPMATIITPNIPEAErILGRKEITGVYEARAAA 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 162 HQLLKCGVSAVLLKGGH-LIGSKA-RDFFTDG-KCEFWLAHTK-IPKTRVRGTGCALSSAISSAIALGYSLKDAIVVAKM 237
Cdd:PTZ00347 391 QALAQYGSRYVLVKGGHdLIDPEAcRDVLYDReKDRFYEFTANrIATINTHGTGCTLASAISSFLARGYTVPDAVERAIG 470
|
250
....*....|..
gi 500791842 238 YVQQGIRQNFKV 249
Cdd:PTZ00347 471 YVHEAIVRSCGV 482
|
|
| PRK08573 |
PRK08573 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
9-249 |
2.64e-43 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 236297 [Multi-domain] Cd Length: 448 Bit Score: 158.74 E-value: 2.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 9 SIGGSDCSGGAGCQADILTCRDFNVHAASIITTITAQNAEQVLKINYCDSDLIQKQIQALKETLPPTVIKLGLLGTKEIV 88
Cdd:PRK08573 7 TIAGSDSGGGAGIEADLKTFAALGVHGAVAITSVTAQNTYEVRAIHDLPPEVVAAQIEAVWEDMGIDAAKTGMLSNREII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 89 TAVASYLKNYSGKVVCDPVLNSTSGVLLHASDYLDLLKKLLFPHVDLLTPNIPEAEILIQNKIHTFSDIISAAHQLLK-C 167
Cdd:PRK08573 87 EAVAKTVSKYGFPLVVDPVMIAKSGAPLLREDAVDALIKRLLPLATVVTPNRPEAEKLTGMKIRSVEDARKAAKYIVEeL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 168 GVSAVLLKGGHLIGSKARD-FFTDGKCEFWLAhTKIPKTRVRGTGCALSSAISSAIALGYSLKDAIVVAKMYVQQGIRQN 246
Cdd:PRK08573 167 GAEAVVVKGGHLEGEEAVDvLYHNGTFREFRA-PRVESGCTHGTGCSFSAAIAAGLAKGLDPEEAIKTAKKFITMAIKYG 245
|
...
gi 500791842 247 FKV 249
Cdd:PRK08573 246 VKI 248
|
|
| PRK02615 |
PRK02615 |
thiamine phosphate synthase; |
299-476 |
2.56e-38 |
|
thiamine phosphate synthase;
Pssm-ID: 235054 [Multi-domain] Cd Length: 347 Bit Score: 142.71 E-value: 2.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 299 VERLLSYGVRTIQLRIKNASP-QKIKKAvIESVALARHYQAKLFINDYWKLAIEAGAYGVHLGQEDLETADLSAIRAANL 377
Cdd:PRK02615 163 VEAALKGGVTLVQYRDKTADDrQRLEEA-KKLKELCHRYGALFIVNDRVDIALAVDADGVHLGQEDLPLAVARQLLGPEK 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 378 RLGISTHTLYELSRAHAIQPSYVAFGPIYETYSKPMPySARGLEWLRYWCEISPYPVVAIGGINLNRLESVLNAGAVNVA 457
Cdd:PRK02615 242 IIGRSTTNPEEMAKAIAEGADYIGVGPVFPTPTKPGK-APAGLEYLKYAAKEAPIPWFAIGGIDKSNIPEVLQAGAKRVA 320
|
170
....*....|....*....
gi 500791842 458 VISAVTKSKTPQKTVRAFL 476
Cdd:PRK02615 321 VVRAIMGAEDPKQATQELL 339
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
1-245 |
9.74e-37 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 135.58 E-value: 9.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 1 MNQKSIVwSIGGSDCSGGAGCQADILTCRDFNVHAASIITTITAQNAE--QVLKInycDSDLIQKQIQALKeTLPPTVIK 78
Cdd:PRK12413 1 MKTNYIL-AISGNDIFSGGGLHADLATYTRNGLHGFVAVTCLTAMTEKgfEVFPV---DKEIFQQQLDSLK-DVPFSAIK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 79 LGLLGTKEIVTAVASYLKNYSG-KVVCDPVL--NSTSGVllhASDYLDLLKKLLFPHVDLLTPNIPEAEILIQNKIHTFS 155
Cdd:PRK12413 76 IGLLPNVEIAEQALDFIKGHPGiPVVLDPVLvcKETHDV---EVSELRQELIQFFPYVTVITPNLVEAELLSGKEIKTLE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 156 DIISAAHQLLKCGVSAVLLKGGH-LIGSKARDFFTDGKcEFWLAHTKIPKTRVRGTGCALSSAISSAIALGYSLKDAIVV 234
Cdd:PRK12413 153 DMKEAAKKLYDLGAKAVVIKGGNrLSQKKAIDLFYDGK-EFVILESPVLEKNNIGAGCTFASSIASQLVKGKSPLEAVKN 231
|
250
....*....|.
gi 500791842 235 AKMYVQQGIRQ 245
Cdd:PRK12413 232 SKDFVYQAIQQ 242
|
|
| PRK14713 |
PRK14713 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
7-244 |
3.90e-35 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 237797 [Multi-domain] Cd Length: 530 Bit Score: 137.23 E-value: 3.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 7 VWSIGGSDCSGGAGCQADILTCRDFNVHAASIITTITAQNAEQVLKINYCDSDLIQKQIQALKETLPPTVIKLGLLGTKE 86
Cdd:PRK14713 32 VLSIAGTDPSGGAGIQADLKSIAAAGGYGMAVITALVAQNTRGVRAVHVPPADFLRAQLDAVSDDVTVDAVKIGMLGDAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 87 IVTAVASYL-KNYSGKVVCDPVLNSTSG-VLLHASDYLDLLKKLlfPHVDLLTPNIPEAEILIQNKI-HTFSDIISAAHQ 163
Cdd:PRK14713 112 VIDAVRTWLaEHRPPVVVLDPVMVATSGdRLLEEDAEAALRELV--PRADLITPNLPELAVLLGEPPaTTWEEALAQARR 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 164 LLKCGVSAVLLKGGHLIGSKARD--FFTDGKCefwlahTKIPKTRV-----RGTGCALSSAISSAIALGYSLKDAIVVAK 236
Cdd:PRK14713 190 LAAETGTTVLVKGGHLDGQRAPDalVGPDGAV------TEVPGPRVdtrntHGTGCSLSSALATRLGRGGDWAAALRWAT 263
|
....*...
gi 500791842 237 MYVQQGIR 244
Cdd:PRK14713 264 AWLHGAIA 271
|
|
| PRK12412 |
PRK12412 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
9-250 |
1.63e-33 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183512 [Multi-domain] Cd Length: 268 Bit Score: 127.39 E-value: 1.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 9 SIGGSDCSGGAGCQADILTCRDFNVHAASIITTITAQN-----AEQVLKInycDSDLIQKQIQALKETLPPTVIKLGLLG 83
Cdd:PRK12412 6 TIAGSDTSGGAGIQADLKTFQELGVYGMTSLTTIVTMDphngwAHNVFPI---PASTLKPQLETTIEGVGVDALKTGMLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 84 TKEIVTAVASYLKNYSGK-VVCDPVLNST-SGVLLHASDYLDLLKKLLfPHVDLLTPNIPEAEILIQNKIHTFSDIISAA 161
Cdd:PRK12412 83 SVEIIEMVAETIEKHNFKnVVVDPVMVCKgADEALHPETNDCLRDVLV-PKALVVTPNLFEAYQLSGVKINSLEDMKEAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 162 HQLLKCGVSAVLLKGGHLIGS-KARDFFTDGKCEFWLAHTKIPKTRVRGTGCALSSAISSAIALGYSLKDAIVVAKMYVQ 240
Cdd:PRK12412 162 KKIHALGAKYVLIKGGSKLGTeTAIDVLYDGETFDLLESEKIDTTNTHGAGCTYSAAITAELAKGKPVKEAVKTAKEFIT 241
|
250
....*....|
gi 500791842 241 QGIRQNFKVN 250
Cdd:PRK12412 242 AAIRYSFKIN 251
|
|
| PRK12616 |
PRK12616 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
9-250 |
1.33e-30 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183624 Cd Length: 270 Bit Score: 119.76 E-value: 1.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 9 SIGGSDCSGGAGCQADILTCRDFNVHAASIITTITAQNAE-----QVLKInycDSDLIQKQIQALKETLPPTVIKLGLLG 83
Cdd:PRK12616 8 TIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAMDPEnswdhQVFPI---DTDTIRAQLSTIVDGIGVDAMKTGMLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 84 TKEIVTAVASYLKNYSGK-VVCDPVL--NSTSGVLL--HASDYLDLLKkllfPHVDLLTPNIPEAEILIQ-NKIHTFSDI 157
Cdd:PRK12616 85 TVDIIELAADTIKEKQLKnVVIDPVMvcKGANEVLYpeHAEALREQLA----PLATVITPNLFEAGQLSGmGEIKTVEQM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 158 ISAAHQLLKCGVSAVLLKGG-HLIGSKARDFFTDGKCEFWLAHTKIPKTRVRGTGCALSSAISSAIALGYSLKDAIVVAK 236
Cdd:PRK12616 161 KEAAKKIHELGAQYVVITGGgKLKHEKAVDVLYDGETAEVLESEMIDTPYTHGAGCTFSAAVTAELAKGSEVKEAIYAAK 240
|
250
....*....|....
gi 500791842 237 MYVQQGIRQNFKVN 250
Cdd:PRK12616 241 EFITAAIKESFPLN 254
|
|
| PRK09517 |
PRK09517 |
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ... |
7-244 |
2.05e-29 |
|
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; Provisional
Pssm-ID: 169939 [Multi-domain] Cd Length: 755 Bit Score: 122.00 E-value: 2.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 7 VWSIGGSDCSGGAGCQADILTCRDFNVHAASIITTITAQNAEQVLKINYCDSDLIQKQIQALKETLPPTVIKLGLLGTKE 86
Cdd:PRK09517 244 VLSIAGTDPTGGAGIQADLKSIAAGGGYGMCVVTALVAQNTHGVNTIHTPPLTFLEEQLEAVFSDVTVDAVKLGMLGSAD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 87 IVTAVASYLKNYS-GKVVCDPVLNSTSG-VLLHASDYLDLLKKLlfPHVDLLTPNIPE-AEILIQNKIHTFSDIISAAHQ 163
Cdd:PRK09517 324 TVDLVASWLGSHEhGPVVLDPVMVATSGdRLLDADATEALRRLA--VHVDVVTPNIPElAVLCGEAPAITMDEAIAQARG 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 164 LLKCGVSAVLLKGGHLIGSKARD-FFTDGKCEFWLAHTKIPKTRVRGTGCALSSAISSAIALGYSLKDAIVVAKMYVQQG 242
Cdd:PRK09517 402 FARTHGTIVIVKGGHLTGDLADNaVVRPDGSVHQVENPRVNTTNSHGTGCSLSAALATLIAAGESVEKALEWATRWLNEA 481
|
..
gi 500791842 243 IR 244
Cdd:PRK09517 482 LR 483
|
|
| PRK08999 |
PRK08999 |
Nudix family hydrolase; |
290-461 |
2.43e-26 |
|
Nudix family hydrolase;
Pssm-ID: 236361 [Multi-domain] Cd Length: 312 Bit Score: 108.81 E-value: 2.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 290 YPIVDSVEW--------VERLLSYGVRTIQLRIKNASPQKIKKAVIESVALARHYQAKLFINDYWKLAIEAGAYGVHLGQ 361
Cdd:PRK08999 133 YLITPEGEDgdaaflarLERALAAGIRLIQLRAPQLPPAAYRALARAALGLCRRAGAQLLLNGDPELAEDLGADGVHLTS 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 362 EDLetADLSAiR--AANLRLGISTHTLYELSRAHAIQPSYVAFGPIYETYSKPmpySARGLEWLRY--WCEISPYPVVAI 437
Cdd:PRK08999 213 AQL--AALAA-RplPAGRWVAASCHDAEELARAQRLGVDFAVLSPVQPTASHP---GAAPLGWEGFaaLIAGVPLPVYAL 286
|
170 180
....*....|....*....|....
gi 500791842 438 GGINLNRLESVLNAGAVNVAVISA 461
Cdd:PRK08999 287 GGLGPGDLEEAREHGAQGIAGIRG 310
|
|
| PTZ00493 |
PTZ00493 |
phosphomethylpyrimidine kinase; Provisional |
1-244 |
4.71e-22 |
|
phosphomethylpyrimidine kinase; Provisional
Pssm-ID: 240440 Cd Length: 321 Bit Score: 96.60 E-value: 4.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 1 MNQKSIVWSIGGSDCSGGAGCQADILTCRDFNVHAASIITTITAQNAEQVLKINYCDSDLIQKQIQALKETLPPTVIKLG 80
Cdd:PTZ00493 1 MEGVSNILSIAGSDSCGGAGMQADIKTAMGLGCHCCTALVVLTAQNTKEVKRIVEIEEKFIVEQLDSIFADVTIDVVKLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 81 LLGTKEIVTAVASYLKNYSGK------VVCDPVLNSTSGVLLHASDYLDLLKKLLF-PHVDLLTPNIPEAEILIQ----- 148
Cdd:PTZ00493 81 VLYSKKIISLVHNYITNMNKKrgkkllVVFDPVFVSSSGCLLVENLEYIKFALDLIcPISCIITPNFYECKVILEaldcq 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 149 ---NKIHTfSDIISAAHQLLKcgVSAVLLKG----------------GHLIGSKARDFFTDGKCE------------FWL 197
Cdd:PTZ00493 161 mdlSKANM-TELCKLVTEKLN--INACLFKScnvgensaeenevyavDHLCIRNVGSYPTGEKQQidaggvtylydvYKL 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 500791842 198 AHTKIPKTRVRGTGCALSSAISSAIALGYSLKDAIVVAKMYVQQGIR 244
Cdd:PTZ00493 238 RSKRKPGKDIHGTGCTLSTAIACYLAKKHNILQSCIESKKYIYNCIR 284
|
|
| PRK07695 |
PRK07695 |
thiazole tautomerase TenI; |
339-475 |
8.17e-18 |
|
thiazole tautomerase TenI;
Pssm-ID: 181086 [Multi-domain] Cd Length: 201 Bit Score: 81.61 E-value: 8.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 339 KLFINDYWKLAIEAGAYGVHLGQEDLetaDLSAIRA--ANLRLGISTHTLYELSRAHAIQPSYVAFGPIYETYSKP-MPy 415
Cdd:PRK07695 59 KLIINDRVDIALLLNIHRVQLGYRSF---SVRSVREkfPYLHVGYSVHSLEEAIQAEKNGADYVVYGHVFPTDCKKgVP- 134
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 500791842 416 sARGLEWLRywcEISPY---PVVAIGGINLNRLESVLNAGAVNVAVISAVTKSKTPQKTVRAF 475
Cdd:PRK07695 135 -ARGLEELS---DIARAlsiPVIAIGGITPENTRDVLAAGVSGIAVMSGIFSSANPYSKAKRY 193
|
|
| PRK09517 |
PRK09517 |
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ... |
299-476 |
1.37e-17 |
|
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; Provisional
Pssm-ID: 169939 [Multi-domain] Cd Length: 755 Bit Score: 85.80 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 299 VERLLSYGVRTIQLRIKNASPQKIKKAVIESVALARHYQAKLFINDYWKLAIEAGAYgVHLGQEDLETADLSAIRAANLR 378
Cdd:PRK09517 25 VDSAISGGVSVVQLRDKNAGVEDVRAAAKELKELCDARGVALVVNDRLDVAVELGLH-VHIGQGDTPYTQARRLLPAHLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 379 LGISTHTLYEL-------SRAHAIQPSYVAFGPIYETYSKPMPYSARGLEWLRYWCEISPY---PVVAIGGINLNRLESV 448
Cdd:PRK09517 104 LGLTIETLDQLeaviaqcAETGVALPDVIGIGPVASTATKPDAPPALGVDGIAEIAAVAQDhgiASVAIGGVGLRNAAEL 183
|
170 180
....*....|....*....|....*...
gi 500791842 449 LNAGAVNVAVISAVTKSKTPQKTVRAFL 476
Cdd:PRK09517 184 AATGIDGLCVVSAIMAAANPAAAARELR 211
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
80-255 |
1.18e-15 |
|
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: 77.11 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 80 GLLGTKEIVTAVASYLKNY-----SGKVVCDPVLNSTSGVLLHASDYLDLLKKLLFPHVDLLTPNIPEAEILIQNKIHTF 154
Cdd:COG2240 81 GYLGSAEQGDIIADFVARVkaanpDALYLCDPVMGDNGKGYYVFPGIAEFIMRRLVPLADIITPNLTELALLTGRPYETL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 155 SDIISAAHQLLKCGVSAVLLKGGHLIGSKARDF----FTDGkcEFWLAHT-KIPKTRVrGTGCALSSAISSAIALGYSLK 229
Cdd:COG2240 161 EEALAAARALLALGPKIVVVTSVPLDDTPADKIgnlaVTAD--GAWLVETpLLPFSPN-GTGDLFAALLLAHLLRGKSLE 237
|
170 180
....*....|....*....|....*.
gi 500791842 230 DAIVVAKMYVQQGIRQNFKVNTQELM 255
Cdd:COG2240 238 EALERAAAFVYEVLERTAAAGSDELL 263
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
80-238 |
1.35e-12 |
|
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: 67.61 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 80 GLLGTKEIVTAVASYLK-----NYSGKVVCDPVLNSTSGVLLHASDYLDLLKKLLFPHVDLLTPNIPEAEILIQNKIHTF 154
Cdd:cd01173 79 GYLGSAEQVEAVAEIVKrlkekNPNLLYVCDPVMGDNGKLYVVAEEIVPVYRDLLVPLADIITPNQFELELLTGKKINDL 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 155 SDIISAAHQLLKCGVSAVLLKGGHLIGSKA-RDFFTDGKCEFWLAHTKIP-KTRVRGTGCALSSAISSAIALGYSLKDA- 231
Cdd:cd01173 159 EDAKAAARALHAKGPKTVVVTSVELADDDRiEMLGSTATEAWLVQRPKIPfPAYFNGTGDLFAALLLARLLKGKSLAEAl 238
|
....*...
gi 500791842 232 -IVVAKMY 238
Cdd:cd01173 239 eKALNFVH 246
|
|
| pyridox_kin |
TIGR00687 |
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ... |
80-180 |
3.40e-09 |
|
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: 57.92 E-value: 3.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 80 GLLGTKEIVTAVASYLK-----NYSGKVVCDPVLNSTSGVLLHASDYLDLLKKLLFPHVDLLTPNIPEAEILIQNKIHTF 154
Cdd:TIGR00687 81 GYLGSAEQVAMVVGIVRqvkqaNPQALYVCDPVMGDPWKGCYVAPDLLEVYREKAIPVADIITPNQFELELLTGRRINTE 160
|
90 100
....*....|....*....|....*.
gi 500791842 155 SDIISAAHQLLKCGVSAVLLKggHLI 180
Cdd:TIGR00687 161 EEALAAADALIAMGPDIVLVT--HLI 184
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
130-232 |
8.96e-08 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 53.50 E-value: 8.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 130 FPHVDLLTPNIPEAEILIQNKIHTFSDIISAAHQLLKCGVSAVLLKgghlIGSKARDFFTDGKCEFWLAhtkIPKTRVR- 208
Cdd:pfam00294 178 LPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVT----LGADGALVVEGDGEVHVPA---VPKVKVVd 250
|
90 100
....*....|....*....|....*.
gi 500791842 209 --GTGCALSSAISSAIALGYSLKDAI 232
Cdd:pfam00294 251 ttGAGDSFVGGFLAGLLAGKSLEEAL 276
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
38-232 |
2.03e-07 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 52.44 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 38 IITTITAQNAEQVLKINYCDSDLIQKQIQALKET----------------LPPTViklgllgTKEIVTAVASYLKNYSGK 101
Cdd:COG1105 88 INIKIVDPSDGTETEINEPGPEISEEELEALLERleellkegdwvvlsgsLPPGV-------PPDFYAELIRLARARGAK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 102 VVCDpvlnsTSGVLLHASDYLdllkkllfpHVDLLTPNIPEAEILIQNKIHTFSDIISAAHQLLKCGVSAVLLkgghlig 181
Cdd:COG1105 161 VVLD-----TSGEALKAALEA---------GPDLIKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVV------- 219
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 500791842 182 SKARD---FFTDGKCefWLAhtKIPKTRVR---GTGCALSSAISSAIALGYSLKDAI 232
Cdd:COG1105 220 SLGADgalLVTEDGV--YRA--KPPKVEVVstvGAGDSMVAGFLAGLARGLDLEEAL 272
|
|
| KGPDC_HPS |
cd04726 |
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate ... |
292-475 |
9.95e-06 |
|
3-Keto-L-gulonate 6-phosphate decarboxylase (KGPDC) and D-arabino-3-hexulose-6-phosphate synthase (HPS). KGPDC catalyzes the formation of L-xylulose 5-phosphate and carbon dioxide from 3-keto-L-gulonate 6-phosphate as part of the anaerobic pathway for L-ascorbate utilization in some eubacteria. HPS catalyzes the formation of D-arabino-3-hexulose-6-phosphate from D-ribulose 5-phosphate and formaldehyde in microorganisms that can use formaldehyde as a carbon source. Both catalyze reactions that involve the Mg2+-assisted formation and stabilization of 1,2-enediolate reaction intermediates.
Pssm-ID: 240077 [Multi-domain] Cd Length: 202 Bit Score: 46.42 E-value: 9.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 292 IVDSVEWVER----LLSYGVRTIQlRIKNASPQKIKKAVIEsVALARHYQAKLfindywklAIEAGA-YGVHLGQEDLET 366
Cdd:cd04726 22 VPDGVDIIEAgtplIKSEGMEAVR-ALREAFPDKIIVADLK-TADAGALEAEM--------AFKAGAdIVTVLGAAPLST 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 367 ADlSAIRAANlRLG-------ISTHTLYELSRAHAIQPSYVafgpIYET-YSKPMPYSARGLEWLRYWCEISPYPVVAIG 438
Cdd:cd04726 92 IK-KAVKAAK-KYGkevqvdlIGVEDPEKRAKLLKLGVDIV----ILHRgIDAQAAGGWWPEDDLKKVKKLLGVKVAVAG 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 500791842 439 GINLNRLESVLNAGAVNVAVISAVTKSKTPQKTVRAF 475
Cdd:cd04726 166 GITPDTLPEFKKAGADIVIVGRAITGAADPAEAAREF 202
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
49-237 |
2.05e-05 |
|
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: 46.40 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 49 QVLKINY-----CDSDLIQKQIQALKETLP-PTVIKL-----GLLgTKEIVTAVASYLKNYSGKVVCDPVLNSTSGvllh 117
Cdd:cd01172 104 QLLRVDReddspLSAEEEQRLIERIAERLPeADVVILsdygkGVL-TPRVIEALIAAARELGIPVLVDPKGRDYSK---- 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 118 asdyldllkkllFPHVDLLTPNIPEAEILIQNKIHTFSDIISAAHQLL-KCGVSAVLLKGG------HLIGSKARDFFtd 190
Cdd:cd01172 179 ------------YRGATLLTPNEKEAREALGDEINDDDELEAAGEKLLeLLNLEALLVTLGeegmtlFERDGEVQHIP-- 244
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 500791842 191 gkcefwlAHTKIPKTrVRGTGCALSSAISSAIALGYSLKDA---------IVVAKM 237
Cdd:cd01172 245 -------ALAKEVYD-VTGAGDTVIATLALALAAGADLEEAaflanaaagVVVGKV 292
|
|
| PTZ00344 |
PTZ00344 |
pyridoxal kinase; Provisional |
80-175 |
3.66e-05 |
|
pyridoxal kinase; Provisional
Pssm-ID: 240372 [Multi-domain] Cd Length: 296 Bit Score: 45.46 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 80 GLLGTKEIVTAVASYLK-----NYSGKVVCDPVLNSTSgvLLHASDYLDLLKKLLFPHVDLLTPNIPEAEILIQNKIHTF 154
Cdd:PTZ00344 84 GYINSADILREVLATVKeikelRPKLIFLCDPVMGDDG--KLYVKEEVVDAYRELIPYADVITPNQFEASLLSGVEVKDL 161
|
90 100
....*....|....*....|.
gi 500791842 155 SDIISAAHQLLKCGVSAVLLK 175
Cdd:PTZ00344 162 SDALEAIDWFHEQGIPVVVIT 182
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
86-223 |
4.20e-05 |
|
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: 44.39 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 86 EIVTAVASYLKNYSGKVVCDPVLNSTSGVLLhasdyldlLKKLLFPHVDLLTPNIPEAEILIQNKIHTFSDIISAAHQLL 165
Cdd:cd00287 71 EAVLDALEEARRRGVPVVLDPGPRAVRLDGE--------ELEKLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLL 142
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 500791842 166 KCGVSAVLLKGGHlIGSKArdfFTDGKcefWLAHTKIPKTRVR---GTGCALSSAISSAIA 223
Cdd:cd00287 143 SKGPKVVIVTLGE-KGAIV---ATRGG---TEVHVPAFPVKVVdttGAGDAFLAALAAGLA 196
|
|
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
10-235 |
5.86e-05 |
|
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: 44.53 E-value: 5.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 10 IGGSDCSGGAGcqadILTCRDFnVHA-ASIITTITAQNAEQVLKINYCD---SDLIQKQIQALKETLP-PTVIKLGL-LG 83
Cdd:cd01171 14 IGGSRGYTGAA----YLAALAA-LRAgAGLVTVATPPEAAAVIKSYSPElmvHPLLETDIEELLELLErADAVVIGPgLG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 84 TKEIVTAVASYLKNYSGKVVCDpvlnstSGVLLHASDYLDLLKkllFPHVDLLTPNIPEAEILIQNKIHTFSDIISAAHQ 163
Cdd:cd01171 89 RDEEAAEILEKALAKDKPLVLD------ADALNLLADEPSLIK---RYGPVVLTPHPGEFARLLGALVEEIQADRLAAAR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 500791842 164 LL--KCGVsAVLLKGghligskARDFFTDGKCEFWLAHTKIPKTRVRGTGCALSSAISSAIALGYSLKDAIVVA 235
Cdd:cd01171 160 EAaaKLGA-TVVLKG-------AVTVIADPDGRVYVNPTGNPGLATGGSGDVLAGIIAALLAQGLSPLEAAALA 225
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
84-235 |
7.37e-05 |
|
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: 44.49 E-value: 7.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 84 TKEIVTAVASYLKNYSGKVVCDPvlNSTSGVLLHAsdylDLLKKLLFPHVDLLTPNIPEAEILIQnkihtFSDIISAAHQ 163
Cdd:COG0524 143 PREALLAALEAARAAGVPVSLDP--NYRPALWEPA----RELLRELLALVDILFPNEEEAELLTG-----ETDPEEAAAA 211
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 500791842 164 LLKCGVSAVLLKGGHLiGSKArdfFTDGKcefwLAHTKIPKTRVR-GTGC--ALSSAISSAIALGYSLKDAIVVA 235
Cdd:COG0524 212 LLARGVKLVVVTLGAE-GALL---YTGGE----VVHVPAFPVEVVdTTGAgdAFAAGFLAGLLEGLDLEEALRFA 278
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
130-232 |
8.59e-05 |
|
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: 44.46 E-value: 8.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 130 FPHVDLLTPNIPEAEILIQNKIHTFSDIISAAHQLLKCGVSAVLLKgghlIGSKARDFFTDGKCEFwlahtkIPKTRVR- 208
Cdd:cd01174 173 LALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVT----LGAKGALLASGGEVEH------VPAFKVKa 242
|
90 100
....*....|....*....|....*...
gi 500791842 209 ----GTGCALSSAISSAIALGYSLKDAI 232
Cdd:cd01174 243 vdttGAGDTFIGALAAALARGLSLEEAI 270
|
|
| PRK07105 |
PRK07105 |
pyridoxamine kinase; Validated |
80-250 |
1.10e-04 |
|
pyridoxamine kinase; Validated
Pssm-ID: 180840 [Multi-domain] Cd Length: 284 Bit Score: 44.14 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 80 GLLGTKEIVTAVASYLKNYSGK---VVCDPVL--------NSTSGVLLHASDYLDllkkllfpHVDLLTPNIPEAEILIQ 148
Cdd:PRK07105 82 GYLGSPRQIQIVSDFIKYFKKKdllVVVDPVMgdngklyqGFDQEMVEEMRKLIQ--------KADVITPNLTEACLLLD 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 149 ----NKIHTFSDIISAAHQLLKCGVSAVLLKG----GHLIGSKARDFFTDgkcEFWLA-HTKIPkTRVRGTGCALSSAIS 219
Cdd:PRK07105 154 kpylEKSYSEEEIKQLLRKLADLGPKIVIITSvpfeDGKIGVAYYDRATD---RFWKVfCKYIP-AHYPGTGDIFTSVIT 229
|
170 180 190
....*....|....*....|....*....|.
gi 500791842 220 SAIALGYSLKDAIVVAKMYVQQGIRQNFKVN 250
Cdd:PRK07105 230 GSLLQGDSLPIALDRAVQFIEKGIRATLGLK 260
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
131-235 |
3.10e-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: 42.69 E-value: 3.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 131 PHVDLLTPNIPEAEILIQNKIHTFSDIISAAHQLLKCGVSAVLLKGGH---LIGSKardfftDGKCEFWLAHTKIPKT-- 205
Cdd:cd01941 175 HAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAkgvLLSSR------EGGVETKLFPAPQPETvv 248
|
90 100 110
....*....|....*....|....*....|
gi 500791842 206 RVRGTGCALSSAISSAIALGYSLKDAIVVA 235
Cdd:cd01941 249 NVTGAGDAFVAGLVAGLLEGMSLDDSLRFA 278
|
|
| PLN02978 |
PLN02978 |
pyridoxal kinase |
80-174 |
6.32e-03 |
|
pyridoxal kinase
Pssm-ID: 215529 [Multi-domain] Cd Length: 308 Bit Score: 38.57 E-value: 6.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500791842 80 GLLGTKEIVTAVASY---LKNYSGKV--VCDPVLNStSGVLLHASDYLDLLKKLLFPHVDLLTPNIPEAEILIQNKIHTF 154
Cdd:PLN02978 93 GYIGSVSFLRTVLRVvkkLRSVNPNLtyVCDPVLGD-EGKLYVPPELVPVYREKVVPLATMLTPNQFEAEQLTGIRIVTE 171
|
90 100
....*....|....*....|
gi 500791842 155 SDIISAAHQLLKCGVSAVLL 174
Cdd:PLN02978 172 EDAREACAILHAAGPSKVVI 191
|
|
| |
