|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14713 |
PRK14713 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
2-514 |
0e+00 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 237797 [Multi-domain] Cd Length: 530 Bit Score: 643.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 2 PAVPRVLSIAGTDPTGGAGIQADLKSIAAAGGYGMSAVTALVAQNTQGVREVHTPPVEFLRAQLTAVASDVTIDAVKIGM 81
Cdd:PRK14713 27 AATPRVLSIAGTDPSGGAGIQADLKSIAAAGGYGMAVITALVAQNTRGVRAVHVPPADFLRAQLDAVSDDVTVDAVKIGM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 82 LGSAAIVAEVSRFLAQLSDVPVVLDPVMVATSGDRLLDRDAEAAVRELCARATVVTPNLKELAVLTQTAEATTLEEAIAH 161
Cdd:PRK14713 107 LGDAEVIDAVRTWLAEHRPPVVVLDPVMVATSGDRLLEEDAEAALRELVPRADLITPNLPELAVLLGEPPATTWEEALAQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 162 ATAWSADTRTTVIVKGGHLRGDLADNAVVTPDGAVHRVSCPRVDTPHTHGTGCSLSSALATRLGAGASLSDALSWSTRWL 241
Cdd:PRK14713 187 ARRLAAETGTTVLVKGGHLDGQRAPDALVGPDGAVTEVPGPRVDTRNTHGTGCSLSSALATRLGRGGDWAAALRWATAWL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 242 HEAISHAAALEVGQGHGPVDHGHRARRLAAAASTVPArfysdvTSTAAAPAPHVSAAGPETARLWELTGDAWQSITQLPF 321
Cdd:PRK14713 267 HGAIAAGAALQVGTGNGPVDHFHRARRLAADASAEAG------VSAEPAPDAVVGPAGPFTAALWQASGPIREAIEDLPF 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 322 IQALGTGTLREEDFAFYLAQDAQYLNQYSKALARLAALAPDAGAQLHWASGAAECLAVEMSLHKDWIAHHtttvpsTALT 401
Cdd:PRK14713 341 VRALADGTLPEEAFEFYLAQDALYLNGYSRALARLAALAPDPAEQVFWAQSAQACLEVESELHRSWLGDR------DADT 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 402 APSRVTSAYTDFLVSTTHTDDYVVAAAAVLPCYWLYAEVG--LHLAAQNSPEHPYNAWITQYGGEEFLTGVRAAIALVEE 479
Cdd:PRK14713 415 APSPVTLAYTDFLLARAAGGSYAVGAAAVLPCFWLYAEVGaeLHARAGNPDDHPYAEWLQTYADPEFAAATRRAIAFVDR 494
|
490 500 510
....*....|....*....|....*....|....*
gi 1080393322 480 ALTAADPATRSRATRAYLAACWHEVDFFDQADRRW 514
Cdd:PRK14713 495 AFRAASPAERAAMARAFLTACRYELEFFDQARRRA 529
|
|
| PRK09517 |
PRK09517 |
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ... |
2-512 |
0e+00 |
|
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; Provisional
Pssm-ID: 169939 [Multi-domain] Cd Length: 755 Bit Score: 565.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 2 PAVPRVLSIAGTDPTGGAGIQADLKSIAAAGGYGMSAVTALVAQNTQGVREVHTPPVEFLRAQLTAVASDVTIDAVKIGM 81
Cdd:PRK09517 239 PSAPRVLSIAGTDPTGGAGIQADLKSIAAGGGYGMCVVTALVAQNTHGVNTIHTPPLTFLEEQLEAVFSDVTVDAVKLGM 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 82 LGSAAIVAEVSRFLAQLSDVPVVLDPVMVATSGDRLLDRDAEAAVRELCARATVVTPNLKELAVLTQTAEATTLEEAIAH 161
Cdd:PRK09517 319 LGSADTVDLVASWLGSHEHGPVVLDPVMVATSGDRLLDADATEALRRLAVHVDVVTPNIPELAVLCGEAPAITMDEAIAQ 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 162 ATAWSADTRTTVIVKGGHLRGDLADNAVVTPDGAVHRVSCPRVDTPHTHGTGCSLSSALATRLGAGASLSDALSWSTRWL 241
Cdd:PRK09517 399 ARGFARTHGTIVIVKGGHLTGDLADNAVVRPDGSVHQVENPRVNTTNSHGTGCSLSAALATLIAAGESVEKALEWATRWL 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 242 HEAISHAAALEVGQGHGPVDHGHRARRLAAAASTVPARFYS--------DVTSTAAAPAPHVSAAGPETARLWELTGDAW 313
Cdd:PRK09517 479 NEALRHADHLAVGSGNGPVDHGHLARRLTHAAETTPWAHLRagataasfTTPSTVKSPAPRIEPAGPFTRALWEASGDII 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 314 QSITQLPFIQALGTGTLREEDFAFYLAQDAQYLNQYSKALARLAALAPDAGAQLHWASGAAECLAVEMSLHKDWIAHHtt 393
Cdd:PRK09517 559 AEINDSDFIRMLGDGTLRRPEFDFYIDQDAQYLRQYSRALARLSSIAPDSHAQVEWAQSAAECIVVEAELHRSYLSGK-- 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 394 tvpsTALTAPSRVTSAYTDFLVSTTHTDDYVVAAAAVLPCYWLYAEVGLHLAAQNSPEHPYNAWITQYGGEEFLTGVRAA 473
Cdd:PRK09517 637 ----EAPSAPSPVTMAYTDFLIARTYTEDYVVGVAAVLPCYWLYAEIGLMLAEQNHDEHPYKDWLNTYSGEEFIAGTRAA 712
|
490 500 510
....*....|....*....|....*....|....*....
gi 1080393322 474 IALVEEALTAADPATRSRATRAYLAACWHEVDFFDQADR 512
Cdd:PRK09517 713 IARVEKALENAGPEQRVDAARAFLSASVHEREFFDQATR 751
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
8-264 |
1.13e-109 |
|
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: 326.22 E-value: 1.13e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 8 LSIAGTDPTGGAGIQADLKSIAAAGGYGMSAVTALVAQNTQGVREVHTPPVEFLRAQLTAVASDVTIDAVKIGMLGSAAI 87
Cdd:COG0351 1 LTIAGSDPSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVTGVHPVPPEFVAAQLRAVLEDIPVDAIKIGMLGSAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 88 VAEVSRFLAQLSDVPVVLDPVMVATSGDRLLDRDAEAAVRE-LCARATVVTPNLKELAVLTQTaEATTLEEAIAHATAWS 166
Cdd:COG0351 81 IEAVAEILADYPLVPVVLDPVMVAKSGDRLLDEDAVEALRElLLPLATVVTPNLPEAEALLGI-EITTLDDMREAAKALL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 167 ADTRTTVIVKGGHLRGDLADNAVVTPDGaVHRVSCPRVDTPHTHGTGCSLSSALATRLGAGASLSDALSWSTRWLHEAIs 246
Cdd:COG0351 160 ELGAKAVLVKGGHLPGDEAVDVLYDGDG-VREFSAPRIDTGNTHGTGCTLSSAIAALLAKGLDLEEAVREAKEYVTQAI- 237
|
250
....*....|....*...
gi 1080393322 247 hAAALEVGQGHGPVDHGH 264
Cdd:COG0351 238 -RAALRLGMGHGPVNHFA 254
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
14-261 |
3.23e-102 |
|
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: 306.72 E-value: 3.23e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 14 DPTGGAGIQADLKSIAAAGGYGMSAVTALVAQNTQGVREVHTPPVEFLRAQLTAVASDVTIDAVKIGMLGSAAIVAEVSR 93
Cdd:pfam08543 1 DSSGGAGIQADLKTFSALGVYGMSVITALTAQNTLGVQGVHPLPPEFVAAQLDAVLEDIPVDAVKTGMLGSAEIIEAVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 94 FLAQLsDVPVVLDPVMVATSGDRLLDRDAEAAVRE-LCARATVVTPNLKELAVLTQTaEATTLEEAIAHATAWSADTRTT 172
Cdd:pfam08543 81 KLDKY-GVPVVLDPVMVAKSGDSLLDDEAIEALKEeLLPLATLITPNLPEAEALTGR-KIKTLEDMKEAAKKLLALGAKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 173 VIVKGGHLRGDLADNA-VVTPDGAVHRVSCPRVDTPHTHGTGCSLSSALATRLGAGASLSDALSWSTRWLHEAISHaaAL 251
Cdd:pfam08543 159 VLIKGGHLEGEEAVVTdVLYDGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKEYVTEAIRD--AL 236
|
250
....*....|
gi 1080393322 252 EVGQGHGPVD 261
Cdd:pfam08543 237 NLGKGHGPVN 246
|
|
| HMPP_kinase |
cd01169 |
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ... |
6-248 |
1.81e-101 |
|
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: 304.81 E-value: 1.81e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 6 RVLSIAGTDPTGGAGIQADLKSIAAAGGYGMSAVTALVAQNTQGVREVHTPPVEFLRAQLTAVASDVTIDAVKIGMLGSA 85
Cdd:cd01169 1 VVLTIAGSDSSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVFGVHPVPPEFVAAQLDAVLEDIPVDAIKIGMLGSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 86 AIVAEVSRFLAQLSDVPVVLDPVMVATSGDRLLDRDAEAAVRE-LCARATVVTPNLKELAVLTQTAEATTLEEAIAhATA 164
Cdd:cd01169 81 EIIEAVAEALKDYPDIPVVLDPVMVAKSGDSLLDDDAIEALRElLLPLATLITPNLPEAELLTGLEIATEEDMMKA-AKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 165 WSADTRTTVIVKGGHLRGDLADNAVVTPDGAVHRVScPRVDTPHTHGTGCSLSSALATRLGAGASLSDALSWSTRWLHEA 244
Cdd:cd01169 160 LLALGAKAVLIKGGHLPGDEAVDVLYDGGGFFEFES-PRIDTKNTHGTGCTLSSAIAANLAKGLSLEEAVREAKEYVTQA 238
|
....
gi 1080393322 245 ISHA 248
Cdd:cd01169 239 IRNA 242
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
1-262 |
4.07e-100 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 302.43 E-value: 4.07e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 1 MPAVPRVLSIAGTDPTGGAGIQADLKSIAAAGGYGMSAVTALVAQNTQGVREVHTPPVEFLRAQLTAVASDVTIDAVKIG 80
Cdd:PRK06427 1 MMKRPIALTIAGSDSGGGAGIQADLKTFQALGVYGMSAITALTAQNTLGVQRVHPIPPEFVAAQLDAVFSDIRIDAVKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 81 MLGSAAIVAEVSRFLAQLSDVPVVLDPVMVATSGDRLLDRDAEAAVRE-LCARATVVTPNLKELAVLTQTAEATTLEEAI 159
Cdd:PRK06427 81 MLASAEIIETVAEALKRYPIPPVVLDPVMIAKSGDPLLADDAVAALRErLLPLATLITPNLPEAEALTGLPIADTEDEMK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 160 AHATAWSADTRTTVIVKGGHLRGDL-ADNAVVTPDGaVHRVSCPRVDTPHTHGTGCSLSSALATRLGAGASLSDALSWST 238
Cdd:PRK06427 161 AAARALHALGCKAVLIKGGHLLDGEeSVDWLFDGEG-EERFSAPRIPTKNTHGTGCTLSAAIAAELAKGASLLDAVQTAK 239
|
250 260
....*....|....*....|....
gi 1080393322 239 RWLHEAISHaaALEVGQGHGPVDH 262
Cdd:PRK06427 240 DYVTRAIRH--ALEIGQGHGPVNH 261
|
|
| HMP-P_kinase |
TIGR00097 |
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ... |
7-262 |
6.40e-87 |
|
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: 268.01 E-value: 6.40e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 7 VLSIAGTDPTGGAGIQADLKSIAAAGGYGMSAVTALVAQNTQGVREVHTPPVEFLRAQLTAVASDVTIDAVKIGMLGSAA 86
Cdd:TIGR00097 1 ALTIAGSDSGGGAGIQADLKTFSALGVFGTSVITALTAQNTRGVTGVYPIPPDFVEAQLDAVFSDIPVDAAKTGMLASAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 87 IVAEVSRFLAQLSDVPVVLDPVMVATSGDRLLDRDAEAAVRE-LCARATVVTPNLKELAVLTQTaEATTLEEAIAHATAW 165
Cdd:TIGR00097 81 IVEAVARKLREYPVRPLVVDPVMVAKSGAPLLEEEAIEALRKrLLPLATLITPNLPEAEALLGT-KIRTEQDMIKAAKKL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 166 SADTRTTVIVKGGHLRGDLAdNAVVTPDGAVHRVSCPRVDTPHTHGTGCSLSSALATRLGAGASLSDALSWSTRWLHEAI 245
Cdd:TIGR00097 160 RELGPKAVLIKGGHLEGDQA-VDVLFDGGEIHILKAPRIETKNTHGTGCTLSAAIAANLAKGLSLKEAVKEAKEFVTGAI 238
|
250
....*....|....*..
gi 1080393322 246 SHaaALEVGQGHGPVDH 262
Cdd:TIGR00097 239 RY--GLNIGHGHGPLNH 253
|
|
| TenA_C-like |
cd19365 |
uncharacterized TenA_C proteins; This family of TenA proteins belongs to the TenA_C class as ... |
302-510 |
6.71e-87 |
|
uncharacterized TenA_C proteins; This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect. This family includes mostly uncharacterized TenA_C- like proteins.
Pssm-ID: 381700 [Multi-domain] Cd Length: 205 Bit Score: 265.91 E-value: 6.71e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 302 TARLWELTGDAWQSITQLPFIQALGTGTLREEDFAFYLAQDAQYLNQYSKALARLAALAPDAGAQLHWASGAAECLAVEM 381
Cdd:cd19365 1 TEALWEAIAPIYAAILAHPFIRELADGTLPREKFRFYLAQDALYLRDYARALALLAARAPDPEEQVFFARFAAGAIEVER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 382 SLHKDWIAHHtttvPSTALTAPSRVTSAYTDFLVSTTHTDDYVVAAAAVLPCYWLYAEVGLHLAAQNSPEHPYNAWITQY 461
Cdd:cd19365 81 ELHRSFLGEF----GIDAAAEPSPVTLAYTSFLLATAATGPYAVAVAAVLPCFWIYAEVGKRLAAAASPNHPYQDWIDTY 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1080393322 462 GGEEFLTGVRAAIALVEEALTAADPATRSRATRAYLAACWHEVDFFDQA 510
Cdd:cd19365 157 SDEEFAEAVRRAIAIVDRLAAEASPEERARMLEAFLRASRLEWMFWDAA 205
|
|
| PRK08573 |
PRK08573 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
4-261 |
1.76e-66 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 236297 [Multi-domain] Cd Length: 448 Bit Score: 221.53 E-value: 1.76e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 4 VPRVLSIAGTDPTGGAGIQADLKSIAAAGGYGMSAVTALVAQNTQGVREVHTPPVEFLRAQLTAVASDVTIDAVKIGMLG 83
Cdd:PRK08573 2 IPVALTIAGSDSGGGAGIEADLKTFAALGVHGAVAITSVTAQNTYEVRAIHDLPPEVVAAQIEAVWEDMGIDAAKTGMLS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 84 SAAIVAEVSRFLAQLsDVPVVLDPVMVATSGDRLLDRDA-EAAVRELCARATVVTPNLKELAVLTQTaEATTLEEAIAHA 162
Cdd:PRK08573 82 NREIIEAVAKTVSKY-GFPLVVDPVMIAKSGAPLLREDAvDALIKRLLPLATVVTPNRPEAEKLTGM-KIRSVEDARKAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 163 TAWSADTRTT-VIVKGGHLRGDLADNaVVTPDGAVHRVSCPRVDTPHTHGTGCSLSSALATRLGAGASLSDALSWSTRWL 241
Cdd:PRK08573 160 KYIVEELGAEaVVVKGGHLEGEEAVD-VLYHNGTFREFRAPRVESGCTHGTGCSFSAAIAAGLAKGLDPEEAIKTAKKFI 238
|
250 260
....*....|....*....|
gi 1080393322 242 HEAISHaaALEVGQGHGPVD 261
Cdd:PRK08573 239 TMAIKY--GVKIGKGHCPVN 256
|
|
| PLN02898 |
PLN02898 |
HMP-P kinase/thiamin-monophosphate pyrophosphorylase |
4-262 |
1.37e-65 |
|
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
Pssm-ID: 215486 [Multi-domain] Cd Length: 502 Bit Score: 220.41 E-value: 1.37e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 4 VPRVLSIAGTDPTGGAGIQADLKSIAAAGGYGMSAVTALVAQNTQGVREVHTPPVEFLRAQLTAVASDVTIDAVKIGMLG 83
Cdd:PLN02898 9 VPHVLTVAGSDSGAGAGIQADIKACAARGVYCTTAITAVTAQNTVGVQGVHAVPLDFVAEQLKSVLSDMPVDVVKTGMLP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 84 SAAIVAEVSRFLAQLSDVPVVLDPVMVATSGDRLLDRDAEAAVRE-LCARATVVTPNLKELAVLTQTAEATTLEEAIAHA 162
Cdd:PLN02898 89 SAEIVKVLCQALKEFPVKALVVDPVMVSTSGDVLAGPSILSALREeLLPLATIVTPNVKEASALLGGDPLETVADMRSAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 163 TAWSADTRTTVIVKGGHLRGDLADNAVVTPDGAVHRVSCPRVDTPHTHGTGCSLSSALATRLGAGASLSDALSWSTRWLH 242
Cdd:PLN02898 169 KELHKLGPRYVLVKGGHLPDSLDAVDVLYDGTEFHELRSSRIKTRNTHGTGCTLASCIAAELAKGSDMLSAVKVAKRYVE 248
|
250 260
....*....|....*....|.
gi 1080393322 243 EAISHAAALEVGQG-HGPVDH 262
Cdd:PLN02898 249 TALEYSKDIGIGNGaQGPFNH 269
|
|
| TenA |
COG0819 |
Aminopyrimidine aminohydrolase TenA (thiamine salvage pathway) [Coenzyme transport and ... |
302-510 |
4.93e-65 |
|
Aminopyrimidine aminohydrolase TenA (thiamine salvage pathway) [Coenzyme transport and metabolism];
Pssm-ID: 440581 [Multi-domain] Cd Length: 218 Bit Score: 210.12 E-value: 4.93e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 302 TARLWELTGDAWQSITQLPFIQALGTGTLREEDFAFYLAQDAQYLNQYSKALARLAALAPDAGAQLHWASGAAECLAVEM 381
Cdd:COG0819 4 SERLREAAAPIWEAILEHPFVQGLADGTLPREAFRHYLVQDYLYLEHFARALALAAAKAPDLEDMRFLAGLAAGLLEVEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 382 SLHKDWIAHHTTTVPSTALTAPSRVTSAYTDFLVSTTHTDDYVVAAAAVLPCYWLYAEVGLHLAA-QNSPEHPYNAWITQ 460
Cdd:COG0819 84 ALHERYAAELGISEEELEATPPSPTTRAYTSYLLAAAASGDYAELLAALLPCEWGYAEIGKRLAErPLPPDHPYAEWIET 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1080393322 461 YGGEEFLTGVRAAIALVEEALTAADPATRSRATRAYLAACWHEVDFFDQA 510
Cdd:COG0819 164 YASEEFQELVEWLIALLDRLAATASEAERERLEEAFRTASRLEYAFWDMA 213
|
|
| PTZ00347 |
PTZ00347 |
phosphomethylpyrimidine kinase; Provisional |
3-262 |
1.08e-53 |
|
phosphomethylpyrimidine kinase; Provisional
Pssm-ID: 240375 [Multi-domain] Cd Length: 504 Bit Score: 189.02 E-value: 1.08e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 3 AVPRVLSIAGTDPTGGAGIQADLKSIAAAGGYGMSAVTALVAQNTQGVREVHTPPVEFLRAQLTAVASDVTIDAVKIGML 82
Cdd:PTZ00347 229 KIPTVLTVSGSDSGGGAGHQADLKTLEALGVYSTSALTSLTAQNTKGVQQIQVVNEDFFAAQIDSVMSDFNISVVKLGLV 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 83 GSAAIVAEVSRflaQLSDVPVVLDPVMVATSGDRLL-DRDAEAAVRELCAR----ATVVTPNLKELAVLTQTAEATTLEE 157
Cdd:PTZ00347 309 PTARQLEIVIE---KLKNLPMVVDPVLVATSGDDLVaQKNADDVLAMYKERifpmATIITPNIPEAERILGRKEITGVYE 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 158 AIAHATAWSADTRTTVIVKGGHLRGDLADNAVVTPDGAVHR---VSCPRVDTPHTHGTGCSLSSALATRLGAGASLSDAL 234
Cdd:PTZ00347 386 ARAAAQALAQYGSRYVLVKGGHDLIDPEACRDVLYDREKDRfyeFTANRIATINTHGTGCTLASAISSFLARGYTVPDAV 465
|
250 260
....*....|....*....|....*....
gi 1080393322 235 SWSTRWLHEAISHAAALEVGQG-HGPVDH 262
Cdd:PTZ00347 466 ERAIGYVHEAIVRSCGVPLGQGtNRPLVH 494
|
|
| TenA_C_BhTenA-like |
cd19366 |
TenA_C proteins similar to Bacillus halodurans TenA; This family of TenA proteins belongs to ... |
302-510 |
7.25e-42 |
|
TenA_C proteins similar to Bacillus halodurans TenA; This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. This family includes Bacillus halodurans TenA which participates in a salvage pathway where the thiamine degradation product 2-methyl-4-formylamino-5-aminomethylpyrimidine (formylamino-HMP) is hydrolyzed first to amino-HMP by the YlmB protein, and the amino-HMP is then hydrolyzed by TenA to produce HMP. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect.
Pssm-ID: 381701 [Multi-domain] Cd Length: 213 Bit Score: 148.86 E-value: 7.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 302 TARLWELTGDAWQSITQLPFIQALGTGTLREEDFAFYLAQDAQYLNQYSKALARLAALAPDagaqLHWASGAAEC----L 377
Cdd:cd19366 2 SERLREKAKPIWEAGLEHPFVQGLGDGTLDKEKFKFYLKQDYLYLIDYARVFALGAAKADD----LETMGRFAELlhgtL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 378 AVEMSLHKDWIAHHTTTVPSTALTAPSRVTSAYTDFLVSTTHTDDYVVAAAAVLPCYWLYAEVGLHLAAQN--SPEHPYN 455
Cdd:cd19366 78 NTEMDLHRQYAAEFGITEEELEATEPSPTTLAYTSYMLRTAQTGTLAELLAALLPCAWGYAEIGKRLAEQGgaLEHNPYR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1080393322 456 AWITQYGGEEFLTGVRAAIALVEEALTAADPATRSRATRAYLAACWHEVDFFDQA 510
Cdd:cd19366 158 EWIEMYSSDEFTELADWLIDLLDELAEGKSEAELERLEEIFLTSSRYEYMFWDMA 212
|
|
| TenA_PqqC-like |
cd16099 |
TenA-like proteins including TenA_C and TenA_E proteins, as well as pyrroloquinoline quinone ... |
313-509 |
1.17e-40 |
|
TenA-like proteins including TenA_C and TenA_E proteins, as well as pyrroloquinoline quinone (PQQ) synthesis protein C; TenA proteins participate in thiamin metabolism and can be classified into two classes: TenA_C which has an active site Cys, and TenA_E which does not; TenA_E proteins often have a pair of structurally conserved Glu residues in the active site. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product amino-HMP (4-amino-5-amino-methyl-2-methylpyrimidine) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway; the role of TenA_E proteins is less clear. Arabidopsis thaliana TenA_E hydrolyzes amino-HMP to AMP, and the N-formyl derivative of amino-HMP to amino-HMP, but does not hydrolyze thiamin. Bacillus subtilis TenA_C can hydrolyze amino-HMP to AMP and can catalyze the hydrolysis of thiamin. Saccharomyces cerevisiae THI20 includes a C-terminal tetrameric TenA-like domain fused to an N-terminal ThiD domain, and participates in thiamin biosynthesis, degradation and salvage; the TenA-like domain catalyzes the production of HMP from thiamin degradation products (salvage). Bacillus halodurans TenA_C participates in a salvage pathway where the thiamine degradation product 2-methyl-4-formylamino-5-aminomethylpyrimidine (formylamino-HMP) is hydrolyzed first to amino-HMP by the YlmB protein, and the amino-HMP is then hydrolyzed by TenA to produce HMP. Helicobacter pylori TenA_C is also thought to catalyze a salvage reaction but the pyrimidine substrate has not yet been identified. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect; Pyrococcus furiosus TenA_E lacks appropriate surface charges for DNA interactions. This family also includes bacterial coenzyme pyrroloquinoline quinone (PQQ) synthesis protein C (PQQC), an oxidase involved in the final step of PQQ biosynthesis, and CADD, a Chlamydia protein that interacts with death receptors.
Pssm-ID: 381691 [Multi-domain] Cd Length: 196 Bit Score: 145.19 E-value: 1.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 313 WQSITQLPFIQALGTGTLREEDFAFYLAQDAQYLNQYSKALARLAALAPDAGAQLHWASgAAECLAVEMSLHKDWIAHHT 392
Cdd:cd16099 2 WDAILNHPFVQELAAGTLPREKFRYYLAQDYYYLKDFARALALAAAKAPDLELRTFLAE-LINVLDDELELHEKLLAELG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 393 TTVPSTALTAPSRVTSAYTDFLVSTTHTDDYVVAAAAVLPCYWLYAEVGLHLAAQNSPEHPYNAWITQYGGEEFLTGVRA 472
Cdd:cd16099 81 ISEEDLSEAEPNPATLAYTNHLLRVAARGTPAEGLAALLPCYWSYGEIGRRLAASLPEHPPYRFWIDFYASDEYQELVEE 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 1080393322 473 AIALVEEaLTAADPATRSRATRAYLAACWHEVDFFDQ 509
Cdd:cd16099 161 LLQLLDQ-LAAAGEEEKEELKEIFLTSLRYELMFWDA 196
|
|
| TenA_C_BsTenA-like |
cd19364 |
TenA_C proteins similar to Bacillus subtilis TenA; This family of TenA proteins belongs to the ... |
302-510 |
3.26e-40 |
|
TenA_C proteins similar to Bacillus subtilis TenA; This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. This family includes Bacillus subtilis TenA which has been shown to be a thiaminase II, catalyzing the hydrolysis of thiamine into HMP and 5-(2-hydroxyethyl)-4-methylthiazole (THZ), within thiamine metabolism. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect.
Pssm-ID: 381699 [Multi-domain] Cd Length: 212 Bit Score: 144.25 E-value: 3.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 302 TARLWELTGDAWQSITQLPFIQALGTGTLREEDFAFYLAQDAQYLNQYSKALARLAALAPDAGAQLHWASGAAECLAVEM 381
Cdd:cd19364 2 TEELREAADPLWQKSFEHPFIQGLADGTLPLETFRYYLIQDAYYLKHFAKLHALAAAKADDPAIKALLLEGAQGLAEGEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 382 SLHKDWIAHHTTTVPSTALTAPSRVTSAYTDFLVSTTHTDDYVVAAAAVLPCYWLYAEVGLHLAAQNSPEHPYNAWITQY 461
Cdd:cd19364 82 ALRETFFKELGITEEEIAQTPPAPTAYHYVSHMYRQLNEGSVAEAVAALLPCYWLYQEIGERLADAGSPVPLYQRWIDTY 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1080393322 462 GGEEFLTGVRAAIALVEEALTAADPATRSRATRAYLAACWHEVDFFDQA 510
Cdd:cd19364 162 ASDEFTESVQQQIDLVDRLAEEASEEEREKMKQAFLISSYYELQFWEMA 210
|
|
| PRK12412 |
PRK12412 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
4-263 |
4.49e-40 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183512 [Multi-domain] Cd Length: 268 Bit Score: 145.88 E-value: 4.49e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 4 VPRVLSIAGTDPTGGAGIQADLKSIAAAGGYGMSAVTALVAQN--TQGVREVHTPPVEFLRAQLTAVASDVTIDAVKIGM 81
Cdd:PRK12412 1 LNKALTIAGSDTSGGAGIQADLKTFQELGVYGMTSLTTIVTMDphNGWAHNVFPIPASTLKPQLETTIEGVGVDALKTGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 82 LGSAAIVAEVSRFLAQLSDVPVVLDPVMVATSGDRLLDRDAEAAVRE-LCARATVVTPNLKELAVLTQTAEATT--LEEA 158
Cdd:PRK12412 81 LGSVEIIEMVAETIEKHNFKNVVVDPVMVCKGADEALHPETNDCLRDvLVPKALVVTPNLFEAYQLSGVKINSLedMKEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 159 IAHATAWSADtrtTVIVKGGHLRGdlADNAV-VTPDGAVHRV-SCPRVDTPHTHGTGCSLSSALATRLGAGASLSDALSW 236
Cdd:PRK12412 161 AKKIHALGAK---YVLIKGGSKLG--TETAIdVLYDGETFDLlESEKIDTTNTHGAGCTYSAAITAELAKGKPVKEAVKT 235
|
250 260
....*....|....*....|....*..
gi 1080393322 237 STRWLHEAISHAAALEvgQGHGPVDHG 263
Cdd:PRK12412 236 AKEFITAAIRYSFKIN--EYVGPTHHG 260
|
|
| PRK12616 |
PRK12616 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
6-262 |
3.98e-39 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183624 Cd Length: 270 Bit Score: 143.26 E-value: 3.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 6 RVLSIAGTDPTGGAGIQADLKSIAAAGGYGMSAVTALVAQNTQGVREVHTPPV--EFLRAQLTAVASDVTIDAVKIGMLG 83
Cdd:PRK12616 5 KALTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAMDPENSWDHQVFPIdtDTIRAQLSTIVDGIGVDAMKTGMLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 84 SAAIVAEVSRFLAQLSDVPVVLDPVMVATSGDRLLDRDAEAAVRELCAR-ATVVTPNLKELAVLTQTAEATTLEEAIAHA 162
Cdd:PRK12616 85 TVDIIELAADTIKEKQLKNVVIDPVMVCKGANEVLYPEHAEALREQLAPlATVITPNLFEAGQLSGMGEIKTVEQMKEAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 163 TAWSA-DTRTTVIVKGGHLRGDLADNavVTPDG-AVHRVSCPRVDTPHTHGTGCSLSSALATRLGAGASLSDALSWSTRW 240
Cdd:PRK12616 165 KKIHElGAQYVVITGGGKLKHEKAVD--VLYDGeTAEVLESEMIDTPYTHGAGCTFSAAVTAELAKGSEVKEAIYAAKEF 242
|
250 260
....*....|....*....|..
gi 1080393322 241 LHEAISHaaALEVGQGHGPVDH 262
Cdd:PRK12616 243 ITAAIKE--SFPLNQYVGPTKH 262
|
|
| COG1992 |
COG1992 |
Predicted transcriptional regulator fused phosphomethylpyrimidine kinase (thiamin biosynthesis) ... |
17-262 |
2.04e-31 |
|
Predicted transcriptional regulator fused phosphomethylpyrimidine kinase (thiamin biosynthesis) [General function prediction only];
Pssm-ID: 441595 [Multi-domain] Cd Length: 432 Bit Score: 126.02 E-value: 2.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 17 GGAGIQADLKSIAAAGGYGMSAVTALVAQNTQGVREVHTPPVEFLRAQLTAVASDVTIDAVKIGMLGSAAIV-AEVSRFL 95
Cdd:COG1992 2 GGGGGGADAKTAAALGAGGGGTTTAVTVTATTTVTGVGSDPPPPVEVQQQAVAADDDVDDAKTGMLMTATIVeVVAVVVK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 96 AQLSDVPVVLDPVMVATSGDRLLDRDAEAAVRELcARATVVTPNLKELAVLTQTAEATTLEEAIAHATAWSADTRTTVIV 175
Cdd:COG1992 82 SRDKPLVVVVVPVAVAAAGLGLLLAEAELAKLLL-PLLATVTPNEPEVEELLLPTIRSLLAEARAARLALQEEGADALGV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 176 KGGHLRGDLADNaVVTPDGAVHRVSCPRVDTPHTHGTGCSLSSALATRLGAGASLSDALSWSTRWLHEAISHaaALEVGQ 255
Cdd:COG1992 161 KGGHVSGDAVVD-VLEDERDVETFRHPRLVTEATHGSGCTFSAAIAALLAKGLSLEEAVRGAKLFLLHAIRY--GLLVGK 237
|
....*..
gi 1080393322 256 GHGPVDH 262
Cdd:COG1992 238 GVGPVNH 244
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
6-248 |
3.97e-31 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 120.94 E-value: 3.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 6 RVLSIAGTDPTGGAGIQADLKSIAAAGGYGMSAVTALVAQNTQGVrEVHTPPVEFLRAQLTAVaSDVTIDAVKIGMLGSA 85
Cdd:PRK12413 5 YILAISGNDIFSGGGLHADLATYTRNGLHGFVAVTCLTAMTEKGF-EVFPVDKEIFQQQLDSL-KDVPFSAIKIGLLPNV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 86 AIVAEVSRFLAQLSDVPVVLDPVMVATSGDrlldrDAE-AAVRELCAR----ATVVTPNLKELAVLTQTaEATTLEEAIA 160
Cdd:PRK12413 83 EIAEQALDFIKGHPGIPVVLDPVLVCKETH-----DVEvSELRQELIQffpyVTVITPNLVEAELLSGK-EIKTLEDMKE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 161 HATAWSADTRTTVIVKGGHlRGDlADNAV-VTPDG-AVHRVSCPRVDTPHThGTGCSLSSALATRLGAGASLSDALSWST 238
Cdd:PRK12413 157 AAKKLYDLGAKAVVIKGGN-RLS-QKKAIdLFYDGkEFVILESPVLEKNNI-GAGCTFASSIASQLVKGKSPLEAVKNSK 233
|
250
....*....|
gi 1080393322 239 RWLHEAISHA 248
Cdd:PRK12413 234 DFVYQAIQQS 243
|
|
| TenA_C_ScTHI20-like |
cd19367 |
TenA_C family similar to the C-terminal TenA_C domain of Saccharomyces cerevisiae THI20 ... |
311-510 |
1.98e-27 |
|
TenA_C family similar to the C-terminal TenA_C domain of Saccharomyces cerevisiae THI20 protein; This TenA family belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. Saccharomyces cerevisiae THI20 includes a C-terminal tetrameric TenA-like domain fused to an N-terminal HMP kinase/HMP-P kinase (ThiD-like) domain, and participates in thiamin biosynthesis, degradation and salvage; the TenA-like domain catalyzes the production of HMP from thiamin degradation products (salvage). A majority of this family are single-domain TenA_C- like proteins; some however have additional domains such as a ThiD domain. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect.
Pssm-ID: 381702 [Multi-domain] Cd Length: 204 Bit Score: 109.14 E-value: 1.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 311 DAWQSITQLPFIQALGTGTLREEDFAFYLAQDAQYLNQYSKALARLAALAPDAgAQLHWASGAAECLAVEMSLHKDWIAH 390
Cdd:cd19367 1 PIWKAYTNHPFVRQLADGTLPLESFRHYLKQDYLYLIHYARAHALAAYKAPTL-EDIRAAAAILLAILEEMELHVKYCAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 391 HTTTVPSTALTAPSRVTSAYTDFLVSTTHTDDYVVAAAAVLPCYWLYAEVGLHLAAQ---NSPEHPYNAWITQYGGEEFL 467
Cdd:cd19367 80 WGISEEELEATPESPATLAYTRYVLDVGLSGDLLDLLVALAPCLLGYGEIGLRLAADpatKLEGNPYWSWIETYASDEYQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1080393322 468 TGVRAAIALVEEALTAADPATR-SRATRAYLAACWHEVDFFDQA 510
Cdd:cd19367 160 EAVREGIELLEKLAAERPSPARlEELVKIFATATRLEIGFWDMG 203
|
|
| PTZ00493 |
PTZ00493 |
phosphomethylpyrimidine kinase; Provisional |
1-248 |
2.25e-26 |
|
phosphomethylpyrimidine kinase; Provisional
Pssm-ID: 240440 Cd Length: 321 Bit Score: 109.31 E-value: 2.25e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 1 MPAVPRVLSIAGTDPTGGAGIQADLKSIAAAGGYGMSAVTALVAQNTQGVREVHTPPVEFLRAQLTAVASDVTIDAVKIG 80
Cdd:PTZ00493 1 MEGVSNILSIAGSDSCGGAGMQADIKTAMGLGCHCCTALVVLTAQNTKEVKRIVEIEEKFIVEQLDSIFADVTIDVVKLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 81 MLGSAAIVAEVSRFLAQLS-----DVPVVLDPVMVATSGDRLLDR--DAEAAVRELCARATVVTPNLKELAVLTQT---- 149
Cdd:PTZ00493 81 VLYSKKIISLVHNYITNMNkkrgkKLLVVFDPVFVSSSGCLLVENleYIKFALDLICPISCIITPNFYECKVILEAldcq 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 150 -----AEATTLEEAIAHATAWSA--------DTRTT-----------VIVKGGHLRGDLA---DNAVVTPDGAVHRVSCP 202
Cdd:PTZ00493 161 mdlskANMTELCKLVTEKLNINAclfkscnvGENSAeenevyavdhlCIRNVGSYPTGEKqqiDAGGVTYLYDVYKLRSK 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1080393322 203 RVDTPHTHGTGCSLSSALATRLGAGASLSDALSWSTRWLHEAISHA 248
Cdd:PTZ00493 241 RKPGKDIHGTGCTLSTAIACYLAKKHNILQSCIESKKYIYNCIRYA 286
|
|
| PTZ00347 |
PTZ00347 |
phosphomethylpyrimidine kinase; Provisional |
294-510 |
2.96e-26 |
|
phosphomethylpyrimidine kinase; Provisional
Pssm-ID: 240375 [Multi-domain] Cd Length: 504 Bit Score: 111.98 E-value: 2.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 294 HVSAAGPETARLWELTGDAWQSITQLPFIQALGTGTLREEDFAFYLAQDAQYLNQYSKALARLAA---LAPDAGAQLHWA 370
Cdd:PTZ00347 6 HEPVFGGLSEALWKENQDLAMMSLHLPFVQGLGDGTLDQNAFRTYIAQDTLYLNGYIRILSYCITksdVTATGGGLLELL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 371 SGAAECLAvemSLHKDWIahhtttvPSTALTAPSRVTSAYTDFLVSTTHTDDY--VVAAAAVLPCYWLYAEVGLHLAAQN 448
Cdd:PTZ00347 86 KGVLEELK---NCHHHYI-------DNPDAAGPEAACRKYVDFLLASGNADTLgpSVVIAAVIPCARLYAWVGQELTNEV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080393322 449 --SPEHPYNAWITQYGGEEFLTGVRAAIALVEealTAADPATRSRATRAYLAACWHEVDFFDQA 510
Cdd:PTZ00347 156 elTESHPFRRWLLSYSDEPINTSVEQLESLLD---KYIRPGEFSEVAQAYRRAMELEYDFFDSF 216
|
|
| TenA_C_AtTH2-like |
cd19368 |
TenA_C family similar to the N-terminal TenA_C domain of Arabidopsis thaliana thiamine ... |
320-509 |
5.37e-26 |
|
TenA_C family similar to the N-terminal TenA_C domain of Arabidopsis thaliana thiamine requiring 2; This TenA family belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. Arabidopsis thaliana TH2 is an orphan enzyme thiamin monophosphate phosphatase which has a haloacid dehalogenase (HAD) family domain fused to its TenA_C domain, it's TenA_C domain has thiamin salvage hydrolase activity against amino-HMP. This family includes mostly uncharacterized single-domain TenA_C- like proteins; some however have additional domains such as a HAD family domain or a kinase domain It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect.
Pssm-ID: 381703 [Multi-domain] Cd Length: 210 Bit Score: 105.40 E-value: 5.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 320 PFIQALGTGTLREEDFAFYLAQDAQYLNQYSKALARLAALAPD--AGAQLHW-ASGAAEclavEMSLH----KDWIAHHT 392
Cdd:cd19368 20 PFVVGLAAGNLPLDSFRHYISQDAHFLEAFARAYELAEAKADDdeDKKAIRElRKGVLE----ELKLHdsyaEEWGVDLP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 393 TTVPstaltaPSRVTSAYTDFLVSTTHTDDYVVA--AAAVLPCYWLYAEVGLHLAA--QNSPEHPYNAWITQYGGEEFLt 468
Cdd:cd19368 96 KEVT------PDPATRKYTDFLLATASGKVKVAAytLAAMAPCMRLYAFLGQELARalDDTEDHPYKKWIDTYSSQEFE- 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1080393322 469 gvraAIALVEEALTAADPATRSRATRAYLAACWH-----EVDFFDQ 509
Cdd:cd19368 169 ----ALALQLEDLLDKLSASLTGEELEALEKLYRramklEVEFFAA 210
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
73-251 |
9.46e-26 |
|
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: 106.39 E-value: 9.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 73 TIDAVKIGMLGSAAIVAEVSRFLAQL----SDVPVVLDPVMvatsGD--RLL---DRDAEAAVRELCARATVVTPNLKEL 143
Cdd:COG2240 74 EFDAVLSGYLGSAEQGDIIADFVARVkaanPDALYLCDPVM----GDngKGYyvfPGIAEFIMRRLVPLADIITPNLTEL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 144 AVLTQTaEATTLEEAIAHATAWSADTRTTVIVKGGHLRGDLAD---NAVVTPDGAVHrVSCPRVDtPHTHGTGCSLSSAL 220
Cdd:COG2240 150 ALLTGR-PYETLEEALAAARALLALGPKIVVVTSVPLDDTPADkigNLAVTADGAWL-VETPLLP-FSPNGTGDLFAALL 226
|
170 180 190
....*....|....*....|....*....|.
gi 1080393322 221 ATRLGAGASLSDALSWSTRWLHEAISHAAAL 251
Cdd:COG2240 227 LAHLLRGKSLEEALERAAAFVYEVLERTAAA 257
|
|
| TENA_THI-4 |
pfam03070 |
TENA/THI-4/PQQC family; Members of this family are found in all the three major phyla of life: ... |
313-510 |
2.70e-25 |
|
TENA/THI-4/PQQC family; Members of this family are found in all the three major phyla of life: archaebacteria, eubacteria, and eukaryotes. In Bacillus subtilis, TENA is one of a number of proteins that enhance the expression of extracellular enzymes, such as alkaline protease, neutral protease and levansucrase. The THI-4 protein, which is involved in thiamine biosynthesis, is also a member of this family. The C-terminal part of these proteins consistently show significant sequence similarity to TENA proteins. This similarity was first noted with the Neurospora crassa THI-4. This family includes bacterial coenzyme PQQ synthesis protein C or PQQC proteins. Pyrroloquinoline quinone (PQQ) is the prosthetic group of several bacterial enzymes,including methanol dehydrogenase of methylotrophs and the glucose dehydrogenase of a number of bacteria. PQQC has been found to be required in the synthesis of PQQ but its function is unclear. The exact molecular function of members of this family is uncertain.
Pssm-ID: 397272 [Multi-domain] Cd Length: 210 Bit Score: 103.20 E-value: 2.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 313 WQSITQLPFIQALGTGTLREEDFAFYLAQDAQYLNQYSKALARLAALAPDAGAQLHWASGAAECLAVEMSLHKDWIAHHT 392
Cdd:pfam03070 8 WKFYINHPFVQALAKGTLPREQFQGYVIQDYLYLVNFARVLAIIASKSPDLEVRREWENRIVDHDGNEIELHLRLAEALG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 393 TTVPSTALTAPSRVTSAYTDFLVSTTHTDDYVVAAAAVLPCYWLYAEVGLHLAA--QNSPEHPYNAWITQYGGEEFLTGV 470
Cdd:pfam03070 88 LSREDLSAYKPLPATRAYVRYLLDFARRGSWLEAVAALLPCLFVYQEIASRLGEkiRALEGPEYYEWVKTYASEYFRAAV 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1080393322 471 RAAIALVEEALTAADPATRSRATRAYLAACWHEVDFFDQA 510
Cdd:pfam03070 168 EEAKRLLDRLLAYVSDEQLEELQEIFLKALEFEYSFWTMA 207
|
|
| TenA_C_SaTenA-like |
cd19360 |
TenA_C proteins similar to Staphylococcus aureus TenA (SaTenA); This family of TenA proteins ... |
302-509 |
2.76e-25 |
|
TenA_C proteins similar to Staphylococcus aureus TenA (SaTenA); This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. This family includes Staphylococcus aureus TenA (SaTenA) which plays two essential roles in thiamin metabolism: in the deamination of aminopyrimidine to HMP, and in hydrolyzing thiamin into HMP and 5-(2-hydroxyethyl)4-methylthiazole (THZ). It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect. SaTenA is then also a putative transcriptional regulator controlling the secretion of extracellular proteases such as subtilisin-type proteases in bacteria. This family includes mostly uncharacterized TenA like proteins.
Pssm-ID: 381695 [Multi-domain] Cd Length: 211 Bit Score: 103.44 E-value: 2.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 302 TARLWELTGDAWQSITQLPFIQALGTGTLREEDFAFYLAQDAQYLNQYSKALARLAALAPD-AGAQLHWasgaaecLAVE 380
Cdd:cd19360 2 SEELREEAQPILEAIYAHPFVQGIAAGELPKEALIHYVQQDYEYLNAFLKVYALAIAKSDTrEDMRFFL-------EQIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 381 MSLHKDWIAHHT------TTVPSTALTAPSRVTSAYTDFLVSTTHTDDYVVAAAAVLPCYWLYAEVGLHLAA--QNSPEH 452
Cdd:cd19360 75 FILNGESHAHQNlcevagVDYEELQGAPWAPTADHYIKHMYYAARTGDLGDILAALLPCPWTYVELAKRLIEegKPTPDN 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1080393322 453 PYNAWITQY--GGEEFLTGVRAAIaLVEEALTaADPATRSRATRAYLAACWHEVDFFDQ 509
Cdd:cd19360 155 PFYEWIDFYadDEMDGLTDQLFAR-LDRLAEK-ASEEERERAKQAFLKSCQLEWRFWEM 211
|
|
| salvage_TenA |
TIGR04306 |
thiaminase II; The TenA protein of Bacillus subtilis and Staphylococcus aurues, and the ... |
313-510 |
3.37e-25 |
|
thiaminase II; The TenA protein of Bacillus subtilis and Staphylococcus aurues, and the C-terminal region of trifunctional protein Thi20p from Saccharomyces cerevisiae, perform cleavages on thiamine and related compounds to produce 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP), a substrate a salvage pathway for thiamine biosynthesis. The gene symbol tenA, for Transcription ENhancement A, reflects a misleading early characterization as a regulatory protein. This family is related to PqqC from the PQQ biosynthesis system (see TIGR02111), heme oxygenase (pfam01126), and CADD (Chlamydia protein Associating with Death Domains), a putative folate metabolism enzyme (see TIGR04305).
Pssm-ID: 213919 [Multi-domain] Cd Length: 208 Bit Score: 103.04 E-value: 3.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 313 WQSITQLPFIQALGTGTLREEDFAFYLAQDAQYLNQYSKALARLAALAPDAGAQLHWASGAAECLAVEMSLHKDWIAHHT 392
Cdd:TIGR04306 5 WDDYINHPFVQKIGDGTLERDKFRFYIEQDYAYLVEYAKVHALGGSKACDEDMEKELVEQIQGGVETEMGQHKRLAEVLG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 393 TTVPSTALTA-PSRVTSAYTDFLVSTTHTDDYVVAAAAVLPCYWLYAEVGLHLAA-QNSPEHP-YNAWITQYGGEEFLTG 469
Cdd:TIGR04306 85 ISDEEYFQKIkPGPALRSYTSYMYDVSRRGNWQELVAALLPCLWGYGEAATKLKGkHTAPEHSvYHKWIETYSSSWFREA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1080393322 470 VRAAIALVEEALTAADPATRSRATRAYLAACWHEVDFFDQA 510
Cdd:TIGR04306 165 VNEGENLLNHLAETSSPEELEKLKTIFAESCEYEYNFWTMA 205
|
|
| TenA_C_HP1287-like |
cd19361 |
TenA_C proteins similar to Helicobacter pylori TenA (HP1287; This family of TenA proteins ... |
302-508 |
6.07e-25 |
|
TenA_C proteins similar to Helicobacter pylori TenA (HP1287; This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. This family includes Helicobacter pylori TenA (HP1287) protein which is thought to catalyze a salvage reaction in thiamin metabolism, however its pyrimidine substrate has not yet been identified. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect. HP1287 may contribute to stomach colonization and persistence.
Pssm-ID: 381696 [Multi-domain] Cd Length: 212 Bit Score: 102.27 E-value: 6.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 302 TARLWELTGDAWQSITQLPFIQALGTGTLREEDFAFYLAQDAQYLNQYSKALARLAALAPDAGAQLHWASGAAECLAVEM 381
Cdd:cd19361 2 SERLYEAVEDIWDSYYEHPFVQGIADGTLDIEKFRFYMIQDYLYLLDYAKVFALGVAKAKDEEVMRFFADLINAILNEEM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 382 SLHKDWIAHHTTTVPSTALTAPSRVTSAYTDFLVSTTHTDDYVVAAAAVLPCYWLYAEVGLHLAAQN--SPEHP-YNAWI 458
Cdd:cd19361 82 DIHRGYMKRLGITEEEIENTKPALDNLSYTSYMLSVAYEGGIAEILAAILSCSWSYEYIAKKLVERYpaALEHEfYGEWV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1080393322 459 TQYGGEEFLTGVRAAIALVEEALTAADPATRSRATRAYLAACWHEVDFFD 508
Cdd:cd19361 162 KGYSSEEYAEANQELIDLLDRLTEDISEEQIEKLEEIFVNCSRYELKFWD 211
|
|
| TenA_C_PH1161-like |
cd19363 |
uncharacterized TenA_C proteins similar to Pyrococcus horikoshii PH1161; This family of TenA ... |
302-510 |
2.06e-23 |
|
uncharacterized TenA_C proteins similar to Pyrococcus horikoshii PH1161; This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; only one of the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect. This family includes functionally uncharacterized TenA like proteins such as Pyrococcus horikoshii PH1161 protein.
Pssm-ID: 381698 [Multi-domain] Cd Length: 210 Bit Score: 98.17 E-value: 2.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 302 TARLWELTGDAWQSITQLPFIQALGTGTLREEDFAFYLAQDAQYLNQYSKALARLAALAPDAGAQLHWASGAAECLAVEM 381
Cdd:cd19363 2 TGKLRRDADDIWKKILNHPFVVELYSGTLPMEKFKFYLLQDYNYLVGSTKNLSILASKAESLDLMRELLELAYGEATTEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 382 SLHKDWIAHHTTTvPSTALTA-PSRVTSAYTDFLVSTTHTDDYVVAAAAVLPCYWLYAEVGLHLAAQ--NSPEHPYNAWI 458
Cdd:cd19363 82 ANYEELLDELGLS-LEDAIKVePFPTNVAYMNFLLSTSSLGSFYEGLAALLPCFWSYLEIAEYHKDKlsENPNDIYRDWA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1080393322 459 TQYGGEEFLTGVRAAIALVEEALTAADpatRSRATRAYLAACWHEVDFFDQA 510
Cdd:cd19363 161 SVYLSKEYKELVERLRRIVDKYGEGEP---FEKLKRIFKTASKYEYMFWDAA 209
|
|
| TenA_C_Bt3146-like |
cd19359 |
uncharacterized TenA_C proteins similar to Bacteroides thetaiotaomicron Bt3146; This family of ... |
302-508 |
1.66e-21 |
|
uncharacterized TenA_C proteins similar to Bacteroides thetaiotaomicron Bt3146; This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; only one of the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect. This family includes mostly uncharacterized TenA-like proteins such as Bacteroides thetaiotaomicron Bt3146.
Pssm-ID: 381694 [Multi-domain] Cd Length: 206 Bit Score: 92.41 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 302 TARLWELTGDAWQSITQLPFIQALGTGTLREEDFAFYLAQDAQYLNQYSKALARLAALAPDAG-AQLHWASGAAECLAVE 380
Cdd:cd19359 1 IDKLWNDNEDLWDKALNNPFCQGMADGTLDLDGFGYYMVQDYYYCINYVRFKALRAAKAPDPDlLAFLAAKIKSYLDYAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 381 MSLhKDWIAHhtTTVPSTALTA-PSRVTSAYTDFLVSTTHTDDYVVAAAAVLPCYWLYAEVGLHL--AAQNSPEHPYNAW 457
Cdd:cd19359 81 DFL-KTCHIK--LGIPDVVDGVkPSPALKAYVDFERSVAESEDWFYLLVAMIPCIYLWYWLANQLneDPSDKNTNFYKTW 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1080393322 458 ITQYGGEEflTGVRAAIALVEEALtAADPATRSRATRAYLAACWHEVDFFD 508
Cdd:cd19359 158 IEPNLPDP--SSAKQLEFFLNANA-AWSKIDREKANEIFRQAMQLEINFFN 205
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
75-245 |
3.39e-20 |
|
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: 89.95 E-value: 3.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 75 DAVKIGMLGSAAIVAEVSRFLAQL----SDVPVVLDPVMvatsGD--RLL--DRDAEAAVRE-LCARATVVTPNLKELAV 145
Cdd:cd01173 74 DAVLTGYLGSAEQVEAVAEIVKRLkeknPNLLYVCDPVM----GDngKLYvvAEEIVPVYRDlLVPLADIITPNQFELEL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 146 LTQTaEATTLEEAIAHATAWSADTRTTVIVKGGHLRGDLADNAVVTPDGAVHRVSCPRVDTP-HTHGTGCSLSSALATRL 224
Cdd:cd01173 150 LTGK-KINDLEDAKAAARALHAKGPKTVVVTSVELADDDRIEMLGSTATEAWLVQRPKIPFPaYFNGTGDLFAALLLARL 228
|
170 180
....*....|....*....|.
gi 1080393322 225 GAGASLSDALSWSTRWLHEAI 245
Cdd:cd01173 229 LKGKSLAEALEKALNFVHEVL 249
|
|
| TenA_E_Spr0628-like |
cd19358 |
TenA_E proteins similar to Streptococcus pneumoniae Spr0628 and Saccharomyces cerevisiae S288C ... |
302-510 |
2.74e-19 |
|
TenA_E proteins similar to Streptococcus pneumoniae Spr0628 and Saccharomyces cerevisiae S288C PET18; This family of TenA proteins belongs to the TenA_E class, and lacks the conserved active site Cys residue of the TenA_C class; most have a pair of structurally conserved Glu residues in the active site. TenA_C proteins (EC 3.5.99.2; aminopyrimidine aminohydrolase, also known as thiaminase II) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway; the role of TenA_E proteins is less clear. Arabidopsis thaliana TenA_E (not belonging to this family) hydrolyzes amino-HMP to AMP, and the N-formyl derivative of amino-HMP to amino-HMP. Members of this family include the putative thiaminase Streptococcus pneumoniae Spr0628, and Saccharomyces cerevisiae S288C PET18, a protein of unknown function whose expression is induced in the absence of thiamin. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect. Many proteins in this family have yet to be characterized.
Pssm-ID: 381693 [Multi-domain] Cd Length: 209 Bit Score: 86.08 E-value: 2.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 302 TARLWELTGDAWQSITQLPFIQALGTGTLREEDFAFYLAQDAQYLNQYSKALARLAALAPDAGAQLHWASGAAECLAVEM 381
Cdd:cd19358 2 SDRLRAANAEDWDAAVTHRFVRELCAGTLPDAVLARYLVQDYQFVETFLRLLGKAVAKAPDLEAKLRLARFLGFLANDEN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 382 SLHKDWIAHHTTTVPSTALTAPSRVTSAYTDFLVSTTHTDDYVVAAAAVLPCYWLYAEVGLHlAAQNSPEHPYNA-WITQ 460
Cdd:cd19358 82 DYFERAFAALGVSEADREAPPLLPATRAFIDLMLEAARSGSYAEILTVLLVAEWLYLDWASR-AAAAAPLRFKHQeWIDL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1080393322 461 YGGEEFLTGVRAAIALVEEAltAADPATRSRATRAYLAACWHEVDFFDQA 510
Cdd:cd19358 161 HSGPEFEAWVDFLRDEVDRV--GPTEEERERLEAVFARAVELEIAFFDAA 208
|
|
| TenA_C-like |
cd19369 |
uncharacterized TenA_C proteins; This family of TenA proteins belongs to the TenA_C class as ... |
311-508 |
1.90e-18 |
|
uncharacterized TenA_C proteins; This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect. This family includes mostly uncharacterized TenA_C- like proteins.
Pssm-ID: 381704 [Multi-domain] Cd Length: 202 Bit Score: 83.82 E-value: 1.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 311 DAWQSITQLPFIQALGTGTLREEDFAFYLAQDAQYLNQYSKALARLAALAPDAGAQLHWASGAAECLAVEMSLH------ 384
Cdd:cd19369 1 PIWEQYLEHPFIKELGEGTLDKEKFKNYLIQDSLYLKEYAKVFAMGIYKSRTMKEMQFFYSSLSFVNEDETATRikylke 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 385 ----KDWIAHHTttvpstaltaPSRVTSAYTDFLVSTTHTDDYVVAAAAVLPCYWLYAEVGLHLAAQNSPE---HPYNAW 457
Cdd:cd19369 81 fgltDEDIEKIE----------PLPENKAYTDYMLGIAKTGDVKEILMAVLPCMLSYYYIFKELVKKYKDNlesNPYKDW 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1080393322 458 ITQYGGEEFLTGVRAAIALVEEALTAADPATRSRATRAYLAACWHEVDFFD 508
Cdd:cd19369 151 IEDYASEEYAEYCKEWIDFADRLCENLSEEEKEKLKEIFRKASLYELKFWD 201
|
|
| TenA_E_At3g16990-like |
cd19357 |
TenA_E proteins similar to Arabidopsis thaliana At3g16990; This family of TenA proteins ... |
302-508 |
2.96e-13 |
|
TenA_E proteins similar to Arabidopsis thaliana At3g16990; This family of TenA proteins belongs to the TenA_E class, and lacks the conserved active site Cys residue of the TenA_C class; most have a pair of structurally conserved Glu residues in the active site. TenA_C proteins (EC 3.5.99.2; aminopyrimidine aminohydrolase, also known as thiaminase II) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway; the role of TenA_E proteins is less clear. Members of this family include Arabidopsis thaliana At3g16990, Zea mays GRMZM2G080501, and Pyrococcus furiosus PF1337, among others. Arabidopsis thaliana TenA_E hydrolyzes amino-HMP to AMP, and the N-formyl derivative of amino-HMP to amino-HMP, but does not hydrolyze thiamin; nor does it have activity with other thiamine degradation products such as thiamine mono- or diphosphate, oxythiamine, oxothiamine, thiamine disulfide, desthiothiamine or thiochrome as substrates. Structural studies of P. furiosus PF1337 strongly support its enzymatic function in thiamine biosynthesis. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect.
Pssm-ID: 381692 [Multi-domain] Cd Length: 217 Bit Score: 68.88 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 302 TARLWELTGDAWQSITQLPFIQALGTGTLREEDFAFYLAQDAQYLNQYSKALARLAALAPDAGAQLHWA--SGAAECLAV 379
Cdd:cd19357 1 TSHLLSLHPALYTAATQHPFLRAAADGTLPKEALSRWLAQDRLYVQAYIRFLGSLLARAPLPSSSLNQRllDVLLGALAN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 380 ---EMSLHKDWIAHHTTTVPSTAlTAPSRVTSAYTDFLVSTTHTDDYVVAAAAVL----PCY---WlyAEVGLHLAAQNS 449
Cdd:cd19357 81 lrrELAFFEETAAEYGLDLPGLG-VPPSPATRAYVDFLASLASEGVSYLEGLVVLwateKVYldaW--SYARSFLPSDAD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1080393322 450 PEHPYNAWITQYGGEEFLTGVRAAIALVEEALTAADPATRSRATRAYLAACWHEVDFFD 508
Cdd:cd19357 158 GGALYREFIPNWTSPEFAAFVDRLGDLVDEALEQAGEEVLERAEEVWRRVLELEEAFWP 216
|
|
| PRK07105 |
PRK07105 |
pyridoxamine kinase; Validated |
71-245 |
3.28e-12 |
|
pyridoxamine kinase; Validated
Pssm-ID: 180840 [Multi-domain] Cd Length: 284 Bit Score: 66.86 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 71 DVTIDAVKIGMLGSAAIVAEVSRFLAQLS--DVPVVLDPVMvatsGD--RL---LDRDAEAAVRELCARATVVTPNLKEL 143
Cdd:PRK07105 73 NLKFDAIYSGYLGSPRQIQIVSDFIKYFKkkDLLVVVDPVM----GDngKLyqgFDQEMVEEMRKLIQKADVITPNLTEA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 144 AVLTQTA--EATTLEEAI-AHATAWSADTRTTVIVKG----GHLRGDLADNAvvtPDGAVHRVSCPRVDTpHTHGTGCSL 216
Cdd:PRK07105 149 CLLLDKPylEKSYSEEEIkQLLRKLADLGPKIVIITSvpfeDGKIGVAYYDR---ATDRFWKVFCKYIPA-HYPGTGDIF 224
|
170 180
....*....|....*....|....*....
gi 1080393322 217 SSALATRLGAGASLSDALSWSTRWLHEAI 245
Cdd:PRK07105 225 TSVITGSLLQGDSLPIALDRAVQFIEKGI 253
|
|
| pdxK |
PRK08176 |
pyridoxine/pyridoxal/pyridoxamine kinase; |
76-233 |
1.13e-11 |
|
pyridoxine/pyridoxal/pyridoxamine kinase;
Pssm-ID: 181269 [Multi-domain] Cd Length: 281 Bit Score: 65.45 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 76 AVKIGMLGSAAIVAEVSRFLAQL----SDVPVVLDPVMVAT-SGDRLLDRDAEAAVRELCARATVVTPNLKELAVLTqTA 150
Cdd:PRK08176 91 AVTTGYMGSASQIKILAEWLTALradhPDLLIMVDPVIGDIdSGIYVKPDLPEAYRQHLLPLAQGLTPNIFELEILT-GK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 151 EATTLEEAIAHATAWSADTRTTVIVKGGHLRGDLADN--AVVTPDGaVHRVSCPRVDTpHTHGTGCSLSSALATRLGAGA 228
Cdd:PRK08176 170 PCRTLDSAIAAAKSLLSDTLKWVVITSAAGNEENQEMqvVVVTADS-VNVISHPRVDT-DLKGTGDLFCAELVSGLLKGK 247
|
....*
gi 1080393322 229 SLSDA 233
Cdd:PRK08176 248 ALTDA 252
|
|
| TenA_C_SsTenA-1-like |
cd19362 |
uncharacterized TenA_C proteins similar to Sulfolobus solfataricus TenA-1 (Sso2206); This ... |
304-481 |
4.13e-11 |
|
uncharacterized TenA_C proteins similar to Sulfolobus solfataricus TenA-1 (Sso2206); This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; only one of the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect. This family includes mostly uncharacterized TenA like proteins such as Sulfolobus solfataricus putative TenA-like thiaminase (Tena-1, Sso2206).
Pssm-ID: 381697 [Multi-domain] Cd Length: 200 Bit Score: 62.46 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 304 RLWELTGDAWQSITQLPFIQALGTGTLREEDFAFYLAQDAQYLNQYSKALARLAALAP---------------DAGAQLH 368
Cdd:cd19362 3 NLKNLVGDLWNKYVRHEFVERMRDGTLPLDNFRYYLIQDSKYVEEMLRALLRASSKAPldkaikilnsvfsgrDKGMEVH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 369 wasgaaECLAVEMSLHKDWIAHhtttvpstalTAPSRVTSAYTDFLV--STTHTDDYVVAAAavlPCYWLYAEVGLHLAa 446
Cdd:cd19362 83 ------KFLYSELGITEDEIRR----------TGYNLVNYAYTRHLYyySTLGWPQFLAAWA---PCMWGYSEIGKYVL- 142
|
170 180 190
....*....|....*....|....*....|....*
gi 1080393322 447 qNSPEHPYNAWITQYGGEEFLTGVRAAIalveEAL 481
Cdd:cd19362 143 -NSPNELYKTWASFYASKDYKKRVEAIL----EAL 172
|
|
| PRK05756 |
PRK05756 |
pyridoxal kinase PdxY; |
63-245 |
4.05e-10 |
|
pyridoxal kinase PdxY;
Pssm-ID: 235592 [Multi-domain] Cd Length: 286 Bit Score: 60.65 E-value: 4.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 63 AQLTAVASDV-------TIDAVKIGMLGSAAIVAEVSRFLAQLSDV-PVVL---DPVMvatsGDR---LLDRD--AEAAV 126
Cdd:PRK05756 57 SHLTEIVQGIadigwlgECDAVLSGYLGSAEQGEAILDAVRRVKAAnPQALyfcDPVM----GDPekgCIVAPgvAEFLR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 127 RELCARATVVTPNLKELAVLTQtAEATTLEEAIAHATAWSADTRTTVIVKGGHLRGDLAD---NAVVTPDGAVHrVSCPR 203
Cdd:PRK05756 133 DRALPAADIITPNLFELEWLSG-RPVETLEDAVAAARALIARGPKIVLVTSLARAGYPADrfeMLLVTADGAWH-ISRPL 210
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1080393322 204 VDTPH-THGTGCSLSSALATRLGAGASLSDALSWSTRWLHEAI 245
Cdd:PRK05756 211 VDFMRqPVGVGDLTSALFLARLLQGGSLEEALEHTTAAVYEVM 253
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
72-224 |
2.51e-07 |
|
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: 50.94 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 72 VTIDAVKIGMLGSA-AIVAEVSRFLAQlSDVPVVLDPVMVATSGDRlldrdaeAAVRELCARATVVTPNLKELAVLTQtA 150
Cdd:cd00287 56 VGADAVVISGLSPApEAVLDALEEARR-RGVPVVLDPGPRAVRLDG-------EELEKLLPGVDILTPNEEEAEALTG-R 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1080393322 151 EATTLEEAIAHATAWSADTRTTVIVKGGHlRGDLadnaVVTPDGAVHRVSCPRVDTPHTHGTGCSLSSALATRL 224
Cdd:cd00287 127 RDLEVKEAAEAAALLLSKGPKVVIVTLGE-KGAI----VATRGGTEVHVPAFPVKVVDTTGAGDAFLAALAAGL 195
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
84-261 |
5.26e-07 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 51.29 E-value: 5.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 84 SAAIVAEVSRFLAQLsDVPVVLDpvmvaTSGDRLLdrdaeAAVRelcARATVVTPNLKELAVLTQTaEATTLEEAIAHAT 163
Cdd:COG1105 143 PPDFYAELIRLARAR-GAKVVLD-----TSGEALK-----AALE---AGPDLIKPNLEELEELLGR-PLETLEDIIAAAR 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 164 AWSADTRTTVIV-KGGhlRGDLAdnavVTPDGAVHrVSCPRVDTPHTHGTGCSLSSALATRLGAGASLSDALSWSTrwlh 242
Cdd:COG1105 208 ELLERGAENVVVsLGA--DGALL----VTEDGVYR-AKPPKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAV---- 276
|
170
....*....|....*....
gi 1080393322 243 eAISHAAALEVGQGHGPVD 261
Cdd:COG1105 277 -AAGAAAALSPGTGLPDRE 294
|
|
| Nnr2 |
COG0063 |
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport ... |
6-256 |
9.64e-07 |
|
NAD(P)H-hydrate repair enzyme Nnr, NAD(P)H-hydrate dehydratase domain [Nucleotide transport and metabolism];
Pssm-ID: 439833 Cd Length: 280 Bit Score: 50.51 E-value: 9.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 6 RVLSIAGTDPTGGAGIqadLKSIAAA-GGYGMsaVTALVAQNTQGVREVHTP-----PVEFLRAQLTAVASdvtIDAVKI 79
Cdd:COG0063 28 HVLVIGGSRGYPGAAV---LAARAALrAGAGL--VTVAVPESAAPAVAAALPelmviPLPEEDELLELLER---ADAVVI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 80 GM-LGSAAIVAEVSRFLAQLSDVPVVLDpvmvatsGD--RLLDRDAEaaVRELCARATVVTPNLKELAVLTQTAEATTLE 156
Cdd:COG0063 100 GPgLGRDEETRELLRALLEAADKPLVLD-------ADalNLLAEDPE--LLAALPAPTVLTPHPGEFARLLGCSVAEIQA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 157 EAIAHATAWSADTRTTVIVKGghlrgdlADNAVVTPDGAVHRVScprVDTPH--THGTGCSLSSALATRLGAGASLSDAL 234
Cdd:COG0063 171 DRLEAAREAAKRYGAVVVLKG-------AGTVIAAPDGRVYINP---TGNPGlaTAGSGDVLAGIIAGLLAQGLDPFEAA 240
|
250 260
....*....|....*....|..
gi 1080393322 235 SWSTrWLHEAISHAAALEVGQG 256
Cdd:COG0063 241 AAGV-YLHGLAGDLAAEERGRG 261
|
|
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
6-261 |
1.47e-06 |
|
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: 49.53 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 6 RVLSIAGTDPTGGAGIqadLKSIAAA-GGYGMsaVTALVAQNTQGVREVHTPPV---EFLRAQLTAVASDVT-IDAVKIG 80
Cdd:cd01171 10 RVLVIGGSRGYTGAAY---LAALAALrAGAGL--VTVATPPEAAAVIKSYSPELmvhPLLETDIEELLELLErADAVVIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 81 M-LGSAAIVAEVSRFLAQlSDVPVVLDpvmvatsGD--RLLDRDAEAAVRElcaRATVVTPNLKELAVLTQTAEATTLEE 157
Cdd:cd01171 85 PgLGRDEEAAEILEKALA-KDKPLVLD-------ADalNLLADEPSLIKRY---GPVVLTPHPGEFARLLGALVEEIQAD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 158 AIAHATAWSADTRTTVIVKGghlrgdlADNAVVTPDGAVHRVS--CPRVDTPhthGTGCSLSSALATRLGAGASLSDALS 235
Cdd:cd01171 154 RLAAAREAAAKLGATVVLKG-------AVTVIADPDGRVYVNPtgNPGLATG---GSGDVLAGIIAALLAQGLSPLEAAA 223
|
250 260
....*....|....*....|....*.
gi 1080393322 236 WSTrWLHEAISHAAALEVGQGHGPVD 261
Cdd:cd01171 224 LAV-YLHGLAGDLAAKKKGAGLTAAD 248
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
40-236 |
4.98e-06 |
|
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: 48.34 E-value: 4.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 40 TALVAQNTQGVREVHTPPVEFLRAQLTAVASDVtIDAVKIGMLGSAAIVAEVSR-----FLAQL--SDVPVVLDPvmvat 112
Cdd:COG0524 92 LAFILVDPDGERTIVFYRGANAELTPEDLDEAL-LAGADILHLGGITLASEPPReallaALEAAraAGVPVSLDP----- 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 113 SGDRLLDRDAEAAVRELCARATVVTPNLKELAVLTQTaeaTTLEEAIAHATAWSADtrtTVIVKGGhlrgdlADNAVVTP 192
Cdd:COG0524 166 NYRPALWEPARELLRELLALVDILFPNEEEAELLTGE---TDPEEAAAALLARGVK---LVVVTLG------AEGALLYT 233
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1080393322 193 DGAVHRVSCPRVDTPHTHGTGCSLSSALATRLGAGASLSDALSW 236
Cdd:COG0524 234 GGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRF 277
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
101-234 |
6.15e-06 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 48.11 E-value: 6.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 101 VPVVLDPVMvatsgdrlldrDAEAAVRELCARATVVTPNLKELAVLTQtAEATTLEEAIAHATAWSADTRTTVIVKGGhl 180
Cdd:pfam00294 160 DPNLLDPLG-----------AAREALLELLPLADLLKPNEEELEALTG-AKLDDIEEALAALHKLLAKGIKTVIVTLG-- 225
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1080393322 181 rgdlADNA-VVTPDGAVHRVSCPRVDTPHTHGTGCSLSSALATRLGAGASLSDAL 234
Cdd:pfam00294 226 ----ADGAlVVEGDGEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEAL 276
|
|
| Carb_kinase |
pfam01256 |
Carbohydrate kinase; This family is related to pfam02110 and pfam00294 implying that it also ... |
7-254 |
1.01e-05 |
|
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: 46.97 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 7 VLSIAGTDPTGGAGIQADLKsiAAAGGYGMsaVTALVAQNTQGVREVHTPPVE---FLRAQLTAVASDvTIDAVKIGM-L 82
Cdd:pfam01256 1 VLVIGGSKDYTGAPLLAALA--ALRSGAGL--VSVATDSEAIAVLKSPLPEVMvhpLPETSSILEKLS-RYDAVVIGPgL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 83 GSAAIVAEVSRFlAQLSDVPVVLDpvmvaTSGDRLLDRDAEAAVRElcaRATVVTPNLKELAVLTQTAEAttLEEAIAH- 161
Cdd:pfam01256 76 GRDEKGKAALEE-VLAKDCPLVID-----ADALNLLAINNEKPARE---GPTVLTPHPGEFERLCGLAGI--LGDDRLEa 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 162 ATAWSADTRTTVIVKGGHlrgdladNAVVTPDGAVHRVScprVDTPH--THGTGCSLSSALATRLGAGASLSDALSWSTr 239
Cdd:pfam01256 145 ARELAQKLNGTILLKGNV-------TVIAAPGGEVWINS---TGNSAlaKGGSGDVLAGLIGGLLAQNEDPYDAAIAAA- 213
|
250
....*....|....*
gi 1080393322 240 WLHEAISHAAALEVG 254
Cdd:pfam01256 214 WLHGAASDLAAENHG 228
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
89-254 |
8.90e-05 |
|
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. FruK plays an important role in the predominant pathway for fructose utilisation.This group also contains tagatose-6-phophate kinase, an enzyme of the tagatose 6-phosphate pathway, which responsible for breakdown of the galactose moiety during lactose metabolism by bacteria such as L. lactis.
Pssm-ID: 238570 [Multi-domain] Cd Length: 289 Bit Score: 44.45 E-value: 8.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 89 AEVSRfLAQLSDVPVVLDpvmvaTSGDRLLdrdaeAAVRelcARATVVTPNLKELAVLTQTaEATTLEEAIAHATAWSAD 168
Cdd:cd01164 148 AELVR-LAREKGARVILD-----TSGEALL-----AALA---AKPFLIKPNREELEELFGR-PLGDEEDVIAAARKLIER 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 169 TRTTVIVKGGhlrgdlADNAV-VTPDGaVHRVSCPRVDTPHTHGTGCSLSSALATRLGAGASLSDALSWSTrwlheAISH 247
Cdd:cd01164 213 GAENVLVSLG------ADGALlVTKDG-VYRASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAV-----AAGS 280
|
....*..
gi 1080393322 248 AAALEVG 254
Cdd:cd01164 281 ATAFSPG 287
|
|
| PTZ00344 |
PTZ00344 |
pyridoxal kinase; Provisional |
74-159 |
2.96e-03 |
|
pyridoxal kinase; Provisional
Pssm-ID: 240372 [Multi-domain] Cd Length: 296 Bit Score: 39.68 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080393322 74 IDAVKIGMLGSAAIVAEVSRFLAQLSD----VPVVLDPVMvatsGDR---LLDRDAEAAVRELCARATVVTPNLKELAVL 146
Cdd:PTZ00344 78 YTYVLTGYINSADILREVLATVKEIKElrpkLIFLCDPVM----GDDgklYVKEEVVDAYRELIPYADVITPNQFEASLL 153
|
90
....*....|...
gi 1080393322 147 TqTAEATTLEEAI 159
Cdd:PTZ00344 154 S-GVEVKDLSDAL 165
|
|
| |
