|
Name |
Accession |
Description |
Interval |
E-value |
| HMPP_kinase |
cd01169 |
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ... |
39-296 |
7.27e-122 |
|
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: 358.35 E-value: 7.27e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 39 LTIAGSDCSGGAGIQADLKTMTSLGVYGMSAITCLVAENAGGVDSVEEMSPAFVESQIDCCIRDIPCHVVKTGMLGSPEI 118
Cdd:cd01169 3 LTIAGSDSSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVFGVHPVPPEFVAAQLDAVLEDIPVDAIKIGMLGSAEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 119 VKAVARSAKKFNFSKLVVDPVMVATSGDSLVTKDIVSVLNEELLPLTYLVTPNIPEAIVLAKNQgldisnINSVSDMERC 198
Cdd:cd01169 83 IEAVAEALKDYPDIPVVLDPVMVAKSGDSLLDDDAIEALRELLLPLATLITPNLPEAELLTGLE------IATEEDMMKA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 199 AAVIHKLGPKHVLLKGGHMPVNnlglkssddedlRVVDILYDGNRFYHFSSSYLKKGEVHGTGCTLSSAIASFLAWEHSL 278
Cdd:cd01169 157 AKALLALGAKAVLIKGGHLPGD------------EAVDVLYDGGGFFEFESPRIDTKNTHGTGCTLSSAIAANLAKGLSL 224
|
250
....*....|....*...
gi 19113317 279 TEAVQFGIDYVHGAITHS 296
Cdd:cd01169 225 EEAVREAKEYVTQAIRNA 242
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
39-300 |
5.84e-121 |
|
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: 356.27 E-value: 5.84e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 39 LTIAGSDCSGGAGIQADLKTMTSLGVYGMSAITCLVAENAGGVDSVEEMSPAFVESQIDCCIRDIPCHVVKTGMLGSPEI 118
Cdd:COG0351 1 LTIAGSDPSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVTGVHPVPPEFVAAQLRAVLEDIPVDAIKIGMLGSAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 119 VKAVARSAKKFNFSKLVVDPVMVATSGDSLVTKDIVSVLNEELLPLTYLVTPNIPEAIVLAknqGLDisnINSVSDMERC 198
Cdd:COG0351 81 IEAVAEILADYPLVPVVLDPVMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALL---GIE---ITTLDDMREA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 199 AAVIHKLGPKHVLLKGGHMPvnnlglkssddeDLRVVDILYDGNRFYHFSSSYLKKGEVHGTGCTLSSAIASFLAWEHSL 278
Cdd:COG0351 155 AKALLELGAKAVLVKGGHLP------------GDEAVDVLYDGDGVREFSAPRIDTGNTHGTGCTLSSAIAALLAKGLDL 222
|
250 260
....*....|....*....|..
gi 19113317 279 TEAVQFGIDYVHGAITHSPPIN 300
Cdd:COG0351 223 EEAVREAKEYVTQAIRAALRLG 244
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
36-299 |
3.46e-116 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 344.80 E-value: 3.46e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 36 PVSLTIAGSDCSGGAGIQADLKTMTSLGVYGMSAITCLVAENAGGVDSVEEMSPAFVESQIDCCIRDIPCHVVKTGMLGS 115
Cdd:PRK06427 5 PIALTIAGSDSGGGAGIQADLKTFQALGVYGMSAITALTAQNTLGVQRVHPIPPEFVAAQLDAVFSDIRIDAVKIGMLAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 116 PEIVKAVARSAKKFNFSKLVVDPVMVATSGDSLVTKDIVSVLNEELLPLTYLVTPNIPEAIVLAknqGLDIsnINSVSDM 195
Cdd:PRK06427 85 AEIIETVAEALKRYPIPPVVLDPVMIAKSGDPLLADDAVAALRERLLPLATLITPNLPEAEALT---GLPI--ADTEDEM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 196 ERCAAVIHKLGPKHVLLKGGHMPvnnlglkssddEDLRVVDILYDGNRFYHFSSSYLKKGEVHGTGCTLSSAIASFLAWE 275
Cdd:PRK06427 160 KAAARALHALGCKAVLIKGGHLL-----------DGEESVDWLFDGEGEERFSAPRIPTKNTHGTGCTLSAAIAAELAKG 228
|
250 260
....*....|....*....|....
gi 19113317 276 HSLTEAVQFGIDYVHGAITHSPPI 299
Cdd:PRK06427 229 ASLLDAVQTAKDYVTRAIRHALEI 252
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
45-300 |
1.00e-114 |
|
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: 340.23 E-value: 1.00e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 45 DCSGGAGIQADLKTMTSLGVYGMSAITCLVAENAGGVDSVEEMSPAFVESQIDCCIRDIPCHVVKTGMLGSPEIVKAVAR 124
Cdd:pfam08543 1 DSSGGAGIQADLKTFSALGVYGMSVITALTAQNTLGVQGVHPLPPEFVAAQLDAVLEDIPVDAVKTGMLGSAEIIEAVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 125 SAKKFNFsKLVVDPVMVATSGDSLVTKDIVSVLNEELLPLTYLVTPNIPEAIVLAKnqgldiSNINSVSDMERCAAVIHK 204
Cdd:pfam08543 81 KLDKYGV-PVVLDPVMVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTG------RKIKTLEDMKEAAKKLLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 205 LGPKHVLLKGGHMPvnnlglkssdDEDLRVVDILYDGNRFYHFSSSYLKKGEVHGTGCTLSSAIASFLAWEHSLTEAVQF 284
Cdd:pfam08543 154 LGAKAVLIKGGHLE----------GEEAVVTDVLYDGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLAKGLSLPEAVRE 223
|
250
....*....|....*.
gi 19113317 285 GIDYVHGAITHSPPIN 300
Cdd:pfam08543 224 AKEYVTEAIRDALNLG 239
|
|
| HMP-P_kinase |
TIGR00097 |
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ... |
39-296 |
3.85e-100 |
|
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: 303.06 E-value: 3.85e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 39 LTIAGSDCSGGAGIQADLKTMTSLGVYGMSAITCLVAENAGGVDSVEEMSPAFVESQIDCCIRDIPCHVVKTGMLGSPEI 118
Cdd:TIGR00097 2 LTIAGSDSGGGAGIQADLKTFSALGVFGTSVITALTAQNTRGVTGVYPIPPDFVEAQLDAVFSDIPVDAAKTGMLASAEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 119 VKAVARSAKKFNFSKLVVDPVMVATSGDSLVTKDIVSVLNEELLPLTYLVTPNIPEAIVLAKNQgldisnINSVSDMERC 198
Cdd:TIGR00097 82 VEAVARKLREYPVRPLVVDPVMVAKSGAPLLEEEAIEALRKRLLPLATLITPNLPEAEALLGTK------IRTEQDMIKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 199 AAVIHKLGPKHVLLKGGHMpvnnlglkssddEDLRVVDILYDGNRFYHFSSSYLKKGEVHGTGCTLSSAIASFLAWEHSL 278
Cdd:TIGR00097 156 AKKLRELGPKAVLIKGGHL------------EGDQAVDVLFDGGEIHILKAPRIETKNTHGTGCTLSAAIAANLAKGLSL 223
|
250
....*....|....*...
gi 19113317 279 TEAVQFGIDYVHGAITHS 296
Cdd:TIGR00097 224 KEAVKEAKEFVTGAIRYG 241
|
|
| TenA_C_ScTHI20-like |
cd19367 |
TenA_C family similar to the C-terminal TenA_C domain of Saccharomyces cerevisiae THI20 ... |
335-533 |
5.64e-92 |
|
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: 280.17 E-value: 5.64e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 335 PAWKEYINHKFTNMLAKGTLPLPAFQDYLKQDYLYLVNFARAYSLKGYKENTFPNILEAAQSVIHVIEEKELHVSMCSSY 414
Cdd:cd19367 1 PIWKAYTNHPFVRQLADGTLPLESFRHYLKQDYLYLIHYARAHALAAYKAPTLEDIRAAAAILLAILEEMELHVKYCAEW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 415 GVSLQDLKSCEESPACTAYSRYILDTGAAQDVAALDFVQAPCLIGYYVIAARLMKEPFRNPQG-PYQKWVDNYFCEDYLS 493
Cdd:cd19367 81 GISEEELEATPESPATLAYTRYVLDVGLSGDLLDLLVALAPCLLGYGEIGLRLAADPATKLEGnPYWSWIETYASDEYQE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 19113317 494 AVRRGCRQIEEIVLK-LSPERIQELIEIFIRATKFETLFWE 533
Cdd:cd19367 161 AVREGIELLEKLAAErPSPARLEELVKIFATATRLEIGFWD 201
|
|
| TENA_THI-4 |
pfam03070 |
TENA/THI-4/PQQC family; Members of this family are found in all the three major phyla of life: ... |
330-539 |
4.46e-76 |
|
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: 239.57 E-value: 4.46e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 330 HPQVVPAWKEYINHKFTNMLAKGTLPLPAFQDYLKQDYLYLVNFARAYSLKGYKENTFPNILE-AAQSVIHVIEEKELHV 408
Cdd:pfam03070 1 HPQLRPIWKFYINHPFVQALAKGTLPREQFQGYVIQDYLYLVNFARVLAIIASKSPDLEVRREwENRIVDHDGNEIELHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 409 SMCSSYGVSLQDLKSCEESPACTAYSRYILDTGAAQDVAALDFVQAPCLIGYYVIAARlMKEPFRNPQGP-YQKWVDNYF 487
Cdd:pfam03070 81 RLAEALGLSREDLSAYKPLPATRAYVRYLLDFARRGSWLEAVAALLPCLFVYQEIASR-LGEKIRALEGPeYYEWVKTYA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 19113317 488 CEDYLSAVRRGCRQIEEIVLKLSPERIQELIEIFIRATKFETLFWeTPYYEY 539
Cdd:pfam03070 160 SEYFRAAVEEAKRLLDRLLAYVSDEQLEELQEIFLKALEFEYSFW-TMALDA 210
|
|
| TenA |
COG0819 |
Aminopyrimidine aminohydrolase TenA (thiamine salvage pathway) [Coenzyme transport and ... |
335-536 |
2.13e-59 |
|
Aminopyrimidine aminohydrolase TenA (thiamine salvage pathway) [Coenzyme transport and metabolism];
Pssm-ID: 440581 [Multi-domain] Cd Length: 218 Bit Score: 196.26 E-value: 2.13e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 335 PAWKEYINHKFTNMLAKGTLPLPAFQDYLKQDYLYLVNFARAYSLKGYKENTFPNILEAAQSVIHVIE-EKELHVSMCSS 413
Cdd:COG0819 13 PIWEAILEHPFVQGLADGTLPREAFRHYLVQDYLYLEHFARALALAAAKAPDLEDMRFLAGLAAGLLEvELALHERYAAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 414 YGVSLQDLKSCEESPACTAYSRYILDTGAAQD----VAALdfvqAPCLIGYYVIAARLMKEPfRNPQGPYQKWVDNYFCE 489
Cdd:COG0819 93 LGISEEELEATPPSPTTRAYTSYLLAAAASGDyaelLAAL----LPCEWGYAEIGKRLAERP-LPPDHPYAEWIETYASE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 19113317 490 DYLSAVRRGCRQIEEIVLKLSPERIQELIEIFIRATKFETLFWETPY 536
Cdd:COG0819 168 EFQELVEWLIALLDRLAATASEAERERLEEAFRTASRLEYAFWDMAY 214
|
|
| salvage_TenA |
TIGR04306 |
thiaminase II; The TenA protein of Bacillus subtilis and Staphylococcus aurues, and the ... |
333-536 |
4.94e-34 |
|
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: 128.08 E-value: 4.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 333 VVPAWKEYINHKFTNMLAKGTLPLPAFQDYLKQDYLYLVNFARAYSLKGYKENTFPNILEAAQSVIHVIE-EKELHVSMC 411
Cdd:TIGR04306 1 VKPIWDDYINHPFVQKIGDGTLERDKFRFYIEQDYAYLVEYAKVHALGGSKACDEDMEKELVEQIQGGVEtEMGQHKRLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 412 SSYGVSLQD-LKSCEESPACTAYSRYILDTG----AAQDVAALdfvqAPCLIGYYVIAARLMKEPFRNPQGPYQKWVDNY 486
Cdd:TIGR04306 81 EVLGISDEEyFQKIKPGPALRSYTSYMYDVSrrgnWQELVAAL----LPCLWGYGEAATKLKGKHTAPEHSVYHKWIETY 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 19113317 487 FCEDYLSAVRRGCRQIEEIVLKLSPERIQELIEIFIRATKFETLFWETPY 536
Cdd:TIGR04306 157 SSSWFREAVNEGENLLNHLAETSSPEELEKLKTIFAESCEYEYNFWTMAY 206
|
|
| PTZ00347 |
PTZ00347 |
phosphomethylpyrimidine kinase; Provisional |
328-537 |
4.00e-13 |
|
phosphomethylpyrimidine kinase; Provisional
Pssm-ID: 240375 [Multi-domain] Cd Length: 504 Bit Score: 71.53 E-value: 4.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 328 LSHPQVVPA-----WKEY-------INHKFTNMLAKGTLPLPAFQDYLKQDYLYLVNFARAYSLKGYKENTFPNILEAAQ 395
Cdd:PTZ00347 4 FYHEPVFGGlsealWKENqdlammsLHLPFVQGLGDGTLDQNAFRTYIAQDTLYLNGYIRILSYCITKSDVTATGGGLLE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 396 SVIHVIEE-KELHvsmcSSYgvsLQDLKSCEESPACTAYSRYILDTGAAQDVAALDFVQA--PCLIGYYVIAARLMKEPF 472
Cdd:PTZ00347 84 LLKGVLEElKNCH----HHY---IDNPDAAGPEAACRKYVDFLLASGNADTLGPSVVIAAviPCARLYAWVGQELTNEVE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113317 473 RNPQGPYQKWVDNYFCEDylsaVRRGCRQIEEIVLK-LSPERIQELIEIFIRATKFETLFWETPYY 537
Cdd:PTZ00347 157 LTESHPFRRWLLSYSDEP----INTSVEQLESLLDKyIRPGEFSEVAQAYRRAMELEYDFFDSFGY 218
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| HMPP_kinase |
cd01169 |
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ... |
39-296 |
7.27e-122 |
|
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: 358.35 E-value: 7.27e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 39 LTIAGSDCSGGAGIQADLKTMTSLGVYGMSAITCLVAENAGGVDSVEEMSPAFVESQIDCCIRDIPCHVVKTGMLGSPEI 118
Cdd:cd01169 3 LTIAGSDSSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVFGVHPVPPEFVAAQLDAVLEDIPVDAIKIGMLGSAEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 119 VKAVARSAKKFNFSKLVVDPVMVATSGDSLVTKDIVSVLNEELLPLTYLVTPNIPEAIVLAKNQgldisnINSVSDMERC 198
Cdd:cd01169 83 IEAVAEALKDYPDIPVVLDPVMVAKSGDSLLDDDAIEALRELLLPLATLITPNLPEAELLTGLE------IATEEDMMKA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 199 AAVIHKLGPKHVLLKGGHMPVNnlglkssddedlRVVDILYDGNRFYHFSSSYLKKGEVHGTGCTLSSAIASFLAWEHSL 278
Cdd:cd01169 157 AKALLALGAKAVLIKGGHLPGD------------EAVDVLYDGGGFFEFESPRIDTKNTHGTGCTLSSAIAANLAKGLSL 224
|
250
....*....|....*...
gi 19113317 279 TEAVQFGIDYVHGAITHS 296
Cdd:cd01169 225 EEAVREAKEYVTQAIRNA 242
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
39-300 |
5.84e-121 |
|
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: 356.27 E-value: 5.84e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 39 LTIAGSDCSGGAGIQADLKTMTSLGVYGMSAITCLVAENAGGVDSVEEMSPAFVESQIDCCIRDIPCHVVKTGMLGSPEI 118
Cdd:COG0351 1 LTIAGSDPSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVTGVHPVPPEFVAAQLRAVLEDIPVDAIKIGMLGSAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 119 VKAVARSAKKFNFSKLVVDPVMVATSGDSLVTKDIVSVLNEELLPLTYLVTPNIPEAIVLAknqGLDisnINSVSDMERC 198
Cdd:COG0351 81 IEAVAEILADYPLVPVVLDPVMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALL---GIE---ITTLDDMREA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 199 AAVIHKLGPKHVLLKGGHMPvnnlglkssddeDLRVVDILYDGNRFYHFSSSYLKKGEVHGTGCTLSSAIASFLAWEHSL 278
Cdd:COG0351 155 AKALLELGAKAVLVKGGHLP------------GDEAVDVLYDGDGVREFSAPRIDTGNTHGTGCTLSSAIAALLAKGLDL 222
|
250 260
....*....|....*....|..
gi 19113317 279 TEAVQFGIDYVHGAITHSPPIN 300
Cdd:COG0351 223 EEAVREAKEYVTQAIRAALRLG 244
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
36-299 |
3.46e-116 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 344.80 E-value: 3.46e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 36 PVSLTIAGSDCSGGAGIQADLKTMTSLGVYGMSAITCLVAENAGGVDSVEEMSPAFVESQIDCCIRDIPCHVVKTGMLGS 115
Cdd:PRK06427 5 PIALTIAGSDSGGGAGIQADLKTFQALGVYGMSAITALTAQNTLGVQRVHPIPPEFVAAQLDAVFSDIRIDAVKIGMLAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 116 PEIVKAVARSAKKFNFSKLVVDPVMVATSGDSLVTKDIVSVLNEELLPLTYLVTPNIPEAIVLAknqGLDIsnINSVSDM 195
Cdd:PRK06427 85 AEIIETVAEALKRYPIPPVVLDPVMIAKSGDPLLADDAVAALRERLLPLATLITPNLPEAEALT---GLPI--ADTEDEM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 196 ERCAAVIHKLGPKHVLLKGGHMPvnnlglkssddEDLRVVDILYDGNRFYHFSSSYLKKGEVHGTGCTLSSAIASFLAWE 275
Cdd:PRK06427 160 KAAARALHALGCKAVLIKGGHLL-----------DGEESVDWLFDGEGEERFSAPRIPTKNTHGTGCTLSAAIAAELAKG 228
|
250 260
....*....|....*....|....
gi 19113317 276 HSLTEAVQFGIDYVHGAITHSPPI 299
Cdd:PRK06427 229 ASLLDAVQTAKDYVTRAIRHALEI 252
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
45-300 |
1.00e-114 |
|
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: 340.23 E-value: 1.00e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 45 DCSGGAGIQADLKTMTSLGVYGMSAITCLVAENAGGVDSVEEMSPAFVESQIDCCIRDIPCHVVKTGMLGSPEIVKAVAR 124
Cdd:pfam08543 1 DSSGGAGIQADLKTFSALGVYGMSVITALTAQNTLGVQGVHPLPPEFVAAQLDAVLEDIPVDAVKTGMLGSAEIIEAVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 125 SAKKFNFsKLVVDPVMVATSGDSLVTKDIVSVLNEELLPLTYLVTPNIPEAIVLAKnqgldiSNINSVSDMERCAAVIHK 204
Cdd:pfam08543 81 KLDKYGV-PVVLDPVMVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTG------RKIKTLEDMKEAAKKLLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 205 LGPKHVLLKGGHMPvnnlglkssdDEDLRVVDILYDGNRFYHFSSSYLKKGEVHGTGCTLSSAIASFLAWEHSLTEAVQF 284
Cdd:pfam08543 154 LGAKAVLIKGGHLE----------GEEAVVTDVLYDGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLAKGLSLPEAVRE 223
|
250
....*....|....*.
gi 19113317 285 GIDYVHGAITHSPPIN 300
Cdd:pfam08543 224 AKEYVTEAIRDALNLG 239
|
|
| HMP-P_kinase |
TIGR00097 |
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ... |
39-296 |
3.85e-100 |
|
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: 303.06 E-value: 3.85e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 39 LTIAGSDCSGGAGIQADLKTMTSLGVYGMSAITCLVAENAGGVDSVEEMSPAFVESQIDCCIRDIPCHVVKTGMLGSPEI 118
Cdd:TIGR00097 2 LTIAGSDSGGGAGIQADLKTFSALGVFGTSVITALTAQNTRGVTGVYPIPPDFVEAQLDAVFSDIPVDAAKTGMLASAEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 119 VKAVARSAKKFNFSKLVVDPVMVATSGDSLVTKDIVSVLNEELLPLTYLVTPNIPEAIVLAKNQgldisnINSVSDMERC 198
Cdd:TIGR00097 82 VEAVARKLREYPVRPLVVDPVMVAKSGAPLLEEEAIEALRKRLLPLATLITPNLPEAEALLGTK------IRTEQDMIKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 199 AAVIHKLGPKHVLLKGGHMpvnnlglkssddEDLRVVDILYDGNRFYHFSSSYLKKGEVHGTGCTLSSAIASFLAWEHSL 278
Cdd:TIGR00097 156 AKKLRELGPKAVLIKGGHL------------EGDQAVDVLFDGGEIHILKAPRIETKNTHGTGCTLSAAIAANLAKGLSL 223
|
250
....*....|....*...
gi 19113317 279 TEAVQFGIDYVHGAITHS 296
Cdd:TIGR00097 224 KEAVKEAKEFVTGAIRYG 241
|
|
| TenA_C_ScTHI20-like |
cd19367 |
TenA_C family similar to the C-terminal TenA_C domain of Saccharomyces cerevisiae THI20 ... |
335-533 |
5.64e-92 |
|
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: 280.17 E-value: 5.64e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 335 PAWKEYINHKFTNMLAKGTLPLPAFQDYLKQDYLYLVNFARAYSLKGYKENTFPNILEAAQSVIHVIEEKELHVSMCSSY 414
Cdd:cd19367 1 PIWKAYTNHPFVRQLADGTLPLESFRHYLKQDYLYLIHYARAHALAAYKAPTLEDIRAAAAILLAILEEMELHVKYCAEW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 415 GVSLQDLKSCEESPACTAYSRYILDTGAAQDVAALDFVQAPCLIGYYVIAARLMKEPFRNPQG-PYQKWVDNYFCEDYLS 493
Cdd:cd19367 81 GISEEELEATPESPATLAYTRYVLDVGLSGDLLDLLVALAPCLLGYGEIGLRLAADPATKLEGnPYWSWIETYASDEYQE 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 19113317 494 AVRRGCRQIEEIVLK-LSPERIQELIEIFIRATKFETLFWE 533
Cdd:cd19367 161 AVREGIELLEKLAAErPSPARLEELVKIFATATRLEIGFWD 201
|
|
| PLN02898 |
PLN02898 |
HMP-P kinase/thiamin-monophosphate pyrophosphorylase |
33-313 |
2.74e-89 |
|
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
Pssm-ID: 215486 [Multi-domain] Cd Length: 502 Bit Score: 283.97 E-value: 2.74e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 33 RALPVSLTIAGSDCSGGAGIQADLKTMTSLGVYGMSAITCLVAENAGGVDSVEEMSPAFVESQIDCCIRDIPCHVVKTGM 112
Cdd:PLN02898 7 MKVPHVLTVAGSDSGAGAGIQADIKACAARGVYCTTAITAVTAQNTVGVQGVHAVPLDFVAEQLKSVLSDMPVDVVKTGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 113 LGSPEIVKAVARSAKKFNFSKLVVDPVMVATSGDSLVTKDIVSVLNEELLPLTYLVTPNIPEAIVLaknqgLDISNINSV 192
Cdd:PLN02898 87 LPSAEIVKVLCQALKEFPVKALVVDPVMVSTSGDVLAGPSILSALREELLPLATIVTPNVKEASAL-----LGGDPLETV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 193 SDMERCAAVIHKLGPKHVLLKGGHMPvnnlglkssDDEDLrvVDILYDGNRFYHFSSSYLKKGEVHGTGCTLSSAIASFL 272
Cdd:PLN02898 162 ADMRSAAKELHKLGPRYVLVKGGHLP---------DSLDA--VDVLYDGTEFHELRSSRIKTRNTHGTGCTLASCIAAEL 230
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 19113317 273 AWEHSLTEAVQFGIDYVHGAITHSPP--INNCSTNILNHMTRL 313
Cdd:PLN02898 231 AKGSDMLSAVKVAKRYVETALEYSKDigIGNGAQGPFNHLFFL 273
|
|
| PRK14713 |
PRK14713 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
32-535 |
2.26e-78 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 237797 [Multi-domain] Cd Length: 530 Bit Score: 256.25 E-value: 2.26e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 32 RRALPVSLTIAGSDCSGGAGIQADLKTMTSLGVYGMSAITCLVAENAGGVDSVEEMSPAFVESQIDCCIRDIPCHVVKTG 111
Cdd:PRK14713 26 AAATPRVLSIAGTDPSGGAGIQADLKSIAAAGGYGMAVITALVAQNTRGVRAVHVPPADFLRAQLDAVSDDVTVDAVKIG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 112 MLGSPEIVKAVARSAKKFNFSKLVVDPVMVATSGDSLVTKDIVSVLnEELLPLTYLVTPNIPEAIVLAKNQGLDISNins 191
Cdd:PRK14713 106 MLGDAEVIDAVRTWLAEHRPPVVVLDPVMVATSGDRLLEEDAEAAL-RELVPRADLITPNLPELAVLLGEPPATTWE--- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 192 vSDMERCAAVIHKLGPKhVLLKGGHMPvnnlglksSDDEDLRVVD-----ILYDGNRFYHFSSsylkkgevHGTGCTLSS 266
Cdd:PRK14713 182 -EALAQARRLAAETGTT-VLVKGGHLD--------GQRAPDALVGpdgavTEVPGPRVDTRNT--------HGTGCSLSS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 267 AIASFLAWEHSLTEAVQFGIDYVHGAITHSPPIN----NCSTNILNHMTRLRIVPFAPGHFIEYILSHPQVVPA------ 336
Cdd:PRK14713 244 ALATRLGRGGDWAAALRWATAWLHGAIAAGAALQvgtgNGPVDHFHRARRLAADASAEAGVSAEPAPDAVVGPAgpftaa 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 337 -WKEYINHK-------FTNMLAKGTLPLPAFQDYLKQDYLYLVNFARAYSLKGYKENTFPNILEAAQSVIHVIE-EKELH 407
Cdd:PRK14713 324 lWQASGPIReaiedlpFVRALADGTLPEEAFEFYLAQDALYLNGYSRALARLAALAPDPAEQVFWAQSAQACLEvESELH 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 408 VSMCSSYGVSLQdlksceESPACTAYSRYILDTGAAQDVAALDFVQAPCLIGYYVIAARLMKEPFRNPQGPYQKWVDNYF 487
Cdd:PRK14713 404 RSWLGDRDADTA------PSPVTLAYTDFLLARAAGGSYAVGAAAVLPCFWLYAEVGAELHARAGNPDDHPYAEWLQTYA 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 19113317 488 CEDYLSAVRRGCRQIEEIVLKLSPERIQELIEIFIRATKFETLFWETP 535
Cdd:PRK14713 478 DPEFAAATRRAIAFVDRAFRAASPAERAAMARAFLTACRYELEFFDQA 525
|
|
| TENA_THI-4 |
pfam03070 |
TENA/THI-4/PQQC family; Members of this family are found in all the three major phyla of life: ... |
330-539 |
4.46e-76 |
|
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: 239.57 E-value: 4.46e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 330 HPQVVPAWKEYINHKFTNMLAKGTLPLPAFQDYLKQDYLYLVNFARAYSLKGYKENTFPNILE-AAQSVIHVIEEKELHV 408
Cdd:pfam03070 1 HPQLRPIWKFYINHPFVQALAKGTLPREQFQGYVIQDYLYLVNFARVLAIIASKSPDLEVRREwENRIVDHDGNEIELHL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 409 SMCSSYGVSLQDLKSCEESPACTAYSRYILDTGAAQDVAALDFVQAPCLIGYYVIAARlMKEPFRNPQGP-YQKWVDNYF 487
Cdd:pfam03070 81 RLAEALGLSREDLSAYKPLPATRAYVRYLLDFARRGSWLEAVAALLPCLFVYQEIASR-LGEKIRALEGPeYYEWVKTYA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 19113317 488 CEDYLSAVRRGCRQIEEIVLKLSPERIQELIEIFIRATKFETLFWeTPYYEY 539
Cdd:pfam03070 160 SEYFRAAVEEAKRLLDRLLAYVSDEQLEELQEIFLKALEFEYSFW-TMALDA 210
|
|
| PRK08573 |
PRK08573 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
36-299 |
5.60e-71 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 236297 [Multi-domain] Cd Length: 448 Bit Score: 234.24 E-value: 5.60e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 36 PVSLTIAGSDCSGGAGIQADLKTMTSLGVYGMSAITCLVAENAGGVDSVEEMSPAFVESQIDCCIRDIPCHVVKTGMLGS 115
Cdd:PRK08573 3 PVALTIAGSDSGGGAGIEADLKTFAALGVHGAVAITSVTAQNTYEVRAIHDLPPEVVAAQIEAVWEDMGIDAAKTGMLSN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 116 PEIVKAVARSAKKFNFSkLVVDPVMVATSGDSLVTKDIVSVLNEELLPLTYLVTPNIPEAIVLAknqGLDisnINSVSDM 195
Cdd:PRK08573 83 REIIEAVAKTVSKYGFP-LVVDPVMIAKSGAPLLREDAVDALIKRLLPLATVVTPNRPEAEKLT---GMK---IRSVEDA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 196 ERCAAVIHK-LGPKHVLLKGGHMpvnnlglkssddEDLRVVDILYDGNRFYHFSSSYLKKGEVHGTGCTLSSAIASFLAW 274
Cdd:PRK08573 156 RKAAKYIVEeLGAEAVVVKGGHL------------EGEEAVDVLYHNGTFREFRAPRVESGCTHGTGCSFSAAIAAGLAK 223
|
250 260
....*....|....*....|....*
gi 19113317 275 EHSLTEAVQFGIDYVHGAITHSPPI 299
Cdd:PRK08573 224 GLDPEEAIKTAKKFITMAIKYGVKI 248
|
|
| PRK09517 |
PRK09517 |
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ... |
24-535 |
1.58e-65 |
|
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; Provisional
Pssm-ID: 169939 [Multi-domain] Cd Length: 755 Bit Score: 227.16 E-value: 1.58e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 24 DPMGYTIKRRALPVSLTIAGSDCSGGAGIQADLKTMTSLGVYGMSAITCLVAENAGGVDSVEEMSPAFVESQIDCCIRDI 103
Cdd:PRK09517 230 ELQGAFVNSPSAPRVLSIAGTDPTGGAGIQADLKSIAAGGGYGMCVVTALVAQNTHGVNTIHTPPLTFLEEQLEAVFSDV 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 104 PCHVVKTGMLGSPEIVKAVARSAKKFNFSKLVVDPVMVATSGDSLVTKDIVSVLnEELLPLTYLVTPNIPEAIVLAKNQG 183
Cdd:PRK09517 310 TVDAVKLGMLGSADTVDLVASWLGSHEHGPVVLDPVMVATSGDRLLDADATEAL-RRLAVHVDVVTPNIPELAVLCGEAP 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 184 LDisninsvsDMERCAAVIHKLGPKH---VLLKGGHMPVnnlglkssDDEDLRVVdilYDGNRFYHFSSSYLKKGEVHGT 260
Cdd:PRK09517 389 AI--------TMDEAIAQARGFARTHgtiVIVKGGHLTG--------DLADNAVV---RPDGSVHQVENPRVNTTNSHGT 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 261 GCTLSSAIASFLAWEHSLTEAVQFGIDYVHGAITHSPPINNCSTN-ILNHMTRLRIVPFAPG-----HFIEYILSH---- 330
Cdd:PRK09517 450 GCSLSAALATLIAAGESVEKALEWATRWLNEALRHADHLAVGSGNgPVDHGHLARRLTHAAEttpwaHLRAGATAAsftt 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 331 --------PQVVPA-------W-------KEYINHKFTNMLAKGTLPLPAFQDYLKQDYLYLVNFARAYSLKGYKENTFP 388
Cdd:PRK09517 530 pstvkspaPRIEPAgpftralWeasgdiiAEINDSDFIRMLGDGTLRRPEFDFYIDQDAQYLRQYSRALARLSSIAPDSH 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 389 NILEAAQSVIHVIE-EKELHVSMCSSYgvslqdLKSCEESPACTAYSRYILDTGAAQDVAALDFVQAPCLIGYYVIAARL 467
Cdd:PRK09517 610 AQVEWAQSAAECIVvEAELHRSYLSGK------EAPSAPSPVTMAYTDFLIARTYTEDYVVGVAAVLPCYWLYAEIGLML 683
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19113317 468 MKEpfRNPQGPYQKWVDNYFCEDYLSAVRRGCRQIEEIVLKLSPERIQELIEIFIRATKFETLFWETP 535
Cdd:PRK09517 684 AEQ--NHDEHPYKDWLNTYSGEEFIAGTRAAIARVEKALENAGPEQRVDAARAFLSASVHEREFFDQA 749
|
|
| PTZ00347 |
PTZ00347 |
phosphomethylpyrimidine kinase; Provisional |
34-309 |
5.41e-64 |
|
phosphomethylpyrimidine kinase; Provisional
Pssm-ID: 240375 [Multi-domain] Cd Length: 504 Bit Score: 217.52 E-value: 5.41e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 34 ALPVSLTIAGSDCSGGAGIQADLKTMTSLGVYGMSAITCLVAENAGGVDSVEEMSPAFVESQIDCCIRDIPCHVVKTGML 113
Cdd:PTZ00347 229 KIPTVLTVSGSDSGGGAGHQADLKTLEALGVYSTSALTSLTAQNTKGVQQIQVVNEDFFAAQIDSVMSDFNISVVKLGLV 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 114 GSPEIVKAVARSAKKFnfsKLVVDPVMVATSGDSLVTK----DIVSVLNEELLPLTYLVTPNIPEAivlakNQGLDISNI 189
Cdd:PTZ00347 309 PTARQLEIVIEKLKNL---PMVVDPVLVATSGDDLVAQknadDVLAMYKERIFPMATIITPNIPEA-----ERILGRKEI 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 190 NSVSDMERCAAVIHKLGPKHVLLKGGHmpvnnlglKSSDDEDLRvvDILYD--GNRFYHFSSSYLKKGEVHGTGCTLSSA 267
Cdd:PTZ00347 381 TGVYEARAAAQALAQYGSRYVLVKGGH--------DLIDPEACR--DVLYDreKDRFYEFTANRIATINTHGTGCTLASA 450
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 19113317 268 IASFLAWEHSLTEAVQFGIDYVHGAITHS--PPINNCSTNILNH 309
Cdd:PTZ00347 451 ISSFLARGYTVPDAVERAIGYVHEAIVRScgVPLGQGTNRPLVH 494
|
|
| TenA |
COG0819 |
Aminopyrimidine aminohydrolase TenA (thiamine salvage pathway) [Coenzyme transport and ... |
335-536 |
2.13e-59 |
|
Aminopyrimidine aminohydrolase TenA (thiamine salvage pathway) [Coenzyme transport and metabolism];
Pssm-ID: 440581 [Multi-domain] Cd Length: 218 Bit Score: 196.26 E-value: 2.13e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 335 PAWKEYINHKFTNMLAKGTLPLPAFQDYLKQDYLYLVNFARAYSLKGYKENTFPNILEAAQSVIHVIE-EKELHVSMCSS 413
Cdd:COG0819 13 PIWEAILEHPFVQGLADGTLPREAFRHYLVQDYLYLEHFARALALAAAKAPDLEDMRFLAGLAAGLLEvELALHERYAAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 414 YGVSLQDLKSCEESPACTAYSRYILDTGAAQD----VAALdfvqAPCLIGYYVIAARLMKEPfRNPQGPYQKWVDNYFCE 489
Cdd:COG0819 93 LGISEEELEATPPSPTTRAYTSYLLAAAASGDyaelLAAL----LPCEWGYAEIGKRLAERP-LPPDHPYAEWIETYASE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 19113317 490 DYLSAVRRGCRQIEEIVLKLSPERIQELIEIFIRATKFETLFWETPY 536
Cdd:COG0819 168 EFQELVEWLIALLDRLAATASEAERERLEEAFRTASRLEYAFWDMAY 214
|
|
| PRK12412 |
PRK12412 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
35-300 |
1.07e-57 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183512 [Multi-domain] Cd Length: 268 Bit Score: 193.65 E-value: 1.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 35 LPVSLTIAGSDCSGGAGIQADLKTMTSLGVYGMSAITCLVAENA--GGVDSVEEMSPAFVESQIDCCIRDIPCHVVKTGM 112
Cdd:PRK12412 1 LNKALTIAGSDTSGGAGIQADLKTFQELGVYGMTSLTTIVTMDPhnGWAHNVFPIPASTLKPQLETTIEGVGVDALKTGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 113 LGSPEIVKAVARSAKKFNFSKLVVDPVMVATSGDSLVTKDIVSVLNEELLPLTYLVTPNIPEAIVLAknqGLdisNINSV 192
Cdd:PRK12412 81 LGSVEIIEMVAETIEKHNFKNVVVDPVMVCKGADEALHPETNDCLRDVLVPKALVVTPNLFEAYQLS---GV---KINSL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 193 SDMERCAAVIHKLGPKHVLLKGGhmpvNNLGLKSSddedlrvVDILYDGNRFYHFSSSYLKKGEVHGTGCTLSSAIASFL 272
Cdd:PRK12412 155 EDMKEAAKKIHALGAKYVLIKGG----SKLGTETA-------IDVLYDGETFDLLESEKIDTTNTHGAGCTYSAAITAEL 223
|
250 260
....*....|....*....|....*...
gi 19113317 273 AWEHSLTEAVQFGIDYVHGAITHSPPIN 300
Cdd:PRK12412 224 AKGKPVKEAVKTAKEFITAAIRYSFKIN 251
|
|
| PRK12616 |
PRK12616 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
38-300 |
3.40e-47 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183624 Cd Length: 270 Bit Score: 165.99 E-value: 3.40e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 38 SLTIAGSDCSGGAGIQADLKTMTSLGVYGMSAITCLVA---ENAGGvDSVEEMSPAFVESQIDCCIRDIPCHVVKTGMLG 114
Cdd:PRK12616 6 ALTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAmdpENSWD-HQVFPIDTDTIRAQLSTIVDGIGVDAMKTGMLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 115 SPEIVKAVARSAKKFNFSKLVVDPVMVATSGDSLVTKDIVSVLNEELLPLTYLVTPNIPEAIVLAKnqgldISNINSVSD 194
Cdd:PRK12616 85 TVDIIELAADTIKEKQLKNVVIDPVMVCKGANEVLYPEHAEALREQLAPLATVITPNLFEAGQLSG-----MGEIKTVEQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 195 MERCAAVIHKLGPKHVLLKGGhmpvnnlGLKSSDdedlRVVDILYDGNRFYHFSSSYLKKGEVHGTGCTLSSAIASFLAW 274
Cdd:PRK12616 160 MKEAAKKIHELGAQYVVITGG-------GKLKHE----KAVDVLYDGETAEVLESEMIDTPYTHGAGCTFSAAVTAELAK 228
|
250 260
....*....|....*....|....*.
gi 19113317 275 EHSLTEAVQFGIDYVHGAITHSPPIN 300
Cdd:PRK12616 229 GSEVKEAIYAAKEFITAAIKESFPLN 254
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
39-296 |
8.01e-46 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 161.38 E-value: 8.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 39 LTIAGSDCSGGAGIQADLKTMTSLGVYGMSAITCLVAENAGGVDsVEEMSPAFVESQIDcCIRDIPCHVVKTGMLGSPEI 118
Cdd:PRK12413 7 LAISGNDIFSGGGLHADLATYTRNGLHGFVAVTCLTAMTEKGFE-VFPVDKEIFQQQLD-SLKDVPFSAIKIGLLPNVEI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 119 VKAVARSAKKFNFSKLVVDPVMVATSgdslvTKDI-VSVLNEELL---PLTYLVTPNIPEAIVLAknqGLDisnINSVSD 194
Cdd:PRK12413 85 AEQALDFIKGHPGIPVVLDPVLVCKE-----THDVeVSELRQELIqffPYVTVITPNLVEAELLS---GKE---IKTLED 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 195 MERCAAVIHKLGPKHVLLKGGhmpvNNLGLKssddedlRVVDILYDGNRFYHFSSSYLKKGEVhGTGCTLSSAIASFLAW 274
Cdd:PRK12413 154 MKEAAKKLYDLGAKAVVIKGG----NRLSQK-------KAIDLFYDGKEFVILESPVLEKNNI-GAGCTFASSIASQLVK 221
|
250 260
....*....|....*....|..
gi 19113317 275 EHSLTEAVQFGIDYVHGAITHS 296
Cdd:PRK12413 222 GKSPLEAVKNSKDFVYQAIQQS 243
|
|
| TenA_C_BhTenA-like |
cd19366 |
TenA_C proteins similar to Bacillus halodurans TenA; This family of TenA proteins belongs to ... |
335-536 |
3.61e-41 |
|
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: 147.70 E-value: 3.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 335 PAWKEYINHKFTNMLAKGTLPLPAFQDYLKQDYLYLVNFARAYSLKGYKEN------TFPNILeaaQSVIHVieEKELHV 408
Cdd:cd19366 11 PIWEAGLEHPFVQGLGDGTLDKEKFKFYLKQDYLYLIDYARVFALGAAKADdletmgRFAELL---HGTLNT--EMDLHR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 409 SMCSSYGVSLQDLKSCEESPACTAYSRYILDTGAAQDVAALDFVQAPCLIGYYVIAARLMKEPFRNPQGPYQKWVDNYFC 488
Cdd:cd19366 86 QYAAEFGITEEELEATEPSPTTLAYTSYMLRTAQTGTLAELLAALLPCAWGYAEIGKRLAEQGGALEHNPYREWIEMYSS 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 19113317 489 EDYlSAVRRGCRQ-IEEIVLKLSPERIQELIEIFIRATKFETLFWETPY 536
Cdd:cd19366 166 DEF-TELADWLIDlLDELAEGKSEAELERLEEIFLTSSRYEYMFWDMAY 213
|
|
| PTZ00493 |
PTZ00493 |
phosphomethylpyrimidine kinase; Provisional |
39-321 |
7.31e-37 |
|
phosphomethylpyrimidine kinase; Provisional
Pssm-ID: 240440 Cd Length: 321 Bit Score: 139.36 E-value: 7.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 39 LTIAGSDCSGGAGIQADLKTMTSLGVYGMSAITCLVAENAGGVDSVEEMSPAFVESQIDCCIRDIPCHVVKTGMLGSPEI 118
Cdd:PTZ00493 8 LSIAGSDSCGGAGMQADIKTAMGLGCHCCTALVVLTAQNTKEVKRIVEIEEKFIVEQLDSIFADVTIDVVKLGVLYSKKI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 119 VKAVARSAKKFNFSK-----LVVDPVMVATSGDSLVTK-DIVSVLNEELLPLTYLVTPNIPEAIVL--AKNQGLDISNIN 190
Cdd:PTZ00493 88 ISLVHNYITNMNKKRgkkllVVFDPVFVSSSGCLLVENlEYIKFALDLICPISCIITPNFYECKVIleALDCQMDLSKAN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 191 SVsdmERCAAVIHKLGPKHVLLKGGhmpvnNLGLKSSDDEDLRVVDIL-------YDGNR--------------FYHFSS 249
Cdd:PTZ00493 168 MT---ELCKLVTEKLNINACLFKSC-----NVGENSAEENEVYAVDHLcirnvgsYPTGEkqqidaggvtylydVYKLRS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 250 SYLKKGEVHGTGCTLSSAIASFLAWEHSLTEAVQFGIDYVHGAITHSPPINNCSTNiLNHM---------TRLRIVPFAP 320
Cdd:PTZ00493 240 KRKPGKDIHGTGCTLSTAIACYLAKKHNILQSCIESKKYIYNCIRYAYPFGSKSQG-LNHLkasqelptfTDLQVIPIVQ 318
|
.
gi 19113317 321 G 321
Cdd:PTZ00493 319 D 319
|
|
| salvage_TenA |
TIGR04306 |
thiaminase II; The TenA protein of Bacillus subtilis and Staphylococcus aurues, and the ... |
333-536 |
4.94e-34 |
|
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: 128.08 E-value: 4.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 333 VVPAWKEYINHKFTNMLAKGTLPLPAFQDYLKQDYLYLVNFARAYSLKGYKENTFPNILEAAQSVIHVIE-EKELHVSMC 411
Cdd:TIGR04306 1 VKPIWDDYINHPFVQKIGDGTLERDKFRFYIEQDYAYLVEYAKVHALGGSKACDEDMEKELVEQIQGGVEtEMGQHKRLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 412 SSYGVSLQD-LKSCEESPACTAYSRYILDTG----AAQDVAALdfvqAPCLIGYYVIAARLMKEPFRNPQGPYQKWVDNY 486
Cdd:TIGR04306 81 EVLGISDEEyFQKIKPGPALRSYTSYMYDVSrrgnWQELVAAL----LPCLWGYGEAATKLKGKHTAPEHSVYHKWIETY 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 19113317 487 FCEDYLSAVRRGCRQIEEIVLKLSPERIQELIEIFIRATKFETLFWETPY 536
Cdd:TIGR04306 157 SSSWFREAVNEGENLLNHLAETSSPEELEKLKTIFAESCEYEYNFWTMAY 206
|
|
| TenA_PqqC-like |
cd16099 |
TenA-like proteins including TenA_C and TenA_E proteins, as well as pyrroloquinoline quinone ... |
337-533 |
9.39e-34 |
|
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: 126.70 E-value: 9.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 337 WKEYINHKFTNMLAKGTLPLPAFQDYLKQDYLYLVNFARAYSLKGYK--ENTFPNILEAAQSVIHVieEKELHVSMCSSY 414
Cdd:cd16099 2 WDAILNHPFVQELAAGTLPREKFRYYLAQDYYYLKDFARALALAAAKapDLELRTFLAELINVLDD--ELELHEKLLAEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 415 GVSLQDLKSCEESPACTAYSRYILDTGAAQD----VAALdfvqAPCLIGYYVIAARLMKEPFRNPqgPYQKWVDNYFCED 490
Cdd:cd16099 80 GISEEDLSEAEPNPATLAYTNHLLRVAARGTpaegLAAL----LPCYWSYGEIGRRLAASLPEHP--PYRFWIDFYASDE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 19113317 491 YLSAVRRgCRQIEEIVLKLSPERIQELIEIFIRATKFETLFWE 533
Cdd:cd16099 154 YQELVEE-LLQLLDQLAAAGEEEKEELKEIFLTSLRYELMFWD 195
|
|
| TenA_C-like |
cd19369 |
uncharacterized TenA_C proteins; This family of TenA proteins belongs to the TenA_C class as ... |
335-533 |
2.03e-31 |
|
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: 120.41 E-value: 2.03e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 335 PAWKEYINHKFTNMLAKGTLPLPAFQDYLKQDYLYLVNFARAYSLKGYKENTfpniLEAAQ---SVIHVIEEKE--LHVS 409
Cdd:cd19369 1 PIWEQYLEHPFIKELGEGTLDKEKFKNYLIQDSLYLKEYAKVFAMGIYKSRT----MKEMQffySSLSFVNEDEtaTRIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 410 MCSSYGVSLQDLKSCEESPACTAYSRYILDTgaAQDVAALDFVQA--PCLIGYYVIAARLMKEPFRNPQG-PYQKWVDNY 486
Cdd:cd19369 77 YLKEFGLTDEDIEKIEPLPENKAYTDYMLGI--AKTGDVKEILMAvlPCMLSYYYIFKELVKKYKDNLESnPYKDWIEDY 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 19113317 487 FCEDYLSAVRRGCRQIEEIVLKLSPERIQELIEIFIRATKFETLFWE 533
Cdd:cd19369 155 ASEEYAEYCKEWIDFADRLCENLSEEEKEKLKEIFRKASLYELKFWD 201
|
|
| TenA_C-like |
cd19365 |
uncharacterized TenA_C proteins; This family of TenA proteins belongs to the TenA_C class as ... |
335-533 |
4.48e-31 |
|
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: 119.54 E-value: 4.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 335 PAWKEYINHKFTNMLAKGTLPLPAFQDYLKQDYLYLVNFARAYSLKGYKentFPNI------LEAAQSVIHVieEKELHV 408
Cdd:cd19365 10 PIYAAILAHPFIRELADGTLPREKFRFYLAQDALYLRDYARALALLAAR---APDPeeqvffARFAAGAIEV--ERELHR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 409 SMCSSYGVSLQDlkscEESPACTAYSRYILDTGAAQDVAALdfVQA--PCLIGYYVIAARLMKEpfRNPQGPYQKWVDNY 486
Cdd:cd19365 85 SFLGEFGIDAAA----EPSPVTLAYTSFLLATAATGPYAVA--VAAvlPCFWIYAEVGKRLAAA--ASPNHPYQDWIDTY 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 19113317 487 FCEDYLSAVRRGCRQIEEIVLKLSPERIQELIEIFIRATKFETLFWE 533
Cdd:cd19365 157 SDEEFAEAVRRAIAIVDRLAAEASPEERARMLEAFLRASRLEWMFWD 203
|
|
| TenA_C_HP1287-like |
cd19361 |
TenA_C proteins similar to Helicobacter pylori TenA (HP1287; This family of TenA proteins ... |
323-533 |
1.21e-30 |
|
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: 118.84 E-value: 1.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 323 FIEYILShpQVVPAWKEYINHKFTNMLAKGTLPLPAFQDYLKQDYLYLVNFARAYSLKGYKENTFPNILEAAQSVIHVI- 401
Cdd:cd19361 1 LSERLYE--AVEDIWDSYYEHPFVQGIADGTLDIEKFRFYMIQDYLYLLDYAKVFALGVAKAKDEEVMRFFADLINAILn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 402 EEKELHVSMCSSYGVSLQDLKSCEESPACTAYSRYILDTGAAQDVAALDFVQAPCLIGYYVIAARLMKepfRNPQG---- 477
Cdd:cd19361 79 EEMDIHRGYMKRLGITEEEIENTKPALDNLSYTSYMLSVAYEGGIAEILAAILSCSWSYEYIAKKLVE---RYPAAlehe 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 19113317 478 PYQKWVDNYFCEDYLSAVRRGCRQIEEIVLKLSPERIQELIEIFIRATKFETLFWE 533
Cdd:cd19361 156 FYGEWVKGYSSEEYAEANQELIDLLDRLTEDISEEQIEKLEEIFVNCSRYELKFWD 211
|
|
| TenA_C_PH1161-like |
cd19363 |
uncharacterized TenA_C proteins similar to Pyrococcus horikoshii PH1161; This family of TenA ... |
337-536 |
2.59e-27 |
|
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: 109.34 E-value: 2.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 337 WKEYINHKFTNMLAKGTLPLPAFQDYLKQDYLYLVNFARAYSLKGYKENTFPNILEAAqSVIHVIEEKEL--HVSMCSSY 414
Cdd:cd19363 13 WKKILNHPFVVELYSGTLPMEKFKFYLLQDYNYLVGSTKNLSILASKAESLDLMRELL-ELAYGEATTEFanYEELLDEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 415 GVSLQDLKSCEESPACTAYSRYILDT----GAAQDVAALdfvqAPCLIGYYVIAARLMKEPFRNPQGPYQKWVDNYFCED 490
Cdd:cd19363 92 GLSLEDAIKVEPFPTNVAYMNFLLSTsslgSFYEGLAAL----LPCFWSYLEIAEYHKDKLSENPNDIYRDWASVYLSKE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 19113317 491 YLSAVRRgCRQIEEIVLKLSPERiqELIEIFIRATKFETLFWETPY 536
Cdd:cd19363 168 YKELVER-LRRIVDKYGEGEPFE--KLKRIFKTASKYEYMFWDAAY 210
|
|
| TenA_C_BsTenA-like |
cd19364 |
TenA_C proteins similar to Bacillus subtilis TenA; This family of TenA proteins belongs to the ... |
330-536 |
4.87e-27 |
|
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: 108.43 E-value: 4.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 330 HPQVVPAWKEYINHKFTNMLAKGTLPLPAFQDYLKQDYLYLVNFARAYSLKGYKENTFPNILEAAQSVIHVIE-EKELHV 408
Cdd:cd19364 6 REAADPLWQKSFEHPFIQGLADGTLPLETFRYYLIQDAYYLKHFAKLHALAAAKADDPAIKALLLEGAQGLAEgELALRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 409 SMCSSYGVSLQDLKSCEESPACTAYS----RYILDTGAAQDVAALdfvqAPCLIGYYVIAARLMKEPFRNPQgpYQKWVD 484
Cdd:cd19364 86 TFFKELGITEEEIAQTPPAPTAYHYVshmyRQLNEGSVAEAVAAL----LPCYWLYQEIGERLADAGSPVPL--YQRWID 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 19113317 485 NYFCEDYLSAVRRGCRQIEEIVLKLSPERIQELIEIFIRATKFETLFWETPY 536
Cdd:cd19364 160 TYASDEFTESVQQQIDLVDRLAEEASEEEREKMKQAFLISSYYELQFWEMAY 211
|
|
| COG1992 |
COG1992 |
Predicted transcriptional regulator fused phosphomethylpyrimidine kinase (thiamin biosynthesis) ... |
47-315 |
1.01e-26 |
|
Predicted transcriptional regulator fused phosphomethylpyrimidine kinase (thiamin biosynthesis) [General function prediction only];
Pssm-ID: 441595 [Multi-domain] Cd Length: 432 Bit Score: 112.54 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 47 SGGAGIQADLKTMTSLGVYGMSAITCL-----VAENAGGVDSVEEMSPAFVESQIDCCIRDipchvVKTGMLGSPEIVKA 121
Cdd:COG1992 1 GGGGGGGADAKTAAALGAGGGGTTTAVtvtatTTVTGVGSDPPPPVEVQQQAVAADDDVDD-----AKTGMLMTATIVEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 122 VARSAKKFNFSkLVVDPVMVATSGDSLVTKDIVSVLNEELLPLTYLVTPNIPEAivlaknqgLDISNINSVSDMERCAAV 201
Cdd:COG1992 76 VAVVVKSRDKP-LVVVVVPVAVAAAGLGLLLAEAELAKLLLPLLATVTPNEPEV--------EELLLPTIRSLLAEARAA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 202 IhklgpkhvlLKGGHMPVNNLGLKSSDDEDLRVVDILYDGNRFYHFSSSYLKKGEVHGTGCTLSSAIASFLAWEHSLTEA 281
Cdd:COG1992 147 R---------LALQEEGADALGVKGGHVSGDAVVDVLEDERDVETFRHPRLVTEATHGSGCTFSAAIAALLAKGLSLEEA 217
|
250 260 270
....*....|....*....|....*....|....
gi 19113317 282 VQFGIDYVHGAITHSPPINNCStNILNHMTRLRI 315
Cdd:COG1992 218 VRGAKLFLLHAIRYGLLVGKGV-GPVNHLADLRL 250
|
|
| TenA_C_AtTH2-like |
cd19368 |
TenA_C family similar to the N-terminal TenA_C domain of Arabidopsis thaliana thiamine ... |
337-531 |
1.74e-25 |
|
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: 104.24 E-value: 1.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 337 WKEY-------INHKFTNMLAKGTLPLPAFQDYLKQDYLYLVNFARAYSLKGYKENTfpnilEAAQSVIH-----VIEEK 404
Cdd:cd19368 6 WKKNrdealfaLYHPFVVGLAAGNLPLDSFRHYISQDAHFLEAFARAYELAEAKADD-----DEDKKAIRelrkgVLEEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 405 ELHVSMCSSYGVSLQdlKSCEESPACTAYSRYILDT--GAAQDVAALDFVQAPCLIGYYVIAARLMKEPFRNPQGPYQKW 482
Cdd:cd19368 81 KLHDSYAEEWGVDLP--KEVTPDPATRKYTDFLLATasGKVKVAAYTLAAMAPCMRLYAFLGQELARALDDTEDHPYKKW 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 19113317 483 VDNYFCEDYLSAVrrgcRQIEEIVLKLS----PERIQELIEIFIRATKFETLF 531
Cdd:cd19368 159 IDTYSSQEFEALA----LQLEDLLDKLSasltGEELEALEKLYRRAMKLEVEF 207
|
|
| TenA_C_SaTenA-like |
cd19360 |
TenA_C proteins similar to Staphylococcus aureus TenA (SaTenA); This family of TenA proteins ... |
342-533 |
2.03e-21 |
|
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: 92.65 E-value: 2.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 342 NHKFTNMLAKGTLPLPAFQDYLKQDYLYLVNFARAYSLKGYKENTFPNI---LEAAQSVIHviEEKELHVSMCSSYGVSL 418
Cdd:cd19360 18 AHPFVQGIAAGELPKEALIHYVQQDYEYLNAFLKVYALAIAKSDTREDMrffLEQIGFILN--GESHAHQNLCEVAGVDY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 419 QDLKSCEESPACTAYSRYILDTGAAQDVAALDFVQAPCLIGYYVIAARLMKEPFRNPQGPYQKWVDNYFCEDYLSAVRRG 498
Cdd:cd19360 96 EELQGAPWAPTADHYIKHMYYAARTGDLGDILAALLPCPWTYVELAKRLIEEGKPTPDNPFYEWIDFYADDEMDGLTDQL 175
|
170 180 190
....*....|....*....|....*....|....*
gi 19113317 499 CRQIEEIVLKLSPERIQELIEIFIRATKFETLFWE 533
Cdd:cd19360 176 FARLDRLAEKASEEERERAKQAFLKSCQLEWRFWE 210
|
|
| TenA_C_Bt3146-like |
cd19359 |
uncharacterized TenA_C proteins similar to Bacteroides thetaiotaomicron Bt3146; This family of ... |
337-534 |
4.11e-20 |
|
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: 88.56 E-value: 4.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 337 WKEYINHKFTNMLAKGTLPLPAFQDYLKQDYLYLVNFARAYSLKGYKENTFPNILEAAQSVIHVIEEKELHVSMCSSYGV 416
Cdd:cd19359 12 WDKALNNPFCQGMADGTLDLDGFGYYMVQDYYYCINYVRFKALRAAKAPDPDLLAFLAAKIKSYLDYAEDFLKTCHIKLG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 417 SLQDLKSCEESPACTAYSRYILDTGAAQDVAALDFVQAPCLIGYYVIAARLMKEPFRNPQGPYQKWVDNYFCEDYLSavr 496
Cdd:cd19359 92 IPDVVDGVKPSPALKAYVDFERSVAESEDWFYLLVAMIPCIYLWYWLANQLNEDPSDKNTNFYKTWIEPNLPDPSSA--- 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 19113317 497 rgcRQIEEIV---LKLSPERIQELIEIFIRATKFETLFWET 534
Cdd:cd19359 169 ---KQLEFFLnanAAWSKIDREKANEIFRQAMQLEINFFNS 206
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
105-296 |
4.81e-20 |
|
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: 90.21 E-value: 4.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 105 CHVVKTGMLGSPEIVKAVARSAKKF----NFSKLVVDPVMvatsGDSL----VTKDIVSVLNEELLPLTYLVTPNIPEAI 176
Cdd:COG2240 75 FDAVLSGYLGSAEQGDIIADFVARVkaanPDALYLCDPVM----GDNGkgyyVFPGIAEFIMRRLVPLADIITPNLTELA 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 177 VLAknqGLDISNInsvSDMERCAAVIHKLGPKHVLLKgghmpvnnlGLKSSDDEDLRVVDILYDGNRFYHFSSSYLkKGE 256
Cdd:COG2240 151 LLT---GRPYETL---EEALAAARALLALGPKIVVVT---------SVPLDDTPADKIGNLAVTADGAWLVETPLL-PFS 214
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 19113317 257 VHGTGCTLSSAIASFLAWEHSLTEAVQFGIDYVHGAITHS 296
Cdd:COG2240 215 PNGTGDLFAALLLAHLLRGKSLEEALERAAAFVYEVLERT 254
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
79-293 |
4.89e-19 |
|
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: 86.87 E-value: 4.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 79 GGVDSVEEMSpAFVE--SQIDCCIRdipCHVVKTGMLGSPEIVKAVARSAKKFNFS----KLVVDPVMvatsGDS----L 148
Cdd:cd01173 49 GFVLSAEELE-DLLEglEALGLLLE---YDAVLTGYLGSAEQVEAVAEIVKRLKEKnpnlLYVCDPVM----GDNgklyV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 149 VTKDIVSVLNEELLPLTYLVTPNIPEAIVLAKnqgldiSNINSVSDMERCAAVIHKLGPKHVLLKgghmpvnnlGLKSSD 228
Cdd:cd01173 121 VAEEIVPVYRDLLVPLADIITPNQFELELLTG------KKINDLEDAKAAARALHAKGPKTVVVT---------SVELAD 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113317 229 DEDLRVV-DILYDGNRFYHFSSSYlkKGEVHGTGCTLSSAIASFLAWEHSLTEAVQFGIDYVHGAI 293
Cdd:cd01173 186 DDRIEMLgSTATEAWLVQRPKIPF--PAYFNGTGDLFAALLLARLLKGKSLAEALEKALNFVHEVL 249
|
|
| TenA_C_SsTenA-1-like |
cd19362 |
uncharacterized TenA_C proteins similar to Sulfolobus solfataricus TenA-1 (Sso2206); This ... |
337-533 |
2.21e-16 |
|
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: 77.87 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 337 WKEYINHKFTNMLAKGTLPLPAFQDYLKQDYLY----LVNFARAYSLKGYKENTfpNILeaaqSVIHVIEEK--ELHVSM 410
Cdd:cd19362 12 WNKYVRHEFVERMRDGTLPLDNFRYYLIQDSKYveemLRALLRASSKAPLDKAI--KIL----NSVFSGRDKgmEVHKFL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 411 CSSYGVSLQDLKSCEESPACTAYSR---YILDTGAAQDVAALdfvqAPCLIGYYVIAARLMKEPfrNPQgpYQKWVDNYF 487
Cdd:cd19362 86 YSELGITEDEIRRTGYNLVNYAYTRhlyYYSTLGWPQFLAAW----APCMWGYSEIGKYVLNSP--NEL--YKTWASFYA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 19113317 488 CEDYLSAVRRGCRQIEEIvlklspERIQELIEIFIRATKFETLFWE 533
Cdd:cd19362 158 SKDYKKRVEAILEALDSI------EDTEDIKNIFRNSVNFEIMFWD 197
|
|
| PTZ00347 |
PTZ00347 |
phosphomethylpyrimidine kinase; Provisional |
328-537 |
4.00e-13 |
|
phosphomethylpyrimidine kinase; Provisional
Pssm-ID: 240375 [Multi-domain] Cd Length: 504 Bit Score: 71.53 E-value: 4.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 328 LSHPQVVPA-----WKEY-------INHKFTNMLAKGTLPLPAFQDYLKQDYLYLVNFARAYSLKGYKENTFPNILEAAQ 395
Cdd:PTZ00347 4 FYHEPVFGGlsealWKENqdlammsLHLPFVQGLGDGTLDQNAFRTYIAQDTLYLNGYIRILSYCITKSDVTATGGGLLE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 396 SVIHVIEE-KELHvsmcSSYgvsLQDLKSCEESPACTAYSRYILDTGAAQDVAALDFVQA--PCLIGYYVIAARLMKEPF 472
Cdd:PTZ00347 84 LLKGVLEElKNCH----HHY---IDNPDAAGPEAACRKYVDFLLASGNADTLGPSVVIAAviPCARLYAWVGQELTNEVE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 19113317 473 RNPQGPYQKWVDNYFCEDylsaVRRGCRQIEEIVLK-LSPERIQELIEIFIRATKFETLFWETPYY 537
Cdd:PTZ00347 157 LTESHPFRRWLLSYSDEP----INTSVEQLESLLDKyIRPGEFSEVAQAYRRAMELEYDFFDSFGY 218
|
|
| TenA_E_At3g16990-like |
cd19357 |
TenA_E proteins similar to Arabidopsis thaliana At3g16990; This family of TenA proteins ... |
335-533 |
1.51e-12 |
|
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: 66.96 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 335 PAWKEYINHKFTNMLAKGTLPLPAFQDYLKQDYLYLVNFARAyslkgykentFPNILEAAQSVIHVIEEKELHV------ 408
Cdd:cd19357 10 ALYTAATQHPFLRAAADGTLPKEALSRWLAQDRLYVQAYIRF----------LGSLLARAPLPSSSLNQRLLDVllgala 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 409 ----------SMCSSYGVSLQDLKScEESPACTAYSRYILDTGAaqdvAALDFVQApcLIGYYVI---------AARLMK 469
Cdd:cd19357 80 nlrrelaffeETAAEYGLDLPGLGV-PPSPATRAYVDFLASLAS----EGVSYLEG--LVVLWATekvyldawsYARSFL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19113317 470 EPFRNPQGPYQKWVDNYFCEDYLSAVRRGCRQIEEIVLKLSPERIQELIEIFIRATKFETLFWE 533
Cdd:cd19357 153 PSDADGGALYREFIPNWTSPEFAAFVDRLGDLVDEALEQAGEEVLERAEEVWRRVLELEEAFWP 216
|
|
| TenA_E_Spr0628-like |
cd19358 |
TenA_E proteins similar to Streptococcus pneumoniae Spr0628 and Saccharomyces cerevisiae S288C ... |
335-536 |
8.08e-12 |
|
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: 64.51 E-value: 8.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 335 PAWKEYINHKFTNMLAKGTLPLPAFQDYLKQDYLYLVNFARaysLKGY---KENTFPNILEAAQsVIHVIEEKEL---HV 408
Cdd:cd19358 11 EDWDAAVTHRFVRELCAGTLPDAVLARYLVQDYQFVETFLR---LLGKavaKAPDLEAKLRLAR-FLGFLANDENdyfER 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 409 SMcSSYGVSLQDLKSCEESPACTAYSRYILDTGAAQD--------VAA----LDFVQApcligyyviAARLMKEPFrnpq 476
Cdd:cd19358 87 AF-AALGVSEADREAPPLLPATRAFIDLMLEAARSGSyaeiltvlLVAewlyLDWASR---------AAAAAPLRF---- 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 477 gPYQKWVDNYFCEDYLSAVRRGCRQIEEIVLklSPERIQELIEIFIRATKFETLFWETPY 536
Cdd:cd19358 153 -KHQEWIDLHSGPEFEAWVDFLRDEVDRVGP--TEEERERLEAVFARAVELEIAFFDAAY 209
|
|
| PRK07105 |
PRK07105 |
pyridoxamine kinase; Validated |
101-293 |
2.27e-10 |
|
pyridoxamine kinase; Validated
Pssm-ID: 180840 [Multi-domain] Cd Length: 284 Bit Score: 61.47 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 101 RDIPCHVVKTGMLGSPEIVKAVARSAKKFNFSK--LVVDPVMvatsGD-----SLVTKDIVSVLnEELLPLTYLVTPNIP 173
Cdd:PRK07105 72 LNLKFDAIYSGYLGSPRQIQIVSDFIKYFKKKDllVVVDPVM----GDngklyQGFDQEMVEEM-RKLIQKADVITPNLT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 174 EAIVLAKNQGLDISniNSVSDMERCAAVIHKLGPKHVLLKGghMPVnnlglkssDDEDLRVVdiLYD--GNRFYHFSSSY 251
Cdd:PRK07105 147 EACLLLDKPYLEKS--YSEEEIKQLLRKLADLGPKIVIITS--VPF--------EDGKIGVA--YYDraTDRFWKVFCKY 212
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 19113317 252 LKkgeVH--GTGCTLSSAIASFLAWEHSLTEAVQFGIDYVHGAI 293
Cdd:PRK07105 213 IP---AHypGTGDIFTSVITGSLLQGDSLPIALDRAVQFIEKGI 253
|
|
| PTZ00344 |
PTZ00344 |
pyridoxal kinase; Provisional |
106-282 |
2.77e-07 |
|
pyridoxal kinase; Provisional
Pssm-ID: 240372 [Multi-domain] Cd Length: 296 Bit Score: 52.39 E-value: 2.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 106 HVVkTGMLGSPEIVKAVARSAKKFNFSK----LVVDPVMvATSGDSLVTKDIVSVLnEELLPLTYLVTPNIPEAIVLAKn 181
Cdd:PTZ00344 80 YVL-TGYINSADILREVLATVKEIKELRpkliFLCDPVM-GDDGKLYVKEEVVDAY-RELIPYADVITPNQFEASLLSG- 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 182 qgldiSNINSVSDMERCAAVIHKLGPKHVLLKGGHMPVNNLGLK----SSDDEDLRvvdilydgNRFYHFSSSYLkKGEV 257
Cdd:PTZ00344 156 -----VEVKDLSDALEAIDWFHEQGIPVVVITSFREDEDPTHLRfllsCRDKDTKN--------NKRFTGKVPYI-EGRY 221
|
170 180
....*....|....*....|....*..
gi 19113317 258 HGTGCTLSsaiASFLAWEHS--LTEAV 282
Cdd:PTZ00344 222 TGTGDLFA---ALLLAFSHQhpMDLAV 245
|
|
| PLN02978 |
PLN02978 |
pyridoxal kinase |
106-212 |
1.79e-06 |
|
pyridoxal kinase
Pssm-ID: 215529 [Multi-domain] Cd Length: 308 Bit Score: 50.12 E-value: 1.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 106 HVVkTGMLGSPEIVKAVARSAKKFNF--SKL--VVDPVMvATSGDSLVTKDIVSVLNEELLPLTYLVTPNIPEAIVLAkn 181
Cdd:PLN02978 89 HLL-TGYIGSVSFLRTVLRVVKKLRSvnPNLtyVCDPVL-GDEGKLYVPPELVPVYREKVVPLATMLTPNQFEAEQLT-- 164
|
90 100 110
....*....|....*....|....*....|.
gi 19113317 182 qGLDISNINSVsdMERCAAvIHKLGPKHVLL 212
Cdd:PLN02978 165 -GIRIVTEEDA--REACAI-LHAAGPSKVVI 191
|
|
| YXKO-related |
cd01171 |
B.subtilis YXKO protein of unknown function and related proteins. Based on the conservation of ... |
41-293 |
2.13e-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: 49.15 E-value: 2.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 41 IAGSDCSGGAGIqadlktMTSLGVY----GMSAITClVAENAGGVDSV--EEMSPAFVESQIDCCIRDIP-CHVVKTGM- 112
Cdd:cd01171 14 IGGSRGYTGAAY------LAALAALragaGLVTVAT-PPEAAAVIKSYspELMVHPLLETDIEELLELLErADAVVIGPg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 113 LGSPEIVKAVARSAKKFNfSKLVVDpvmvatsGDSL--VTKDIVSVLNEEllplTYLVTPNIPEAIVLaknqgLDISNIN 190
Cdd:cd01171 87 LGRDEEAAEILEKALAKD-KPLVLD-------ADALnlLADEPSLIKRYG----PVVLTPHPGEFARL-----LGALVEE 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 191 SVSDMERCAAVIHKLGPKHVLLKGGhmpvnnlglkssddedlrvVDILYDGNRFYHFS---SSYLKKGevhGTGCTLSSA 267
Cdd:cd01171 150 IQADRLAAAREAAAKLGATVVLKGA-------------------VTVIADPDGRVYVNptgNPGLATG---GSGDVLAGI 207
|
250 260
....*....|....*....|....*.
gi 19113317 268 IASFLAWEHSLTEAVQFGIdYVHGAI 293
Cdd:cd01171 208 IAALLAQGLSPLEAAALAV-YLHGLA 232
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
107-273 |
2.91e-06 |
|
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).
Pssm-ID: 238177 [Multi-domain] Cd Length: 196 Bit Score: 48.25 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 107 VVKTGMLGSPEIVKAVARSAKKFNfSKLVVDPVMVATSGDSLvtkdivsvLNEELLPLTYLVTPNIPEAIVLAKNQGLDI 186
Cdd:cd00287 61 VVISGLSPAPEAVLDALEEARRRG-VPVVLDPGPRAVRLDGE--------ELEKLLPGVDILTPNEEEAEALTGRRDLEV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 187 SNINSVsdmercAAVIHKLGPKHVLLKGGHMpvnnlglkssddedlrvVDILYDGNRFYHFSSSYLKK-GEVHGTGCTLS 265
Cdd:cd00287 132 KEAAEA------AALLLSKGPKVVIVTLGEK-----------------GAIVATRGGTEVHVPAFPVKvVDTTGAGDAFL 188
|
....*...
gi 19113317 266 SAIASFLA 273
Cdd:cd00287 189 AALAAGLA 196
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
113-285 |
1.55e-05 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 46.95 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 113 LGSPEIVKAVARSAKKFNfskLVVDPVMVATSGDSLVTkdivsvlNEELLPLTYLVTPNIPEAIVLAKnqgldiSNINSV 192
Cdd:pfam00294 139 LGLPEATLEELIEAAKNG---GTFDPNLLDPLGAAREA-------LLELLPLADLLKPNEEELEALTG------AKLDDI 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 193 SDMERCAAVIHKLGPKHVLLKgghmpvnnLGLKSSddedlrvvdILYDGNRFYHFSSsyLKKGEV---HGTGCTLSSAIA 269
Cdd:pfam00294 203 EEALAALHKLLAKGIKTVIVT--------LGADGA---------LVVEGDGEVHVPA--VPKVKVvdtTGAGDSFVGGFL 263
|
170
....*....|....*.
gi 19113317 270 SFLAWEHSLTEAVQFG 285
Cdd:pfam00294 264 AGLLAGKSLEEALRFA 279
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
115-296 |
7.64e-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: 44.88 E-value: 7.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 115 SPEIVKAVARSAKKFNfSKLVVDPvmvatsGDSLVTKDIVSVLNEELLPLTYLVTPNIPEAIVLAKnqgldisninsVSD 194
Cdd:COG0524 143 PREALLAALEAARAAG-VPVSLDP------NYRPALWEPARELLRELLALVDILFPNEEEAELLTG-----------ETD 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 195 MERCAAVIHKLGPKHVLLKGGHMPVnnlglkssddedlrvvdILYDGNRFYHFSSsyLKKGEVHGTGC--TLSSAIASFL 272
Cdd:COG0524 205 PEEAAAALLARGVKLVVVTLGAEGA-----------------LLYTGGEVVHVPA--FPVEVVDTTGAgdAFAAGFLAGL 265
|
170 180
....*....|....*....|....
gi 19113317 273 AWEHSLTEAVQFGIdyVHGAITHS 296
Cdd:COG0524 266 LEGLDLEEALRFAN--AAAALVVT 287
|
|
| PRK09355 |
PRK09355 |
hydroxyethylthiazole kinase; Validated |
235-282 |
5.14e-04 |
|
hydroxyethylthiazole kinase; Validated
Pssm-ID: 236477 [Multi-domain] Cd Length: 263 Bit Score: 42.09 E-value: 5.14e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 19113317 235 VDILYDGNRFYHFS--SSYLKKgeVHGTGCTLSSAIASFLAWEHSLTEAV 282
Cdd:PRK09355 166 VDYITDGERVVSVHngHPLMTK--VTGTGCLLSAVVAAFAAVEKDYLEAA 213
|
|
| THZ_kinase |
cd01170 |
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ... |
235-273 |
1.51e-03 |
|
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the hydroxylgroup of Thz. A reaction that allows cells to recycle Thz into the thiamine biosynthesis pathway, as an alternative to its synthesis from cysteine, tyrosine and 1-deoxy-D-xylulose-5-phosphate.
Pssm-ID: 238575 [Multi-domain] Cd Length: 242 Bit Score: 40.60 E-value: 1.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 19113317 235 VDILYDGNRFYHFS--SSYLKKgeVHGTGCTLSSAIASFLA 273
Cdd:cd01170 162 VDYITDGERVVVVKngHPLLTK--ITGTGCLLGAVIAAFLA 200
|
|
| HK |
pfam02110 |
Hydroxyethylthiazole kinase family; |
235-273 |
6.35e-03 |
|
Hydroxyethylthiazole kinase family;
Pssm-ID: 396609 [Multi-domain] Cd Length: 247 Bit Score: 38.51 E-value: 6.35e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 19113317 235 VDILYDGNRFY--HFSSSYLkkGEVHGTGCTLSSAIASFLA 273
Cdd:pfam02110 161 VDYVSDGTSVYviHNGTELL--GKITASGCLLGSVVAAFCA 199
|
|
| pdxK |
PRK08176 |
pyridoxine/pyridoxal/pyridoxamine kinase; |
107-289 |
6.47e-03 |
|
pyridoxine/pyridoxal/pyridoxamine kinase;
Pssm-ID: 181269 [Multi-domain] Cd Length: 281 Bit Score: 38.87 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 107 VVKTGMLGSPEIVKAVAR---SAKKFNFSKLV-VDPVMVATSGDSLVTKDIVSVLNEELLPLTYLVTPNIPEAIVLAknq 182
Cdd:PRK08176 91 AVTTGYMGSASQIKILAEwltALRADHPDLLImVDPVIGDIDSGIYVKPDLPEAYRQHLLPLAQGLTPNIFELEILT--- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19113317 183 GLDISNINSVSDMERCaavihklgpkhvLLKGghmpvnnlGLK---------SSDDEDLRVVDILYDGnrfYHFSSSYLK 253
Cdd:PRK08176 168 GKPCRTLDSAIAAAKS------------LLSD--------TLKwvvitsaagNEENQEMQVVVVTADS---VNVISHPRV 224
|
170 180 190
....*....|....*....|....*....|....*.
gi 19113317 254 KGEVHGTGCTLSSAIASFLAWEHSLTEAVQFGIDYV 289
Cdd:PRK08176 225 DTDLKGTGDLFCAELVSGLLKGKALTDAAHRAGLRV 260
|
|
| |
