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Conserved domains on  [gi|330443752|ref|NP_015446|]
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putative phosphomethylpyrimidine kinase [Saccharomyces cerevisiae S288C]

Protein Classification

TenA family protein( domain architecture ID 10785335)

TenA family protein such as Bacillus halodurans aminopyrimidine aminohydrolase, which catalyzes an amino-pyrimidine hydrolysis reaction at the C5' of the pyrimidine moiety of thiamine compounds, as part of the thiamine salvage pathway

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 55-313 1.02e-95

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: 292.08  E-value: 1.02e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752   55 DSSGGAGVEADIKTITAHRCYAMTCVTTLTAQTPVKVYGAQNIPKKMVSQILDANLQDMKCNVIKTGML-TVDAIEVLHE 133
Cdd:pfam08543   1 DSSGGAGIQADLKTFSALGVYGMSVITALTAQNTLGVQGVHPLPPEFVAAQLDAVLEDIPVDAVKTGMLgSAEIIEAVAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  134 KLLQLGenrPKLVIDPVLCAASDSSPTGKDVVSLIIEKISPFADILTPNISDCFMLLGenREVSKLQDVLEIAKDLSRiT 213
Cdd:pfam08543  81 KLDKYG---VPVVLDPVMVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTG--RKIKTLEDMKEAAKKLLA-L 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  214 NCSNILVKGGHIPcddGKEKHITDVLYlgAEQKFITFKGQFVNTTRTHGAGCTLASAIASNLARGYSLSQSVYGGIEYVQ 293
Cdd:pfam08543 155 GAKAVLIKGGHLE---GEEAVVTDVLY--DGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKEYVT 229

                         250       260
                  ....*....|....*....|
gi 330443752  294 NAIAIGCDVTKkavKVGPIN 313
Cdd:pfam08543 230 EAIRDALNLGK---GHGPVN 246
TENA_THI-4 pfam03070
TENA/THI-4/PQQC family; Members of this family are found in all the three major phyla of life: ...
 361-571 4.24e-85

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: 263.45  E-value: 4.24e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  361 HPKVKPHWDAYVNHEFVKRVADGTLERKKFQFFIEQDYLYLIDYVRVCCVTGSKSPTLEDL-EKDLVIADCARNELNEHe 439
Cdd:pfam03070   1 HPQLRPIWKFYINHPFVQALAKGTLPREQFQGYVIQDYLYLVNFARVLAIIASKSPDLEVRrEWENRIVDHDGNEIELH- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  440 RRLREEFGVKDPDyLQKIKRGPALRAYCRYLIDISRRGNWQEIVVALNPCLMGYVYAVDKVKDKITAAEGSIYSEWCDTC 519
Cdd:pfam03070  80 LRLAEALGLSRED-LSAYKPLPATRAYVRYLLDFARRGSWLEAVAALLPCLFVYQEIASRLGEKIRALEGPEYYEWVKTY 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 330443752  520 ASSFCYQAVLEGERLMNHILETYPPDQLDSLVTIFARGCELETNFWTAAMEY 571
Cdd:pfam03070 159 ASEYFRAAVEEAKRLLDRLLAYVSDEQLEELQEIFLKALEFEYSFWTMALDA 210
 
Name Accession Description Interval E-value
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 55-313 1.02e-95

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: 292.08  E-value: 1.02e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752   55 DSSGGAGVEADIKTITAHRCYAMTCVTTLTAQTPVKVYGAQNIPKKMVSQILDANLQDMKCNVIKTGML-TVDAIEVLHE 133
Cdd:pfam08543   1 DSSGGAGIQADLKTFSALGVYGMSVITALTAQNTLGVQGVHPLPPEFVAAQLDAVLEDIPVDAVKTGMLgSAEIIEAVAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  134 KLLQLGenrPKLVIDPVLCAASDSSPTGKDVVSLIIEKISPFADILTPNISDCFMLLGenREVSKLQDVLEIAKDLSRiT 213
Cdd:pfam08543  81 KLDKYG---VPVVLDPVMVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTG--RKIKTLEDMKEAAKKLLA-L 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  214 NCSNILVKGGHIPcddGKEKHITDVLYlgAEQKFITFKGQFVNTTRTHGAGCTLASAIASNLARGYSLSQSVYGGIEYVQ 293
Cdd:pfam08543 155 GAKAVLIKGGHLE---GEEAVVTDVLY--DGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKEYVT 229

                         250       260
                  ....*....|....*....|
gi 330443752  294 NAIAIGCDVTKkavKVGPIN 313
Cdd:pfam08543 230 EAIRDALNLGK---GHGPVN 246
HMPP_kinase cd01169
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ...
 47-297 5.95e-92

4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two consecutive phosphorylation steps in the thiamine phosphate biosynthesis pathway, leading to the synthesis of vitamin B1. The first step is the phosphorylation of the hydroxyl group of HMP to form 4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate (HMP-P) and then the phophorylation of HMP-P to form 4-amino-5-hydroxymethyl-2-methyl-pyrimidine pyrophosphate (HMP-PP), which is the substrate for the thiamine synthase coupling reaction.


Pssm-ID: 238574 [Multi-domain]  Cd Length: 242  Bit Score: 282.08  E-value: 5.95e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  47 TVMSIAGSDSSGGAGVEADIKTITAHRCYAMTCVTTLTAQTPVKVYGAQNIPKKMVSQILDANLQDMKCNVIKTGML-TV 125
Cdd:cd01169    1 VVLTIAGSDSSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVFGVHPVPPEFVAAQLDAVLEDIPVDAIKIGMLgSA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 126 DAIEVLHEKLLQLGEnrPKLVIDPVLCAASDSSPTGKDVVSLIIEKISPFADILTPNISDCFMLLGenREVSKLQDVLEI 205
Cdd:cd01169   81 EIIEAVAEALKDYPD--IPVVLDPVMVAKSGDSLLDDDAIEALRELLLPLATLITPNLPEAELLTG--LEIATEEDMMKA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 206 AKDLSRiTNCSNILVKGGHIPCDdgkekHITDVLYLGaeQKFITFKGQFVNTTRTHGAGCTLASAIASNLARGYSLSQSV 285
Cdd:cd01169  157 AKALLA-LGAKAVLIKGGHLPGD-----EAVDVLYDG--GGFFEFESPRIDTKNTHGTGCTLSSAIAANLAKGLSLEEAV 228

                        250
                 ....*....|..
gi 330443752 286 YGGIEYVQNAIA 297
Cdd:cd01169  229 REAKEYVTQAIR 240
TENA_THI-4 pfam03070
TENA/THI-4/PQQC family; Members of this family are found in all the three major phyla of life: ...
 361-571 4.24e-85

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: 263.45  E-value: 4.24e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  361 HPKVKPHWDAYVNHEFVKRVADGTLERKKFQFFIEQDYLYLIDYVRVCCVTGSKSPTLEDL-EKDLVIADCARNELNEHe 439
Cdd:pfam03070   1 HPQLRPIWKFYINHPFVQALAKGTLPREQFQGYVIQDYLYLVNFARVLAIIASKSPDLEVRrEWENRIVDHDGNEIELH- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  440 RRLREEFGVKDPDyLQKIKRGPALRAYCRYLIDISRRGNWQEIVVALNPCLMGYVYAVDKVKDKITAAEGSIYSEWCDTC 519
Cdd:pfam03070  80 LRLAEALGLSRED-LSAYKPLPATRAYVRYLLDFARRGSWLEAVAALLPCLFVYQEIASRLGEKIRALEGPEYYEWVKTY 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 330443752  520 ASSFCYQAVLEGERLMNHILETYPPDQLDSLVTIFARGCELETNFWTAAMEY 571
Cdd:pfam03070 159 ASEYFRAAVEEAKRLLDRLLAYVSDEQLEELQEIFLKALEFEYSFWTMALDA 210
salvage_TenA TIGR04306
thiaminase II; The TenA protein of Bacillus subtilis and Staphylococcus aurues, and the ...
 364-571 6.40e-81

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: 252.50  E-value: 6.40e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  364 VKPHWDAYVNHEFVKRVADGTLERKKFQFFIEQDYLYLIDYVRVCCVTGSKSpTLEDLEKDLV--IADCARNELNEHeRR 441
Cdd:TIGR04306   1 VKPIWDDYINHPFVQKIGDGTLERDKFRFYIEQDYAYLVEYAKVHALGGSKA-CDEDMEKELVeqIQGGVETEMGQH-KR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  442 LREEFGVKDPDYLQKIKRGPALRAYCRYLIDISRRGNWQEIVVALNPCLMGYVYAVDKVKDKITAAEGSIYSEWCDTCAS 521
Cdd:TIGR04306  79 LAEVLGISDEEYFQKIKPGPALRSYTSYMYDVSRRGNWQELVAALLPCLWGYGEAATKLKGKHTAPEHSVYHKWIETYSS 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 330443752  522 SFCYQAVLEGERLMNHILETYPPDQLDSLVTIFARGCELETNFWTAAMEY 571
Cdd:TIGR04306 159 SWFREAVNEGENLLNHLAETSSPEELEKLKTIFAESCEYEYNFWTMAYEY 208
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 49-314 1.22e-79

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: 250.73  E-value: 1.22e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  49 MSIAGSDSSGGAGVEADIKTITAHRCYAMTCVTTLTAQTPVKVYGAQNIPKKMVSQILDANLQDMKCNVIKTGML-TVDA 127
Cdd:COG0351    1 LTIAGSDPSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVTGVHPVPPEFVAAQLRAVLEDIPVDAIKIGMLgSAEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 128 IEVLHEKLLQLGEnrPKLVIDPVLCAASDSSPTGKDVVSLIIEKISPFADILTPNISDCFMLLGenREVSKLQDVLEIAK 207
Cdd:COG0351   81 IEAVAEILADYPL--VPVVLDPVMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALLG--IEITTLDDMREAAK 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 208 DLSRiTNCSNILVKGGHIPcddgkEKHITDVLYLGaeQKFITFKGQFVNTTRTHGAGCTLASAIASNLARGYSLSQSVYG 287
Cdd:COG0351  157 ALLE-LGAKAVLVKGGHLP-----GDEAVDVLYDG--DGVREFSAPRIDTGNTHGTGCTLSSAIAALLAKGLDLEEAVRE 228

                        250       260
                 ....*....|....*....|....*..
gi 330443752 288 GIEYVQNAIAIGCDVTKkavKVGPINH 314
Cdd:COG0351  229 AKEYVTQAIRAALRLGM---GHGPVNH 252
TenA_C_ScTHI20-like cd19367
TenA_C family similar to the C-terminal TenA_C domain of Saccharomyces cerevisiae THI20 ...
 366-569 1.55e-69

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: 222.77  E-value: 1.55e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 366 PHWDAYVNHEFVKRVADGTLERKKFQFFIEQDYLYLIDYVRVCCVTGSKSPTLEDLEKDLVIADCARNELNEHERRLrEE 445
Cdd:cd19367    1 PIWKAYTNHPFVRQLADGTLPLESFRHYLKQDYLYLIHYARAHALAAYKAPTLEDIRAAAAILLAILEEMELHVKYC-AE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 446 FGVkDPDYLQKIKRGPALRAYCRYLIDISRRGNWQEIVVALNPCLMGYVYAVDKVKDKI-TAAEGSIYSEWCDTCASSfC 524
Cdd:cd19367   80 WGI-SEEELEATPESPATLAYTRYVLDVGLSGDLLDLLVALAPCLLGYGEIGLRLAADPaTKLEGNPYWSWIETYASD-E 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 330443752 525 YQ-AVLEGERLMNHILETYP-PDQLDSLVTIFARGCELETNFWTAAM 569
Cdd:cd19367  158 YQeAVREGIELLEKLAAERPsPARLEELVKIFATATRLEIGFWDMGL 204
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 44-318 7.99e-66

bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 215.37  E-value: 7.99e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  44 KLPTVMSIAGSDSSGGAGVEADIKTITAHRCYAMTCVTTLTAQTPVKVYGAQNIPKKMVSQILDANLQDMKCNVIKTGML 123
Cdd:PRK06427   3 KRPIALTIAGSDSGGGAGIQADLKTFQALGVYGMSAITALTAQNTLGVQRVHPIPPEFVAAQLDAVFSDIRIDAVKIGML 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 124 -TVDAIEVLHEKLLQLGEnrPKLVIDPVLCAASDSSPTGKDVVSLIIEKISPFADILTPNISDCFMLLGenREVSKLQDV 202
Cdd:PRK06427  83 aSAEIIETVAEALKRYPI--PPVVLDPVMIAKSGDPLLADDAVAALRERLLPLATLITPNLPEAEALTG--LPIADTEDE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 203 LEIAKDLSRITNCSNILVKGGHipcdDGKEKHITDVLYLGAEqkFITFKGQFVNTTRTHGAGCTLASAIASNLARGYSLS 282
Cdd:PRK06427 159 MKAAARALHALGCKAVLIKGGH----LLDGEESVDWLFDGEG--EERFSAPRIPTKNTHGTGCTLSAAIAAELAKGASLL 232

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 330443752 283 QSVYGGIEYVQNAIAIGCDVTKkavKVGPINHVYAV 318
Cdd:PRK06427 233 DAVQTAKDYVTRAIRHALEIGQ---GHGPVNHFAYL 265
HMP-P_kinase TIGR00097
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ...
 48-314 1.49e-62

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: 206.37  E-value: 1.49e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752   48 VMSIAGSDSSGGAGVEADIKTITAHRCYAMTCVTTLTAQTPVKVYGAQNIPKKMVSQILDANLQDMKCNVIKTGML-TVD 126
Cdd:TIGR00097   1 ALTIAGSDSGGGAGIQADLKTFSALGVFGTSVITALTAQNTRGVTGVYPIPPDFVEAQLDAVFSDIPVDAAKTGMLaSAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  127 AIEVLHEKLLQLGEnrPKLVIDPVLCAASDSSPTGKDVVSLIIEKISPFADILTPNISDCFMLLGEnrEVSKLQDVLEIA 206
Cdd:TIGR00097  81 IVEAVARKLREYPV--RPLVVDPVMVAKSGAPLLEEEAIEALRKRLLPLATLITPNLPEAEALLGT--KIRTEQDMIKAA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  207 KDLsRITNCSNILVKGGHIPCDDGkekhiTDVLYLGAEqkFITFKGQFVNTTRTHGAGCTLASAIASNLARGYSLSQSVY 286
Cdd:TIGR00097 157 KKL-RELGPKAVLIKGGHLEGDQA-----VDVLFDGGE--IHILKAPRIETKNTHGTGCTLSAAIAANLAKGLSLKEAVK 228

                         250       260
                  ....*....|....*....|....*...
gi 330443752  287 GGIEYVQNAIAIGCDVTKkavKVGPINH 314
Cdd:TIGR00097 229 EAKEFVTGAIRYGLNIGH---GHGPLNH 253
TenA COG0819
Aminopyrimidine aminohydrolase TenA (thiamine salvage pathway) [Coenzyme transport and ...
 352-568 1.71e-49

Aminopyrimidine aminohydrolase TenA (thiamine salvage pathway) [Coenzyme transport and metabolism];


Pssm-ID: 440581 [Multi-domain]  Cd Length: 218  Bit Score: 170.45  E-value: 1.71e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 352 GSFFNYLINhpKVKPHWDAYVNHEFVKRVADGTLERKKFQFFIEQDYLYLIDYVRVCCVTGSKSPTLEDLEKDLVIADCA 431
Cdd:COG0819    1 MSFSERLRE--AAAPIWEAILEHPFVQGLADGTLPREAFRHYLVQDYLYLEHFARALALAAAKAPDLEDMRFLAGLAAGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 432 RNELNEHERRLREEFGVkDPDYLQKIKRGPALRAYCRYLIDISRRGNWQEIVVALNPCLMGYVYAVDKVKDKiTAAEGSI 511
Cdd:COG0819   79 LEVELALHERYAAELGI-SEEELEATPPSPTTRAYTSYLLAAAASGDYAELLAALLPCEWGYAEIGKRLAER-PLPPDHP 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 330443752 512 YSEWCDTCASSFCYQAVLEGERLMNHILETYPPDQLDSLVTIFARGCELETNFWTAA 568
Cdd:COG0819  157 YAEWIETYASEEFQELVEWLIALLDRLAATASEAERERLEEAFRTASRLEYAFWDMA 213
PTZ00347 PTZ00347
phosphomethylpyrimidine kinase; Provisional
 372-568 1.31e-09

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240375 [Multi-domain]  Cd Length: 504  Bit Score: 60.75  E-value: 1.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 372 VNHEFVKRVADGTLERKKFQFFIEQDYLYLIDYVRVCCVTGSKSPTLEDLEKDLVIADCARNELneheRRLREEFgVKDP 451
Cdd:PTZ00347  29 LHLPFVQGLGDGTLDQNAFRTYIAQDTLYLNGYIRILSYCITKSDVTATGGGLLELLKGVLEEL----KNCHHHY-IDNP 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 452 DylqKIKRGPALRAYCRYLIDISRRGNWQEIVV--ALNPCLMGYVYAVDKVKDKITAAEGSIYSEWCdtcaSSFCYQAVL 529
Cdd:PTZ00347 104 D---AAGPEAACRKYVDFLLASGNADTLGPSVViaAVIPCARLYAWVGQELTNEVELTESHPFRRWL----LSYSDEPIN 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 330443752 530 EGERLMNHILETY-PPDQLDSLVTIFARGCELETNFWTAA 568
Cdd:PTZ00347 177 TSVEQLESLLDKYiRPGEFSEVAQAYRRAMELEYDFFDSF 216
 
Name Accession Description Interval E-value
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 55-313 1.02e-95

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: 292.08  E-value: 1.02e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752   55 DSSGGAGVEADIKTITAHRCYAMTCVTTLTAQTPVKVYGAQNIPKKMVSQILDANLQDMKCNVIKTGML-TVDAIEVLHE 133
Cdd:pfam08543   1 DSSGGAGIQADLKTFSALGVYGMSVITALTAQNTLGVQGVHPLPPEFVAAQLDAVLEDIPVDAVKTGMLgSAEIIEAVAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  134 KLLQLGenrPKLVIDPVLCAASDSSPTGKDVVSLIIEKISPFADILTPNISDCFMLLGenREVSKLQDVLEIAKDLSRiT 213
Cdd:pfam08543  81 KLDKYG---VPVVLDPVMVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTG--RKIKTLEDMKEAAKKLLA-L 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  214 NCSNILVKGGHIPcddGKEKHITDVLYlgAEQKFITFKGQFVNTTRTHGAGCTLASAIASNLARGYSLSQSVYGGIEYVQ 293
Cdd:pfam08543 155 GAKAVLIKGGHLE---GEEAVVTDVLY--DGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKEYVT 229

                         250       260
                  ....*....|....*....|
gi 330443752  294 NAIAIGCDVTKkavKVGPIN 313
Cdd:pfam08543 230 EAIRDALNLGK---GHGPVN 246
HMPP_kinase cd01169
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ...
 47-297 5.95e-92

4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two consecutive phosphorylation steps in the thiamine phosphate biosynthesis pathway, leading to the synthesis of vitamin B1. The first step is the phosphorylation of the hydroxyl group of HMP to form 4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate (HMP-P) and then the phophorylation of HMP-P to form 4-amino-5-hydroxymethyl-2-methyl-pyrimidine pyrophosphate (HMP-PP), which is the substrate for the thiamine synthase coupling reaction.


Pssm-ID: 238574 [Multi-domain]  Cd Length: 242  Bit Score: 282.08  E-value: 5.95e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  47 TVMSIAGSDSSGGAGVEADIKTITAHRCYAMTCVTTLTAQTPVKVYGAQNIPKKMVSQILDANLQDMKCNVIKTGML-TV 125
Cdd:cd01169    1 VVLTIAGSDSSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVFGVHPVPPEFVAAQLDAVLEDIPVDAIKIGMLgSA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 126 DAIEVLHEKLLQLGEnrPKLVIDPVLCAASDSSPTGKDVVSLIIEKISPFADILTPNISDCFMLLGenREVSKLQDVLEI 205
Cdd:cd01169   81 EIIEAVAEALKDYPD--IPVVLDPVMVAKSGDSLLDDDAIEALRELLLPLATLITPNLPEAELLTG--LEIATEEDMMKA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 206 AKDLSRiTNCSNILVKGGHIPCDdgkekHITDVLYLGaeQKFITFKGQFVNTTRTHGAGCTLASAIASNLARGYSLSQSV 285
Cdd:cd01169  157 AKALLA-LGAKAVLIKGGHLPGD-----EAVDVLYDG--GGFFEFESPRIDTKNTHGTGCTLSSAIAANLAKGLSLEEAV 228

                        250
                 ....*....|..
gi 330443752 286 YGGIEYVQNAIA 297
Cdd:cd01169  229 REAKEYVTQAIR 240
TENA_THI-4 pfam03070
TENA/THI-4/PQQC family; Members of this family are found in all the three major phyla of life: ...
 361-571 4.24e-85

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: 263.45  E-value: 4.24e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  361 HPKVKPHWDAYVNHEFVKRVADGTLERKKFQFFIEQDYLYLIDYVRVCCVTGSKSPTLEDL-EKDLVIADCARNELNEHe 439
Cdd:pfam03070   1 HPQLRPIWKFYINHPFVQALAKGTLPREQFQGYVIQDYLYLVNFARVLAIIASKSPDLEVRrEWENRIVDHDGNEIELH- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  440 RRLREEFGVKDPDyLQKIKRGPALRAYCRYLIDISRRGNWQEIVVALNPCLMGYVYAVDKVKDKITAAEGSIYSEWCDTC 519
Cdd:pfam03070  80 LRLAEALGLSRED-LSAYKPLPATRAYVRYLLDFARRGSWLEAVAALLPCLFVYQEIASRLGEKIRALEGPEYYEWVKTY 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 330443752  520 ASSFCYQAVLEGERLMNHILETYPPDQLDSLVTIFARGCELETNFWTAAMEY 571
Cdd:pfam03070 159 ASEYFRAAVEEAKRLLDRLLAYVSDEQLEELQEIFLKALEFEYSFWTMALDA 210
salvage_TenA TIGR04306
thiaminase II; The TenA protein of Bacillus subtilis and Staphylococcus aurues, and the ...
 364-571 6.40e-81

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: 252.50  E-value: 6.40e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  364 VKPHWDAYVNHEFVKRVADGTLERKKFQFFIEQDYLYLIDYVRVCCVTGSKSpTLEDLEKDLV--IADCARNELNEHeRR 441
Cdd:TIGR04306   1 VKPIWDDYINHPFVQKIGDGTLERDKFRFYIEQDYAYLVEYAKVHALGGSKA-CDEDMEKELVeqIQGGVETEMGQH-KR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  442 LREEFGVKDPDYLQKIKRGPALRAYCRYLIDISRRGNWQEIVVALNPCLMGYVYAVDKVKDKITAAEGSIYSEWCDTCAS 521
Cdd:TIGR04306  79 LAEVLGISDEEYFQKIKPGPALRSYTSYMYDVSRRGNWQELVAALLPCLWGYGEAATKLKGKHTAPEHSVYHKWIETYSS 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 330443752  522 SFCYQAVLEGERLMNHILETYPPDQLDSLVTIFARGCELETNFWTAAMEY 571
Cdd:TIGR04306 159 SWFREAVNEGENLLNHLAETSSPEELEKLKTIFAESCEYEYNFWTMAYEY 208
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 49-314 1.22e-79

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: 250.73  E-value: 1.22e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  49 MSIAGSDSSGGAGVEADIKTITAHRCYAMTCVTTLTAQTPVKVYGAQNIPKKMVSQILDANLQDMKCNVIKTGML-TVDA 127
Cdd:COG0351    1 LTIAGSDPSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVTGVHPVPPEFVAAQLRAVLEDIPVDAIKIGMLgSAEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 128 IEVLHEKLLQLGEnrPKLVIDPVLCAASDSSPTGKDVVSLIIEKISPFADILTPNISDCFMLLGenREVSKLQDVLEIAK 207
Cdd:COG0351   81 IEAVAEILADYPL--VPVVLDPVMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALLG--IEITTLDDMREAAK 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 208 DLSRiTNCSNILVKGGHIPcddgkEKHITDVLYLGaeQKFITFKGQFVNTTRTHGAGCTLASAIASNLARGYSLSQSVYG 287
Cdd:COG0351  157 ALLE-LGAKAVLVKGGHLP-----GDEAVDVLYDG--DGVREFSAPRIDTGNTHGTGCTLSSAIAALLAKGLDLEEAVRE 228

                        250       260
                 ....*....|....*....|....*..
gi 330443752 288 GIEYVQNAIAIGCDVTKkavKVGPINH 314
Cdd:COG0351  229 AKEYVTQAIRAALRLGM---GHGPVNH 252
TenA_C_ScTHI20-like cd19367
TenA_C family similar to the C-terminal TenA_C domain of Saccharomyces cerevisiae THI20 ...
 366-569 1.55e-69

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: 222.77  E-value: 1.55e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 366 PHWDAYVNHEFVKRVADGTLERKKFQFFIEQDYLYLIDYVRVCCVTGSKSPTLEDLEKDLVIADCARNELNEHERRLrEE 445
Cdd:cd19367    1 PIWKAYTNHPFVRQLADGTLPLESFRHYLKQDYLYLIHYARAHALAAYKAPTLEDIRAAAAILLAILEEMELHVKYC-AE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 446 FGVkDPDYLQKIKRGPALRAYCRYLIDISRRGNWQEIVVALNPCLMGYVYAVDKVKDKI-TAAEGSIYSEWCDTCASSfC 524
Cdd:cd19367   80 WGI-SEEELEATPESPATLAYTRYVLDVGLSGDLLDLLVALAPCLLGYGEIGLRLAADPaTKLEGNPYWSWIETYASD-E 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 330443752 525 YQ-AVLEGERLMNHILETYP-PDQLDSLVTIFARGCELETNFWTAAM 569
Cdd:cd19367  158 YQeAVREGIELLEKLAAERPsPARLEELVKIFATATRLEIGFWDMGL 204
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
 44-318 7.99e-66

bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 215.37  E-value: 7.99e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  44 KLPTVMSIAGSDSSGGAGVEADIKTITAHRCYAMTCVTTLTAQTPVKVYGAQNIPKKMVSQILDANLQDMKCNVIKTGML 123
Cdd:PRK06427   3 KRPIALTIAGSDSGGGAGIQADLKTFQALGVYGMSAITALTAQNTLGVQRVHPIPPEFVAAQLDAVFSDIRIDAVKIGML 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 124 -TVDAIEVLHEKLLQLGEnrPKLVIDPVLCAASDSSPTGKDVVSLIIEKISPFADILTPNISDCFMLLGenREVSKLQDV 202
Cdd:PRK06427  83 aSAEIIETVAEALKRYPI--PPVVLDPVMIAKSGDPLLADDAVAALRERLLPLATLITPNLPEAEALTG--LPIADTEDE 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 203 LEIAKDLSRITNCSNILVKGGHipcdDGKEKHITDVLYLGAEqkFITFKGQFVNTTRTHGAGCTLASAIASNLARGYSLS 282
Cdd:PRK06427 159 MKAAARALHALGCKAVLIKGGH----LLDGEESVDWLFDGEG--EERFSAPRIPTKNTHGTGCTLSAAIAAELAKGASLL 232

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 330443752 283 QSVYGGIEYVQNAIAIGCDVTKkavKVGPINHVYAV 318
Cdd:PRK06427 233 DAVQTAKDYVTRAIRHALEIGQ---GHGPVNHFAYL 265
HMP-P_kinase TIGR00097
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ...
 48-314 1.49e-62

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: 206.37  E-value: 1.49e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752   48 VMSIAGSDSSGGAGVEADIKTITAHRCYAMTCVTTLTAQTPVKVYGAQNIPKKMVSQILDANLQDMKCNVIKTGML-TVD 126
Cdd:TIGR00097   1 ALTIAGSDSGGGAGIQADLKTFSALGVFGTSVITALTAQNTRGVTGVYPIPPDFVEAQLDAVFSDIPVDAAKTGMLaSAE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  127 AIEVLHEKLLQLGEnrPKLVIDPVLCAASDSSPTGKDVVSLIIEKISPFADILTPNISDCFMLLGEnrEVSKLQDVLEIA 206
Cdd:TIGR00097  81 IVEAVARKLREYPV--RPLVVDPVMVAKSGAPLLEEEAIEALRKRLLPLATLITPNLPEAEALLGT--KIRTEQDMIKAA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  207 KDLsRITNCSNILVKGGHIPCDDGkekhiTDVLYLGAEqkFITFKGQFVNTTRTHGAGCTLASAIASNLARGYSLSQSVY 286
Cdd:TIGR00097 157 KKL-RELGPKAVLIKGGHLEGDQA-----VDVLFDGGE--IHILKAPRIETKNTHGTGCTLSAAIAANLAKGLSLKEAVK 228

                         250       260
                  ....*....|....*....|....*...
gi 330443752  287 GGIEYVQNAIAIGCDVTKkavKVGPINH 314
Cdd:TIGR00097 229 EAKEFVTGAIRYGLNIGH---GHGPLNH 253
PRK14713 PRK14713
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
20-568 1.08e-61

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 237797 [Multi-domain]  Cd Length: 530  Bit Score: 212.34  E-value: 1.08e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  20 PSIMTNSTVSINTPPPYLTlacneklPTVMSIAGSDSSGGAGVEADIKTITAHRCYAMTCVTTLTAQTPVKVYGAQNIPK 99
Cdd:PRK14713  11 ATGMSAMTNSAAAASAAAT-------PRVLSIAGTDPSGGAGIQADLKSIAAAGGYGMAVITALVAQNTRGVRAVHVPPA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 100 KMVSQILDANLQDMKCNVIKTGML-TVDAIEVLHEkllQLGENRPK-LVIDPVLCAASDSSPTGKDVVSLIIEkISPFAD 177
Cdd:PRK14713  84 DFLRAQLDAVSDDVTVDAVKIGMLgDAEVIDAVRT---WLAEHRPPvVVLDPVMVATSGDRLLEEDAEAALRE-LVPRAD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 178 ILTPNISDCFMLLGENReVSKLQDVLEIAKDLSRITNCSnILVKGGHIPCDDgkekhiTDVLYLGAEQKFITFKGQFVNT 257
Cdd:PRK14713 160 LITPNLPELAVLLGEPP-ATTWEEALAQARRLAAETGTT-VLVKGGHLDGQR------APDALVGPDGAVTEVPGPRVDT 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 258 TRTHGAGCTLASAIASNLARGYSLSQSVYGGIEYVQNAIAIGcdvtkKAVKV----GPINHVYAVEiPLEKMLTDECFTA 333
Cdd:PRK14713 232 RNTHGTGCSLSSALATRLGRGGDWAAALRWATAWLHGAIAAG-----AALQVgtgnGPVDHFHRAR-RLAADASAEAGVS 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 334 SDAVPKKPIEgsldkiPGGSFFNYLINHpkVKPHWDAYVNHEFVKRVADGTLERKKFQFFIEQDYLYLIDYVRVCCVTGS 413
Cdd:PRK14713 306 AEPAPDAVVG------PAGPFTAALWQA--SGPIREAIEDLPFVRALADGTLPEEAFEFYLAQDALYLNGYSRALARLAA 377

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 414 KSPtleDLEKDLVIADCARNELnEHERRL-REEFGVKDPDylqkIKRGPALRAYCRYLIDISRRGNWQEIVVALNPCLMG 492
Cdd:PRK14713 378 LAP---DPAEQVFWAQSAQACL-EVESELhRSWLGDRDAD----TAPSPVTLAYTDFLLARAAGGSYAVGAAAVLPCFWL 449

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 330443752 493 YVYAVDKVKDKITAAEGSIYSEWCDTCASSFCYQAVLEGERLMNHILETYPPDQLDSLVTIFARGCELETNFWTAA 568
Cdd:PRK14713 450 YAEVGAELHARAGNPDDHPYAEWLQTYADPEFAAATRRAIAFVDRAFRAASPAERAAMARAFLTACRYELEFFDQA 525
PLN02898 PLN02898
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
 40-335 5.64e-59

HMP-P kinase/thiamin-monophosphate pyrophosphorylase


Pssm-ID: 215486 [Multi-domain]  Cd Length: 502  Bit Score: 204.62  E-value: 5.64e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  40 ACNEKLPTVMSIAGSDSSGGAGVEADIKTITAHRCYAMTCVTTLTAQTPVKVYGAQNIPKKMVSQILDANLQDMKCNVIK 119
Cdd:PLN02898   4 ESPMKVPHVLTVAGSDSGAGAGIQADIKACAARGVYCTTAITAVTAQNTVGVQGVHAVPLDFVAEQLKSVLSDMPVDVVK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 120 TGML-TVDAIEVLHEKLlqlgENRP--KLVIDPVLCAASDSSPTGKDVVSLIIEKISPFADILTPNISDCFMLLGeNREV 196
Cdd:PLN02898  84 TGMLpSAEIVKVLCQAL----KEFPvkALVVDPVMVSTSGDVLAGPSILSALREELLPLATIVTPNVKEASALLG-GDPL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 197 SKLQDVLEIAKDLSRItNCSNILVKGGHIPCDdgkeKHITDVLYLGAEqkFITFKGQFVNTTRTHGAGCTLASAIASNLA 276
Cdd:PLN02898 159 ETVADMRSAAKELHKL-GPRYVLVKGGHLPDS----LDAVDVLYDGTE--FHELRSSRIKTRNTHGTGCTLASCIAAELA 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 330443752 277 RGYSLSQSVYGGIEYVQNAIAIGCDVTKKAVKVGPINHVYAVEIPLEKMLTDECFTASD 335
Cdd:PLN02898 232 KGSDMLSAVKVAKRYVETALEYSKDIGIGNGAQGPFNHLFFLKSWAKKSSRQSRFNPRN 290
PTZ00347 PTZ00347
phosphomethylpyrimidine kinase; Provisional
 42-314 1.96e-54

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240375 [Multi-domain]  Cd Length: 504  Bit Score: 192.10  E-value: 1.96e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  42 NEKLPTVMSIAGSDSSGGAGVEADIKTITAHRCYAMTCVTTLTAQTPVKVYGAQNIPKKMVSQILDANLQDMKCNVIKTG 121
Cdd:PTZ00347 227 PMKIPTVLTVSGSDSGGGAGHQADLKTLEALGVYSTSALTSLTAQNTKGVQQIQVVNEDFFAAQIDSVMSDFNISVVKLG 306

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 122 ML-TVDAIEVLHEKLLQLgenrpKLVIDPVLCAASD----SSPTGKDVVSLIIEKISPFADILTPNISDCFMLLGEnREV 196
Cdd:PTZ00347 307 LVpTARQLEIVIEKLKNL-----PMVVDPVLVATSGddlvAQKNADDVLAMYKERIFPMATIITPNIPEAERILGR-KEI 380

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 197 SKLQDVLEIAKDLSRItNCSNILVKGGHipcDDGKEKHITDVLYLGAEQKFITFKGQFVNTTRTHGAGCTLASAIASNLA 276
Cdd:PTZ00347 381 TGVYEARAAAQALAQY-GSRYVLVKGGH---DLIDPEACRDVLYDREKDRFYEFTANRIATINTHGTGCTLASAISSFLA 456

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 330443752 277 RGYSLSQSVYGGIEYVQNAIAIGCDVTKKAVKVGPINH 314
Cdd:PTZ00347 457 RGYTVPDAVERAIGYVHEAIVRSCGVPLGQGTNRPLVH 494
TenA COG0819
Aminopyrimidine aminohydrolase TenA (thiamine salvage pathway) [Coenzyme transport and ...
 352-568 1.71e-49

Aminopyrimidine aminohydrolase TenA (thiamine salvage pathway) [Coenzyme transport and metabolism];


Pssm-ID: 440581 [Multi-domain]  Cd Length: 218  Bit Score: 170.45  E-value: 1.71e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 352 GSFFNYLINhpKVKPHWDAYVNHEFVKRVADGTLERKKFQFFIEQDYLYLIDYVRVCCVTGSKSPTLEDLEKDLVIADCA 431
Cdd:COG0819    1 MSFSERLRE--AAAPIWEAILEHPFVQGLADGTLPREAFRHYLVQDYLYLEHFARALALAAAKAPDLEDMRFLAGLAAGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 432 RNELNEHERRLREEFGVkDPDYLQKIKRGPALRAYCRYLIDISRRGNWQEIVVALNPCLMGYVYAVDKVKDKiTAAEGSI 511
Cdd:COG0819   79 LEVELALHERYAAELGI-SEEELEATPPSPTTRAYTSYLLAAAASGDYAELLAALLPCEWGYAEIGKRLAER-PLPPDHP 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 330443752 512 YSEWCDTCASSFCYQAVLEGERLMNHILETYPPDQLDSLVTIFARGCELETNFWTAA 568
Cdd:COG0819  157 YAEWIETYASEEFQELVEWLIALLDRLAATASEAERERLEEAFRTASRLEYAFWDMA 213
TenA_PqqC-like cd16099
TenA-like proteins including TenA_C and TenA_E proteins, as well as pyrroloquinoline quinone ...
 368-567 3.57e-49

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: 169.07  E-value: 3.57e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 368 WDAYVNHEFVKRVADGTLERKKFQFFIEQDYLYLIDYVRVCCVTGSKSPTLEDLEKDLVIADCARNELNEHErRLREEFG 447
Cdd:cd16099    2 WDAILNHPFVQELAAGTLPREKFRYYLAQDYYYLKDFARALALAAAKAPDLELRTFLAELINVLDDELELHE-KLLAELG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 448 VkDPDYLQKIKRGPALRAYCRYLIDISRRGNWQEIVVALNPCLMGYVYAVDKVKDKitAAEGSIYSEWCDTCASSFCYQA 527
Cdd:cd16099   81 I-SEEDLSEAEPNPATLAYTNHLLRVAARGTPAEGLAALLPCYWSYGEIGRRLAAS--LPEHPPYRFWIDFYASDEYQEL 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 330443752 528 VLEGERLMNHILETYPPDQlDSLVTIFARGCELETNFWTA 567
Cdd:cd16099  158 VEELLQLLDQLAAAGEEEK-EELKEIFLTSLRYELMFWDA 196
PRK09517 PRK09517
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ...
 15-568 9.71e-49

multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 169939 [Multi-domain]  Cd Length: 755  Bit Score: 180.94  E-value: 9.71e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  15 RTAFCPSIMTNSTVSINTPPPYLTLACNEKLPTVMSIAGSDSSGGAGVEADIKTITAHRCYAMTCVTTLTAQTPVKVYGA 94
Cdd:PRK09517 211 RTAFQPTRSPETQTELSQTELQGAFVNSPSAPRVLSIAGTDPTGGAGIQADLKSIAAGGGYGMCVVTALVAQNTHGVNTI 290

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  95 QNIPKKMVSQILDANLQDMKCNVIKTGMLtvDAIEVLHEKLLQLGENRPKLVI-DPVLCAASDSSPTGKDVVSLIIEkIS 173
Cdd:PRK09517 291 HTPPLTFLEEQLEAVFSDVTVDAVKLGML--GSADTVDLVASWLGSHEHGPVVlDPVMVATSGDRLLDADATEALRR-LA 367

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 174 PFADILTPNISDCFMLLGEnREVSKLQDVLEIAKDLSRiTNCSNILVKGGHIPCDDGKEKHITdvlylgAEQKFITFKGQ 253
Cdd:PRK09517 368 VHVDVVTPNIPELAVLCGE-APAITMDEAIAQARGFAR-THGTIVIVKGGHLTGDLADNAVVR------PDGSVHQVENP 439

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 254 FVNTTRTHGAGCTLASAIASNLARGYSLSQSVYGGIEYVQNAIAiGCDVTKKAVKVGPINHVY-------AVEIPLEKML 326
Cdd:PRK09517 440 RVNTTNSHGTGCSLSAALATLIAAGESVEKALEWATRWLNEALR-HADHLAVGSGNGPVDHGHlarrlthAAETTPWAHL 518

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 327 TDECFTASDAVPKKPIEGSLDKIPGGsffnylinhPKVKPHWDA-------YVNHEFVKRVADGTLERKKFQFFIEQDYL 399
Cdd:PRK09517 519 RAGATAASFTTPSTVKSPAPRIEPAG---------PFTRALWEAsgdiiaeINDSDFIRMLGDGTLRRPEFDFYIDQDAQ 589

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 400 YLIDYVRVCCVTGSKSPTLE-DLEKDLVIADCARNELNEHERRLREEFGVKDPdylqkikrGPALRAYCRYLIDISRRGN 478
Cdd:PRK09517 590 YLRQYSRALARLSSIAPDSHaQVEWAQSAAECIVVEAELHRSYLSGKEAPSAP--------SPVTMAYTDFLIARTYTED 661

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 479 WQEIVVALNPCLmgYVYAVDKVKDKITAAEGSIYSEWCDTCASSFCYQAVLEGERLMNHILETYPPDQLDSLVTIFARGC 558
Cdd:PRK09517 662 YVVGVAAVLPCY--WLYAEIGLMLAEQNHDEHPYKDWLNTYSGEEFIAGTRAAIARVEKALENAGPEQRVDAARAFLSAS 739

                        570
                 ....*....|
gi 330443752 559 ELETNFWTAA 568
Cdd:PRK09517 740 VHEREFFDQA 749
PRK08573 PRK08573
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
46-324 1.15e-48

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 236297 [Multi-domain]  Cd Length: 448  Bit Score: 175.30  E-value: 1.15e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  46 PTVMSIAGSDSSGGAGVEADIKTITAHRCYAMTCVTTLTAQTPVKVYGAQNIPKKMVSQILDANLQDMKCNVIKTGML-T 124
Cdd:PRK08573   3 PVALTIAGSDSGGGAGIEADLKTFAALGVHGAVAITSVTAQNTYEVRAIHDLPPEVVAAQIEAVWEDMGIDAAKTGMLsN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 125 VDAIEVLHEKLLQLGenRPkLVIDPVLCAASDSSPTGKDVVSLIIEKISPFADILTPNISDCFMLLGenREVSKLQDVLE 204
Cdd:PRK08573  83 REIIEAVAKTVSKYG--FP-LVVDPVMIAKSGAPLLREDAVDALIKRLLPLATVVTPNRPEAEKLTG--MKIRSVEDARK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 205 IAKDLSRITNCSNILVKGGHIpcdDGKEkhITDVLYLGAeqKFITFKGQFVNTTRTHGAGCTLASAIASNLARGYSLSQS 284
Cdd:PRK08573 158 AAKYIVEELGAEAVVVKGGHL---EGEE--AVDVLYHNG--TFREFRAPRVESGCTHGTGCSFSAAIAAGLAKGLDPEEA 230

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 330443752 285 VYGGIEYVQNAIAIGCDVTKKAvkvGPINHVYAVEIPLEK 324
Cdd:PRK08573 231 IKTAKKFITMAIKYGVKIGKGH---CPVNPMAWIEIPAER 267
TenA_C_BhTenA-like cd19366
TenA_C proteins similar to Bacillus halodurans TenA; This family of TenA proteins belongs to ...
 362-568 7.05e-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: 150.01  E-value: 7.05e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 362 PKVKPHWDAYVNHEFVKRVADGTLERKKFQFFIEQDYLYLIDYVRVCCVTGSKSPTLEDLEKdlvIADCARNELNE---- 437
Cdd:cd19366    7 EKAKPIWEAGLEHPFVQGLGDGTLDKEKFKFYLKQDYLYLIDYARVFALGAAKADDLETMGR---FAELLHGTLNTemdl 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 438 HeRRLREEFGVkDPDYLQKIKRGPALRAYCRYLIDISRRGNWQEIVVALNPCLMGYVYAVDKVKDKITAAEGSIYSEWCD 517
Cdd:cd19366   84 H-RQYAAEFGI-TEEELEATEPSPTTLAYTSYMLRTAQTGTLAELLAALLPCAWGYAEIGKRLAEQGGALEHNPYREWIE 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 330443752 518 TCAS-------SFCYQavlegerLMNHILETYPPDQLDSLVTIFARGCELETNFWTAA 568
Cdd:cd19366  162 MYSSdeftelaDWLID-------LLDELAEGKSEAELERLEEIFLTSSRYEYMFWDMA 212
PRK12412 PRK12412
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
45-314 4.17e-36

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183512 [Multi-domain]  Cd Length: 268  Bit Score: 135.87  E-value: 4.17e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  45 LPTVMSIAGSDSSGGAGVEADIKTITAHRCYAMTCVTTLTAQTPVKVYGAQNIPKKM--VSQILDANLQDMKCNVIKTGM 122
Cdd:PRK12412   1 LNKALTIAGSDTSGGAGIQADLKTFQELGVYGMTSLTTIVTMDPHNGWAHNVFPIPAstLKPQLETTIEGVGVDALKTGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 123 L-TVDAIEVLHEKLLQlgENRPKLVIDPVL-CAASDSSPTGKDVVSLiIEKISPFADILTPNISDCFMLLGenREVSKLQ 200
Cdd:PRK12412  81 LgSVEIIEMVAETIEK--HNFKNVVVDPVMvCKGADEALHPETNDCL-RDVLVPKALVVTPNLFEAYQLSG--VKINSLE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 201 DVLEIAKDLSRItNCSNILVKGGHipcDDGKEKHItDVLYLGaeQKFITFKGQFVNTTRTHGAGCTLASAIASNLARGYS 280
Cdd:PRK12412 156 DMKEAAKKIHAL-GAKYVLIKGGS---KLGTETAI-DVLYDG--ETFDLLESEKIDTTNTHGAGCTYSAAITAELAKGKP 228

                        250       260       270
                 ....*....|....*....|....*....|....
gi 330443752 281 LSQSVYGGIEYVQNAIAIGCDVTKkavKVGPINH 314
Cdd:PRK12412 229 VKEAVKTAKEFITAAIRYSFKINE---YVGPTHH 259
PRK12616 PRK12616
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
49-314 2.45e-34

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183624  Cd Length: 270  Bit Score: 130.94  E-value: 2.45e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  49 MSIAGSDSSGGAGVEADIKTITAHRCYAMTCVTTLTAQTPVKVYGAQNIP------KKMVSQILDAnlqdMKCNVIKTGM 122
Cdd:PRK12616   7 LTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAMDPENSWDHQVFPidtdtiRAQLSTIVDG----IGVDAMKTGM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 123 L-TVDAIEVLHEKLLQlgENRPKLVIDPVLCAASDSSPTGKDVVSLIIEKISPFADILTPNISDCFMLLGENrEVSKLQD 201
Cdd:PRK12616  83 LpTVDIIELAADTIKE--KQLKNVVIDPVMVCKGANEVLYPEHAEALREQLAPLATVITPNLFEAGQLSGMG-EIKTVEQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 202 VLEIAKDLSRItNCSNILVKGGhipcddGKEKH--ITDVLYLGaeQKFITFKGQFVNTTRTHGAGCTLASAIASNLARGY 279
Cdd:PRK12616 160 MKEAAKKIHEL-GAQYVVITGG------GKLKHekAVDVLYDG--ETAEVLESEMIDTPYTHGAGCTFSAAVTAELAKGS 230

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 330443752 280 SLSQSVYGGIEYVQNAIAIGCDVTKkavKVGPINH 314
Cdd:PRK12616 231 EVKEAIYAAKEFITAAIKESFPLNQ---YVGPTKH 262
TenA_C_HP1287-like cd19361
TenA_C proteins similar to Helicobacter pylori TenA (HP1287; This family of TenA proteins ...
 363-565 3.33e-33

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: 126.15  E-value: 3.33e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 363 KVKPHWDAYVNHEFVKRVADGTLERKKFQFFIEQDYLYLIDYVRVCCVTGSKSPTLEDLEK-DLVIADCARNELNEHeRR 441
Cdd:cd19361    8 AVEDIWDSYYEHPFVQGIADGTLDIEKFRFYMIQDYLYLLDYAKVFALGVAKAKDEEVMRFfADLINAILNEEMDIH-RG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 442 LREEFGVkDPDYLQKIKRGPALRAYCRYLIDISRRGNWQEIVVALNPCLMGYVYAVDK-VKDKITAAEGSIYSEWCDTCA 520
Cdd:cd19361   87 YMKRLGI-TEEEIENTKPALDNLSYTSYMLSVAYEGGIAEILAAILSCSWSYEYIAKKlVERYPAALEHEFYGEWVKGYS 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 330443752 521 SSFCYQAVLEGERLMNHILETYPPDQLDSLVTIFARGCELETNFW 565
Cdd:cd19361  166 SEEYAEANQELIDLLDRLTEDISEEQIEKLEEIFVNCSRYELKFW 210
TenA_C-like cd19369
uncharacterized TenA_C proteins; This family of TenA proteins belongs to the TenA_C class as ...
 366-565 3.59e-33

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: 125.80  E-value: 3.59e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 366 PHWDAYVNHEFVKRVADGTLERKKFQFFIEQDYLYLIDYVRVCCVTGSKSPTLEDLEK-----DLVIADcarnELNEHER 440
Cdd:cd19369    1 PIWEQYLEHPFIKELGEGTLDKEKFKNYLIQDSLYLKEYAKVFAMGIYKSRTMKEMQFfysslSFVNED----ETATRIK 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 441 RLReEFGVkDPDYLQKIKRGPALRAYCRYLIDISRRGNWQEIVVALNPCLMGYVYAVDKVKDKITA-AEGSIYSEWCDTC 519
Cdd:cd19369   77 YLK-EFGL-TDEDIEKIEPLPENKAYTDYMLGIAKTGDVKEILMAVLPCMLSYYYIFKELVKKYKDnLESNPYKDWIEDY 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 330443752 520 ASSFCYQAVLEGERLMNHILETYPPDQLDSLVTIFARGCELETNFW 565
Cdd:cd19369  155 ASEEYAEYCKEWIDFADRLCENLSEEEKEKLKEIFRKASLYELKFW 200
TenA_C-like cd19365
uncharacterized TenA_C proteins; This family of TenA proteins belongs to the TenA_C class as ...
 363-568 3.26e-28

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: 111.83  E-value: 3.26e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 363 KVKPHWDAYVNHEFVKRVADGTLERKKFQFFIEQDYLYLIDYVRVCCVTGSKSPTLEDLEKdlvIADCARNELnEHERRL 442
Cdd:cd19365    7 AIAPIYAAILAHPFIRELADGTLPREKFRFYLAQDALYLRDYARALALLAARAPDPEEQVF---FARFAAGAI-EVEREL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 443 REEFgVKDPDYLQKIKRGPALRAYCRYLIDISRRGNWQEIVVALNPCLmgYVYAvdKVKDKITAA--EGSIYSEWCDTCA 520
Cdd:cd19365   83 HRSF-LGEFGIDAAAEPSPVTLAYTSFLLATAATGPYAVAVAAVLPCF--WIYA--EVGKRLAAAasPNHPYQDWIDTYS 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 330443752 521 S-SFCyQAVLEGERLMNHILETYPPDQLDSLVTIFARGCELETNFWTAA 568
Cdd:cd19365  158 DeEFA-EAVRRAIAIVDRLAAEASPEERARMLEAFLRASRLEWMFWDAA 205
PTZ00493 PTZ00493
phosphomethylpyrimidine kinase; Provisional
 43-319 1.12e-25

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240440  Cd Length: 321  Bit Score: 107.77  E-value: 1.12e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  43 EKLPTVMSIAGSDSSGGAGVEADIKTITAHRCYAMTCVTTLTAQTPVKVYGAQNIPKKMVSQILDANLQDMKCNVIKTGM 122
Cdd:PTZ00493   2 EGVSNILSIAGSDSCGGAGMQADIKTAMGLGCHCCTALVVLTAQNTKEVKRIVEIEEKFIVEQLDSIFADVTIDVVKLGV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 123 L-TVDAIEVLHEKLLQLGENRPK---LVIDPVLCAASDSSPTGK-DVVSLIIEKISPFADILTPNISDCFMLLGE---NR 194
Cdd:PTZ00493  82 LySKKIISLVHNYITNMNKKRGKkllVVFDPVFVSSSGCLLVENlEYIKFALDLICPISCIITPNFYECKVILEAldcQM 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 195 EVSKLqDVLEIAKDLSRITNCSNILVKGGHIPCDDGKEKHITDVLYLGAEQKFITFKGQFVNTTR--------------- 259
Cdd:PTZ00493 162 DLSKA-NMTELCKLVTEKLNINACLFKSCNVGENSAEENEVYAVDHLCIRNVGSYPTGEKQQIDAggvtylydvyklrsk 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 330443752 260 ------THGAGCTLASAIASNLARGYSLSQSVYGGIEYVQNAIAIGCDVTKKAVKvgpINHVYAVE 319
Cdd:PTZ00493 241 rkpgkdIHGTGCTLSTAIACYLAKKHNILQSCIESKKYIYNCIRYAYPFGSKSQG---LNHLKASQ 303
COG1992 COG1992
Predicted transcriptional regulator fused phosphomethylpyrimidine kinase (thiamin biosynthesis) ...
 57-324 6.23e-25

Predicted transcriptional regulator fused phosphomethylpyrimidine kinase (thiamin biosynthesis) [General function prediction only];


Pssm-ID: 441595 [Multi-domain]  Cd Length: 432  Bit Score: 107.54  E-value: 6.23e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  57 SGGAGVEADIKTITAHRCYAMTCVTTLTAQTPVKVYGAQNIPKKMVSQILDANLQDMKCNVIKTGML-TVDAIEVLHEKL 135
Cdd:COG1992    1 GGGGGGGADAKTAAALGAGGGGTTTAVTVTATTTVTGVGSDPPPPVEVQQQAVAADDDVDDAKTGMLmTATIVEVVAVVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 136 LQLGENRPKLVIDPVLCAASDSSPTGKDVVSLIIEKISPFADILTPNISDCFMLlgenrEVSKLQDVLEIAKDLSRITNC 215
Cdd:COG1992   81 KSRDKPLVVVVVPVAVAAAGLGLLLAEAELAKLLLPLLATVTPNEPEVEELLLP-----TIRSLLAEARAARLALQEEGA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 216 SNILVKGGHIpcddgkeKHITDVLYLGAEQKFITFKGQFVNTTRTHGAGCTLASAIASNLARGYSLSQSVYGGIEYVQNA 295
Cdd:COG1992  156 DALGVKGGHV-------SGDAVVDVLEDERDVETFRHPRLVTEATHGSGCTFSAAIAALLAKGLSLEEAVRGAKLFLLHA 228

                        250       260
                 ....*....|....*....|....*....
gi 330443752 296 IAIGCDVTKkavKVGPINHVYAVEIPLEK 324
Cdd:COG1992  229 IRYGLLVGK---GVGPVNHLADLRLEAER 254
PRK12413 PRK12413
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
48-296 1.06e-22

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183513 [Multi-domain]  Cd Length: 253  Bit Score: 97.44  E-value: 1.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  48 VMSIAGSDSSGGAGVEADIKTITAHRCYAMTCVTTLTAQTPvKVYGAQNIPKKMVSQILDAnLQDMKCNVIKTGMLTVDA 127
Cdd:PRK12413   6 ILAISGNDIFSGGGLHADLATYTRNGLHGFVAVTCLTAMTE-KGFEVFPVDKEIFQQQLDS-LKDVPFSAIKIGLLPNVE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 128 IEVLHEKLLQLGENRPkLVIDPVL-CAASDSSptgkDVVSLIIEKIS--PFADILTPNISDCFMLLGenREVSKLQDVLE 204
Cdd:PRK12413  84 IAEQALDFIKGHPGIP-VVLDPVLvCKETHDV----EVSELRQELIQffPYVTVITPNLVEAELLSG--KEIKTLEDMKE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 205 IAKDLSRItNCSNILVKGGHipcDDGKEKHItDVLYLGaeQKFITFKGQFVNTTRThGAGCTLASAIASNLARGYSLSQS 284
Cdd:PRK12413 157 AAKKLYDL-GAKAVVIKGGN---RLSQKKAI-DLFYDG--KEFVILESPVLEKNNI-GAGCTFASSIASQLVKGKSPLEA 228

                        250
                 ....*....|..
gi 330443752 285 VYGGIEYVQNAI 296
Cdd:PRK12413 229 VKNSKDFVYQAI 240
TenA_C_PH1161-like cd19363
uncharacterized TenA_C proteins similar to Pyrococcus horikoshii PH1161; This family of TenA ...
 368-568 4.96e-21

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: 91.62  E-value: 4.96e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 368 WDAYVNHEFVKRVADGTLERKKFQFFIEQDYLYLIDYVRVCCVTGSKSPTLEDLEKDLVIA-DCARNELNEHERRLrEEF 446
Cdd:cd19363   13 WKKILNHPFVVELYSGTLPMEKFKFYLLQDYNYLVGSTKNLSILASKAESLDLMRELLELAyGEATTEFANYEELL-DEL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 447 GVkDPDYLQKIKRGPALRAYCRYLIDISRRGNWQEIVVALNPCLMGYVYAVDKVKDKITAAEGSIYSEWCDTCASSFCYQ 526
Cdd:cd19363   92 GL-SLEDAIKVEPFPTNVAYMNFLLSTSSLGSFYEGLAALLPCFWSYLEIAEYHKDKLSENPNDIYRDWASVYLSKEYKE 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 330443752 527 AVLEGERLMNHILETYPPDQLDSlvtIFARGCELETNFWTAA 568
Cdd:cd19363  171 LVERLRRIVDKYGEGEPFEKLKR---IFKTASKYEYMFWDAA 209
TenA_E_Spr0628-like cd19358
TenA_E proteins similar to Streptococcus pneumoniae Spr0628 and Saccharomyces cerevisiae S288C ...
 363-568 3.52e-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: 3.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 363 KVKPHWDAYVNHEFVKRVADGTLERKKFQFFIEQDYLYLIDYVRVCCVTGSKSPTLEDLEKdL--VIADCARNElNEHER 440
Cdd:cd19358    8 ANAEDWDAAVTHRFVRELCAGTLPDAVLARYLVQDYQFVETFLRLLGKAVAKAPDLEAKLR-LarFLGFLANDE-NDYFE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 441 RLREEFGVKDPDYLqKIKRGPALRAYCRYLIDISRRGNWQEIVVALNpclmgyvyavdkvkdkitAAEGsIYSEWCDTCA 520
Cdd:cd19358   86 RAFAALGVSEADRE-APPLLPATRAFIDLMLEAARSGSYAEILTVLL------------------VAEW-LYLDWASRAA 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 330443752 521 SS----FCYQ---------------AVLEGErlmnhiLETYPPD--QLDSLVTIFARGCELETNFWTAA 568
Cdd:cd19358  146 AAaplrFKHQewidlhsgpefeawvDFLRDE------VDRVGPTeeERERLEAVFARAVELEIAFFDAA 208
TenA_C_BsTenA-like cd19364
TenA_C proteins similar to Bacillus subtilis TenA; This family of TenA proteins belongs to the ...
 361-565 4.55e-19

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: 86.08  E-value: 4.55e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 361 HPKVKPHWDAYVNHEFVKRVADGTLERKKFQFFIEQDYLYLIDYVRVCCVTGSKSPTLEDLEKDLVIAdcarNELNEHER 440
Cdd:cd19364    6 REAADPLWQKSFEHPFIQGLADGTLPLETFRYYLIQDAYYLKHFAKLHALAAAKADDPAIKALLLEGA----QGLAEGEL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 441 RLREEF----GVKDPDYLQkikRGPALRAYcRYLIDISR---RGNWQEIVVALNPC--L---MGYVYavdkvkdkitAAE 508
Cdd:cd19364   82 ALRETFfkelGITEEEIAQ---TPPAPTAY-HYVSHMYRqlnEGSVAEAVAALLPCywLyqeIGERL----------ADA 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 509 GS---IYSEWCDTCASSFCYQAVLEGERLMNHILETYPPDQLDSLVTIFARGCELETNFW 565
Cdd:cd19364  148 GSpvpLYQRWIDTYASDEFTESVQQQIDLVDRLAEEASEEEREKMKQAFLISSYYELQFW 207
TenA_C_Bt3146-like cd19359
uncharacterized TenA_C proteins similar to Bacteroides thetaiotaomicron Bt3146; This family of ...
 355-567 6.52e-19

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: 85.48  E-value: 6.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 355 FNYLINHPKVKphWDAYVNHEFVKRVADGTLERKKFQFFIEQDYLYLIDYVR--VCCVTGSKSPTLEDLEKDLV--IADC 430
Cdd:cd19359    1 IDKLWNDNEDL--WDKALNNPFCQGMADGTLDLDGFGYYMVQDYYYCINYVRfkALRAAKAPDPDLLAFLAAKIksYLDY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 431 ARNELNEHERRLREEFGVKdpdylqKIKRGPALRAYCRYLIDISRRGNWQEIVVALNPCLMGYVYAVDKVKDKITAAEGS 510
Cdd:cd19359   79 AEDFLKTCHIKLGIPDVVD------GVKPSPALKAYVDFERSVAESEDWFYLLVAMIPCIYLWYWLANQLNEDPSDKNTN 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 511 IYSEWCDtcaSSFCYQAvleGERLMNHILETY---PPDQLDSLVTIFARGCELETNFWTA 567
Cdd:cd19359  153 FYKTWIE---PNLPDPS---SAKQLEFFLNANaawSKIDREKANEIFRQAMQLEINFFNS 206
TenA_C_SsTenA-1-like cd19362
uncharacterized TenA_C proteins similar to Sulfolobus solfataricus TenA-1 (Sso2206); This ...
 364-569 1.04e-17

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: 81.72  E-value: 1.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 364 VKPHWDAYVNHEFVKRVADGTLERKKFQFFIEQDYLYLIDYVRVCCVTGSKSPtLEDLEKDLVIADCARNELNEHERRLR 443
Cdd:cd19362    8 VGDLWNKYVRHEFVERMRDGTLPLDNFRYYLIQDSKYVEEMLRALLRASSKAP-LDKAIKILNSVFSGRDKGMEVHKFLY 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 444 EEFGVKDpDYLQKIKRGPALRAYCRYLIDISRRGnWQEIVVALNPCLMGYVYAVDKVKDkitaAEGSIYSEWCDTCASSf 523
Cdd:cd19362   87 SELGITE-DEIRRTGYNLVNYAYTRHLYYYSTLG-WPQFLAAWAPCMWGYSEIGKYVLN----SPNELYKTWASFYASK- 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 330443752 524 cyqavlEGERLMNHILETyppdqLDS------LVTIFARGCELETNFWTAAM 569
Cdd:cd19362  160 ------DYKKRVEAILEA-----LDSiedtedIKNIFRNSVNFEIMFWDAAL 200
TenA_C_AtTH2-like cd19368
TenA_C family similar to the N-terminal TenA_C domain of Arabidopsis thaliana thiamine ...
 373-567 2.81e-16

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: 77.67  E-value: 2.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 373 NHEFVKRVADGTLERKKFQFFIEQDYLYLIDYVRVCCVTGSKSPTLEDLEKDLVIADCARNELNEHERRLrEEFGVKDPD 452
Cdd:cd19368   18 YHPFVVGLAAGNLPLDSFRHYISQDAHFLEAFARAYELAEAKADDDEDKKAIRELRKGVLEELKLHDSYA-EEWGVDLPK 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 453 YLQKIkrgPALRAYCRYLIDISRRGNWQ--EIVVALNPCLMGYVYAVDKVKDKITAAEGSIYSEWCDTCASSFCYQAVLE 530
Cdd:cd19368   97 EVTPD---PATRKYTDFLLATASGKVKVaaYTLAAMAPCMRLYAFLGQELARALDDTEDHPYKKWIDTYSSQEFEALALQ 173

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 330443752 531 GERLMNHILETYPPDQLDSLVTIFARGCELETNFWTA 567
Cdd:cd19368  174 LEDLLDKLSASLTGEELEALEKLYRRAMKLEVEFFAA 210
TenA_C_SaTenA-like cd19360
TenA_C proteins similar to Staphylococcus aureus TenA (SaTenA); This family of TenA proteins ...
 363-567 6.44e-14

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: 71.08  E-value: 6.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 363 KVKPHWDAYVNHEFVKRVADGTLERKKFQFFIEQDYLYLIDYVRVCCVTGSKSPTLEDLEKdlvIADCARNELN-EHE-- 439
Cdd:cd19360    8 EAQPILEAIYAHPFVQGIAAGELPKEALIHYVQQDYEYLNAFLKVYALAIAKSDTREDMRF---FLEQIGFILNgESHah 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 440 RRLREEFGVKDPDyLQKIKRGPALRAYCRYLIDISRRGNWQEIVVALNPCLMGYVYAVDKVKDKITAAEGSIYSEWCDtc 519
Cdd:cd19360   85 QNLCEVAGVDYEE-LQGAPWAPTADHYIKHMYYAARTGDLGDILAALLPCPWTYVELAKRLIEEGKPTPDNPFYEWID-- 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 330443752 520 assfCYQAVLEGE------RLMNHILETYPPDQLDSLVTIFARGCELETNFWTA 567
Cdd:cd19360  162 ----FYADDEMDGltdqlfARLDRLAEKASEEERERAKQAFLKSCQLEWRFWEM 211
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 106-296 1.26e-11

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: 64.91  E-value: 1.26e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 106 LDANLQDMKCNVIKTGML-TVDAIEVLHEKLLQLGENRPKL--VIDPVLcaaSDSS---PTGKDVVSLIIEKISPFADIL 179
Cdd:cd01173   64 LEALGLLLEYDAVLTGYLgSAEQVEAVAEIVKRLKEKNPNLlyVCDPVM---GDNGklyVVAEEIVPVYRDLLVPLADII 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 180 TPNISDCFMLLGenREVSKLQDVLEIAKDLSRiTNCSNILVKGghipCDDGKEKHITDVLYLGAEQKFITFKGQFVNTTR 259
Cdd:cd01173  141 TPNQFELELLTG--KKINDLEDAKAAARALHA-KGPKTVVVTS----VELADDDRIEMLGSTATEAWLVQRPKIPFPAYF 213

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 330443752 260 ThGAGCTLASAIASNLARGYSLSQSVYGGIEYVQNAI 296
Cdd:cd01173  214 N-GTGDLFAALLLARLLKGKSLAEALEKALNFVHEVL 249
TenA_E_At3g16990-like cd19357
TenA_E proteins similar to Arabidopsis thaliana At3g16990; This family of TenA proteins ...
 367-565 9.78e-11

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: 61.57  E-value: 9.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 367 HWDAY---VNHEFVKRVADGTLERKKFQFFIEQDYLYLIDYVRVCCVTGSK--SPTLEDLEKDL-VIADC---ARNELNE 437
Cdd:cd19357    8 HPALYtaaTQHPFLRAAADGTLPKEALSRWLAQDRLYVQAYIRFLGSLLARapLPSSSLNQRLLdVLLGAlanLRRELAF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 438 HERRLReEFGVKDPDYLqkIKRGPALRAYCRYLIDISRRG-NWQEIVVALnpclmgyvYAVDKV----------KDKITA 506
Cdd:cd19357   88 FEETAA-EYGLDLPGLG--VPPSPATRAYVDFLASLASEGvSYLEGLVVL--------WATEKVyldawsyarsFLPSDA 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 507 AEGSIYSEWCDTCAS-SFcYQAVLEGERLMNHILETYPPDQLDSLVTIFARGCELETNFW 565
Cdd:cd19357  157 DGGALYREFIPNWTSpEF-AAFVDRLGDLVDEALEQAGEEVLERAEEVWRRVLELEEAFW 215
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 114-295 2.08e-10

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: 61.70  E-value: 2.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 114 KCNVIKTGML-TVDAIEVLHEKLLQLGENRPKL--VIDPV------LCAASDssptgkDVVSLIIEKISPFADILTPNIS 184
Cdd:COG2240   74 EFDAVLSGYLgSAEQGDIIADFVARVKAANPDAlyLCDPVmgdngkGYYVFP------GIAEFIMRRLVPLADIITPNLT 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 185 DCFMLLGenREVSKLQDVLEIAKDLSRITNcSNILVKGghIPCDDGKEKHItDVLYLGAEQKFITF----KGQFvnttrt 260
Cdd:COG2240  148 ELALLTG--RPYETLEEALAAARALLALGP-KIVVVTS--VPLDDTPADKI-GNLAVTADGAWLVEtpllPFSP------ 215

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 330443752 261 HGAGCTLASAIASNLARGYSLSQ-------SVYGGIEYVQNA 295
Cdd:COG2240  216 NGTGDLFAALLLAHLLRGKSLEEaleraaaFVYEVLERTAAA 257
PTZ00347 PTZ00347
phosphomethylpyrimidine kinase; Provisional
 372-568 1.31e-09

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240375 [Multi-domain]  Cd Length: 504  Bit Score: 60.75  E-value: 1.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 372 VNHEFVKRVADGTLERKKFQFFIEQDYLYLIDYVRVCCVTGSKSPTLEDLEKDLVIADCARNELneheRRLREEFgVKDP 451
Cdd:PTZ00347  29 LHLPFVQGLGDGTLDQNAFRTYIAQDTLYLNGYIRILSYCITKSDVTATGGGLLELLKGVLEEL----KNCHHHY-IDNP 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 452 DylqKIKRGPALRAYCRYLIDISRRGNWQEIVV--ALNPCLMGYVYAVDKVKDKITAAEGSIYSEWCdtcaSSFCYQAVL 529
Cdd:PTZ00347 104 D---AAGPEAACRKYVDFLLASGNADTLGPSVViaAVIPCARLYAWVGQELTNEVELTESHPFRRWL----LSYSDEPIN 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 330443752 530 EGERLMNHILETY-PPDQLDSLVTIFARGCELETNFWTAA 568
Cdd:PTZ00347 177 TSVEQLESLLDKYiRPGEFSEVAQAYRRAMELEYDFFDSF 216
PqqC COG5424
Pyrroloquinoline quinone (PQQ) biosynthesis protein C [Coenzyme transport and metabolism];
353-487 1.19e-06

Pyrroloquinoline quinone (PQQ) biosynthesis protein C [Coenzyme transport and metabolism];


Pssm-ID: 444176  Cd Length: 228  Bit Score: 49.89  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 353 SFFNYLINHPKVKPHWdayvNHEFVKRVADGTLERKKFQFFIEQDYLYLIDYVRVCCVTGSKSPTLEDleKDLVIadcaR 432
Cdd:COG5424    6 EFEARLRAEIARRYLL----KHPFLQRLREGKLTREQLRAFALQRYHYVKHFPRYLAAILSRCPDEEL--RRALL----E 75

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 330443752 433 NeLNEHERRLREEFGVK-----------DPDYLQKIKRGPALRAYCRYLIDISRRGNWQEIVVALN 487
Cdd:COG5424   76 N-LYEEDGEGPEEGHIElwlrfaealglDREEVDARPPLPETRAAVDAYVNFCRRRSLLEAVAASL 140
PRK07105 PRK07105
pyridoxamine kinase; Validated
 112-297 8.20e-06

pyridoxamine kinase; Validated


Pssm-ID: 180840 [Multi-domain]  Cd Length: 284  Bit Score: 47.60  E-value: 8.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 112 DMKCNVIKTGML-TVDAIEVLHEKLLQLGENRPKLVIDPVLcaaSDS----SPTGKDVVSLIIEKISPfADILTPNISDC 186
Cdd:PRK07105  73 NLKFDAIYSGYLgSPRQIQIVSDFIKYFKKKDLLVVVDPVM---GDNgklyQGFDQEMVEEMRKLIQK-ADVITPNLTEA 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 187 FMLLGENREVSKLQ--DVLEIAKDLSRItNCSNILVKGghIPCDDGKekhITDVLYLGAEQKFITFKGQFVNttrTH--G 262
Cdd:PRK07105 149 CLLLDKPYLEKSYSeeEIKQLLRKLADL-GPKIVIITS--VPFEDGK---IGVAYYDRATDRFWKVFCKYIP---AHypG 219

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 330443752 263 AGCTLASAIASNLARGYSLSQSVYGGIEYVQNAIA 297
Cdd:PRK07105 220 TGDIFTSVITGSLLQGDSLPIALDRAVQFIEKGIR 254
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 148-285 2.79e-04

pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 43.10  E-value: 2.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752  148 DPVLCaasDSSPTGKDVVSLIIEKispfADILTPNISDCFMLLGENREVskLQDVLEIAKDLSRiTNCSNILVKGGhipc 227
Cdd:pfam00294 160 DPNLL---DPLGAAREALLELLPL----ADLLKPNEEELEALTGAKLDD--IEEALAALHKLLA-KGIKTVIVTLG---- 225

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 330443752  228 DDGkekhiTDVLYLGAEQKFITF-KGQFVNTTrthGAGCTLASAIASNLARGYSLSQSV 285
Cdd:pfam00294 226 ADG-----ALVVEGDGEVHVPAVpKVKVVDTT---GAGDSFVGGFLAGLLAGKSLEEAL 276
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 168-285 3.24e-04

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: 42.95  E-value: 3.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 168 IIEKISPFADILTPNISDCFMLLGEnrevsklQDVLEIAKDLSRItNCSNILVKGGHIPCddgkekhitdVLYLGAEQKF 247
Cdd:COG0524  178 LLRELLALVDILFPNEEEAELLTGE-------TDPEEAAAALLAR-GVKLVVVTLGAEGA----------LLYTGGEVVH 239

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 330443752 248 I-TFKGQFVNTTrthGAGCTLASAIASNLARGYSLSQSV 285
Cdd:COG0524  240 VpAFPVEVVDTT---GAGDAFAAGFLAGLLEGLDLEEAL 275
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 174-285 5.02e-04

Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This reaction is the first step in the ribose metabolism. It traps ribose within the cell after uptake and also prepares the sugar for use in the synthesis of nucleotides and histidine, and for entry into the pentose phosphate pathway. Ribokinase is dimeric in solution.


Pssm-ID: 238579 [Multi-domain]  Cd Length: 292  Bit Score: 42.15  E-value: 5.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 174 PFADILTPNISDCFMLLGEnrEVSKLQDVLEIAKDLSRiTNCSNILVKGGHipcdDGkekhitdVLYLGAEQKFI--TFK 251
Cdd:cd01174  174 ALVDILVPNETEAALLTGI--EVTDEEDAEKAARLLLA-KGVKNVIVTLGA----KG-------ALLASGGEVEHvpAFK 239

                         90       100       110
                 ....*....|....*....|....*....|....
gi 330443752 252 GQFVNTTrthGAGCTLASAIASNLARGYSLSQSV 285
Cdd:cd01174  240 VKAVDTT---GAGDTFIGALAAALARGLSLEEAI 270
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 118-276 6.56e-04

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: 41.31  E-value: 6.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 118 IKTGMLTVDAI---------EVLHEKLLQLGENRPKLVIDPVlcaasdssPTGKDVVSLIIEKISPFADILTPNISDCFM 188
Cdd:cd00287   51 VSVTLVGADAVvisglspapEAVLDALEEARRRGVPVVLDPG--------PRAVRLDGEELEKLLPGVDILTPNEEEAEA 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 189 LLGENREVSKLQDVLEIAKDLSRITncsNILVKGGHIPCddgkekhitdVLYL--GAEQKFITFKGQFVNTTrthGAGCT 266
Cdd:cd00287  123 LTGRRDLEVKEAAEAAALLLSKGPK---VVIVTLGEKGA----------IVATrgGTEVHVPAFPVKVVDTT---GAGDA 186

                        170
                 ....*....|
gi 330443752 267 LASAIASNLA 276
Cdd:cd00287  187 FLAALAAGLA 196
THZ_kinase cd01170
4-methyl-5-beta-hydroxyethylthiazole (Thz) kinase catalyzes the phosphorylation of the ...
 117-276 1.00e-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: 40.99  E-value: 1.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 117 VIKTGMLTVDAIEVLheklLQLGE-----NRPkLVIDPVLCAASdssPTGKDVVSLIIEKISPfaDILTPNISDCFMLLG 191
Cdd:cd01170   54 VINIGTLTSEQIEAM----LKAGKaanqlGKP-VVLDPVGVGAT---SFRTEVAKELLAEGQP--TVIRGNASEIAALAG 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 330443752 192 ENREV-------SKLQDVLEIAKDLSRITNCSnILVKGghiPCDdgkekHITD-----VLYLGAE--QKfITfkgqfvnt 257
Cdd:cd01170  124 LTGLGkgvdsssSDEEDALELAKALARKYGAV-VVVTG---EVD-----YITDgervvVVKNGHPllTK-IT-------- 185

                        170
                 ....*....|....*....
gi 330443752 258 trthGAGCTLASAIASNLA 276
Cdd:cd01170  186 ----GTGCLLGAVIAAFLA 200
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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