|
Name |
Accession |
Description |
Interval |
E-value |
| salvage_TenA |
TIGR04306 |
thiaminase II; The TenA protein of Bacillus subtilis and Staphylococcus aurues, and the ... |
343-550 |
5.98e-118 |
|
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: 346.87 E-value: 5.98e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 343 VKPHWDSYINHEFVKKVADGTLERKKFQFFIEQDYAYLVDYARVHCIAGSKApCLEDMEKELV--IVGGVRTEMGQHeKR 420
Cdd:TIGR04306 1 VKPIWDDYINHPFVQKIGDGTLERDKFRFYIEQDYAYLVEYAKVHALGGSKA-CDEDMEKELVeqIQGGVETEMGQH-KR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 421 LKEVFGVKDPDYFQKIKRGPALRAYSRYFNDVSRRGNWQELVASLTPCLMGYGEALTKMKGKVTAPEGSVYHEWCETYAS 500
Cdd:TIGR04306 79 LAEVLGISDEEYFQKIKPGPALRSYTSYMYDVSRRGNWQELVAALLPCLWGYGEAATKLKGKHTAPEHSVYHKWIETYSS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6324517 501 SWYREAMDEGEKLLNHILETYPPEQLDTLVTIYAEVCELETNFWTAALEY 550
Cdd:TIGR04306 159 SWFREAVNEGENLLNHLAETSSPEELEKLKTIFAESCEYEYNFWTMAYEY 208
|
|
| TenA_C_ScTHI20-like |
cd19367 |
TenA_C family similar to the C-terminal TenA_C domain of Saccharomyces cerevisiae THI20 ... |
345-548 |
4.61e-87 |
|
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: 267.46 E-value: 4.61e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 345 PHWDSYINHEFVKKVADGTLERKKFQFFIEQDYAYLVDYARVHCIAGSKAPCLEDMEKELVIVGGVRTEMGQHEKRLKEv 424
Cdd:cd19367 1 PIWKAYTNHPFVRQLADGTLPLESFRHYLKQDYLYLIHYARAHALAAYKAPTLEDIRAAAAILLAILEEMELHVKYCAE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 425 FGVkDPDYFQKIKRGPALRAYSRYFNDVSRRGNWQELVASLTPCLMGYGEALTKMKGKV-TAPEGSVYHEWCETYASSWY 503
Cdd:cd19367 80 WGI-SEEELEATPESPATLAYTRYVLDVGLSGDLLDLLVALAPCLLGYGEIGLRLAADPaTKLEGNPYWSWIETYASDEY 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6324517 504 REAMDEGEKLLNHILETYP-PEQLDTLVTIYAEVCELETNFWTAAL 548
Cdd:cd19367 159 QEAVREGIELLEKLAAERPsPARLEELVKIFATATRLEIGFWDMGL 204
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
33-292 |
9.30e-87 |
|
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: 268.20 E-value: 9.30e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 33 DPSGGAGIEADVKTITAHRCYAMTCITALNAQTPVKVYSINNTPKEVVFQTLESNLKDMKCNVIKTGML-TAAAIEVLHE 111
Cdd:pfam08543 1 DSSGGAGIQADLKTFSALGVYGMSVITALTAQNTLGVQGVHPLPPEFVAAQLDAVLEDIPVDAVKTGMLgSAEIIEAVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 112 KLLQLGenrPKLVVDPVLVATSGSSLAGKDIVSLITEKVAPFADILTPNIPECYKLLGeeRKVNGLQDIFQIAKDLAKiT 191
Cdd:pfam08543 81 KLDKYG---VPVVLDPVMVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTG--RKIKTLEDMKEAAKKLLA-L 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 192 KCSNILVKGGHIPwndEKEKYITDVLFlgAEQKFIIFKGNFVNTTHTHGTGCTLASAIASNLARGYSLPQSVYGGIEYVQ 271
Cdd:pfam08543 155 GAKAVLIKGGHLE---GEEAVVTDVLY--DGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKEYVT 229
|
250 260
....*....|....*....|.
gi 6324517 272 NAVAIGCDVTKEtvkdNGPIN 292
Cdd:pfam08543 230 EAIRDALNLGKG----HGPVN 246
|
|
| TENA_THI-4 |
pfam03070 |
TENA/THI-4/PQQC family; Members of this family are found in all the three major phyla of life: ... |
340-550 |
2.97e-86 |
|
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: 265.76 E-value: 2.97e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 340 HPKVKPHWDSYINHEFVKKVADGTLERKKFQFFIEQDYAYLVDYARVHCIAGSKAPCLEDM-EKELVIVGGVRTEMGQHe 418
Cdd:pfam03070 1 HPQLRPIWKFYINHPFVQALAKGTLPREQFQGYVIQDYLYLVNFARVLAIIASKSPDLEVRrEWENRIVDHDGNEIELH- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 419 KRLKEVFGVKDPDyFQKIKRGPALRAYSRYFNDVSRRGNWQELVASLTPCLMGYGEALTKMKGKVTAPEGSVYHEWCETY 498
Cdd:pfam03070 80 LRLAEALGLSRED-LSAYKPLPATRAYVRYLLDFARRGSWLEAVAALLPCLFVYQEIASRLGEKIRALEGPEYYEWVKTY 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6324517 499 ASSWYREAMDEGEKLLNHILETYPPEQLDTLVTIYAEVCELETNFWTAALEY 550
Cdd:pfam03070 159 ASEYFRAAVEEAKRLLDRLLAYVSDEQLEELQEIFLKALEFEYSFWTMALDA 210
|
|
| HMPP_kinase |
cd01169 |
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ... |
25-275 |
4.36e-81 |
|
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: 253.58 E-value: 4.36e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 25 TVLSIAGTDPSGGAGIEADVKTITAHRCYAMTCITALNAQTPVKVYSINNTPKEVVFQTLESNLKDMKCNVIKTGML-TA 103
Cdd:cd01169 1 VVLTIAGSDSSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVFGVHPVPPEFVAAQLDAVLEDIPVDAIKIGMLgSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 104 AAIEVLHEKLLQLGEnrPKLVVDPVLVATSGSSLAGKDIVSLITEKVAPFADILTPNIPECYKLLGeeRKVNGLQDIFQI 183
Cdd:cd01169 81 EIIEAVAEALKDYPD--IPVVLDPVMVAKSGDSLLDDDAIEALRELLLPLATLITPNLPEAELLTG--LEIATEEDMMKA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 184 AKDLAKiTKCSNILVKGGHIPwndekEKYITDVLFLGaeQKFIIFKGNFVNTTHTHGTGCTLASAIASNLARGYSLPQSV 263
Cdd:cd01169 157 AKALLA-LGAKAVLIKGGHLP-----GDEAVDVLYDG--GGFFEFESPRIDTKNTHGTGCTLSSAIAANLAKGLSLEEAV 228
|
250
....*....|..
gi 6324517 264 YGGIEYVQNAVA 275
Cdd:cd01169 229 REAKEYVTQAIR 240
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
27-293 |
8.13e-71 |
|
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: 227.23 E-value: 8.13e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 27 LSIAGTDPSGGAGIEADVKTITAHRCYAMTCITALNAQTPVKVYSINNTPKEVVFQTLESNLKDMKCNVIKTGML-TAAA 105
Cdd:COG0351 1 LTIAGSDPSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVTGVHPVPPEFVAAQLRAVLEDIPVDAIKIGMLgSAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 106 IEVLHEKLLQLGEnrPKLVVDPVLVATSGSSLAGKDIVSLITEKVAPFADILTPNIPECYKLLGeeRKVNGLQDIFQIAK 185
Cdd:COG0351 81 IEAVAEILADYPL--VPVVLDPVMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALLG--IEITTLDDMREAAK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 186 DLAKITkCSNILVKGGHIPwndekEKYITDVLFLGaeQKFIIFKGNFVNTTHTHGTGCTLASAIASNLARGYSLPQSVYG 265
Cdd:COG0351 157 ALLELG-AKAVLVKGGHLP-----GDEAVDVLYDG--DGVREFSAPRIDTGNTHGTGCTLSSAIAALLAKGLDLEEAVRE 228
|
250 260 270
....*....|....*....|....*....|..
gi 6324517 266 GIEYVQ----NAVAIGcdvtketvKDNGPINH 293
Cdd:COG0351 229 AKEYVTqairAALRLG--------MGHGPVNH 252
|
|
| PRK14713 |
PRK14713 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
10-547 |
3.78e-62 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 237797 [Multi-domain] Cd Length: 530 Bit Score: 213.11 E-value: 3.78e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 10 TPPPYLTLACNE--KLPTVLSIAGTDPSGGAGIEADVKTITAHRCYAMTCITALNAQTPVKVYSINNTPKEVVFQTLESN 87
Cdd:PRK14713 14 MSAMTNSAAAASaaATPRVLSIAGTDPSGGAGIQADLKSIAAAGGYGMAVITALVAQNTRGVRAVHVPPADFLRAQLDAV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 88 LKDMKCNVIKTGML-TAAAIEVLHEkllQLGENRPKLVV-DPVLVATSGSSLAGKDIVSLITEKVaPFADILTPNIPECY 165
Cdd:PRK14713 94 SDDVTVDAVKIGMLgDAEVIDAVRT---WLAEHRPPVVVlDPVMVATSGDRLLEEDAEAALRELV-PRADLITPNLPELA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 166 KLLGEERKVNGLQDIFQiAKDLAKITKCSnILVKGGHIPWNDekekyiTDVLFLGAEQKFIIFKGNFVNTTHTHGTGCTL 245
Cdd:PRK14713 170 VLLGEPPATTWEEALAQ-ARRLAAETGTT-VLVKGGHLDGQR------APDALVGPDGAVTEVPGPRVDTRNTHGTGCSL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 246 ASAIASNLARGYSLPQSVYGGIEYVQNAVAIGcdVTKETVKDNGPINHVYAVEiPLEKMLSDECFTASDVIPKKPLKsaa 325
Cdd:PRK14713 242 SSALATRLGRGGDWAAALRWATAWLHGAIAAG--AALQVGTGNGPVDHFHRAR-RLAADASAEAGVSAEPAPDAVVG--- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 326 dkiPGGNFYEYLINHpkVKPHWDSYINHEFVKKVADGTLERKKFQFFIEQDYAYLVDYARVHCIAGSKAPcleDMEKELV 405
Cdd:PRK14713 316 ---PAGPFTAALWQA--SGPIREAIEDLPFVRALADGTLPEEAFEFYLAQDALYLNGYSRALARLAALAP---DPAEQVF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 406 IVGGVR----TEMGQHEKRLKevfgvkdpDYFQKIKRGPALRAYSRYFNDVSRRGNWQELVASLTPCLMGYGEALTKMKG 481
Cdd:PRK14713 388 WAQSAQacleVESELHRSWLG--------DRDADTAPSPVTLAYTDFLLARAAGGSYAVGAAAVLPCFWLYAEVGAELHA 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324517 482 KVTAPEGSVYHEWCETYASSWYREAMDEGEKLLNHILETYPPEQLDTLVTIYAEVCELETNFWTAA 547
Cdd:PRK14713 460 RAGNPDDHPYAEWLQTYADPEFAAATRRAIAFVDRAFRAASPAERAAMARAFLTACRYELEFFDQA 525
|
|
| HMP-P_kinase |
TIGR00097 |
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ... |
26-293 |
4.19e-60 |
|
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: 199.44 E-value: 4.19e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 26 VLSIAGTDPSGGAGIEADVKTITAHRCYAMTCITALNAQTPVKVYSINNTPKEVVFQTLESNLKDMKCNVIKTGMLTAAA 105
Cdd:TIGR00097 1 ALTIAGSDSGGGAGIQADLKTFSALGVFGTSVITALTAQNTRGVTGVYPIPPDFVEAQLDAVFSDIPVDAAKTGMLASAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 106 I-EVLHEKLLQLGEnrPKLVVDPVLVATSGSSLAGKDIVSLITEKVAPFADILTPNIPECYKLLGEerKVNGLQDIFQIA 184
Cdd:TIGR00097 81 IvEAVARKLREYPV--RPLVVDPVMVAKSGAPLLEEEAIEALRKRLLPLATLITPNLPEAEALLGT--KIRTEQDMIKAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 185 KDLAKiTKCSNILVKGGHIPWNDEkekyiTDVLFLGAEqkFIIFKGNFVNTTHTHGTGCTLASAIASNLARGYSLPQSVY 264
Cdd:TIGR00097 157 KKLRE-LGPKAVLIKGGHLEGDQA-----VDVLFDGGE--IHILKAPRIETKNTHGTGCTLSAAIAANLAKGLSLKEAVK 228
|
250 260
....*....|....*....|....*....
gi 6324517 265 GGIEYVQNAVAIGCDVTketvKDNGPINH 293
Cdd:TIGR00097 229 EAKEFVTGAIRYGLNIG----HGHGPLNH 253
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
22-297 |
4.59e-60 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 199.58 E-value: 4.59e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 22 KLPTVLSIAGTDPSGGAGIEADVKTITAHRCYAMTCITALNAQTPVKVYSINNTPKEVVFQTLESNLKDMKCNVIKTGML 101
Cdd:PRK06427 3 KRPIALTIAGSDSGGGAGIQADLKTFQALGVYGMSAITALTAQNTLGVQRVHPIPPEFVAAQLDAVFSDIRIDAVKIGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 102 -TAAAIEVLHEKLLQLGEnrPKLVVDPVLVATSGSSLAGKDIVSLITEKVAPFADILTPNIPECYKLLGeeRKVNGLQDI 180
Cdd:PRK06427 83 aSAEIIETVAEALKRYPI--PPVVLDPVMIAKSGDPLLADDAVAALRERLLPLATLITPNLPEAEALTG--LPIADTEDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 181 FQIAKDLAKITKCSNILVKGGHipwnDEKEKYITDVLFLGAEqkFIIFKGNFVNTTHTHGTGCTLASAIASNLARGYSLP 260
Cdd:PRK06427 159 MKAAARALHALGCKAVLIKGGH----LLDGEESVDWLFDGEG--EERFSAPRIPTKNTHGTGCTLSAAIAAELAKGASLL 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 6324517 261 QSVYGGIEYVQNAVAIGCDVtketVKDNGPINHVYAV 297
Cdd:PRK06427 233 DAVQTAKDYVTRAIRHALEI----GQGHGPVNHFAYL 265
|
|
| TenA |
COG0819 |
Aminopyrimidine aminohydrolase TenA (thiamine salvage pathway) [Coenzyme transport and ... |
331-551 |
4.34e-55 |
|
Aminopyrimidine aminohydrolase TenA (thiamine salvage pathway) [Coenzyme transport and metabolism];
Pssm-ID: 440581 [Multi-domain] Cd Length: 218 Bit Score: 185.09 E-value: 4.34e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 331 GNFYEYLINhpKVKPHWDSYINHEFVKKVADGTLERKKFQFFIEQDYAYLVDYARVHCIAGSKAPCLEDMEKELVIVGGV 410
Cdd:COG0819 1 MSFSERLRE--AAAPIWEAILEHPFVQGLADGTLPREAFRHYLVQDYLYLEHFARALALAAAKAPDLEDMRFLAGLAAGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 411 R-TEMGQHEKRLKEvFGVkDPDYFQKIKRGPALRAYSRYFNDVSRRGNWQELVASLTPCLMGYGEALTKMKGKvTAPEGS 489
Cdd:COG0819 79 LeVELALHERYAAE-LGI-SEEELEATPPSPTTRAYTSYLLAAAASGDYAELLAALLPCEWGYAEIGKRLAER-PLPPDH 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6324517 490 VYHEWCETYASSWYREAMDEGEKLLNHILETYPPEQLDTLVTIYAEVCELETNFWTAALEYE 551
Cdd:COG0819 156 PYAEWIETYASEEFQELVEWLIALLDRLAATASEAERERLEEAFRTASRLEYAFWDMAYRLE 217
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| salvage_TenA |
TIGR04306 |
thiaminase II; The TenA protein of Bacillus subtilis and Staphylococcus aurues, and the ... |
343-550 |
5.98e-118 |
|
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: 346.87 E-value: 5.98e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 343 VKPHWDSYINHEFVKKVADGTLERKKFQFFIEQDYAYLVDYARVHCIAGSKApCLEDMEKELV--IVGGVRTEMGQHeKR 420
Cdd:TIGR04306 1 VKPIWDDYINHPFVQKIGDGTLERDKFRFYIEQDYAYLVEYAKVHALGGSKA-CDEDMEKELVeqIQGGVETEMGQH-KR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 421 LKEVFGVKDPDYFQKIKRGPALRAYSRYFNDVSRRGNWQELVASLTPCLMGYGEALTKMKGKVTAPEGSVYHEWCETYAS 500
Cdd:TIGR04306 79 LAEVLGISDEEYFQKIKPGPALRSYTSYMYDVSRRGNWQELVAALLPCLWGYGEAATKLKGKHTAPEHSVYHKWIETYSS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 6324517 501 SWYREAMDEGEKLLNHILETYPPEQLDTLVTIYAEVCELETNFWTAALEY 550
Cdd:TIGR04306 159 SWFREAVNEGENLLNHLAETSSPEELEKLKTIFAESCEYEYNFWTMAYEY 208
|
|
| TenA_C_ScTHI20-like |
cd19367 |
TenA_C family similar to the C-terminal TenA_C domain of Saccharomyces cerevisiae THI20 ... |
345-548 |
4.61e-87 |
|
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: 267.46 E-value: 4.61e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 345 PHWDSYINHEFVKKVADGTLERKKFQFFIEQDYAYLVDYARVHCIAGSKAPCLEDMEKELVIVGGVRTEMGQHEKRLKEv 424
Cdd:cd19367 1 PIWKAYTNHPFVRQLADGTLPLESFRHYLKQDYLYLIHYARAHALAAYKAPTLEDIRAAAAILLAILEEMELHVKYCAE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 425 FGVkDPDYFQKIKRGPALRAYSRYFNDVSRRGNWQELVASLTPCLMGYGEALTKMKGKV-TAPEGSVYHEWCETYASSWY 503
Cdd:cd19367 80 WGI-SEEELEATPESPATLAYTRYVLDVGLSGDLLDLLVALAPCLLGYGEIGLRLAADPaTKLEGNPYWSWIETYASDEY 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6324517 504 REAMDEGEKLLNHILETYP-PEQLDTLVTIYAEVCELETNFWTAAL 548
Cdd:cd19367 159 QEAVREGIELLEKLAAERPsPARLEELVKIFATATRLEIGFWDMGL 204
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
33-292 |
9.30e-87 |
|
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: 268.20 E-value: 9.30e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 33 DPSGGAGIEADVKTITAHRCYAMTCITALNAQTPVKVYSINNTPKEVVFQTLESNLKDMKCNVIKTGML-TAAAIEVLHE 111
Cdd:pfam08543 1 DSSGGAGIQADLKTFSALGVYGMSVITALTAQNTLGVQGVHPLPPEFVAAQLDAVLEDIPVDAVKTGMLgSAEIIEAVAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 112 KLLQLGenrPKLVVDPVLVATSGSSLAGKDIVSLITEKVAPFADILTPNIPECYKLLGeeRKVNGLQDIFQIAKDLAKiT 191
Cdd:pfam08543 81 KLDKYG---VPVVLDPVMVAKSGDSLLDDEAIEALKEELLPLATLITPNLPEAEALTG--RKIKTLEDMKEAAKKLLA-L 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 192 KCSNILVKGGHIPwndEKEKYITDVLFlgAEQKFIIFKGNFVNTTHTHGTGCTLASAIASNLARGYSLPQSVYGGIEYVQ 271
Cdd:pfam08543 155 GAKAVLIKGGHLE---GEEAVVTDVLY--DGGGFYTLEAPRIPTKNTHGTGCTLSAAIAANLAKGLSLPEAVREAKEYVT 229
|
250 260
....*....|....*....|.
gi 6324517 272 NAVAIGCDVTKEtvkdNGPIN 292
Cdd:pfam08543 230 EAIRDALNLGKG----HGPVN 246
|
|
| TENA_THI-4 |
pfam03070 |
TENA/THI-4/PQQC family; Members of this family are found in all the three major phyla of life: ... |
340-550 |
2.97e-86 |
|
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: 265.76 E-value: 2.97e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 340 HPKVKPHWDSYINHEFVKKVADGTLERKKFQFFIEQDYAYLVDYARVHCIAGSKAPCLEDM-EKELVIVGGVRTEMGQHe 418
Cdd:pfam03070 1 HPQLRPIWKFYINHPFVQALAKGTLPREQFQGYVIQDYLYLVNFARVLAIIASKSPDLEVRrEWENRIVDHDGNEIELH- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 419 KRLKEVFGVKDPDyFQKIKRGPALRAYSRYFNDVSRRGNWQELVASLTPCLMGYGEALTKMKGKVTAPEGSVYHEWCETY 498
Cdd:pfam03070 80 LRLAEALGLSRED-LSAYKPLPATRAYVRYLLDFARRGSWLEAVAALLPCLFVYQEIASRLGEKIRALEGPEYYEWVKTY 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 6324517 499 ASSWYREAMDEGEKLLNHILETYPPEQLDTLVTIYAEVCELETNFWTAALEY 550
Cdd:pfam03070 159 ASEYFRAAVEEAKRLLDRLLAYVSDEQLEELQEIFLKALEFEYSFWTMALDA 210
|
|
| HMPP_kinase |
cd01169 |
4-amino-5-hydroxymethyl-2-methyl-pyrimidine phosphate kinase (HMPP-kinase) catalyzes two ... |
25-275 |
4.36e-81 |
|
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: 253.58 E-value: 4.36e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 25 TVLSIAGTDPSGGAGIEADVKTITAHRCYAMTCITALNAQTPVKVYSINNTPKEVVFQTLESNLKDMKCNVIKTGML-TA 103
Cdd:cd01169 1 VVLTIAGSDSSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVFGVHPVPPEFVAAQLDAVLEDIPVDAIKIGMLgSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 104 AAIEVLHEKLLQLGEnrPKLVVDPVLVATSGSSLAGKDIVSLITEKVAPFADILTPNIPECYKLLGeeRKVNGLQDIFQI 183
Cdd:cd01169 81 EIIEAVAEALKDYPD--IPVVLDPVMVAKSGDSLLDDDAIEALRELLLPLATLITPNLPEAELLTG--LEIATEEDMMKA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 184 AKDLAKiTKCSNILVKGGHIPwndekEKYITDVLFLGaeQKFIIFKGNFVNTTHTHGTGCTLASAIASNLARGYSLPQSV 263
Cdd:cd01169 157 AKALLA-LGAKAVLIKGGHLP-----GDEAVDVLYDG--GGFFEFESPRIDTKNTHGTGCTLSSAIAANLAKGLSLEEAV 228
|
250
....*....|..
gi 6324517 264 YGGIEYVQNAVA 275
Cdd:cd01169 229 REAKEYVTQAIR 240
|
|
| ThiD |
COG0351 |
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ... |
27-293 |
8.13e-71 |
|
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: 227.23 E-value: 8.13e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 27 LSIAGTDPSGGAGIEADVKTITAHRCYAMTCITALNAQTPVKVYSINNTPKEVVFQTLESNLKDMKCNVIKTGML-TAAA 105
Cdd:COG0351 1 LTIAGSDPSGGAGIQADLKTFAALGVYGMSVITALTAQNTLGVTGVHPVPPEFVAAQLRAVLEDIPVDAIKIGMLgSAEI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 106 IEVLHEKLLQLGEnrPKLVVDPVLVATSGSSLAGKDIVSLITEKVAPFADILTPNIPECYKLLGeeRKVNGLQDIFQIAK 185
Cdd:COG0351 81 IEAVAEILADYPL--VPVVLDPVMVAKSGDRLLDEDAVEALRELLLPLATVVTPNLPEAEALLG--IEITTLDDMREAAK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 186 DLAKITkCSNILVKGGHIPwndekEKYITDVLFLGaeQKFIIFKGNFVNTTHTHGTGCTLASAIASNLARGYSLPQSVYG 265
Cdd:COG0351 157 ALLELG-AKAVLVKGGHLP-----GDEAVDVLYDG--DGVREFSAPRIDTGNTHGTGCTLSSAIAALLAKGLDLEEAVRE 228
|
250 260 270
....*....|....*....|....*....|..
gi 6324517 266 GIEYVQ----NAVAIGcdvtketvKDNGPINH 293
Cdd:COG0351 229 AKEYVTqairAALRLG--------MGHGPVNH 252
|
|
| TenA_PqqC-like |
cd16099 |
TenA-like proteins including TenA_C and TenA_E proteins, as well as pyrroloquinoline quinone ... |
347-546 |
2.19e-63 |
|
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: 206.05 E-value: 2.19e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 347 WDSYINHEFVKKVADGTLERKKFQFFIEQDYAYLVDYARVHCIAGSKAPCLEDMEKELVIVGGVRTEMGQHEKRLKEVFG 426
Cdd:cd16099 2 WDAILNHPFVQELAAGTLPREKFRYYLAQDYYYLKDFARALALAAAKAPDLELRTFLAELINVLDDELELHEKLLAELGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 427 vkDPDYFQKIKRGPALRAYSRYFNDVSRRGNWQELVASLTPCLMGYGEALTKMKGKvtAPEGSVYHEWCETYASSWYREA 506
Cdd:cd16099 82 --SEEDLSEAEPNPATLAYTNHLLRVAARGTPAEGLAALLPCYWSYGEIGRRLAAS--LPEHPPYRFWIDFYASDEYQEL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6324517 507 MDEGEKLLNHiLETYPPEQLDTLVTIYAEVCELETNFWTA 546
Cdd:cd16099 158 VEELLQLLDQ-LAAAGEEEKEELKEIFLTSLRYELMFWDA 196
|
|
| PRK14713 |
PRK14713 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
10-547 |
3.78e-62 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 237797 [Multi-domain] Cd Length: 530 Bit Score: 213.11 E-value: 3.78e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 10 TPPPYLTLACNE--KLPTVLSIAGTDPSGGAGIEADVKTITAHRCYAMTCITALNAQTPVKVYSINNTPKEVVFQTLESN 87
Cdd:PRK14713 14 MSAMTNSAAAASaaATPRVLSIAGTDPSGGAGIQADLKSIAAAGGYGMAVITALVAQNTRGVRAVHVPPADFLRAQLDAV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 88 LKDMKCNVIKTGML-TAAAIEVLHEkllQLGENRPKLVV-DPVLVATSGSSLAGKDIVSLITEKVaPFADILTPNIPECY 165
Cdd:PRK14713 94 SDDVTVDAVKIGMLgDAEVIDAVRT---WLAEHRPPVVVlDPVMVATSGDRLLEEDAEAALRELV-PRADLITPNLPELA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 166 KLLGEERKVNGLQDIFQiAKDLAKITKCSnILVKGGHIPWNDekekyiTDVLFLGAEQKFIIFKGNFVNTTHTHGTGCTL 245
Cdd:PRK14713 170 VLLGEPPATTWEEALAQ-ARRLAAETGTT-VLVKGGHLDGQR------APDALVGPDGAVTEVPGPRVDTRNTHGTGCSL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 246 ASAIASNLARGYSLPQSVYGGIEYVQNAVAIGcdVTKETVKDNGPINHVYAVEiPLEKMLSDECFTASDVIPKKPLKsaa 325
Cdd:PRK14713 242 SSALATRLGRGGDWAAALRWATAWLHGAIAAG--AALQVGTGNGPVDHFHRAR-RLAADASAEAGVSAEPAPDAVVG--- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 326 dkiPGGNFYEYLINHpkVKPHWDSYINHEFVKKVADGTLERKKFQFFIEQDYAYLVDYARVHCIAGSKAPcleDMEKELV 405
Cdd:PRK14713 316 ---PAGPFTAALWQA--SGPIREAIEDLPFVRALADGTLPEEAFEFYLAQDALYLNGYSRALARLAALAP---DPAEQVF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 406 IVGGVR----TEMGQHEKRLKevfgvkdpDYFQKIKRGPALRAYSRYFNDVSRRGNWQELVASLTPCLMGYGEALTKMKG 481
Cdd:PRK14713 388 WAQSAQacleVESELHRSWLG--------DRDADTAPSPVTLAYTDFLLARAAGGSYAVGAAAVLPCFWLYAEVGAELHA 459
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324517 482 KVTAPEGSVYHEWCETYASSWYREAMDEGEKLLNHILETYPPEQLDTLVTIYAEVCELETNFWTAA 547
Cdd:PRK14713 460 RAGNPDDHPYAEWLQTYADPEFAAATRRAIAFVDRAFRAASPAERAAMARAFLTACRYELEFFDQA 525
|
|
| HMP-P_kinase |
TIGR00097 |
hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; This model represents a ... |
26-293 |
4.19e-60 |
|
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: 199.44 E-value: 4.19e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 26 VLSIAGTDPSGGAGIEADVKTITAHRCYAMTCITALNAQTPVKVYSINNTPKEVVFQTLESNLKDMKCNVIKTGMLTAAA 105
Cdd:TIGR00097 1 ALTIAGSDSGGGAGIQADLKTFSALGVFGTSVITALTAQNTRGVTGVYPIPPDFVEAQLDAVFSDIPVDAAKTGMLASAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 106 I-EVLHEKLLQLGEnrPKLVVDPVLVATSGSSLAGKDIVSLITEKVAPFADILTPNIPECYKLLGEerKVNGLQDIFQIA 184
Cdd:TIGR00097 81 IvEAVARKLREYPV--RPLVVDPVMVAKSGAPLLEEEAIEALRKRLLPLATLITPNLPEAEALLGT--KIRTEQDMIKAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 185 KDLAKiTKCSNILVKGGHIPWNDEkekyiTDVLFLGAEqkFIIFKGNFVNTTHTHGTGCTLASAIASNLARGYSLPQSVY 264
Cdd:TIGR00097 157 KKLRE-LGPKAVLIKGGHLEGDQA-----VDVLFDGGE--IHILKAPRIETKNTHGTGCTLSAAIAANLAKGLSLKEAVK 228
|
250 260
....*....|....*....|....*....
gi 6324517 265 GGIEYVQNAVAIGCDVTketvKDNGPINH 293
Cdd:TIGR00097 229 EAKEFVTGAIRYGLNIG----HGHGPLNH 253
|
|
| PRK06427 |
PRK06427 |
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed |
22-297 |
4.59e-60 |
|
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
Pssm-ID: 180561 [Multi-domain] Cd Length: 266 Bit Score: 199.58 E-value: 4.59e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 22 KLPTVLSIAGTDPSGGAGIEADVKTITAHRCYAMTCITALNAQTPVKVYSINNTPKEVVFQTLESNLKDMKCNVIKTGML 101
Cdd:PRK06427 3 KRPIALTIAGSDSGGGAGIQADLKTFQALGVYGMSAITALTAQNTLGVQRVHPIPPEFVAAQLDAVFSDIRIDAVKIGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 102 -TAAAIEVLHEKLLQLGEnrPKLVVDPVLVATSGSSLAGKDIVSLITEKVAPFADILTPNIPECYKLLGeeRKVNGLQDI 180
Cdd:PRK06427 83 aSAEIIETVAEALKRYPI--PPVVLDPVMIAKSGDPLLADDAVAALRERLLPLATLITPNLPEAEALTG--LPIADTEDE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 181 FQIAKDLAKITKCSNILVKGGHipwnDEKEKYITDVLFLGAEqkFIIFKGNFVNTTHTHGTGCTLASAIASNLARGYSLP 260
Cdd:PRK06427 159 MKAAARALHALGCKAVLIKGGH----LLDGEESVDWLFDGEG--EERFSAPRIPTKNTHGTGCTLSAAIAAELAKGASLL 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 6324517 261 QSVYGGIEYVQNAVAIGCDVtketVKDNGPINHVYAV 297
Cdd:PRK06427 233 DAVQTAKDYVTRAIRHALEI----GQGHGPVNHFAYL 265
|
|
| PLN02898 |
PLN02898 |
HMP-P kinase/thiamin-monophosphate pyrophosphorylase |
18-293 |
1.95e-57 |
|
HMP-P kinase/thiamin-monophosphate pyrophosphorylase
Pssm-ID: 215486 [Multi-domain] Cd Length: 502 Bit Score: 199.61 E-value: 1.95e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 18 ACNEKLPTVLSIAGTDPSGGAGIEADVKTITAHRCYAMTCITALNAQTPVKVYSINNTPKEVVFQTLESNLKDMKCNVIK 97
Cdd:PLN02898 4 ESPMKVPHVLTVAGSDSGAGAGIQADIKACAARGVYCTTAITAVTAQNTVGVQGVHAVPLDFVAEQLKSVLSDMPVDVVK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 98 TGML-TAAAIEVLHEKLlqlgENRP--KLVVDPVLVATSGSSLAGKDIVSLITEKVAPFADILTPNIPECYKLLGEERkV 174
Cdd:PLN02898 84 TGMLpSAEIVKVLCQAL----KEFPvkALVVDPVMVSTSGDVLAGPSILSALREELLPLATIVTPNVKEASALLGGDP-L 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 175 NGLQDIFQIAKDLAKItKCSNILVKGGHIPwnDEKEkyITDVLFLGAEqkFIIFKGNFVNTTHTHGTGCTLASAIASNLA 254
Cdd:PLN02898 159 ETVADMRSAAKELHKL-GPRYVLVKGGHLP--DSLD--AVDVLYDGTE--FHELRSSRIKTRNTHGTGCTLASCIAAELA 231
|
250 260 270
....*....|....*....|....*....|....*....
gi 6324517 255 RGYSLPQSVYGGIEYVQNAVAIGCDVtKETVKDNGPINH 293
Cdd:PLN02898 232 KGSDMLSAVKVAKRYVETALEYSKDI-GIGNGAQGPFNH 269
|
|
| TenA |
COG0819 |
Aminopyrimidine aminohydrolase TenA (thiamine salvage pathway) [Coenzyme transport and ... |
331-551 |
4.34e-55 |
|
Aminopyrimidine aminohydrolase TenA (thiamine salvage pathway) [Coenzyme transport and metabolism];
Pssm-ID: 440581 [Multi-domain] Cd Length: 218 Bit Score: 185.09 E-value: 4.34e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 331 GNFYEYLINhpKVKPHWDSYINHEFVKKVADGTLERKKFQFFIEQDYAYLVDYARVHCIAGSKAPCLEDMEKELVIVGGV 410
Cdd:COG0819 1 MSFSERLRE--AAAPIWEAILEHPFVQGLADGTLPREAFRHYLVQDYLYLEHFARALALAAAKAPDLEDMRFLAGLAAGL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 411 R-TEMGQHEKRLKEvFGVkDPDYFQKIKRGPALRAYSRYFNDVSRRGNWQELVASLTPCLMGYGEALTKMKGKvTAPEGS 489
Cdd:COG0819 79 LeVELALHERYAAE-LGI-SEEELEATPPSPTTRAYTSYLLAAAASGDYAELLAALLPCEWGYAEIGKRLAER-PLPPDH 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6324517 490 VYHEWCETYASSWYREAMDEGEKLLNHILETYPPEQLDTLVTIYAEVCELETNFWTAALEYE 551
Cdd:COG0819 156 PYAEWIETYASEEFQELVEWLIALLDRLAATASEAERERLEEAFRTASRLEYAFWDMAYRLE 217
|
|
| PTZ00347 |
PTZ00347 |
phosphomethylpyrimidine kinase; Provisional |
20-293 |
2.29e-51 |
|
phosphomethylpyrimidine kinase; Provisional
Pssm-ID: 240375 [Multi-domain] Cd Length: 504 Bit Score: 183.63 E-value: 2.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 20 NEKLPTVLSIAGTDPSGGAGIEADVKTITAHRCYAMTCITALNAQTPVKVYSINNTPKEVVFQTLESNLKDMKCNVIKTG 99
Cdd:PTZ00347 227 PMKIPTVLTVSGSDSGGGAGHQADLKTLEALGVYSTSALTSLTAQNTKGVQQIQVVNEDFFAAQIDSVMSDFNISVVKLG 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 100 ML-TAAAIEVLHEKLLQLgenrpKLVVDPVLVATSGSSL----AGKDIVSLITEKVAPFADILTPNIPECYKLLGEeRKV 174
Cdd:PTZ00347 307 LVpTARQLEIVIEKLKNL-----PMVVDPVLVATSGDDLvaqkNADDVLAMYKERIFPMATIITPNIPEAERILGR-KEI 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 175 NGLQDIFQIAKDLAKItKCSNILVKGGHIPWNDEkekYITDVLFLGAEQKFIIFKGNFVNTTHTHGTGCTLASAIASNLA 254
Cdd:PTZ00347 381 TGVYEARAAAQALAQY-GSRYVLVKGGHDLIDPE---ACRDVLYDREKDRFYEFTANRIATINTHGTGCTLASAISSFLA 456
|
250 260 270
....*....|....*....|....*....|....*....
gi 6324517 255 RGYSLPQSVYGGIEYVQNAVAIGCDVTKETvKDNGPINH 293
Cdd:PTZ00347 457 RGYTVPDAVERAIGYVHEAIVRSCGVPLGQ-GTNRPLVH 494
|
|
| PRK09517 |
PRK09517 |
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ... |
4-547 |
3.08e-48 |
|
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; Provisional
Pssm-ID: 169939 [Multi-domain] Cd Length: 755 Bit Score: 179.01 E-value: 3.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 4 STVSINTPPPYLTLACNEKLPTVLSIAGTDPSGGAGIEADVKTITAHRCYAMTCITALNAQTPVKVYSINNTPKEVVFQT 83
Cdd:PRK09517 222 TQTELSQTELQGAFVNSPSAPRVLSIAGTDPTGGAGIQADLKSIAAGGGYGMCVVTALVAQNTHGVNTIHTPPLTFLEEQ 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 84 LESNLKDMKCNVIKTGMLTAAAieVLHEKLLQLGENRPKLVV-DPVLVATSGSSLAGKDIVSLITEkVAPFADILTPNIP 162
Cdd:PRK09517 302 LEAVFSDVTVDAVKLGMLGSAD--TVDLVASWLGSHEHGPVVlDPVMVATSGDRLLDADATEALRR-LAVHVDVVTPNIP 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 163 ECYKLLGeERKVNGLQDIFQIAKDLAKiTKCSNILVKGGHIPWNDEKEKYITdvlflgAEQKFIIFKGNFVNTTHTHGTG 242
Cdd:PRK09517 379 ELAVLCG-EAPAITMDEAIAQARGFAR-THGTIVIVKGGHLTGDLADNAVVR------PDGSVHQVENPRVNTTNSHGTG 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 243 CTLASAIASNLARGYSLPQSVYGGIEYVQNAVAIGCDVtkETVKDNGPINHVY-------AVEIPLEKMLSDECFTASDV 315
Cdd:PRK09517 451 CSLSAALATLIAAGESVEKALEWATRWLNEALRHADHL--AVGSGNGPVDHGHlarrlthAAETTPWAHLRAGATAASFT 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 316 IPKKPLKSAADKIPGGnfyeylinhPKVKPHWDS-------YINHEFVKKVADGTLERKKFQFFIEQDYAYLVDYARVHC 388
Cdd:PRK09517 529 TPSTVKSPAPRIEPAG---------PFTRALWEAsgdiiaeINDSDFIRMLGDGTLRRPEFDFYIDQDAQYLRQYSRALA 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 389 IAGSKAPcleDMEKELV----IVGGVRTEMGQHEKRLKEVFGVKDPdyfqkikrGPALRAYSRYFNDVSRRGNWQELVAS 464
Cdd:PRK09517 600 RLSSIAP---DSHAQVEwaqsAAECIVVEAELHRSYLSGKEAPSAP--------SPVTMAYTDFLIARTYTEDYVVGVAA 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 465 LTPCLMGYGEALTKMKGKvtAPEGSVYHEWCETYASSWYREAMDEGEKLLNHILETYPPEQLDTLVTIYAEVCELETNFW 544
Cdd:PRK09517 669 VLPCYWLYAEIGLMLAEQ--NHDEHPYKDWLNTYSGEEFIAGTRAAIARVEKALENAGPEQRVDAARAFLSASVHEREFF 746
|
...
gi 6324517 545 TAA 547
Cdd:PRK09517 747 DQA 749
|
|
| TenA_C_BhTenA-like |
cd19366 |
TenA_C proteins similar to Bacillus halodurans TenA; This family of TenA proteins belongs to ... |
333-547 |
3.18e-46 |
|
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: 161.19 E-value: 3.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 333 FYEYLinHPKVKPHWDSYINHEFVKKVADGTLERKKFQFFIEQDYAYLVDYARVHCIAGSKAPCLEDMEK--ELvIVGGV 410
Cdd:cd19366 1 FSERL--REKAKPIWEAGLEHPFVQGLGDGTLDKEKFKFYLKQDYLYLIDYARVFALGAAKADDLETMGRfaEL-LHGTL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 411 RTEMGQHEKRLKEvFGVkDPDYFQKIKRGPALRAYSRYFNDVSRRGNWQELVASLTPCLMGYGEALTKMKGKVTAPEGSV 490
Cdd:cd19366 78 NTEMDLHRQYAAE-FGI-TEEELEATEPSPTTLAYTSYMLRTAQTGTLAELLAALLPCAWGYAEIGKRLAEQGGALEHNP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6324517 491 YHEWCETYASSWYREAMDEGEKLLNHILETYPPEQLDTLVTIYAEVCELETNFWTAA 547
Cdd:cd19366 156 YREWIEMYSSDEFTELADWLIDLLDELAEGKSEAELERLEEIFLTSSRYEYMFWDMA 212
|
|
| PRK08573 |
PRK08573 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
24-303 |
4.62e-44 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 236297 [Multi-domain] Cd Length: 448 Bit Score: 162.20 E-value: 4.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 24 PTVLSIAGTDPSGGAGIEADVKTITA---HRCYAMTCITALNAQTpvkVYSINNTPKEVVFQTLESNLKDMKCNVIKTGM 100
Cdd:PRK08573 3 PVALTIAGSDSGGGAGIEADLKTFAAlgvHGAVAITSVTAQNTYE---VRAIHDLPPEVVAAQIEAVWEDMGIDAAKTGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 101 L-TAAAIEVLHEKLLQLGenRPkLVVDPVLVATSGSSLAGKDIVSLITEKVAPFADILTPNIPECYKLLGeeRKVNGLQD 179
Cdd:PRK08573 80 LsNREIIEAVAKTVSKYG--FP-LVVDPVMIAKSGAPLLREDAVDALIKRLLPLATVVTPNRPEAEKLTG--MKIRSVED 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 180 IFQIAKDLAKITKCSNILVKGGHIpwndEKEKYItDVLFLGAeqKFIIFKGNFVNTTHTHGTGCTLASAIASNLARGYSL 259
Cdd:PRK08573 155 ARKAAKYIVEELGAEAVVVKGGHL----EGEEAV-DVLYHNG--TFREFRAPRVESGCTHGTGCSFSAAIAAGLAKGLDP 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 6324517 260 PQSVYGGIEYVQNAVAIGCDVTketvKDNGPINHVYAVEIPLEK 303
Cdd:PRK08573 228 EEAIKTAKKFITMAIKYGVKIG----KGHCPVNPMAWIEIPAER 267
|
|
| TenA_C-like |
cd19369 |
uncharacterized TenA_C proteins; This family of TenA proteins belongs to the TenA_C class as ... |
345-544 |
5.67e-34 |
|
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: 127.73 E-value: 5.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 345 PHWDSYINHEFVKKVADGTLERKKFQFFIEQDYAYLVDYARVHCIAGSKAPCLEDMEKELVIVGGV-RTEMGQHEKRLKE 423
Cdd:cd19369 1 PIWEQYLEHPFIKELGEGTLDKEKFKNYLIQDSLYLKEYAKVFAMGIYKSRTMKEMQFFYSSLSFVnEDETATRIKYLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 424 vFGVkDPDYFQKIKRGPALRAYSRYFNDVSRRGNWQELVASLTPCLMGYGEALTKMKGKVTAP-EGSVYHEWCETYASSW 502
Cdd:cd19369 81 -FGL-TDEDIEKIEPLPENKAYTDYMLGIAKTGDVKEILMAVLPCMLSYYYIFKELVKKYKDNlESNPYKDWIEDYASEE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6324517 503 YREAMDEGEKLLNHILETYPPEQLDTLVTIYAEVCELETNFW 544
Cdd:cd19369 159 YAEYCKEWIDFADRLCENLSEEEKEKLKEIFRKASLYELKFW 200
|
|
| TenA_C_HP1287-like |
cd19361 |
TenA_C proteins similar to Helicobacter pylori TenA (HP1287; This family of TenA proteins ... |
335-544 |
1.41e-32 |
|
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: 124.23 E-value: 1.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 335 EYLINhpKVKPHWDSYINHEFVKKVADGTLERKKFQFFIEQDYAYLVDYARVHCIAGSKAPCLEDMEKELVIVGGVR-TE 413
Cdd:cd19361 3 ERLYE--AVEDIWDSYYEHPFVQGIADGTLDIEKFRFYMIQDYLYLLDYAKVFALGVAKAKDEEVMRFFADLINAILnEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 414 MGQHEKRLKEvFGVkDPDYFQKIKRGPALRAYSRYFNDVSRRGNWQELVASLTPCLMGY---GEALTKMKGKvtAPEGSV 490
Cdd:cd19361 81 MDIHRGYMKR-LGI-TEEEIENTKPALDNLSYTSYMLSVAYEGGIAEILAAILSCSWSYeyiAKKLVERYPA--ALEHEF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 6324517 491 YHEWCETYASSWYREAMDEGEKLLNHILETYPPEQLDTLVTIYAEVCELETNFW 544
Cdd:cd19361 157 YGEWVKGYSSEEYAEANQELIDLLDRLTEDISEEQIEKLEEIFVNCSRYELKFW 210
|
|
| TenA_C-like |
cd19365 |
uncharacterized TenA_C proteins; This family of TenA proteins belongs to the TenA_C class as ... |
342-547 |
1.07e-29 |
|
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: 115.69 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 342 KVKPHWDSYINHEFVKKVADGTLERKKFQFFIEQDYAYLVDYARVHCIAGSKAPCLEDMEK--ELViVGGVRTEMGQHEK 419
Cdd:cd19365 7 AIAPIYAAILAHPFIRELADGTLPREKFRFYLAQDALYLRDYARALALLAARAPDPEEQVFfaRFA-AGAIEVERELHRS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 420 RLKEvFGVKDPdyfqkIKRGPALRAYSRYFNDVSRRGNWQELVASLTPCLMGY---GEALTKmkgkvTAPEGSVYHEWCE 496
Cdd:cd19365 86 FLGE-FGIDAA-----AEPSPVTLAYTSFLLATAATGPYAVAVAAVLPCFWIYaevGKRLAA-----AASPNHPYQDWID 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 6324517 497 TYASSWYREAMDEGEKLLNHILETYPPEQLDTLVTIYAEVCELETNFWTAA 547
Cdd:cd19365 155 TYSDEEFAEAVRRAIAIVDRLAAEASPEERARMLEAFLRASRLEWMFWDAA 205
|
|
| TenA_C_BsTenA-like |
cd19364 |
TenA_C proteins similar to Bacillus subtilis TenA; This family of TenA proteins belongs to the ... |
340-549 |
2.58e-26 |
|
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: 106.50 E-value: 2.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 340 HPKVKPHWDSYINHEFVKKVADGTLERKKFQFFIEQDYAYLVDYARVHCIAGSKAPCLEDMEKELVIVGGVR-TEMGQHE 418
Cdd:cd19364 6 REAADPLWQKSFEHPFIQGLADGTLPLETFRYYLIQDAYYLKHFAKLHALAAAKADDPAIKALLLEGAQGLAeGELALRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 419 KRLKEVfGVKDPDYFQkikRGPALRAYSrYFNDVSR---RGNWQELVASLTPCLMGY---GEALTKMKGKVtapegSVYH 492
Cdd:cd19364 86 TFFKEL-GITEEEIAQ---TPPAPTAYH-YVSHMYRqlnEGSVAEAVAALLPCYWLYqeiGERLADAGSPV-----PLYQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6324517 493 EWCETYASSWYREAMDEGEKLLNHILETYPPEQLDTLVTIYAEVCELETNFWTAALE 549
Cdd:cd19364 156 RWIDTYASDEFTESVQQQIDLVDRLAEEASEEEREKMKQAFLISSYYELQFWEMAYT 212
|
|
| TenA_C_PH1161-like |
cd19363 |
uncharacterized TenA_C proteins similar to Pyrococcus horikoshii PH1161; This family of TenA ... |
347-547 |
4.51e-26 |
|
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: 105.87 E-value: 4.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 347 WDSYINHEFVKKVADGTLERKKFQFFIEQDYAYLVDYARVHCIAGSKAPCLEDMEKELVIVGG-VRTEMGQHEKRLKEVf 425
Cdd:cd19363 13 WKKILNHPFVVELYSGTLPMEKFKFYLLQDYNYLVGSTKNLSILASKAESLDLMRELLELAYGeATTEFANYEELLDEL- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 426 GVkDPDYFQKIKRGPALRAYSRYFNDVSRRGNWQELVASLTPCLMGYGEALTKMKGKVTAPEGSVYHEWCETYASSWYRE 505
Cdd:cd19363 92 GL-SLEDAIKVEPFPTNVAYMNFLLSTSSLGSFYEGLAALLPCFWSYLEIAEYHKDKLSENPNDIYRDWASVYLSKEYKE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 6324517 506 AMDEGEKLLNHILETYPPEQLDtlvTIYAEVCELETNFWTAA 547
Cdd:cd19363 171 LVERLRRIVDKYGEGEPFEKLK---RIFKTASKYEYMFWDAA 209
|
|
| PRK12412 |
PRK12412 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
23-293 |
1.71e-24 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183512 [Multi-domain] Cd Length: 268 Bit Score: 103.13 E-value: 1.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 23 LPTVLSIAGTDPSGGAGIEADVKTITAHRCYAMTCITALNAQTPVKVYSINNTPKEV--VFQTLESNLKDMKCNVIKTGM 100
Cdd:PRK12412 1 LNKALTIAGSDTSGGAGIQADLKTFQELGVYGMTSLTTIVTMDPHNGWAHNVFPIPAstLKPQLETTIEGVGVDALKTGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 101 LTAAAIEVLHEKLLQlGENRPKLVVDPVLVATSGSSLAGKDIVSLITEKVAPFADILTPNIPECYKLLGeeRKVNGLQDI 180
Cdd:PRK12412 81 LGSVEIIEMVAETIE-KHNFKNVVVDPVMVCKGADEALHPETNDCLRDVLVPKALVVTPNLFEAYQLSG--VKINSLEDM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 181 FQIAKDLAKItKCSNILVKGGH-IPwndekEKYITDVLFLGaeQKFIIFKGNFVNTTHTHGTGCTLASAIASNLARGYSL 259
Cdd:PRK12412 158 KEAAKKIHAL-GAKYVLIKGGSkLG-----TETAIDVLYDG--ETFDLLESEKIDTTNTHGAGCTYSAAITAELAKGKPV 229
|
250 260 270
....*....|....*....|....*....|....*..
gi 6324517 260 PQSVYGGIEYVQNAVaigcdvtKETVKDN---GPINH 293
Cdd:PRK12412 230 KEAVKTAKEFITAAI-------RYSFKINeyvGPTHH 259
|
|
| PRK12616 |
PRK12616 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
27-293 |
3.17e-22 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183624 Cd Length: 270 Bit Score: 96.65 E-value: 3.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 27 LSIAGTDPSGGAGIEADVKTITAHRCYAMTCITALNAQTPV-----KVYSINNtpkEVVFQTLESNLKDMKCNVIKTGML 101
Cdd:PRK12616 7 LTIAGSDSSGGAGIQADLKTFQEKNVYGMTALTVVVAMDPEnswdhQVFPIDT---DTIRAQLSTIVDGIGVDAMKTGML 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 102 TAAAIEVLHEKLLQLGENRpKLVVDPVLVATSGSSLAGKDIVSLITEKVAPFADILTPNIPECYKLLGEErKVNGLQDIF 181
Cdd:PRK12616 84 PTVDIIELAADTIKEKQLK-NVVIDPVMVCKGANEVLYPEHAEALREQLAPLATVITPNLFEAGQLSGMG-EIKTVEQMK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 182 QIAKDLAKITKCSNILVKGGHIpwndEKEKYItDVLFLGaeQKFIIFKGNFVNTTHTHGTGCTLASAIASNLARGYSLPQ 261
Cdd:PRK12616 162 EAAKKIHELGAQYVVITGGGKL----KHEKAV-DVLYDG--ETAEVLESEMIDTPYTHGAGCTFSAAVTAELAKGSEVKE 234
|
250 260 270
....*....|....*....|....*....|....*
gi 6324517 262 SVYGGIEYVQNAVaigcdvtKETVKDN---GPINH 293
Cdd:PRK12616 235 AIYAAKEFITAAI-------KESFPLNqyvGPTKH 262
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
26-274 |
6.70e-21 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 92.05 E-value: 6.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 26 VLSIAGTDPSGGAGIEADVKTITAHRCY---AMTCITALNAqtpvKVYSINNTPKEVVFQTLESnLKDMKCNVIKTGMLT 102
Cdd:PRK12413 6 ILAISGNDIFSGGGLHADLATYTRNGLHgfvAVTCLTAMTE----KGFEVFPVDKEIFQQQLDS-LKDVPFSAIKIGLLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 103 AAAIEVLHEKLLQLGENRPkLVVDPVLVATSGSSLAgkdiVSLITE---KVAPFADILTPNIPECYKLLGeeRKVNGLQD 179
Cdd:PRK12413 81 NVEIAEQALDFIKGHPGIP-VVLDPVLVCKETHDVE----VSELRQeliQFFPYVTVITPNLVEAELLSG--KEIKTLED 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 180 IFQIAKDL----AKitkcsNILVKGGhipwNDEKEKYITDVLFLGaeQKFIIFKgNFVNTTHTHGTGCTLASAIASNLAR 255
Cdd:PRK12413 154 MKEAAKKLydlgAK-----AVVIKGG----NRLSQKKAIDLFYDG--KEFVILE-SPVLEKNNIGAGCTFASSIASQLVK 221
|
250
....*....|....*....
gi 6324517 256 GYSLPQSVYGGIEYVQNAV 274
Cdd:PRK12413 222 GKSPLEAVKNSKDFVYQAI 240
|
|
| PTZ00493 |
PTZ00493 |
phosphomethylpyrimidine kinase; Provisional |
21-217 |
1.72e-20 |
|
phosphomethylpyrimidine kinase; Provisional
Pssm-ID: 240440 Cd Length: 321 Bit Score: 92.36 E-value: 1.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 21 EKLPTVLSIAGTDPSGGAGIEADVKTITAHRCYAMTCITALNAQTPVKVYSINNTPKEVVFQTLESNLKDMKCNVIKTGM 100
Cdd:PTZ00493 2 EGVSNILSIAGSDSCGGAGMQADIKTAMGLGCHCCTALVVLTAQNTKEVKRIVEIEEKFIVEQLDSIFADVTIDVVKLGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 101 L-TAAAIEVLHEKLLQLGENRPK---LVVDPVLVATSGSSLAGK-DIVSLITEKVAPFADILTPNIPECYKLLgeeRKVN 175
Cdd:PTZ00493 82 LySKKIISLVHNYITNMNKKRGKkllVVFDPVFVSSSGCLLVENlEYIKFALDLICPISCIITPNFYECKVIL---EALD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6324517 176 GLQDIFQI-AKDLAK-ITKCSNI---LVKGGHIPWN--DEKEKYITDVL 217
Cdd:PTZ00493 159 CQMDLSKAnMTELCKlVTEKLNInacLFKSCNVGENsaEENEVYAVDHL 207
|
|
| TenA_C_SaTenA-like |
cd19360 |
TenA_C proteins similar to Staphylococcus aureus TenA (SaTenA); This family of TenA proteins ... |
333-546 |
6.32e-20 |
|
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: 88.41 E-value: 6.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 333 FYEYLINhpKVKPHWDSYINHEFVKKVADGTLERKKFQFFIEQDYAYLVDYARVHCIAGSKAPCLEDMEKELVIVGGV-R 411
Cdd:cd19360 1 FSEELRE--EAQPILEAIYAHPFVQGIAAGELPKEALIHYVQQDYEYLNAFLKVYALAIAKSDTREDMRFFLEQIGFIlN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 412 TEMGQHEKrLKEVFGVKDPDyFQKIKRGPALRAYSRYFNDVSRRGNWQELVASLTPCLMGYGEALTKMKGKVTAPEGSVY 491
Cdd:cd19360 79 GESHAHQN-LCEVAGVDYEE-LQGAPWAPTADHYIKHMYYAARTGDLGDILAALLPCPWTYVELAKRLIEEGKPTPDNPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6324517 492 HEWCETYASSWYREAMDEGEKLLNHILETYPPEQLDTLVTIYAEVCELETNFWTA 546
Cdd:cd19360 157 YEWIDFYADDEMDGLTDQLFARLDRLAEKASEEERERAKQAFLKSCQLEWRFWEM 211
|
|
| TenA_C_SsTenA-1-like |
cd19362 |
uncharacterized TenA_C proteins similar to Sulfolobus solfataricus TenA-1 (Sso2206); This ... |
343-548 |
7.11e-20 |
|
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: 87.88 E-value: 7.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 343 VKPHWDSYINHEFVKKVADGTLERKKFQFFIEQDYAYLVDYARVHCIAGSKAPcLEDMEKEL-VIVGGVRTEMGQHEKRL 421
Cdd:cd19362 8 VGDLWNKYVRHEFVERMRDGTLPLDNFRYYLIQDSKYVEEMLRALLRASSKAP-LDKAIKILnSVFSGRDKGMEVHKFLY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 422 KEVfGVKDpDYFQKIKRGPALRAYSRYFNDVSRRGnWQELVASLTPCLMGYGEAltkmkGK-VTAPEGSVYHEWCETYAS 500
Cdd:cd19362 87 SEL-GITE-DEIRRTGYNLVNYAYTRHLYYYSTLG-WPQFLAAWAPCMWGYSEI-----GKyVLNSPNELYKTWASFYAS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 6324517 501 SWYR-------EAMDEgekllnhiletypPEQLDTLVTIYAEVCELETNFWTAAL 548
Cdd:cd19362 159 KDYKkrveailEALDS-------------IEDTEDIKNIFRNSVNFEIMFWDAAL 200
|
|
| TenA_C_Bt3146-like |
cd19359 |
uncharacterized TenA_C proteins similar to Bacteroides thetaiotaomicron Bt3146; This family of ... |
334-546 |
7.53e-20 |
|
uncharacterized TenA_C proteins similar to Bacteroides thetaiotaomicron Bt3146; This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; only one of the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect. This family includes mostly uncharacterized TenA-like proteins such as Bacteroides thetaiotaomicron Bt3146.
Pssm-ID: 381694 [Multi-domain] Cd Length: 206 Bit Score: 87.79 E-value: 7.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 334 YEYLINHPKVKphWDSYINHEFVKKVADGTLERKKFQFFIEQDYAYLVDYARVHCIAGSKAP-------CLEDMEKELVI 406
Cdd:cd19359 1 IDKLWNDNEDL--WDKALNNPFCQGMADGTLDLDGFGYYMVQDYYYCINYVRFKALRAAKAPdpdllafLAAKIKSYLDY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 407 VGGVRTEMGQHEKRLKEVFGvkdpdyfqkIKRGPALRAYSRYFNDVSRRGNWQELVASLTPCLMGYGEALTKMKGKVTAP 486
Cdd:cd19359 79 AEDFLKTCHIKLGIPDVVDG---------VKPSPALKAYVDFERSVAESEDWFYLLVAMIPCIYLWYWLANQLNEDPSDK 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324517 487 EGSVYHEWCETYAsswyreAMDEGEKLLNHILETY---PPEQLDTLVTIYAEVCELETNFWTA 546
Cdd:cd19359 150 NTNFYKTWIEPNL------PDPSSAKQLEFFLNANaawSKIDREKANEIFRQAMQLEINFFNS 206
|
|
| TenA_C_AtTH2-like |
cd19368 |
TenA_C family similar to the N-terminal TenA_C domain of Arabidopsis thaliana thiamine ... |
351-546 |
1.95e-19 |
|
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: 86.91 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 351 INHEFVKKVADGTLERKKFQFFIEQDYAYLVDYARVHCIAGSKAPCLEDME--KELviVGGVRTEMGQHEKRLKEvFGVK 428
Cdd:cd19368 17 LYHPFVVGLAAGNLPLDSFRHYISQDAHFLEAFARAYELAEAKADDDEDKKaiREL--RKGVLEELKLHDSYAEE-WGVD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 429 DPDYFQKIkrgPALRAYSRYFNDVSRRGNWQ--ELVASLTPCLMGYGEALTKMKGKVTAPEGSVYHEWCETYASSWYREA 506
Cdd:cd19368 94 LPKEVTPD---PATRKYTDFLLATASGKVKVaaYTLAAMAPCMRLYAFLGQELARALDDTEDHPYKKWIDTYSSQEFEAL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6324517 507 MDEGEKLLNHILETYPPEQLDTLVTIYAEVCELETNFWTA 546
Cdd:cd19368 171 ALQLEDLLDKLSASLTGEELEALEKLYRRAMKLEVEFFAA 210
|
|
| TenA_E_Spr0628-like |
cd19358 |
TenA_E proteins similar to Streptococcus pneumoniae Spr0628 and Saccharomyces cerevisiae S288C ... |
333-548 |
7.14e-18 |
|
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: 82.23 E-value: 7.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 333 FYEYLINhpKVKPHWDSYINHEFVKKVADGTLERKKFQFFIEQDYAYLVDYARVHCIAGSKAPcleDMEKELVIVGG--- 409
Cdd:cd19358 1 FSDRLRA--ANAEDWDAAVTHRFVRELCAGTLPDAVLARYLVQDYQFVETFLRLLGKAVAKAP---DLEAKLRLARFlgf 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 410 -VRTEMGQHEKRLKEvFGVKDPDYFqKIKRGPALRAYSRYFNDVSRRGNWQELVASLTPClmgygealtkmkgkvtapEG 488
Cdd:cd19358 76 lANDENDYFERAFAA-LGVSEADRE-APPLLPATRAFIDLMLEAARSGSYAEILTVLLVA------------------EW 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6324517 489 sVYHEWCETYASS-----WYRE--AMDEGEKL------LNHILETYPP--EQLDTLVTIYAEVCELETNFWTAAL 548
Cdd:cd19358 136 -LYLDWASRAAAAaplrfKHQEwiDLHSGPEFeawvdfLRDEVDRVGPteEERERLEAVFARAVELEIAFFDAAY 209
|
|
| COG1992 |
COG1992 |
Predicted transcriptional regulator fused phosphomethylpyrimidine kinase (thiamin biosynthesis) ... |
35-303 |
2.67e-15 |
|
Predicted transcriptional regulator fused phosphomethylpyrimidine kinase (thiamin biosynthesis) [General function prediction only];
Pssm-ID: 441595 [Multi-domain] Cd Length: 432 Bit Score: 78.26 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 35 SGGAGIEADVKTITAHRCYAMTCITALNAQTPVKVYSINNTPKEVVFQTLESNLKDMKCNVIKTGMLTAAAIEVlhEKLL 114
Cdd:COG1992 1 GGGGGGGADAKTAAALGAGGGGTTTAVTVTATTTVTGVGSDPPPPVEVQQQAVAADDDVDDAKTGMLMTATIVE--VVAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 115 QLGENRPKLVVDPVLVATSGSSLAGKDIVSLITEKVAPFADILTPNIPECYKLLGEERKVngLQDIFQIAKDLAKITKCS 194
Cdd:COG1992 79 VVKSRDKPLVVVVVPVAVAAAGLGLLLAEAELAKLLLPLLATVTPNEPEVEELLLPTIRS--LLAEARAARLALQEEGAD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 195 NILVKGGHIpwndekeKYITDVLFLGAEQKFIIFKGNFVNTTHTHGTGCTLASAIASNLARGYSLPQSVYGGIEYVQNAV 274
Cdd:COG1992 157 ALGVKGGHV-------SGDAVVDVLEDERDVETFRHPRLVTEATHGSGCTFSAAIAALLAKGLSLEEAVRGAKLFLLHAI 229
|
250 260
....*....|....*....|....*....
gi 6324517 275 AIGCDVtketVKDNGPINHVYAVEIPLEK 303
Cdd:COG1992 230 RYGLLV----GKGVGPVNHLADLRLEAER 254
|
|
| TenA_E_At3g16990-like |
cd19357 |
TenA_E proteins similar to Arabidopsis thaliana At3g16990; This family of TenA proteins ... |
346-544 |
2.34e-10 |
|
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: 60.41 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 346 HWDSY---INHEFVKKVADGTLERKKFQFFIEQDYAYLVDYARvhCIAG--SKAPCLE-DMEKEL--VIVGG---VRTEM 414
Cdd:cd19357 8 HPALYtaaTQHPFLRAAADGTLPKEALSRWLAQDRLYVQAYIR--FLGSllARAPLPSsSLNQRLldVLLGAlanLRREL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 415 GQHEKRLKEVFGVKDPDYFQKikrGPALRAYSRYFNDVSRRGnwqelvasltpclMGYGEALT----------------K 478
Cdd:cd19357 86 AFFEETAAEYGLDLPGLGVPP---SPATRAYVDFLASLASEG-------------VSYLEGLVvlwatekvyldawsyaR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6324517 479 MKGKVTAPEGSVYHEWCETYASSWYREAMDEGEKLLNHILETYPPEQLDTLVTIYAEVCELETNFW 544
Cdd:cd19357 150 SFLPSDADGGALYREFIPNWTSPEFAAFVDRLGDLVDEALEQAGEEVLERAEEVWRRVLELEEAFW 215
|
|
| PTZ00347 |
PTZ00347 |
phosphomethylpyrimidine kinase; Provisional |
351-547 |
3.11e-10 |
|
phosphomethylpyrimidine kinase; Provisional
Pssm-ID: 240375 [Multi-domain] Cd Length: 504 Bit Score: 62.67 E-value: 3.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 351 INHEFVKKVADGTLERKKFQFFIEQDYAYLVDYARVHCIAGSKAPCLEDMEKELVIVGGVRTEMGQHEKRLkevfgVKDP 430
Cdd:PTZ00347 29 LHLPFVQGLGDGTLDQNAFRTYIAQDTLYLNGYIRILSYCITKSDVTATGGGLLELLKGVLEELKNCHHHY-----IDNP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 431 DyfqKIKRGPALRAYSRYFNDVSRRGNWQELV--ASLTPCLMGYGEALTKMKGKVTAPEGSVYHEWCETYASswyrEAMD 508
Cdd:PTZ00347 104 D---AAGPEAACRKYVDFLLASGNADTLGPSVviAAVIPCARLYAWVGQELTNEVELTESHPFRRWLLSYSD----EPIN 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 6324517 509 EGEKLLNHILETY-PPEQLDTLVTIYAEVCELETNFWTAA 547
Cdd:PTZ00347 177 TSVEQLESLLDKYiRPGEFSEVAQAYRRAMELEYDFFDSF 216
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
78-263 |
8.88e-10 |
|
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: 59.52 E-value: 8.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 78 EVVFQTLESNLKDMKCNVIKTGML-TAAAIEVLHEKLLQLGENRPKL--VVDPVLvATSGSSL-AGKDIVSLITEKVAPF 153
Cdd:cd01173 58 EDLLEGLEALGLLLEYDAVLTGYLgSAEQVEAVAEIVKRLKEKNPNLlyVCDPVM-GDNGKLYvVAEEIVPVYRDLLVPL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 154 ADILTPNIPECYKLLGeeRKVNGLQDIFQIAKDLAKiTKCSNILVKGGHIPWNDEKEKYITDvlflgAEQKFIIFKGNFV 233
Cdd:cd01173 137 ADIITPNQFELELLTG--KKINDLEDAKAAARALHA-KGPKTVVVTSVELADDDRIEMLGST-----ATEAWLVQRPKIP 208
|
170 180 190
....*....|....*....|....*....|
gi 6324517 234 NTTHTHGTGCTLASAIASNLARGYSLPQSV 263
Cdd:cd01173 209 FPAYFNGTGDLFAALLLARLLKGKSLAEAL 238
|
|
| PqqC |
COG5424 |
Pyrroloquinoline quinone (PQQ) biosynthesis protein C [Coenzyme transport and metabolism]; |
332-546 |
2.49e-09 |
|
Pyrroloquinoline quinone (PQQ) biosynthesis protein C [Coenzyme transport and metabolism];
Pssm-ID: 444176 Cd Length: 228 Bit Score: 57.60 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 332 NFYEYLINHPKVKPHWdsyiNHEFVKKVADGTLERKKFQFFIEQDYAYlvdyarVHCIAGSKAPCL---EDMEKELVIVG 408
Cdd:COG5424 6 EFEARLRAEIARRYLL----KHPFLQRLREGKLTREQLRAFALQRYHY------VKHFPRYLAAILsrcPDEELRRALLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 409 GVRTEMGQ-----HEK---RLKEVFGVkDPDYFQKIKRGPALRAYSRYFNDVSRRGNWQELVASL------TPCLMGY-G 473
Cdd:COG5424 76 NLYEEDGEgpeegHIElwlRFAEALGL-DREEVDARPPLPETRAAVDAYVNFCRRRSLLEAVAASltaegfAPEISRErL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6324517 474 EALTKMKGkVTAPEGSVYHEWCETYAsswyREAMDEGEKLLNHILETypPEQLDTLVTIYAEVCELETNFWTA 546
Cdd:COG5424 155 EGLLEHYG-LPDEEALEYFRLHAELD----PRHAEEALELVLRLADT--PEDQEAALEAARFKLDLLWAFLDA 220
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
92-303 |
1.42e-08 |
|
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: 55.92 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 92 KCNVIKTGMLTAAA-IEVLHEKLLQLGENRPKL--VVDPVLvATSGSSLAGKD-IVSLITEKVAPFADILTPNIPECYKL 167
Cdd:COG2240 74 EFDAVLSGYLGSAEqGDIIADFVARVKAANPDAlyLCDPVM-GDNGKGYYVFPgIAEFIMRRLVPLADIITPNLTELALL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 168 LGEErkVNGLQDIFQIAKDLAKITKcSNILVKGghIPWNDEKEKYItDVLFLGAEQKFII--------FKGN---Fvntt 236
Cdd:COG2240 153 TGRP--YETLEEALAAARALLALGP-KIVVVTS--VPLDDTPADKI-GNLAVTADGAWLVetpllpfsPNGTgdlF---- 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6324517 237 hthgtgctlASAIASNLARGYSLPQSvyggieyVQNAVAIGCDVTKETVKDNGPinhvyavEIPLEK 303
Cdd:COG2240 223 ---------AALLLAHLLRGKSLEEA-------LERAAAFVYEVLERTAAAGSD-------ELLLEA 266
|
|
| pyridox_kin |
TIGR00687 |
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal ... |
92-187 |
7.55e-03 |
|
pyridoxal kinase; E. coli has an enzyme PdxK that acts in vitro as a pyridoxine/pyridoxal/pyridoxamine kinase, but mutants lacking PdxK activity retain a specific pyridoxal kinase, PdxY. PdxY acts in the salvage pathway of pyridoxal 5'-phosphate biosynthesis. Mammalian forms of pyridoxal kinase are more similar to PdxY than to PdxK. The PdxK isozyme is omitted from the seed alignment but scores above the trusted cutoff.ThiD and related proteins form an outgroup. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridoxine]
Pssm-ID: 273221 [Multi-domain] Cd Length: 287 Bit Score: 38.66 E-value: 7.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6324517 92 KCNVIKTGML-TAAAIEVLHEKLLQLGENRPKLV--VDPVLVATSGSSLAGKDIVSLITEKVAPFADILTPNIPECYKLL 168
Cdd:TIGR00687 74 QCDAVLSGYLgSAEQVAMVVGIVRQVKQANPQALyvCDPVMGDPWKGCYVAPDLLEVYREKAIPVADIITPNQFELELLT 153
|
90
....*....|....*....
gi 6324517 169 GeeRKVNGLQDIFQIAKDL 187
Cdd:TIGR00687 154 G--RRINTEEEALAAADAL 170
|
|
| |
