|
Name |
Accession |
Description |
Interval |
E-value |
| MltB |
COG2951 |
Membrane-bound lytic murein transglycosylase B [Cell wall/membrane/envelope biogenesis]; |
20-325 |
2.65e-148 |
|
Membrane-bound lytic murein transglycosylase B [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442193 [Multi-domain] Cd Length: 326 Bit Score: 434.98 E-value: 2.65e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 20 CADPAFDRCLAGLQSQAAAKGVDAASFQRFTAGLVPDPSVLPLLDAQPEFTTPIWDYLASLVDSQRVTDGQAMLVTHREL 99
Cdd:COG2951 23 AAAADFAAWVAAFRQEAAAAGISRATLDAALAGATPDPRVIELDRRQPEFTKPWWDYLARFVSPARIARGRAFLRQHAAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 100 LSRLSEQTGVDPATIVAVWGVESDYGRVTGKRPLLVSLATLSCAGRRQPFFRGEFLALLSLLQQGDLSADGLTGSWAGAF 179
Cdd:COG2951 103 LARIEQRYGVPAEIIVAIWGVETNYGRYMGNFPVLDALATLAFDGRRAEFFRGELIAALKILQRGDIDPDQMKGSWAGAM 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 180 GQTQFMPSTYARIAVDGDGDGRRDLVASIPDALASTANYLVKAGWERARPWGMEVTLPRGFDASKAGRTRRQPLQAWQTA 259
Cdd:COG2951 183 GQTQFMPSSYLRYAVDFDGDGRRDLWNSPPDALASTANYLKKHGWQRGQPWGYEVRLPAGFDYALAGLKPRRTLAEWAAL 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1379540447 260 GLLGTDGKPlaptgLPAETPAALLLPAGATGPAFLVFRNYDAIYAYNAAESYALSIALLADRLRGG 325
Cdd:COG2951 263 GVRPADGRP-----LPADGPASLLLPAGANGPAFLVTPNFYVITRYNRSDLYALAVGHLADRIAGA 323
|
|
| MltB_2 |
TIGR02283 |
lytic murein transglycosylase; Members of this family are closely related to the MltB family ... |
24-324 |
2.15e-146 |
|
lytic murein transglycosylase; Members of this family are closely related to the MltB family lytic murein transglycosylases described by TIGR02282 and are likewise all proteobacterial, although that family and this one form clearly distinct clades. Several species have one member of each family. Many members of this family (unlike the MltB family) contain an additional C-terminal domain, a putative peptidoglycan binding domain (pfam01471), not included in region described by this model. Many sequences appear to contain N-terminal lipoprotein attachment sites, as does E. coli MltB in TIGR02282. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 274067 [Multi-domain] Cd Length: 300 Bit Score: 429.10 E-value: 2.15e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 24 AFDRCLAGLQSQAAAKGVDAASFQRFTAGLV-PDPSVLPLLDAQPEFTTPIWDYLASLVDSQRVTDGQAMLVTHRELLSR 102
Cdd:TIGR02283 1 GFDAWLAQLRAEAAAKGISAATFDRAFAGIKePDQSVLNLDRNQPEFTQTFWDYLSRRVSPRRIAIGRAMLQRYAALLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 103 LSEQTGVDPATIVAVWGVESDYGRVTGKRPLLVSLATLSCAGRRQPFFRGEFLALLSLLQQGDLSADGLTGSWAGAFGQT 182
Cdd:TIGR02283 81 IEKRYGVPAEILLAIWGMESDFGAYQGKFDVIRSLATLAYDGRRKDYFRTELIAALKILQRGDLTRAAMKGSWAGAMGQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 183 QFMPSTYARIAVDGDGDGRRDLVASIPDALASTANYLVKAGWERARPWGMEVTLPRGFDASKAGRTRRQPLQAWQTAGLL 262
Cdd:TIGR02283 161 QFLPSSYLNYAVDFDGDGRRDIWNSVPDALASTANYLVNGGWKRGEPWGYEVQLPAGFDYALSGSQIKKPIAEWQRLGVT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1379540447 263 GTDGKPLapTGLPAETPAALLLPAGATGPAFLVFRNYDAIYAYNAAESYALSIALLADRLRG 324
Cdd:TIGR02283 241 RVDGRPL--PASAANAEASLLLPDGRKGPAFLVTPNFRVIKEWNRSDYYALTIGLLADRIAG 300
|
|
| SLT_2 |
pfam13406 |
Transglycosylase SLT domain; This family is related to the SLT domain pfam01464. |
24-320 |
7.21e-134 |
|
Transglycosylase SLT domain; This family is related to the SLT domain pfam01464.
Pssm-ID: 404311 [Multi-domain] Cd Length: 292 Bit Score: 396.54 E-value: 7.21e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 24 AFDRCLAGLQSQAAAKGVDAASFQRFTAGLVPDPSVLPLLDAQPEFTTPIWDYLASLVDSQRVTDGQAMLVTHRELLSRL 103
Cdd:pfam13406 1 GFDAWVAAFRQEAAAAGISRATLDAAFAGVEPDPRVIELDRRQPEFTKPWWDYLSRFVTPARIARGRAFLQEHAALLARI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 104 SEQTGVDPATIVAVWGVESDYGRVTGKRPLLVSLATLSCAGRRQPFFRGEFLALLSLLQQGDLSADGLTGSWAGAFGQTQ 183
Cdd:pfam13406 81 EKRYGVPPEIIVAIWGVETNYGRYMGNFPVLDALATLAFDGRRSEFFRKELIAALKILDRGDLDPEQLKGSWAGAMGQTQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 184 FMPSTYARIAVDGDGDGRRDLVASIPDALASTANYLVKAGWERARPWGMEVTLPRGFDASKAGRTRRQPLQAWQTAGLLG 263
Cdd:pfam13406 161 FMPSSYLAYAVDFDGDGRRDLWNSPPDALASVANYLKQHGWQPGEPWGREVRLPAGFDYSLAGLGTRKPLAEWAALGVRP 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1379540447 264 TDGKPLAPTGlpaetPAALLLPAGATGPAFLVFRNYDAIYAYNAAESYALSIALLAD 320
Cdd:pfam13406 241 ADGGPPLADA-----EASLLLPAGANGPAFLVYDNFYVITRYNRSDLYALAVGHLAD 292
|
|
| YeaD |
COG0676 |
D-hexose-6-phosphate mutarotase [Carbohydrate transport and metabolism]; |
439-720 |
3.15e-113 |
|
D-hexose-6-phosphate mutarotase [Carbohydrate transport and metabolism];
Pssm-ID: 440440 Cd Length: 296 Bit Score: 343.77 E-value: 3.15e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 439 TGLTTGDFHGFPSLLIDTPFSTAAISLFGGQLVSFVPKGGQDVMWLSP-SAQQPPTPIRGGAPVCWPYFGRQDQTGDVPA 517
Cdd:COG0676 13 PSVSLRGPGGLPVLRIDNPGARATIALQGAHVLSWQPAGEEPVLWLSPaAAFEPGKAIRGGVPVCWPWFGPHPSDPGLPA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 518 HGFVRTVAWQLTESRrEDDGTVVLTLTPPRLDDL------ALRLRMTLRIGRTLEQRLITENISGASVRFTQALHNYFHV 591
Cdd:COG0676 93 HGFARTRPWQLTEHR-EDDGGVILTLTLTDSEATralwphAFELELTVTLGETLTLELTTTNTGDQPFSFTQALHTYFAV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 592 GDALNVSVQGLDGLDYLDKYENYATAhRQQGDWSLrdprdPGRSDRIYTNAGGRYTLTDPVLGRRIVIATEGSRSLVVWN 671
Cdd:COG0676 172 GDIEQVRVSGLEGARYIDKLDGGAEK-QQEGPLTF-----TGETDRVYLDPPAPLTIHDPGLKRRIRIAKSGSSSVVVWN 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1379540447 672 PGEEAGKKMADVG-DGWRDYVCLEAANAGPDVIELAPGASHTLSQTISVE 720
Cdd:COG0676 246 PWAEKAASMADMPdDGYRTMVCVETANALDDAVTLAPGESHTLSQTISVE 295
|
|
| D-hex-6-P-epi_like |
cd09020 |
D-hexose-6-phosphate epimerase-like; D-Hexose-6-phosphate epimerase Ymr099c from Saccharomyces ... |
452-718 |
5.73e-109 |
|
D-hexose-6-phosphate epimerase-like; D-Hexose-6-phosphate epimerase Ymr099c from Saccharomyces cerevisiae belongs to the large superfamily of aldose-1-epimerases. Its active site is very similar to the catalytic site of galactose mutarotase, the best studied member of the superfamily. It also contains the conserved glutamate and histidine residues that have been shown in galactose mutarotase to be critical for catalysis, the glutamate serving as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen. In addition Ymr099c contains 2 conserved arginine residues which are involved in phosphate binding, and exhibits hexose-6-phosphate mutarotase activity on glucose-6-P, galactose-6-P and mannose-6-P.
Pssm-ID: 185697 Cd Length: 269 Bit Score: 331.50 E-value: 5.73e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 452 LLIDTPFSTAAISLFGGQLVSFVPKGGQDVMWLSPSAQ-QPPTPIRGGAPVCWPYFGRQDQTGDVPAHGFVRTVAWQLTE 530
Cdd:cd09020 2 IVLDHPGASAEIALQGAQVLSWKPKGGQDLLWLSPQAPfDGGKAIRGGIPVCWPWFGPHGPNADLPAHGFARTRLWELLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 531 SRREDDGT-VVLTLTPPRLD------DLALRLRMTLRiGRTLEQRLITENISGASVRFTQALHNYFHVGDALNVSVQGLD 603
Cdd:cd09020 82 VSEDEDGVtVSLELDDTDETraiwphAFELRLTVTLG-FDTLELELTVTNTGDKPFSFTAALHTYFRVSDIEQVRVEGLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 604 GLDYLDKYENYATahRQQGDwslrDPRDPGRSDRIYTNAGGRYTLTDPVLGRRIVIATEGSRSLVVWNPGEEAGKKMADV 683
Cdd:cd09020 161 GATYLDKLTDQRE--KVQGG----AVTFDGEVDRVYLNTPAPLTIDDPAWGRRIRIEKSGSPSAVVWNPWIEKAARMADF 234
|
250 260 270
....*....|....*....|....*....|....*.
gi 1379540447 684 G-DGWRDYVCLEAANAGpDVIELAPGASHTLSQTIS 718
Cdd:cd09020 235 PdDGYRRMVCVEAANVA-DPVTLAPGESHTLSQTIS 269
|
|
| Aldose_epim |
pfam01263 |
Aldose 1-epimerase; |
453-718 |
4.87e-39 |
|
Aldose 1-epimerase;
Pssm-ID: 396013 Cd Length: 300 Bit Score: 146.39 E-value: 4.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 453 LIDTPFSTAAISLFGGQLVSFVPKGG-QDVMWLSPS------------AQQPPTPIRG--------GAPVCWPYFGRqdq 511
Cdd:pfam01263 5 LTNGNGLSATISLYGATLLSLKVPGKlREVLLGSDDaegylkdsnyfgATLGPYANRIangrfeldGIPYCLPQNGP--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 512 tGDVPAHGFVRTVAWQLTESRREDDGTVVLTLTPPRLDDL--ALRLRMTLRIGRTLEQRLITENIS-GASVRFTQALHNY 588
Cdd:pfam01263 82 -GKNPLHGGARGRIWEVEEVKPDDGVTVTLVLDPDGEEGYpgDLEARVTYTLNEDNELTIEYEATNdGKPTPFNLGNHPY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 589 FHVGDALN---VSVQGLDGLDYLDKY-ENYATAHRQQGDWSLRDPR----DPGRSDRIYTNAGGRYTLTDPVLGRRIVIA 660
Cdd:pfam01263 161 FNLSGDIDiheLQIEADEYLEVDDDLiPTGELKDVKGTPFDFRQPTpigeDILGYDHVYLLDPLKAVIIDPDPGSGIVLE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 661 TEGSR-SLVVWNPGEEAGKKMADVGD-GWRDYVCLEAANAGPDVIELAPGASHTLSQTIS 718
Cdd:pfam01263 241 VSTTQpGLVVYTPNFLKGKYLSDEGFaLETQFLPDEPNHPEFPSIILKPGESYTAETSYS 300
|
|
| PRK10760 |
PRK10760 |
murein hydrolase B; Provisional |
58-325 |
1.74e-29 |
|
murein hydrolase B; Provisional
Pssm-ID: 236754 [Multi-domain] Cd Length: 359 Bit Score: 120.61 E-value: 1.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 58 SVLPLLDAQPEFTTP------IWD-YLASLVDSQRVTDGQAMLVTHRELLSRLSEQTGVDPATIVAVWGVESDYGRVTGK 130
Cdd:PRK10760 90 WVLRLMDRQAPTTRPpsgpngAWLrYRKKFITPDNVQNGVVFWNQYEDALNRAWQVYGVPPEIIVGIIGVETRWGRVMGK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 131 RPLLVSLATLSCA-GRRQPFFRGEFLALLSLLQQGDLSADGLTGSWAGAFGQTQFMPSTYARIAVDGDGDGRRDLVASIp 209
Cdd:PRK10760 170 TRILDALATLSFNyPRRAEYFSGELETFLLMARDEGDDPLNLRGSFAGAMGYGQFMPSSFKQYAVDFNGDGHINLWDPV- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 210 DALASTANYLVKAGWERARPW-----GMEVTLPRGFDAskagrtrRQPLQAWQTAGllgtdgkpLAPTG-LPAETPAALL 283
Cdd:PRK10760 249 DAIGSVANYFKAHGWVKGDQVavpanGQAPGLENGFKT-------RYSVSQLAAAG--------LTPQQpLGNHQQASLL 313
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1379540447 284 -LPAGATGPAFLVFRNYDAIYAYNAAESYALSIALLAD---RLRGG 325
Cdd:PRK10760 314 rLDVGTGYQYWYGLPNFYTITRYNHSTHYAMAVWQLGQavaLARVG 359
|
|
| Slt35-like |
cd13399 |
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ... |
108-228 |
1.17e-19 |
|
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic transglycosylase Slt35 and Pseudomonas aeruginosa Sltb1. Lytic transglycosylase (LT) catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc) as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).
Pssm-ID: 381602 [Multi-domain] Cd Length: 108 Bit Score: 84.67 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 108 GVDPATIVAVWGVESDYGRVTGkrpllvslatlscagrrqpffrgeflallsllqqgdlsadgltGSWAGAFGQTQFMPS 187
Cdd:cd13399 2 GVPPGILAAILGVESGFGPNAG-------------------------------------------GSPAGAQGIAQFMPS 38
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1379540447 188 TYARIAVDGDGDGRRDLvASIPDALASTANYLVKAGWERAR 228
Cdd:cd13399 39 TWKAYGVDGNGDGKADP-FNPEDAIASAANYLCRHGWDLNA 78
|
|
| PGRP |
COG3409 |
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ... |
330-398 |
3.51e-11 |
|
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442635 [Multi-domain] Cd Length: 69 Bit Score: 59.15 E-value: 3.51e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1379540447 330 AAWPTDEPGLGRPERRELQQLLLARGHQIGEADGMVGSATRRAIQVEQTRLGLqPADGRPGQRILTALR 398
Cdd:COG3409 1 ASAPTLRLGDSGEDVRELQQRLNALGYYPGPVDGIFGPATEAAVRAFQRANGL-PVDGIVGPATWAALR 68
|
|
| PG_binding_1 |
pfam01471 |
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ... |
341-397 |
1.48e-08 |
|
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.
Pssm-ID: 460223 [Multi-domain] Cd Length: 57 Bit Score: 51.36 E-value: 1.48e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1379540447 341 RPERRELQQLLLARGHQIGEADGMVGSATRRAIQVEQTRLGLqPADGRPGQRILTAL 397
Cdd:pfam01471 2 GEDVKELQRYLNRLGYYPGPVDGYFGPSTEAAVKAFQRAFGL-PVDGIVDPETLAAL 57
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MltB |
COG2951 |
Membrane-bound lytic murein transglycosylase B [Cell wall/membrane/envelope biogenesis]; |
20-325 |
2.65e-148 |
|
Membrane-bound lytic murein transglycosylase B [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442193 [Multi-domain] Cd Length: 326 Bit Score: 434.98 E-value: 2.65e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 20 CADPAFDRCLAGLQSQAAAKGVDAASFQRFTAGLVPDPSVLPLLDAQPEFTTPIWDYLASLVDSQRVTDGQAMLVTHREL 99
Cdd:COG2951 23 AAAADFAAWVAAFRQEAAAAGISRATLDAALAGATPDPRVIELDRRQPEFTKPWWDYLARFVSPARIARGRAFLRQHAAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 100 LSRLSEQTGVDPATIVAVWGVESDYGRVTGKRPLLVSLATLSCAGRRQPFFRGEFLALLSLLQQGDLSADGLTGSWAGAF 179
Cdd:COG2951 103 LARIEQRYGVPAEIIVAIWGVETNYGRYMGNFPVLDALATLAFDGRRAEFFRGELIAALKILQRGDIDPDQMKGSWAGAM 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 180 GQTQFMPSTYARIAVDGDGDGRRDLVASIPDALASTANYLVKAGWERARPWGMEVTLPRGFDASKAGRTRRQPLQAWQTA 259
Cdd:COG2951 183 GQTQFMPSSYLRYAVDFDGDGRRDLWNSPPDALASTANYLKKHGWQRGQPWGYEVRLPAGFDYALAGLKPRRTLAEWAAL 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1379540447 260 GLLGTDGKPlaptgLPAETPAALLLPAGATGPAFLVFRNYDAIYAYNAAESYALSIALLADRLRGG 325
Cdd:COG2951 263 GVRPADGRP-----LPADGPASLLLPAGANGPAFLVTPNFYVITRYNRSDLYALAVGHLADRIAGA 323
|
|
| MltB_2 |
TIGR02283 |
lytic murein transglycosylase; Members of this family are closely related to the MltB family ... |
24-324 |
2.15e-146 |
|
lytic murein transglycosylase; Members of this family are closely related to the MltB family lytic murein transglycosylases described by TIGR02282 and are likewise all proteobacterial, although that family and this one form clearly distinct clades. Several species have one member of each family. Many members of this family (unlike the MltB family) contain an additional C-terminal domain, a putative peptidoglycan binding domain (pfam01471), not included in region described by this model. Many sequences appear to contain N-terminal lipoprotein attachment sites, as does E. coli MltB in TIGR02282. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 274067 [Multi-domain] Cd Length: 300 Bit Score: 429.10 E-value: 2.15e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 24 AFDRCLAGLQSQAAAKGVDAASFQRFTAGLV-PDPSVLPLLDAQPEFTTPIWDYLASLVDSQRVTDGQAMLVTHRELLSR 102
Cdd:TIGR02283 1 GFDAWLAQLRAEAAAKGISAATFDRAFAGIKePDQSVLNLDRNQPEFTQTFWDYLSRRVSPRRIAIGRAMLQRYAALLAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 103 LSEQTGVDPATIVAVWGVESDYGRVTGKRPLLVSLATLSCAGRRQPFFRGEFLALLSLLQQGDLSADGLTGSWAGAFGQT 182
Cdd:TIGR02283 81 IEKRYGVPAEILLAIWGMESDFGAYQGKFDVIRSLATLAYDGRRKDYFRTELIAALKILQRGDLTRAAMKGSWAGAMGQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 183 QFMPSTYARIAVDGDGDGRRDLVASIPDALASTANYLVKAGWERARPWGMEVTLPRGFDASKAGRTRRQPLQAWQTAGLL 262
Cdd:TIGR02283 161 QFLPSSYLNYAVDFDGDGRRDIWNSVPDALASTANYLVNGGWKRGEPWGYEVQLPAGFDYALSGSQIKKPIAEWQRLGVT 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1379540447 263 GTDGKPLapTGLPAETPAALLLPAGATGPAFLVFRNYDAIYAYNAAESYALSIALLADRLRG 324
Cdd:TIGR02283 241 RVDGRPL--PASAANAEASLLLPDGRKGPAFLVTPNFRVIKEWNRSDYYALTIGLLADRIAG 300
|
|
| SLT_2 |
pfam13406 |
Transglycosylase SLT domain; This family is related to the SLT domain pfam01464. |
24-320 |
7.21e-134 |
|
Transglycosylase SLT domain; This family is related to the SLT domain pfam01464.
Pssm-ID: 404311 [Multi-domain] Cd Length: 292 Bit Score: 396.54 E-value: 7.21e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 24 AFDRCLAGLQSQAAAKGVDAASFQRFTAGLVPDPSVLPLLDAQPEFTTPIWDYLASLVDSQRVTDGQAMLVTHRELLSRL 103
Cdd:pfam13406 1 GFDAWVAAFRQEAAAAGISRATLDAAFAGVEPDPRVIELDRRQPEFTKPWWDYLSRFVTPARIARGRAFLQEHAALLARI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 104 SEQTGVDPATIVAVWGVESDYGRVTGKRPLLVSLATLSCAGRRQPFFRGEFLALLSLLQQGDLSADGLTGSWAGAFGQTQ 183
Cdd:pfam13406 81 EKRYGVPPEIIVAIWGVETNYGRYMGNFPVLDALATLAFDGRRSEFFRKELIAALKILDRGDLDPEQLKGSWAGAMGQTQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 184 FMPSTYARIAVDGDGDGRRDLVASIPDALASTANYLVKAGWERARPWGMEVTLPRGFDASKAGRTRRQPLQAWQTAGLLG 263
Cdd:pfam13406 161 FMPSSYLAYAVDFDGDGRRDLWNSPPDALASVANYLKQHGWQPGEPWGREVRLPAGFDYSLAGLGTRKPLAEWAALGVRP 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1379540447 264 TDGKPLAPTGlpaetPAALLLPAGATGPAFLVFRNYDAIYAYNAAESYALSIALLAD 320
Cdd:pfam13406 241 ADGGPPLADA-----EASLLLPAGANGPAFLVYDNFYVITRYNRSDLYALAVGHLAD 292
|
|
| YeaD |
COG0676 |
D-hexose-6-phosphate mutarotase [Carbohydrate transport and metabolism]; |
439-720 |
3.15e-113 |
|
D-hexose-6-phosphate mutarotase [Carbohydrate transport and metabolism];
Pssm-ID: 440440 Cd Length: 296 Bit Score: 343.77 E-value: 3.15e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 439 TGLTTGDFHGFPSLLIDTPFSTAAISLFGGQLVSFVPKGGQDVMWLSP-SAQQPPTPIRGGAPVCWPYFGRQDQTGDVPA 517
Cdd:COG0676 13 PSVSLRGPGGLPVLRIDNPGARATIALQGAHVLSWQPAGEEPVLWLSPaAAFEPGKAIRGGVPVCWPWFGPHPSDPGLPA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 518 HGFVRTVAWQLTESRrEDDGTVVLTLTPPRLDDL------ALRLRMTLRIGRTLEQRLITENISGASVRFTQALHNYFHV 591
Cdd:COG0676 93 HGFARTRPWQLTEHR-EDDGGVILTLTLTDSEATralwphAFELELTVTLGETLTLELTTTNTGDQPFSFTQALHTYFAV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 592 GDALNVSVQGLDGLDYLDKYENYATAhRQQGDWSLrdprdPGRSDRIYTNAGGRYTLTDPVLGRRIVIATEGSRSLVVWN 671
Cdd:COG0676 172 GDIEQVRVSGLEGARYIDKLDGGAEK-QQEGPLTF-----TGETDRVYLDPPAPLTIHDPGLKRRIRIAKSGSSSVVVWN 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1379540447 672 PGEEAGKKMADVG-DGWRDYVCLEAANAGPDVIELAPGASHTLSQTISVE 720
Cdd:COG0676 246 PWAEKAASMADMPdDGYRTMVCVETANALDDAVTLAPGESHTLSQTISVE 295
|
|
| D-hex-6-P-epi_like |
cd09020 |
D-hexose-6-phosphate epimerase-like; D-Hexose-6-phosphate epimerase Ymr099c from Saccharomyces ... |
452-718 |
5.73e-109 |
|
D-hexose-6-phosphate epimerase-like; D-Hexose-6-phosphate epimerase Ymr099c from Saccharomyces cerevisiae belongs to the large superfamily of aldose-1-epimerases. Its active site is very similar to the catalytic site of galactose mutarotase, the best studied member of the superfamily. It also contains the conserved glutamate and histidine residues that have been shown in galactose mutarotase to be critical for catalysis, the glutamate serving as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen. In addition Ymr099c contains 2 conserved arginine residues which are involved in phosphate binding, and exhibits hexose-6-phosphate mutarotase activity on glucose-6-P, galactose-6-P and mannose-6-P.
Pssm-ID: 185697 Cd Length: 269 Bit Score: 331.50 E-value: 5.73e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 452 LLIDTPFSTAAISLFGGQLVSFVPKGGQDVMWLSPSAQ-QPPTPIRGGAPVCWPYFGRQDQTGDVPAHGFVRTVAWQLTE 530
Cdd:cd09020 2 IVLDHPGASAEIALQGAQVLSWKPKGGQDLLWLSPQAPfDGGKAIRGGIPVCWPWFGPHGPNADLPAHGFARTRLWELLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 531 SRREDDGT-VVLTLTPPRLD------DLALRLRMTLRiGRTLEQRLITENISGASVRFTQALHNYFHVGDALNVSVQGLD 603
Cdd:cd09020 82 VSEDEDGVtVSLELDDTDETraiwphAFELRLTVTLG-FDTLELELTVTNTGDKPFSFTAALHTYFRVSDIEQVRVEGLE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 604 GLDYLDKYENYATahRQQGDwslrDPRDPGRSDRIYTNAGGRYTLTDPVLGRRIVIATEGSRSLVVWNPGEEAGKKMADV 683
Cdd:cd09020 161 GATYLDKLTDQRE--KVQGG----AVTFDGEVDRVYLNTPAPLTIDDPAWGRRIRIEKSGSPSAVVWNPWIEKAARMADF 234
|
250 260 270
....*....|....*....|....*....|....*.
gi 1379540447 684 G-DGWRDYVCLEAANAGpDVIELAPGASHTLSQTIS 718
Cdd:cd09020 235 PdDGYRRMVCVEAANVA-DPVTLAPGESHTLSQTIS 269
|
|
| MltB |
TIGR02282 |
lytic murein transglycosylase B; This family consists of lytic murein transglycosylases ... |
35-322 |
4.96e-53 |
|
lytic murein transglycosylase B; This family consists of lytic murein transglycosylases (murein hydrolases) in the family of MltB, which is a membrane-bound lipoprotein in Escherichia coli. The N-terminal lipoprotein modification motif is conserved in about half the members of this family. The term Slt35 describes a naturally occurring soluble fragment of MltB. Members of this family never contain the putative peptidoglycan binding domain described by pfam01471, which is associated with several classes of bacterial cell wall lytic enzymes. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 274066 [Multi-domain] Cd Length: 290 Bit Score: 184.90 E-value: 4.96e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 35 QAAAKGVDAASFQRFTAGLVPDPSVLPLLDAQPEFTTPiWD-YLASLVDSQRVTDGQAMLVTHRELLSRLSEQTGVDPAT 113
Cdd:TIGR02282 7 LVAKHGFDRAQLEAILAQAKYNDEVIRLIDNPAESAKP-WLeYRGIFITPKRIQDGVEFWKQHEDALNRAEQRYGVPPEI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 114 IVAVWGVESDYGRVTGKRPLLVSLATLSCA-GRRQPFFRGEFLALLSLLQQGDLSADGLTGSWAGAFGQTQFMPSTYARI 192
Cdd:TIGR02282 86 IVAIIGVETNYGRNMGKYRVLDALTTLAFDyPRRATFFRGELGQFLLLAREEQLDPLTLKGSYAGAMGYPQFMPSSYRQY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 193 AVDGDGDGRRDLVASIPDALASTANYLVKAGWERARPWGMEVTL--PRGFDASKAGRTRrqplqaWQTAGLLGTDGKPLA 270
Cdd:TIGR02282 166 AVDFDGDGHIDLWNSPDDAIGSVANYFHAHGWVRGDPVAVPATGaaPGDQLPNKFAKPH------YSLSQLAAAGLIPQA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1379540447 271 PtgLPAETPAALL-LPAGATGPAFLVFRNYDAIYAYNAAESYALSIALLADRL 322
Cdd:TIGR02282 240 P--LGNEQKASLVdLDVGGGDQYWLGLPNFYAITRYNRSTFYAMAVYQLSQAL 290
|
|
| Aldose_epim |
pfam01263 |
Aldose 1-epimerase; |
453-718 |
4.87e-39 |
|
Aldose 1-epimerase;
Pssm-ID: 396013 Cd Length: 300 Bit Score: 146.39 E-value: 4.87e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 453 LIDTPFSTAAISLFGGQLVSFVPKGG-QDVMWLSPS------------AQQPPTPIRG--------GAPVCWPYFGRqdq 511
Cdd:pfam01263 5 LTNGNGLSATISLYGATLLSLKVPGKlREVLLGSDDaegylkdsnyfgATLGPYANRIangrfeldGIPYCLPQNGP--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 512 tGDVPAHGFVRTVAWQLTESRREDDGTVVLTLTPPRLDDL--ALRLRMTLRIGRTLEQRLITENIS-GASVRFTQALHNY 588
Cdd:pfam01263 82 -GKNPLHGGARGRIWEVEEVKPDDGVTVTLVLDPDGEEGYpgDLEARVTYTLNEDNELTIEYEATNdGKPTPFNLGNHPY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 589 FHVGDALN---VSVQGLDGLDYLDKY-ENYATAHRQQGDWSLRDPR----DPGRSDRIYTNAGGRYTLTDPVLGRRIVIA 660
Cdd:pfam01263 161 FNLSGDIDiheLQIEADEYLEVDDDLiPTGELKDVKGTPFDFRQPTpigeDILGYDHVYLLDPLKAVIIDPDPGSGIVLE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 661 TEGSR-SLVVWNPGEEAGKKMADVGD-GWRDYVCLEAANAGPDVIELAPGASHTLSQTIS 718
Cdd:pfam01263 241 VSTTQpGLVVYTPNFLKGKYLSDEGFaLETQFLPDEPNHPEFPSIILKPGESYTAETSYS 300
|
|
| PRK10760 |
PRK10760 |
murein hydrolase B; Provisional |
58-325 |
1.74e-29 |
|
murein hydrolase B; Provisional
Pssm-ID: 236754 [Multi-domain] Cd Length: 359 Bit Score: 120.61 E-value: 1.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 58 SVLPLLDAQPEFTTP------IWD-YLASLVDSQRVTDGQAMLVTHRELLSRLSEQTGVDPATIVAVWGVESDYGRVTGK 130
Cdd:PRK10760 90 WVLRLMDRQAPTTRPpsgpngAWLrYRKKFITPDNVQNGVVFWNQYEDALNRAWQVYGVPPEIIVGIIGVETRWGRVMGK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 131 RPLLVSLATLSCA-GRRQPFFRGEFLALLSLLQQGDLSADGLTGSWAGAFGQTQFMPSTYARIAVDGDGDGRRDLVASIp 209
Cdd:PRK10760 170 TRILDALATLSFNyPRRAEYFSGELETFLLMARDEGDDPLNLRGSFAGAMGYGQFMPSSFKQYAVDFNGDGHINLWDPV- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 210 DALASTANYLVKAGWERARPW-----GMEVTLPRGFDAskagrtrRQPLQAWQTAGllgtdgkpLAPTG-LPAETPAALL 283
Cdd:PRK10760 249 DAIGSVANYFKAHGWVKGDQVavpanGQAPGLENGFKT-------RYSVSQLAAAG--------LTPQQpLGNHQQASLL 313
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1379540447 284 -LPAGATGPAFLVFRNYDAIYAYNAAESYALSIALLAD---RLRGG 325
Cdd:PRK10760 314 rLDVGTGYQYWYGLPNFYTITRYNHSTHYAMAVWQLGQavaLARVG 359
|
|
| Aldose_epim |
cd01081 |
aldose 1-epimerase superfamily; Aldose 1-epimerases or mutarotases are key enzymes of ... |
459-701 |
2.57e-20 |
|
aldose 1-epimerase superfamily; Aldose 1-epimerases or mutarotases are key enzymes of carbohydrate metabolism; they catalyze the interconversion of the alpha- and beta-anomers of hexose sugars such as glucose and galactose. This interconversion is an important step that allows anomer specific metabolic conversion of sugars. Studies of the catalytic mechanism of the best known member of the family, galactose mutarotase, have shown a glutamate and a histidine residue to be critical for catalysis; the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate and the histidine as the active site acid to protonate the C-5 ring oxygen.
Pssm-ID: 185695 [Multi-domain] Cd Length: 284 Bit Score: 91.76 E-value: 2.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 459 STAAISLFGGQLVSFVPKGGQDVMWLSPSAQQPPT-PIRGGAPVCWPYFGR---------------QDQTGDVPAHGFVR 522
Cdd:cd01081 1 AVAVIAPRGANIISLKVKGDVDLLWGYPDAEEYPLaPTGGGGAILFPFANRisdgrytfdgkqyplNEDEGGNAIHGFVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 523 TVAWQLTESrREDDGTVVLTLTPPRLD-----DLALRLRMTLRiGRTLEQRLITENISGASVRFTQALHNYFHVGDA--- 594
Cdd:cd01081 81 NLPWRVVAT-DEEEASVTLSYDLNDGPggypfPLELTVTYTLD-ADTLTITFTVTNLGDEPMPFGLGWHPYFGLPGVaie 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 595 -----LNVSVQGLDGLDYLDKYEnyaTAHRQQGDWSLRDPRDPGRSDRIYTNAGG-----RYTLTDPVLGRRIVIATEGS 664
Cdd:cd01081 159 dlrlrVPASKVLPLDDLLPPTGE---LEVPGEEDFRLGRPLGGGELDDCFLLLGNdagtaEARLEDPDSRISVEFETGWP 235
|
250 260 270
....*....|....*....|....*....|....*..
gi 1379540447 665 RsLVVWNPgeeagkkmadvGDGWRDYVCLEAANAGPD 701
Cdd:cd01081 236 F-WQVYTG-----------DGGRRGSVAIEPMTSAPD 260
|
|
| GalM |
COG2017 |
Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism]; |
460-720 |
9.91e-20 |
|
Galactose mutarotase or related enzyme [Carbohydrate transport and metabolism];
Pssm-ID: 441620 [Multi-domain] Cd Length: 309 Bit Score: 90.72 E-value: 9.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 460 TAAISLFGGQLVSF-VP-KGGQDVMWLSPSAQQPPTPiRGGAPVCWPYFGR--------QDQT-------GDVPAHGFVR 522
Cdd:COG2017 18 RAVIPEYGATLTSLrVPdKDGRDVLLGFDDLEDDPPW-AYGGAILGPYANRiadgrftlDGKTyqlpineGPNALHGGAR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 523 TVAWQLTEsrrEDDGTVVLTLTPPrlDD------LALRLRMTLRiGRTLEQRLITENISGASVRFTQALHNYFHVGDALN 596
Cdd:COG2017 97 DRPWEVEE---QSEDSVTLSLTSP--DEegypgnLELTVTYTLT-DNGLTITYTATNLGDKPTPFNLGNHPYFNLPGEGG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 597 VSVQG----LDGLDYLDKYENY----ATAHRQQGDWSLRDPRDPGRS--DRIYT--NAGGRY--TLTDPVLGRRIVIATE 662
Cdd:COG2017 171 GDIDDhrlqIPADEYLPVDEGLiptgELAPVAGTPFDFREPRPLGDGgfDHAFVglDSDGRPaaRLTDPDSGRRLEVSTD 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1379540447 663 GSRSLVVWNPgeeagkkmaDVGDGWRDYVCLEA----ANA-----GPDVIELAPGASHTLSQTISVE 720
Cdd:COG2017 251 EFPGLQVYTG---------NFLDPGRDGVCLEPqtgpPDApnhpgFEGLIVLAPGETYSATTRIRFS 308
|
|
| Slt35-like |
cd13399 |
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic ... |
108-228 |
1.17e-19 |
|
Slt35-like lytic transglycosylase; Lytic transglycosylase similar to Escherichia coli lytic transglycosylase Slt35 and Pseudomonas aeruginosa Sltb1. Lytic transglycosylase (LT) catalyzes the cleavage of the beta-1,4-glycosidic bond between N-acetylmuramic acid (MurNAc) and N-acetyl-D-glucosamine (GlcNAc) as do "goose-type" lysozymes. However, in addition to this, they also make a new glycosidic bond with the C6 hydroxyl group of the same muramic acid residue. Proteins similar to this this family include the soluble and insoluble membrane-bound LTs in bacteria, the LTs in bacteriophage lambda, as well as the eukaryotic "goose-type" lysozymes (goose egg-white lysozyme; GEWL).
Pssm-ID: 381602 [Multi-domain] Cd Length: 108 Bit Score: 84.67 E-value: 1.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 108 GVDPATIVAVWGVESDYGRVTGkrpllvslatlscagrrqpffrgeflallsllqqgdlsadgltGSWAGAFGQTQFMPS 187
Cdd:cd13399 2 GVPPGILAAILGVESGFGPNAG-------------------------------------------GSPAGAQGIAQFMPS 38
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1379540447 188 TYARIAVDGDGDGRRDLvASIPDALASTANYLVKAGWERAR 228
Cdd:cd13399 39 TWKAYGVDGNGDGKADP-FNPEDAIASAANYLCRHGWDLNA 78
|
|
| Aldose_epim_Slr1438 |
cd09025 |
Aldose 1-epimerase, similar to Synechocystis Slr1438; Proteins similar to Synechocystis ... |
466-718 |
8.34e-19 |
|
Aldose 1-epimerase, similar to Synechocystis Slr1438; Proteins similar to Synechocystis Slr1438 are uncharacterized members of aldose-1-epimerase superfamily. Aldose 1-epimerases or mutarotases are key enzymes of carbohydrate metabolism, catalyzing the interconversion of the alpha- and beta-anomers of hexose sugars such as glucose and galactose. This interconversion is an important step that allows anomer specific metabolic conversion of sugars. Studies of the catalytic mechanism of the best known member of the family, galactose mutarotase, have shown a glutamate and a histidine residue to be critical for catalysis; the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen.
Pssm-ID: 185702 Cd Length: 271 Bit Score: 86.92 E-value: 8.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 466 FGGQLVSFVpKGGQDVMWLSPSA-QQPPTPIRGGAPVCWPYFGRQD--------QTGDVPAHGFVRTVAWQLTESRREDD 536
Cdd:cd09025 21 RGGLITRWT-VQGRELLYLDEERfADPAKSVRGGIPILFPICGNLPddgyplagQEYTLKQHGFARDLPWEVELLGDGAG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 537 GTVVLTLTP------PrlddLALRLRMTLRI-GRTLEQRLITENISGASVRFTQALHNYFHVGDALNVSVQGL--DGLDY 607
Cdd:cd09025 100 LTLTLRDNEatravyP----FDFELELTYRLaGNTLEIAQRVHNLGDQPMPFSFGFHPYFAVPDKAKLSLDLPptRCFDQ 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 608 L-DKYENYA--TAHRQQG-DWSLRDprdpgrsdriytnaGGRYTLTDPVLGRRI-VIATEGSRSLVVWN-PGeeagkkma 681
Cdd:cd09025 176 KtDEEANTPgqFDETEEGvDLLFRP--------------LGPASLTDGARGLKItLDHDEPFSNLVVWTdKG-------- 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1379540447 682 dvgdgwRDYVCLE-------AANAGPDVIELAPGASHTLSQTIS 718
Cdd:cd09025 234 ------KDFVCLEpwtgprnALNTGERLLLLPPGETEEASVRIQ 271
|
|
| PGRP |
COG3409 |
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope ... |
330-398 |
3.51e-11 |
|
Peptidoglycan-binding (PGRP) domain of peptidoglycan hydrolases [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442635 [Multi-domain] Cd Length: 69 Bit Score: 59.15 E-value: 3.51e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1379540447 330 AAWPTDEPGLGRPERRELQQLLLARGHQIGEADGMVGSATRRAIQVEQTRLGLqPADGRPGQRILTALR 398
Cdd:COG3409 1 ASAPTLRLGDSGEDVRELQQRLNALGYYPGPVDGIFGPATEAAVRAFQRANGL-PVDGIVGPATWAALR 68
|
|
| Aldose_epim_lacX |
cd09024 |
Aldose 1-epimerase, similar to Lactococcus lactis lacX; Proteins similar to Lactococcus lactis ... |
460-719 |
5.64e-09 |
|
Aldose 1-epimerase, similar to Lactococcus lactis lacX; Proteins similar to Lactococcus lactis lacX are uncharacterized members of aldose-1-epimerase superfamily. Aldose 1-epimerases or mutarotases are key enzymes of carbohydrate metabolism, catalyzing the interconversion of the alpha- and beta-anomers of hexose sugars such as glucose and galactose. This interconversion is an important step that allows anomer specific metabolic conversion of sugars. Studies of the catalytic mechanism of the best known member of the family, galactose mutarotase, have shown a glutamate and a histidine residue to be critical for catalysis; the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen.
Pssm-ID: 185701 Cd Length: 288 Bit Score: 57.94 E-value: 5.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 460 TAAISLFGGQLVSFVPKG-GQDVMWlspsaQQPPTPIRGGAPVCWPYFGR--------QDQTGDVPAHGFVRTVAWQLTE 530
Cdd:cd09024 9 TVTISEHGAELTSIKDKKtGREYLW-----QGDPAYWGRHAPILFPIVGRlkddtytiDGKTYPMPQHGFARDMEFEVVE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 531 srrEDDGTVVLTLTpprlDD---LAL-----RLRMTLRI-GRTLEQRLITENISgasvrfTQALhnYFHVG--DALNVSV 599
Cdd:cd09024 84 ---QSDDSVTFELT----DNeetLKVypfdfELRVTYTLeGNTLKVTYEVKNPD------DKTM--PFSIGghPAFNCPL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 600 -QGLDGLDY---LDKYENYATAHRQQGDWSLRDPRDPGRSDR--------------IYTNAGGR-YTLTDPVLGRRIVIA 660
Cdd:cd09024 149 dEGEKFEDYyleFEPKEELERIPLVGPLGLLGEKKPLLLNEGtlplthdlfdddalIFDNLKSReVTLKSKKTGHGVTVD 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1379540447 661 TEGSRSLVVWNPGEEAgkkmadvgdgwrDYVCLE-----AANAG--------PDVIELAPGASHTLSQTISV 719
Cdd:cd09024 229 FDDFPYLGIWSKPNGA------------PFVCIEpwyglADSVGfdgdledkEGINKLEPGESFEASYSITI 288
|
|
| PG_binding_1 |
pfam01471 |
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This ... |
341-397 |
1.48e-08 |
|
Putative peptidoglycan binding domain; This domain is composed of three alpha helices. This domain is found at the N or C terminus of a variety of enzymes involved in bacterial cell wall degradation. This domain may have a general peptidoglycan binding function. This family is found N-terminal to the catalytic domain of matrixins. The domain is found to bind peptidoglycan experimentally.
Pssm-ID: 460223 [Multi-domain] Cd Length: 57 Bit Score: 51.36 E-value: 1.48e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1379540447 341 RPERRELQQLLLARGHQIGEADGMVGSATRRAIQVEQTRLGLqPADGRPGQRILTAL 397
Cdd:pfam01471 2 GEDVKELQRYLNRLGYYPGPVDGYFGPSTEAAVKAFQRAFGL-PVDGIVDPETLAAL 57
|
|
| Aldose_epim_Ec_YihR |
cd09022 |
Aldose 1-epimerase, similar to Escherichia coli YihR; Proteins similar to Escherichia coli ... |
460-717 |
7.05e-03 |
|
Aldose 1-epimerase, similar to Escherichia coli YihR; Proteins similar to Escherichia coli YihR are uncharacterized members of aldose-1-epimerase superfamily. Aldose 1-epimerases or mutarotases are key enzymes of carbohydrate metabolism, catalyzing the interconversion of the alpha- and beta-anomers of hexose sugars such as glucose and galactose. This interconversion is an important step that allows anomer specific metabolic conversion of sugars. Studies of the catalytic mechanism of the best known member of the family, galactose mutarotase, have shown a glutamate and a histidine residue to be critical for catalysis; the glutamate serves as the active site base to initiate the reaction by removing the proton from the C-1 hydroxyl group of the sugar substrate, and the histidine as the active site acid to protonate the C-5 ring oxygen.
Pssm-ID: 185699 Cd Length: 284 Bit Score: 39.09 E-value: 7.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 460 TAAISLFGGQLVSFVpKGGQDVMWlSPSAQQPPTPIRGGAPVCWP--------YFGRQDQTGDV--PA-----HGFVRTV 524
Cdd:cd09022 2 RAVVTEVGAGLRSLT-VGGRDLVE-PYPADEVPPGAAGQVLAPWPnriadgryTFDGVEHQLPItePErgnaiHGLVRWA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 525 AWQLTEsrrEDDGTVVLTLTPPRLD----DLALRLRMTLRiGRTLEQRLITENISGASVRFTQALHNYFHVGDA------ 594
Cdd:cd09022 80 DWQLVE---HTDSSVTLRTRIPPQPgypfTLELTVTYELD-DDGLTVTLTATNVGDEPAPFGVGFHPYLSAGGApldect 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1379540447 595 ---------------LNVSVQGLDGLDYlDKYENYATAHRQQGD-WSLRDPRDPGRSdriytnaggRYTLTDPVLGRRIV 658
Cdd:cd09022 156 ltlpadtwlpvderlLPTGTEPVAGTPY-DFRTGRRLGGTALDTaFTDLTRDADGRA---------RARLTGPDGRGVEL 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1379540447 659 IATEGSRSLVVWNPGEEAgkkmadvGDGWRDYVCLE-------AANAGPDVIELAPGASHTLSQTI 717
Cdd:cd09022 226 WADESFPWVQVFTADTLP-------PPGRRRGLAVEpmtcppnAFNSGTDLIVLAPGETHTASWGI 284
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