|
Name |
Accession |
Description |
Interval |
E-value |
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
1-432 |
0e+00 |
|
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 (N-acetylglucosamine-phosphate mutase), is an essential enzyme found in eukaryotes that reversibly catalyzes the conversion of GlcNAc-6-phosphate into GlcNAc-1-phosphate as part of the UDP-N-acetylglucosamine (UDP-GlcNAc) biosynthetic pathway. UDP-GlcNAc is an essential metabolite that serves as the biosynthetic precursor of many glycoproteins and mucopolysaccharides. AGM1 is a member of the alpha-D-phosphohexomutase superfamily, which catalyzes the intramolecular phosphoryl transfer of sugar substrates. The alpha-D-phosphohexomutases have four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100088 Cd Length: 513 Bit Score: 740.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 1 MLAPSWEEHATCLANAEEQDMQRVLIDI--SEKEAVNLQQDAFVVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTT 78
Cdd:cd03086 62 MLEESWEPYATQLANASDDELLVLVLMLisVKELNIDLSVPANVFVGRDTRPSGPALLQALLDGLKALGGNVIDYGLVTT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 79 PQLHYMVYCRNTGGRYGKATIEGYYQKLSKAFVELTKQASCSGDEYRSLKVDCANGIGALKLREMEHYFSQGLSVQLFND 158
Cdd:cd03086 142 PQLHYLVRAANTEGAYGEPTEEGYYEKLSKAFNELYNLLQDGGDEPEKLVVDCANGVGALKLKELLKRLKKGLSVKIIND 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 159 GSKG--KLNHLCGADFVKSHQKPPQGMEIK-SNERCCSFDGDADRIVYYYHDADGHFHLIDGDKIATLISSFLKELL--V 233
Cdd:cd03086 222 GEEGpeLLNDGCGADYVKTKQKPPRGFELKpPGVRCCSFDGDADRLVYFYPDSSNKFHLLDGDKIATLFAKFIKELLkkA 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 234 EIGESLNIGVVQTAYANGSSTRYLEEVMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGTALFSTAVEMKIKqSAEQL 313
Cdd:cd03086 302 GEELKLTIGVVQTAYANGASTKYLEDVLKVPVVCTPTGVKHLHHAAEEFDIGVYFEANGHGTVLFSESALAKIE-ENSSL 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 314 EDKKRKAAKMLENIIDLFNQAAGDAISDMLVIEAILALKGLTVQQWDALYTDLPNRQLKVQVADRRVISTTDAERQAVTP 393
Cdd:cd03086 381 SDEQEKAAKTLLAFSRLINQTVGDAISDMLAVELILAALGWSPQDWDNLYTDLPNRQLKVKVPDRSVIKTTDAERRLVEP 460
|
410 420 430
....*....|....*....|....*....|....*....
gi 315707008 394 PGLQEAINDLVKKYKLSRAFVRPSGTEDVVRVYAEADSQ 432
Cdd:cd03086 461 KGLQDKIDAIVAKYNNGRAFVRPSGTEDVVRVYAEAATQ 499
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
1-434 |
0e+00 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 538.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 1 MLAPSWEEHATCLANAE-EQDMQRVLIDISEKEAVNL---QQDAFVVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLL 76
Cdd:PLN02895 85 MLPQAWEPFADALANAPdPDALVQLIREFVKKENIPAvggNPPAEVLLGRDTRPSGPALLAAALKGVRAIGARAVDMGIL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 77 TTPQLHYMVYCRNTGGrygKATIEGYYQKLSKAF---VELTKQASCSGDEYRSLKVDCANGIGALKLREMEHYFSqGLSV 153
Cdd:PLN02895 165 TTPQLHWMVRAANKGM---KATESDYFEQLSSSFralLDLIPNGSGDDRADDKLVVDGANGVGAEKLETLKKALG-GLDL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 154 QLFNDG--SKGKLNHLCGADFVKSHQKPPQGMEIK-SNERCCSFDGDADRIVYYYHDADG-HFHLIDGDKIATLISSFLK 229
Cdd:PLN02895 241 EVRNSGkeGEGVLNEGVGADFVQKEKVPPTGFASKdVGLRCASLDGDADRLVYFYVSSAGsKIDLLDGDKIASLFALFIK 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 230 ELLVEIGES---------LNIGVVQTAYANGSSTRYLEEVMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGTALFST 300
Cdd:PLN02895 321 EQLRILNGNgnekpeellVRLGVVQTAYANGASTAYLKQVLGLEVVCTPTGVKYLHEAAAEFDIGVYFEANGHGTVLFSE 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 301 AVEMKIKQSAEQLEDKKR-----KAAKMLENIIDLFNQAAGDAISDMLVIEAILALKGLTVQQWDALYTDLPNRQLKVQV 375
Cdd:PLN02895 401 RFLDWLEAAAAELSSKAKgseahKAARRLLAVSRLINQAVGDALSGLLLVEAILQYRGWSLAEWNALYQDLPSRQLKVKV 480
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 315707008 376 ADRRVISTTDAERQAVTPPGLQEAINDLVKKYKLSRAFVRPSGTEDVVRVYAEADSQVR 434
Cdd:PLN02895 481 ADRTAITTTDAETVVVRPAGLQDAIDAEVAKYPRGRAFVRPSGTEDVVRVYAEASTQEA 539
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
42-434 |
7.18e-30 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 120.69 E-value: 7.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 42 VVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMVYCRNTGG--------------------RYGK----- 96
Cdd:COG1109 44 VVVGRDTRLSSPMLARALAAGLASAGIDVYDLGLVPTPALAFAVRHLGADGgimitashnppeyngikffdADGGklspe 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 97 --ATIEGYYQKLSKAFVELTKQASCS-----GDEY--------------RSLKV--DCANGIGALK----LREMehyfsq 149
Cdd:COG1109 124 eeKEIEALIEKEDFRRAEAEEIGKVTriedvLEAYiealkslvdealrlRGLKVvvDCGNGAAGGVaprlLREL------ 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 150 GLSVQLFN---DGSKGklNHLCG---------ADFVKSHqkppqGMEIksnerCCSFDGDADRI--VyyyhDADGHFhlI 215
Cdd:COG1109 198 GAEVIVLNaepDGNFP--NHNPNpepenledlIEAVKET-----GADL-----GIAFDGDADRLgvV----DEKGRF--L 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 216 DGDKIATLISSFLKEllveigESLNIGVVQTAyangSSTRYLEEVMK---VPVYCTKTGVKHLHHKAQEFD--IGvyFEA 290
Cdd:COG1109 260 DGDQLLALLARYLLE------KGPGGTVVVTV----MSSLALEDIAEkhgGEVVRTKVGFKYIKEKMRETGavLG--GEE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 291 NGHgtalfstavemkikqsaeqledkkrkaakmlenIIDLFNQAAGDAI-SDMLVIEaILALKGLTVQQWDALYTDLPNR 369
Cdd:COG1109 328 SGG---------------------------------IIFPDFVPTDDGIlAALLLLE-LLAKQGKSLSELLAELPRYPQP 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 315707008 370 QLKVQVADRRVISTTDAE-RQAVTPPGLQEAINDLvkKYKL---SRAFVRPSGTEDVVRVYAEADSQVR 434
Cdd:COG1109 374 EINVRVPDEEKIGAVMEKlREAVEDKEELDTIDGV--KVDLedgGWVLVRPSGTEPLLRVYAEAKDEEE 440
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
42-432 |
8.10e-15 |
|
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been characterized as the archaeal protein responsible for the second step of UDP-GlcNAc biosynthesis. This GlmM protein catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. The first-characterized bacterial GlmM protein is modeled by TIGR01455. These two families are members of the larger phosphoglucomutase/phosphomannomutase family (characterized by three domains: pfam02878, pfam02879 and pfam02880), but are not nearest neighbors to each other. This model also includes a number of sequences from non-archaea in the Bacteroides, Chlorobi, Chloroflexi, Planctomycetes and Spirochaetes lineages. Evidence supporting their inclusion in this equivalog as having the same activity comes from genomic context and phylogenetic profiling. A large number of these organisms are known to produce exo-polysaccharide and yet only appeared to contain the GlmS enzyme of the GlmSMU pathway for UDP-GlcNAc biosynthesis (GenProp0750). In some organisms including Leptospira, this archaeal GlmM is found adjacent to the GlmS as well as a putative GlmU non-orthologous homolog. Phylogenetic profiling of the GlmS-only pattern using PPP identifies members of this archaeal GlmM family as the highest-scoring result. [Central intermediary metabolism, Amino sugars]
Pssm-ID: 274906 Cd Length: 443 Bit Score: 76.01 E-value: 8.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 42 VVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYmvYCRNTGGRYG---------------K---------- 96
Cdd:TIGR03990 38 VVVGRDTRTSGPMLENAVIAGLLSTGCDVVDLGIAPTPTLQY--AVRELGADGGimitashnppeyngiKllnsdgtels 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 97 ----ATIEGYYQKLSKAFVELTKQASCSGDEY--------------------RSLKV--DCANGIGALK----LREMehy 146
Cdd:TIGR03990 116 reqeEEIEEIAESGDFERADWDEIGTVTSDEDaiddyieaildkvdveairkKGFKVvvDCGNGAGSLTtpylLREL--- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 147 fsqGLSVQLFNDGSKGK------------LNHLC------GADFVKSHqkppqgmeiksnerccsfDGDADRIVYYyhDA 208
Cdd:TIGR03990 193 ---GCKVITLNCQPDGTfpgrnpeptpenLKDLSalvkatGADLGIAH------------------DGDADRLVFI--DE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 209 DGHFhlIDGDKIATLissFLKELLVEIGESLnigVVqtayaNGSSTRYLEEVMK---VPVYCTKTGVKHLHHKAQEFDIG 285
Cdd:TIGR03990 250 KGRF--IGGDYTLAL---FAKYLLEHGGGKV---VT-----NVSSSRAVEDVAErhgGEVIRTKVGEVNVAEKMKEEGAV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 286 VYFEANGHgtalfstavemkikqsaeqledkkrkaakmlenIIDLFNQAAGDAISDMLVIEAILALKGLTVQQWDALYTD 365
Cdd:TIGR03990 317 FGGEGNGG---------------------------------WIFPDHHYCRDGLMAAALFLELLAEEGKPLSELLAELPK 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 366 LPNRQLKVQVADRRVISTTDAERQAVTppglQEAINDL--VK-KYKLSRAFVRPSGTEDVVRVYAEADSQ 432
Cdd:TIGR03990 364 YPMSKEKVELPDEDKEEVMEAVEEEFA----DAEIDTIdgVRiDFEDGWVLVRPSGTEPIVRIYAEAKTE 429
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
42-85 |
1.47e-07 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 50.30 E-value: 1.47e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 315707008 42 VVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMV 85
Cdd:pfam02878 43 VVVGRDTRYSSRELARALAAGLASNGVEVILLGLLPTPAVSFAT 86
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
1-432 |
0e+00 |
|
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 (N-acetylglucosamine-phosphate mutase), is an essential enzyme found in eukaryotes that reversibly catalyzes the conversion of GlcNAc-6-phosphate into GlcNAc-1-phosphate as part of the UDP-N-acetylglucosamine (UDP-GlcNAc) biosynthetic pathway. UDP-GlcNAc is an essential metabolite that serves as the biosynthetic precursor of many glycoproteins and mucopolysaccharides. AGM1 is a member of the alpha-D-phosphohexomutase superfamily, which catalyzes the intramolecular phosphoryl transfer of sugar substrates. The alpha-D-phosphohexomutases have four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100088 Cd Length: 513 Bit Score: 740.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 1 MLAPSWEEHATCLANAEEQDMQRVLIDI--SEKEAVNLQQDAFVVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTT 78
Cdd:cd03086 62 MLEESWEPYATQLANASDDELLVLVLMLisVKELNIDLSVPANVFVGRDTRPSGPALLQALLDGLKALGGNVIDYGLVTT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 79 PQLHYMVYCRNTGGRYGKATIEGYYQKLSKAFVELTKQASCSGDEYRSLKVDCANGIGALKLREMEHYFSQGLSVQLFND 158
Cdd:cd03086 142 PQLHYLVRAANTEGAYGEPTEEGYYEKLSKAFNELYNLLQDGGDEPEKLVVDCANGVGALKLKELLKRLKKGLSVKIIND 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 159 GSKG--KLNHLCGADFVKSHQKPPQGMEIK-SNERCCSFDGDADRIVYYYHDADGHFHLIDGDKIATLISSFLKELL--V 233
Cdd:cd03086 222 GEEGpeLLNDGCGADYVKTKQKPPRGFELKpPGVRCCSFDGDADRLVYFYPDSSNKFHLLDGDKIATLFAKFIKELLkkA 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 234 EIGESLNIGVVQTAYANGSSTRYLEEVMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGTALFSTAVEMKIKqSAEQL 313
Cdd:cd03086 302 GEELKLTIGVVQTAYANGASTKYLEDVLKVPVVCTPTGVKHLHHAAEEFDIGVYFEANGHGTVLFSESALAKIE-ENSSL 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 314 EDKKRKAAKMLENIIDLFNQAAGDAISDMLVIEAILALKGLTVQQWDALYTDLPNRQLKVQVADRRVISTTDAERQAVTP 393
Cdd:cd03086 381 SDEQEKAAKTLLAFSRLINQTVGDAISDMLAVELILAALGWSPQDWDNLYTDLPNRQLKVKVPDRSVIKTTDAERRLVEP 460
|
410 420 430
....*....|....*....|....*....|....*....
gi 315707008 394 PGLQEAINDLVKKYKLSRAFVRPSGTEDVVRVYAEADSQ 432
Cdd:cd03086 461 KGLQDKIDAIVAKYNNGRAFVRPSGTEDVVRVYAEAATQ 499
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
1-434 |
0e+00 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 538.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 1 MLAPSWEEHATCLANAE-EQDMQRVLIDISEKEAVNL---QQDAFVVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLL 76
Cdd:PLN02895 85 MLPQAWEPFADALANAPdPDALVQLIREFVKKENIPAvggNPPAEVLLGRDTRPSGPALLAAALKGVRAIGARAVDMGIL 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 77 TTPQLHYMVYCRNTGGrygKATIEGYYQKLSKAF---VELTKQASCSGDEYRSLKVDCANGIGALKLREMEHYFSqGLSV 153
Cdd:PLN02895 165 TTPQLHWMVRAANKGM---KATESDYFEQLSSSFralLDLIPNGSGDDRADDKLVVDGANGVGAEKLETLKKALG-GLDL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 154 QLFNDG--SKGKLNHLCGADFVKSHQKPPQGMEIK-SNERCCSFDGDADRIVYYYHDADG-HFHLIDGDKIATLISSFLK 229
Cdd:PLN02895 241 EVRNSGkeGEGVLNEGVGADFVQKEKVPPTGFASKdVGLRCASLDGDADRLVYFYVSSAGsKIDLLDGDKIASLFALFIK 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 230 ELLVEIGES---------LNIGVVQTAYANGSSTRYLEEVMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGTALFST 300
Cdd:PLN02895 321 EQLRILNGNgnekpeellVRLGVVQTAYANGASTAYLKQVLGLEVVCTPTGVKYLHEAAAEFDIGVYFEANGHGTVLFSE 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 301 AVEMKIKQSAEQLEDKKR-----KAAKMLENIIDLFNQAAGDAISDMLVIEAILALKGLTVQQWDALYTDLPNRQLKVQV 375
Cdd:PLN02895 401 RFLDWLEAAAAELSSKAKgseahKAARRLLAVSRLINQAVGDALSGLLLVEAILQYRGWSLAEWNALYQDLPSRQLKVKV 480
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 315707008 376 ADRRVISTTDAERQAVTPPGLQEAINDLVKKYKLSRAFVRPSGTEDVVRVYAEADSQVR 434
Cdd:PLN02895 481 ADRTAITTTDAETVVVRPAGLQDAIDAEVAKYPRGRAFVRPSGTEDVVRVYAEASTQEA 539
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
1-432 |
2.19e-174 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 500.72 E-value: 2.19e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 1 MLAPSWEEHATCLANAE-EQDMQRVLIDISEKEAVNLQQD-----------AFVVIGRDTRPSSEKLSQSVIDGVTVLGG 68
Cdd:PTZ00302 102 MLEESWEKICTDFANARtGEDLVSVLMDCLTEHGIKLSNLkldlnksncskAKVHVGRDTRPSSPELVSALLRGLKLLIG 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 69 QFH-DYGLLTTPQLHYMVYCRNTGGR-YGKATIEGYYQKLSKAFVELTKQASCSGDEYRS------LKVDCANGIGALKL 140
Cdd:PTZ00302 182 SNVrNFGIVTTPQLHFLVAFANGLGVdVVESSDELYYAYLLAAFKELYRTLQEGGPVDLTqnnskiLVVDCANGVGGYKI 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 141 REMEHYFSQ---GLSVQLFNDGSKGKLNHLCGADFVKSHQKPPQGMEIK---SNERCCSFDGDADRIVYYYHDADGH--F 212
Cdd:PTZ00302 262 KRFFEALKQlgiEIIPININCDEEELLNDKCGADYVQKTRKPPRAMKEWpgdEETRVASFDGDADRLVYFFPDKDGDdkW 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 213 HLIDGDKIATLISSFLKELLVEIG--ESLNIGVVQTAYANGSSTRYLEEVMK-VPVYCTKTGVKHLHHKAQEFDIGVYFE 289
Cdd:PTZ00302 342 VLLDGDRIAILYAMLIKKLLGKIQlkKKLDIGVVQTAYANGASTNYLNELLGrLRVYCAPTGVKNLHPKAHKYDIGIYFE 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 290 ANGHGTALFStavEMKIKQSAEQLEDK--KRKAAKMLENIIDLFNQAAGDAISDMLVIEAILALKGLTVQQWDALYTDLP 367
Cdd:PTZ00302 422 ANGHGTVLFN---EKALAEWAKFLAKQnaLNSACRQLEKFLRLFNQTIGDAISDLLAVELALAFLGLSFQDWLNLYTDLP 498
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 315707008 368 NRQLKVQVADRRVISTTDAERQAVTPPGLQEAINDLVKKYK-LSRAFVRPSGTEDVVRVYAEADSQ 432
Cdd:PTZ00302 499 SRQDKVTVKDRTLITNTEDETRLLEPKGLQDKIDAIVSKYDnAARAFIRPSGTEPVVRVYAEAPTL 564
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
94-432 |
1.80e-31 |
|
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this family include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). These enzymes play important and diverse roles in carbohydrate metabolism in organisms from bacteria to humans. Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100086 [Multi-domain] Cd Length: 355 Bit Score: 123.24 E-value: 1.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 94 YGKATIEGYYQKL-SKAFVELTKQAScsgdeyRSLKVDCANGIGALKLREM-EHYfsqGLSVQLFN---DGSKGKLNHLC 168
Cdd:cd03084 87 KAVDILQRYFEALkKLFDVAALSNKK------FKVVVDSVNGVGGPIAPQLlEKL---GAEVIPLNcepDGNFGNINPDP 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 169 GADfvKSHQKPPQGMEIKSNERCCSFDGDADRIVYYYHDadghFHLIDGDKIATLISsflKELLVEIGesLNIGVVQTAY 248
Cdd:cd03084 158 GSE--TNLKQLLAVVKAEKADFGVAFDGDADRLIVVDEN----GGFLDGDELLALLA---VELFLTFN--PRGGVVKTVV 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 249 ANGSSTRYLEEvMKVPVYCTKTGVKHLHHKAQEFDIGVYFEANGHGtalfstavemkikqsaeqledkkrkaakmleniI 328
Cdd:cd03084 227 SSGALDKVAKK-LGIKVIRTKTGFKWVGEAMQEGDVVLGGEESGGV---------------------------------I 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 329 DLFNQAAGDAISDMLVIEAILALKGLTVQQWDALYTDLPNRQLKVQvadrrvisttdaerqavtppglqeaindlvkkyk 408
Cdd:cd03084 273 FPEFHPGRDGISAALLLLEILANLGKSLSELFSELPRYYYIRLKVR---------------------------------- 318
|
330 340
....*....|....*....|....
gi 315707008 409 lSRAFVRPSGTEDVVRVYAEADSQ 432
Cdd:cd03084 319 -GWVLVRASGTEPAIRIYAEADTQ 341
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
42-434 |
7.18e-30 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 120.69 E-value: 7.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 42 VVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMVYCRNTGG--------------------RYGK----- 96
Cdd:COG1109 44 VVVGRDTRLSSPMLARALAAGLASAGIDVYDLGLVPTPALAFAVRHLGADGgimitashnppeyngikffdADGGklspe 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 97 --ATIEGYYQKLSKAFVELTKQASCS-----GDEY--------------RSLKV--DCANGIGALK----LREMehyfsq 149
Cdd:COG1109 124 eeKEIEALIEKEDFRRAEAEEIGKVTriedvLEAYiealkslvdealrlRGLKVvvDCGNGAAGGVaprlLREL------ 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 150 GLSVQLFN---DGSKGklNHLCG---------ADFVKSHqkppqGMEIksnerCCSFDGDADRI--VyyyhDADGHFhlI 215
Cdd:COG1109 198 GAEVIVLNaepDGNFP--NHNPNpepenledlIEAVKET-----GADL-----GIAFDGDADRLgvV----DEKGRF--L 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 216 DGDKIATLISSFLKEllveigESLNIGVVQTAyangSSTRYLEEVMK---VPVYCTKTGVKHLHHKAQEFD--IGvyFEA 290
Cdd:COG1109 260 DGDQLLALLARYLLE------KGPGGTVVVTV----MSSLALEDIAEkhgGEVVRTKVGFKYIKEKMRETGavLG--GEE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 291 NGHgtalfstavemkikqsaeqledkkrkaakmlenIIDLFNQAAGDAI-SDMLVIEaILALKGLTVQQWDALYTDLPNR 369
Cdd:COG1109 328 SGG---------------------------------IIFPDFVPTDDGIlAALLLLE-LLAKQGKSLSELLAELPRYPQP 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 315707008 370 QLKVQVADRRVISTTDAE-RQAVTPPGLQEAINDLvkKYKL---SRAFVRPSGTEDVVRVYAEADSQVR 434
Cdd:COG1109 374 EINVRVPDEEKIGAVMEKlREAVEDKEELDTIDGV--KVDLedgGWVLVRPSGTEPLLRVYAEAKDEEE 440
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
42-432 |
4.91e-21 |
|
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the alpha-D-phosphohexomutase superfamily. It is required for the interconversion of glucosamine-6-phosphate and glucosamine-1-phosphate in the biosynthetic pathway of UDP-N-acetylglucosamine, an essential precursor to components of the cell envelope. In order to be active, GlmM must be phosphorylated, which can occur via autophosphorylation or by the Ser/Thr kinase StkP. GlmM functions in a classical ping-pong bi-bi mechanism with glucosamine-1,6-diphosphate as an intermediate. Other members of the alpha-D-phosphohexomutase superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100095 Cd Length: 434 Bit Score: 94.86 E-value: 4.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 42 VVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMVycrntggRYGKATI---------------------E 100
Cdd:cd05802 40 VLIGKDTRISGYMLESALAAGLTSAGVDVLLLGVIPTPAVAYLT-------RKLRADAgvvisashnpfedngikffssD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 101 GYyqKLSKAfVEL---------------------TKQASCSGDEY-------------RSLKV--DCANG----IGALKL 140
Cdd:cd05802 113 GY--KLPDE-VEEeiealidkelelpptgekigrVYRIDDARGRYieflkstfpkdllSGLKIvlDCANGaaykVAPEVF 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 141 REMehyfsqGLSVQLFNDGSKG-KLNHLCGADFVKSHQKppqgmEIKSNERCC--SFDGDADRIVYYyhDADGhfHLIDG 217
Cdd:cd05802 190 REL------GAEVIVINNAPDGlNINVNCGSTHPESLQK-----AVLENGADLgiAFDGDADRVIAV--DEKG--NIVDG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 218 DKIATLISSFLKELlveiGESLNIGVVQTAYANGSSTRYLEEvMKVPVYCTKTGVKHLHHKAQE--FDIGVyfEANGHgt 295
Cdd:cd05802 255 DQILAICARDLKER----GRLKGNTVVGTVMSNLGLEKALKE-LGIKLVRTKVGDRYVLEEMLKhgANLGG--EQSGH-- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 296 alfstavemkikqsaeqledkkrkaakmlenIIDLFNQAAGDAISDMLVIEAILALKGLTVQQWDALYTDLPNRQLKVQV 375
Cdd:cd05802 326 -------------------------------IIFLDHSTTGDGLLTALQLLAIMKRSGKSLSELASDMKLYPQVLVNVRV 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 315707008 376 ADRRVISttdaerqavTPPGLQEAINDLVKKYKLS-RAFVRPSGTEDVVRVYAEADSQ 432
Cdd:cd05802 375 KDKKALL---------ENPRVQAAIAEAEKELGGEgRVLVRPSGTEPLIRVMVEGEDE 423
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
42-432 |
8.10e-15 |
|
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been characterized as the archaeal protein responsible for the second step of UDP-GlcNAc biosynthesis. This GlmM protein catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. The first-characterized bacterial GlmM protein is modeled by TIGR01455. These two families are members of the larger phosphoglucomutase/phosphomannomutase family (characterized by three domains: pfam02878, pfam02879 and pfam02880), but are not nearest neighbors to each other. This model also includes a number of sequences from non-archaea in the Bacteroides, Chlorobi, Chloroflexi, Planctomycetes and Spirochaetes lineages. Evidence supporting their inclusion in this equivalog as having the same activity comes from genomic context and phylogenetic profiling. A large number of these organisms are known to produce exo-polysaccharide and yet only appeared to contain the GlmS enzyme of the GlmSMU pathway for UDP-GlcNAc biosynthesis (GenProp0750). In some organisms including Leptospira, this archaeal GlmM is found adjacent to the GlmS as well as a putative GlmU non-orthologous homolog. Phylogenetic profiling of the GlmS-only pattern using PPP identifies members of this archaeal GlmM family as the highest-scoring result. [Central intermediary metabolism, Amino sugars]
Pssm-ID: 274906 Cd Length: 443 Bit Score: 76.01 E-value: 8.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 42 VVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYmvYCRNTGGRYG---------------K---------- 96
Cdd:TIGR03990 38 VVVGRDTRTSGPMLENAVIAGLLSTGCDVVDLGIAPTPTLQY--AVRELGADGGimitashnppeyngiKllnsdgtels 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 97 ----ATIEGYYQKLSKAFVELTKQASCSGDEY--------------------RSLKV--DCANGIGALK----LREMehy 146
Cdd:TIGR03990 116 reqeEEIEEIAESGDFERADWDEIGTVTSDEDaiddyieaildkvdveairkKGFKVvvDCGNGAGSLTtpylLREL--- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 147 fsqGLSVQLFNDGSKGK------------LNHLC------GADFVKSHqkppqgmeiksnerccsfDGDADRIVYYyhDA 208
Cdd:TIGR03990 193 ---GCKVITLNCQPDGTfpgrnpeptpenLKDLSalvkatGADLGIAH------------------DGDADRLVFI--DE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 209 DGHFhlIDGDKIATLissFLKELLVEIGESLnigVVqtayaNGSSTRYLEEVMK---VPVYCTKTGVKHLHHKAQEFDIG 285
Cdd:TIGR03990 250 KGRF--IGGDYTLAL---FAKYLLEHGGGKV---VT-----NVSSSRAVEDVAErhgGEVIRTKVGEVNVAEKMKEEGAV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 286 VYFEANGHgtalfstavemkikqsaeqledkkrkaakmlenIIDLFNQAAGDAISDMLVIEAILALKGLTVQQWDALYTD 365
Cdd:TIGR03990 317 FGGEGNGG---------------------------------WIFPDHHYCRDGLMAAALFLELLAEEGKPLSELLAELPK 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 366 LPNRQLKVQVADRRVISTTDAERQAVTppglQEAINDL--VK-KYKLSRAFVRPSGTEDVVRVYAEADSQ 432
Cdd:TIGR03990 364 YPMSKEKVELPDEDKEEVMEAVEEEFA----DAEIDTIdgVRiDFEDGWVLVRPSGTEPIVRIYAEAKTE 429
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
42-432 |
6.46e-14 |
|
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100089 Cd Length: 439 Bit Score: 73.37 E-value: 6.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 42 VVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYmvYCRNTG----------------------------GR 93
Cdd:cd03087 36 VVVGRDTRTSGPMLKNAVIAGLLSAGCDVIDIGIVPTPALQY--AVRKLGdagvmitashnppeyngiklvnpdgtefSR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 94 YGKATIEGYYqkLSKAF-------VELTKQASCSGDEY-------------RSLKV--DCANGIGALK----LREMehyf 147
Cdd:cd03087 114 EQEEEIEEII--FSERFrrvawdeVGSVRREDSAIDEYieaildkvdidggKGLKVvvDCGNGAGSLTtpylLREL---- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 148 sqGLSVQLFN---DG---------SKGKLNHLC------GADFVKSHqkppqgmeiksnerccsfDGDADRIVYYyhDAD 209
Cdd:cd03087 188 --GCKVITLNanpDGffpgrppepTPENLSELMelvratGADLGIAH------------------DGDADRAVFV--DEK 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 210 GHFhlIDGDKIATLISsflKELLVEIGeslniGVVQTAYangSSTRYLEEVMK---VPVYCTKTGVKHLHHKAQEFDIGV 286
Cdd:cd03087 246 GRF--IDGDKLLALLA---KYLLEEGG-----GKVVTPV---DASMLVEDVVEeagGEVIRTPVGDVHVAEEMIENGAVF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 287 YFEANGHG-TALFSTAVemkikqsaeqleDKKRKAAKMLEniidlfnqaagdaisdmLVIEAilalKGLtvqqwDALYTD 365
Cdd:cd03087 313 GGEPNGGWiFPDHQLCR------------DGIMTAALLLE-----------------LLAEE----KPL-----SELLDE 354
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 315707008 366 LPNRQLKvqvadRRVISTTDAERQAVtPPGLQEAINDLVKK------YKLSR----AFVRPSGTEDVVRVYAEADSQ 432
Cdd:cd03087 355 LPKYPLL-----REKVECPDEKKEEV-MEAVEEELSDADEDvdtidgVRIEYedgwVLIRPSGTEPKIRITAEAKTE 425
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
42-230 |
5.36e-08 |
|
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the reversible conversion of 1-phospho to 6-phospho-sugars (e.g. between mannose-1-phosphate and mannose-6-phosphate or glucose-1-phosphate and glucose-6-phosphate) via a bisphosphorylated sugar intermediate. The reaction involves two phosphoryl transfers, with an intervening 180 degree reorientation of the reaction intermediate during catalysis. Reorientation of the intermediate occurs without dissociation from the active site of the enzyme and is thus, a simple example of processivity, as defined by multiple rounds of catalysis without release of substrate. Glucose-6-phosphate and glucose-1-phosphate are known to be utilized for energy metabolism and cell surface construction, respectively. PMM/PGM belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the phosphoglucomutases (PGM1 and PGM2). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100091 Cd Length: 443 Bit Score: 54.83 E-value: 5.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 42 VVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHY-----------MV--------Y-----CRNTGGRYG-- 95
Cdd:cd03089 39 VVVGRDGRLSSPELAAALIEGLLAAGCDVIDIGLVPTPVLYFatfhldadggvMItashnppeYngfkiVIGGGPLSGed 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 96 ----KATIEGYYQKLSKAFVELTKQasCSGDEY------------RSLK--VDCANGIGALKLREMEhyfsQGL---SVQ 154
Cdd:cd03089 119 iqalRERAEKGDFAAATGRGSVEKV--DILPDYidrllsdiklgkRPLKvvVDAGNGAAGPIAPQLL----EALgceVIP 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 155 LFN--DGS----------KGKLNHLC------GADFvkshqkppqGMeiksnerccSFDGDADRIVYYyhDADGHFhlID 216
Cdd:cd03089 193 LFCepDGTfpnhhpdptdPENLEDLIaavkenGADL---------GI---------AFDGDGDRLGVV--DEKGEI--IW 250
|
250
....*....|....*
gi 315707008 217 GDKIATLISS-FLKE 230
Cdd:cd03089 251 GDRLLALFARdILKR 265
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
42-85 |
1.47e-07 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 50.30 E-value: 1.47e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 315707008 42 VVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMV 85
Cdd:pfam02878 43 VVVGRDTRYSSRELARALAAGLASNGVEVILLGLLPTPAVSFAT 86
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
394-434 |
3.09e-07 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 47.65 E-value: 3.09e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 315707008 394 PGLQEAINDLVKKYKL--SRAFVRPSGTEDVVRVYAEADSQVR 434
Cdd:pfam00408 16 AAILKVFADAEKILGEdgRRLDVRPSGTEPVLRVMVEGDSDEE 58
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
42-432 |
4.14e-06 |
|
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate guanyltransferase domain in a protein of unknown function that is found in both prokaryotes and eukaryotes. This domain belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100096 Cd Length: 445 Bit Score: 48.84 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 42 VVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHYMVycRNTG-------------------------GRY-- 94
Cdd:cd05803 40 IVVGRDGRPSGPMLEKIVIGALLACGCDVIDLGIAPTPTVQVLV--RQSQasggiiitashnppqwnglkfigpdGEFlt 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 95 ---GKATIEGYYQK---------------------------LSKAFVELTKQAScsgdeyRSLKV--DCANGIGALKLRE 142
Cdd:cd05803 118 pdeGEEVLSCAEAGsaqkagydqlgevtfsedaiaehidkvLALVDVDVIKIRE------RNFKVavDSVNGAGGLLIPR 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 143 MEHyfSQGLSVQLFNDGSKGKLNHlcgadfvkshqkPPQgmEIKSN---------ERCCSF----DGDADRIVyyyhdad 209
Cdd:cd05803 192 LLE--KLGCEVIVLNCEPTGLFPH------------TPE--PLPENltqlcaavkESGADVgfavDPDADRLA------- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 210 ghfhLIDGDKIA-----TLISSFLkELLVEIGESLNIGVvqtayaNGSSTRYLEEVMK---VPVYCTKTGVKHLHHKAQE 281
Cdd:cd05803 249 ----LVDEDGRPigeeyTLALAVD-YVLKYGGRKGPVVV------NLSTSRALEDIARkhgVPVFRSAVGEANVVEKMKE 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 282 FDIGVYFEANGhgtalfstavemkikqsaeqledkkrkaakmleNIIDLFNQAAGDAISDMLVIEAILALKGLTVQQWDA 361
Cdd:cd05803 318 VDAVIGGEGNG---------------------------------GVILPDVHYGRDSLVGIALVLQLLAASGKPLSEIVD 364
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 315707008 362 LYTDLPNRQLKVQVADR---RVISTTDAE---RQAVTPPGLQEAINDlvkkyklSRAFVRPSGTEDVVRVYAEADSQ 432
Cdd:cd05803 365 ELPQYYISKTKVTIAGEaleRLLKKLEAYfkdAEASTLDGLRLDSED-------SWVHVRPSNTEPIVRIIAEAPTQ 434
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
194-431 |
9.55e-05 |
|
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily and is found in both archaea and bacteria. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four structural domains (subdomains) with a centrally located active site formed by four loops, one from each subdomain. All four subdomains are included in this alignment model.
Pssm-ID: 100093 Cd Length: 461 Bit Score: 44.47 E-value: 9.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 194 FDGDADRI--VyyyhDADGHFhlIDGDKIATLISSFLKELLVEIGeslniGVVQTAyangSSTRYLEEVMK---VPVYCT 268
Cdd:cd05800 241 TDGDADRIgaV----DEKGNF--LDPNQILALLLDYLLENKGLRG-----PVVKTV----STTHLIDRIAEkhgLPVYET 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 269 KTGVKHLhhkaqefdigvyfeanghgtalfstavemkikqsaeqledkkrkAAKMLENIIDLFNQAAG-----------D 337
Cdd:cd05800 306 PVGFKYI--------------------------------------------AEKMLEEDVLIGGEESGglgirghiperD 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 338 AI-SDMLVIEAIlALKGLTVqqwDALYTDLpnrQLKVQVA--DRRVISTTDAERQAVT-----PPGLQEAINDLVK---- 405
Cdd:cd05800 342 GIlAGLLLLEAV-AKTGKPL---SELVAEL---EEEYGPSyyDRIDLRLTPAQKEAILeklknEPPLSIAGGKVDEvnti 414
|
250 260 270
....*....|....*....|....*....|..
gi 315707008 406 ---KYKL---SRAFVRPSGTEDVVRVYAEADS 431
Cdd:cd05800 415 dgvKLVLedgSWLLIRPSGTEPLLRIYAEAPS 446
|
|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
42-83 |
3.40e-04 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 42.66 E-value: 3.40e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 315707008 42 VVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHY 83
Cdd:PRK09542 38 VVIGHDMRDSSPELAAAFAEGVTAQGLDVVRIGLASTDQLYF 79
|
|
| PLN02371 |
PLN02371 |
phosphoglucosamine mutase family protein |
30-79 |
6.54e-04 |
|
phosphoglucosamine mutase family protein
Pssm-ID: 215211 [Multi-domain] Cd Length: 583 Bit Score: 41.97 E-value: 6.54e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 315707008 30 EKEAVNLQQDAFVVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTP 79
Cdd:PLN02371 106 EKKKADGSGELRVSVGRDPRISGPRLADAVFAGLASAGLDVVDMGLATTP 155
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
216-294 |
2.14e-03 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 37.81 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 315707008 216 DGDKIATLISSFLKELLVEIGeslNIGVVQTAyangSSTRYLEEVMK---VPVYCTKTGVKHLHHKAQEFDIGVYFEANG 292
Cdd:pfam02880 1 DGDQILALLAKYLLEQGKLPP---GAGVVKTV----MSSLGLDRVAKklgGKLVRTPVGDKYVKEKMREEGALFGGEESG 73
|
..
gi 315707008 293 HG 294
Cdd:pfam02880 74 HI 75
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
42-83 |
7.82e-03 |
|
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose 6-phosphate to mannose-1-phosphate in the second of three steps in the GDP-mannose pathway, in which GDP-D-mannose is synthesized from fructose-6-phosphate. In Mycobacterium tuberculosis, the causative agent of tuberculosis, PMM is involved in the biosynthesis of mannosylated lipoglycans that participate in the association of mycobacteria with host macrophage phagocytic receptors. ManB belongs to the the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include the phosphoglucomutases (PGM1 and PGM2), phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.
Pssm-ID: 100090 Cd Length: 459 Bit Score: 38.34 E-value: 7.82e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 315707008 42 VVIGRDTRPSSEKLSQSVIDGVTVLGGQFHDYGLLTTPQLHY 83
Cdd:cd03088 39 VAVGRDLRPSSPRIAAACAAALRDAGFRVVDCGAVPTPALAL 80
|
|
| |
