|
Name |
Accession |
Description |
Interval |
E-value |
| PRK15414 |
PRK15414 |
phosphomannomutase; |
2-447 |
0e+00 |
|
phosphomannomutase;
Pssm-ID: 185312 Cd Length: 456 Bit Score: 730.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 2 QLNCFKAYDIRGRIPDELNDEVAYRIGRAYAQFLQPGKVIVGRDVRLSSAGLCAALARGLTAGGADVIDIGLCGTEEVYF 81
Cdd:PRK15414 3 KLTCFKAYDIRGKLGEELNEDIAWRIGRAYGEFLKPKTIVLGGDVRLTSETLKLALAKGLQDAGVDVLDIGMSGTEEIYF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 82 ATFYSRADGGIMVTASHNPMDYNGMKLVREGSRPISGDSGLHEIRRLAEKGDFLPAERT--GTIETTDMKVPYIRHLLGY 159
Cdd:PRK15414 83 ATFHLGVDGGIEVTASHNPMDYNGMKLVREGARPISGDTGLRDVQRLAEANDFPPVDETkrGRYQQINLRDAYVDHLFGY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 160 IDATRLRPLKIVVNAGNGCAGPVLDFLERQL-----PFEVFKICHEPDGTFPNGIPNPLLPENRDITSQAVLEHGAALGI 234
Cdd:PRK15414 163 INVKNLTPLKLVINSGNGAAGPVVDAIEARFkalgaPVELIKVHNTPDGNFPNGIPNPLLPECRDDTRNAVIKHGADMGI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 235 AWDGDFDRCFLFDEQGRFIEGYYIVGLLAEAFLAREPGAKIIHDPRLTWNTIDMVHAAGGVPVMSKTGHAFIKERMRLED 314
Cdd:PRK15414 243 AFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKNPGAKIIHDPRLSWNTVDVVTAAGGTPVMSKTGHAFIKERMRKED 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 315 AAYGGEMSAHHYFRDFAYCDSGMIPWLLVLELMCRKRKLLSELVGERMAKFPASGEINRVLDDPQGALARVEAAYAPLGP 394
Cdd:PRK15414 323 AIYGGEMSAHHYFRDFAYCDSGMIPWLLVAELVCLKGKTLGELVRDRMAAFPASGEINSKLAQPVEAINRVEQHFSREAL 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1224026142 395 AIDRTDGLSMEFADWRFNLRSSNTEPVLRLNVESRGDAALMEAKTAELLALLD 447
Cdd:PRK15414 403 AVDRTDGISMTFADWRFNLRSSNTEPVVRLNVESRGDVPLMEARTRTLLTLLN 455
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
5-446 |
0e+00 |
|
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: 587.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 5 CFKAYDIRGRIPDELNDEVAYRIGRAYAQFLQ---PGKVIVGRDVRLSSAGLCAALARGLTAGGADVIDIGLCGTEEVYF 81
Cdd:cd03089 1 IFRAYDIRGIAGEELTEEIAYAIGRAFGSWLLekgAKKVVVGRDGRLSSPELAAALIEGLLAAGCDVIDIGLVPTPVLYF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 82 ATFYSRADGGIMVTASHNPMDYNGMKLVREGsRPISGDsGLHEIRRLAEKGDFLPAERTGTIETTDMKVPYIRHLLGYID 161
Cdd:cd03089 81 ATFHLDADGGVMITASHNPPEYNGFKIVIGG-GPLSGE-DIQALRERAEKGDFAAATGRGSVEKVDILPDYIDRLLSDIK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 162 AtRLRPLKIVVNAGNGCAGPVLDFLERQLPFEVFKICHEPDGTFPNGIPNPLLPENRDITSQAVLEHGAALGIAWDGDFD 241
Cdd:cd03089 159 L-GKRPLKVVVDAGNGAAGPIAPQLLEALGCEVIPLFCEPDGTFPNHHPDPTDPENLEDLIAAVKENGADLGIAFDGDGD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 242 RCFLFDEQGRFIEGYYIVGLLAEAFLAREPGAKIIHDPRLTWNTIDMVHAAGGVPVMSKTGHAFIKERMRLEDAAYGGEM 321
Cdd:cd03089 238 RLGVVDEKGEIIWGDRLLALFARDILKRNPGATIVYDVKCSRNLYDFIEEAGGKPIMWKTGHSFIKAKMKETGALLAGEM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 322 SAHHYFRD-FAYCDSGMIPWLLVLELMCRKRKLLSELVGERMaKFPASGEINRVL--DDPQGALARVEAAYAPLGPAIDR 398
Cdd:cd03089 318 SGHIFFKDrWYGFDDGIYAALRLLELLSKSGKTLSELLADLP-KYFSTPEIRIPVteEDKFAVIERLKEHFEFPGAEIID 396
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1224026142 399 TDGLSMEFADWRFNLRSSNTEPVLRLNVESRGDAALmEAKTAELLALL 446
Cdd:cd03089 397 IDGVRVDFEDGWGLVRASNTEPVLVLRFEADTEEGL-EEIKAELRKLL 443
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
4-448 |
3.50e-169 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 483.16 E-value: 3.50e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 4 NCFKAYDIRGRIPDELNDEVAYRIGRAYAQFLQP---GKVIVGRDVRLSSAGLCAALARGLTAGGADVIDIGLCGTEEVY 80
Cdd:COG1109 5 KLFGTDGIRGIVGEELTPEFVLKLGRAFGTYLKEkggPKVVVGRDTRLSSPMLARALAAGLASAGIDVYDLGLVPTPALA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 81 FATFYSRADGGIMVTASHNPMDYNGMKLVREGSRPISGDSgLHEIRRLAEKGDFLPAE--RTGTIETT-DMKVPYIRHLL 157
Cdd:COG1109 85 FAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEE-EKEIEALIEKEDFRRAEaeEIGKVTRIeDVLEAYIEALK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 158 GYID-ATRLRPLKIVVNAGNGCAGPVLDFLERQLPFEVFKICHEPDGTFPNGIPNPLlPENRDITSQAVLEHGAALGIAW 236
Cdd:COG1109 164 SLVDeALRLRGLKVVVDCGNGAAGGVAPRLLRELGAEVIVLNAEPDGNFPNHNPNPE-PENLEDLIEAVKETGADLGIAF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 237 DGDFDRCFLFDEQGRFIEGYYIVGLLAEAFLAREPGAKIIHDPRLTWNTIDMVHAAGGVPVMSKTGHAFIKERMRLEDAA 316
Cdd:COG1109 243 DGDADRLGVVDEKGRFLDGDQLLALLARYLLEKGPGGTVVVTVMSSLALEDIAEKHGGEVVRTKVGFKYIKEKMRETGAV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 317 YGGEMSAHHYFRDFAYCDSGMIPWLLVLELMCRKRKLLSELVgERMAKFPaSGEINRVLDD---PQGALARVEAAYAPLG 393
Cdd:COG1109 323 LGGEESGGIIFPDFVPTDDGILAALLLLELLAKQGKSLSELL-AELPRYP-QPEINVRVPDeekIGAVMEKLREAVEDKE 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1224026142 394 PaIDRTDGLSMEFADW-RFNLRSSNTEPVLRLNVESRgDAALMEAKTAELLALLDA 448
Cdd:COG1109 401 E-LDTIDGVKVDLEDGgWVLVRPSGTEPLLRVYAEAK-DEEEAEELLAELAELVEE 454
|
|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
6-449 |
2.86e-142 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 414.38 E-value: 2.86e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 6 FKAYDIRGRIPDELNDEVAYRIGRAYAQFLQP---GKVIVGRDVRLSSAGLCAALARGLTAGGADVIDIGLCGTEEVYFA 82
Cdd:PRK09542 1 IKAYDVRGVVGEQIDEDLVRDVGAAFARLMRAegaTTVVIGHDMRDSSPELAAAFAEGVTAQGLDVVRIGLASTDQLYFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 83 TfysradG-----GIMVTASHNPMDYNGMKLVREGSRPISGDSGLHEIRRLAEKGdfLPA--ERTGTIETTDMKVPYIRH 155
Cdd:PRK09542 81 S------GlldcpGAMFTASHNPAAYNGIKLCRAGAKPVGQDTGLAAIRDDLIAG--VPAydGPPGTVTERDVLADYAAF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 156 LLGYIDATRLRPLKIVVNAGNGCAGPVLDFLERQLPFEVFKICHEPDGTFPNGIPNPLLPEN-RDItSQAVLEHGAALGI 234
Cdd:PRK09542 153 LRSLVDLSGIRPLKVAVDAGNGMGGHTVPAVLGGLPITLLPLYFELDGTFPNHEANPLDPANlVDL-QAFVRETGADIGL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 235 AWDGDFDRCFLFDEQGRFIEGYYIVGLLAEAFLAREPGAKIIHDPRLTWNTIDMVHAAGGVPVMSKTGHAFIKERMRLED 314
Cdd:PRK09542 232 AFDGDADRCFVVDERGQPVSPSAVTALVAARELAREPGATIIHNLITSRAVPELVAERGGTPVRTRVGHSFIKALMAETG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 315 AAYGGEMSAHHYFRDFAYCDSGMIPWLLVLELMCRKRKLLSELVGErMAKFPASGEINRVLDDPQGALARVEAAYAPLGP 394
Cdd:PRK09542 312 AIFGGEHSAHYYFRDFWGADSGMLAALHVLAALGEQDRPLSELMAD-YQRYAASGEINSTVADAPARMEAVLKAFADRIV 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1224026142 395 AIDRTDGLSMEFAD--WrFNLRSSNTEPVLRLNVESRgDAALMEAKTAELLALLDAQ 449
Cdd:PRK09542 391 SVDHLDGVTVDLGDgsW-FNLRASNTEPLLRLNVEAR-TEEEVDALVDEVLAIIRAQ 445
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
1-429 |
1.08e-106 |
|
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: 323.31 E-value: 1.08e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 1 MQLncFKAYDIRGRIPDELNDEVAYRIGRAYAQFLQPGKVIVGRDVRLSSAGLCAALARGLTAGGADVIDIGLCGTEEVY 80
Cdd:TIGR03990 1 MLL--FGTSGIRGIVGEELTPELALKVGKAFGTYLRGGKVVVGRDTRTSGPMLENAVIAGLLSTGCDVVDLGIAPTPTLQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 81 FATFYSRADGGIMVTASHNPMDYNGMKLVREGSRPISGDSGlHEIRRLAEKGDFLPA--ERTGTIETT-DMKVPYIRHLL 157
Cdd:TIGR03990 79 YAVRELGADGGIMITASHNPPEYNGIKLLNSDGTELSREQE-EEIEEIAESGDFERAdwDEIGTVTSDeDAIDDYIEAIL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 158 GYIDATRLR--PLKIVVNAGNGCAGPVLDFLERQLPFEVFKICHEPDGTFPNGIPNPlLPENRDITSQAVLEHGAALGIA 235
Cdd:TIGR03990 158 DKVDVEAIRkkGFKVVVDCGNGAGSLTTPYLLRELGCKVITLNCQPDGTFPGRNPEP-TPENLKDLSALVKATGADLGIA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 236 WDGDFDRCFLFDEQGRFIEGYYIVGLLAEaFLAREPGAKIIhdprltwNTI-------DMVHAAGGVPVMSKTGHAFIKE 308
Cdd:TIGR03990 237 HDGDADRLVFIDEKGRFIGGDYTLALFAK-YLLEHGGGKVV-------TNVsssraveDVAERHGGEVIRTKVGEVNVAE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 309 RMRLEDAAYGGEMSAHHYFRDFAYCDSGMIPWLLVLELMCRKRKLLSELVgERMAKFPAS-GEINRVLDDPQGALARVEA 387
Cdd:TIGR03990 309 KMKEEGAVFGGEGNGGWIFPDHHYCRDGLMAAALFLELLAEEGKPLSELL-AELPKYPMSkEKVELPDEDKEEVMEAVEE 387
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1224026142 388 AYAPLgpAIDRTDGLSMEFADWRFNLRSSNTEPVLRLNVESR 429
Cdd:TIGR03990 388 EFADA--EIDTIDGVRIDFEDGWVLVRPSGTEPIVRIYAEAK 427
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
11-429 |
2.17e-81 |
|
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: 257.88 E-value: 2.17e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 11 IRGRIPDELNDEVAYRIGRAYAQFLQPGKVIVGRDVRLSSAGLCAALARGLTAGGADVIDIGLCGTEEVYFATfYSRADG 90
Cdd:cd03087 7 IRGVVGEELTPELALKVGKALGTYLGGGTVVVGRDTRTSGPMLKNAVIAGLLSAGCDVIDIGIVPTPALQYAV-RKLGDA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 91 GIMVTASHNPMDYNGMKLVREGSRPISgDSGLHEIRRLAEKGDFLPAE--RTGTIETTD-MKVPYIRHLLGYIDATRLRP 167
Cdd:cd03087 86 GVMITASHNPPEYNGIKLVNPDGTEFS-REQEEEIEEIIFSERFRRVAwdEVGSVRREDsAIDEYIEAILDKVDIDGGKG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 168 LKIVVNAGNGCAGPVLDFLERQLPFEVFKICHEPDGTFPNGIPNPlLPENRDITSQAVLEHGAALGIAWDGDFDRCFLFD 247
Cdd:cd03087 165 LKVVVDCGNGAGSLTTPYLLRELGCKVITLNANPDGFFPGRPPEP-TPENLSELMELVRATGADLGIAHDGDADRAVFVD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 248 EQGRFIEGYYIVGLLAEAFLAREPGaKIIhdprLTWNT----IDMVHAAGGVPVMSKTGHAFIKERMRLEDAAYGGEMSA 323
Cdd:cd03087 244 EKGRFIDGDKLLALLAKYLLEEGGG-KVV----TPVDAsmlvEDVVEEAGGEVIRTPVGDVHVAEEMIENGAVFGGEPNG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 324 HHYFRDFAYCDSGMIPWLLVLELMCRKRKlLSELVGERMAKFPASGEINRVLDDPQGALARVEAAYAPLGPAIDRTDGLS 403
Cdd:cd03087 319 GWIFPDHQLCRDGIMTAALLLELLAEEKP-LSELLDELPKYPLLREKVECPDEKKEEVMEAVEEELSDADEDVDTIDGVR 397
|
410 420
....*....|....*....|....*.
gi 1224026142 404 MEFADWRFNLRSSNTEPVLRLNVESR 429
Cdd:cd03087 398 IEYEDGWVLIRPSGTEPKIRITAEAK 423
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
11-444 |
6.12e-71 |
|
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: 230.83 E-value: 6.12e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 11 IRGRIPDELNDEVAYRIGRAYAQFL----QPGKVIVGRDVRLSSAGLCAALARGLTAGGADVIDIGLCGTEEVYFATFYS 86
Cdd:cd05802 7 IRGVANEPLTPELALKLGRAAGKVLgkggGRPKVLIGKDTRISGYMLESALAAGLTSAGVDVLLLGVIPTPAVAYLTRKL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 87 RADGGIMVTASHNPMDYNGMKLVREGSRPISgDSGLHEIRRLAEKGDFLPAERTG---TIETTDMKVPYIRHLLGYIDAT 163
Cdd:cd05802 87 RADAGVVISASHNPFEDNGIKFFSSDGYKLP-DEVEEEIEALIDKELELPPTGEKigrVYRIDDARGRYIEFLKSTFPKD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 164 RLRPLKIVVNAGNG----CAGPVLdfleRQLPFEVFKICHEPDG---------TFPNGIpnpllpenrditSQAVLEHGA 230
Cdd:cd05802 166 LLSGLKIVLDCANGaaykVAPEVF----RELGAEVIVINNAPDGlninvncgsTHPESL------------QKAVLENGA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 231 ALGIAWDGDFDRCFLFDEQGRFIEGYYIVGLLAEAFLAREpgakiihdpRLTWNTI--------DMVHA---AGGVPVMS 299
Cdd:cd05802 230 DLGIAFDGDADRVIAVDEKGNIVDGDQILAICARDLKERG---------RLKGNTVvgtvmsnlGLEKAlkeLGIKLVRT 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 300 KTGHAFIKERMRLEDAAYGGEMSAHHYFRDFAYCDSGMIPWLLVLELMCRKRKLLSELVGErMAKFP------------A 367
Cdd:cd05802 301 KVGDRYVLEEMLKHGANLGGEQSGHIIFLDHSTTGDGLLTALQLLAIMKRSGKSLSELASD-MKLYPqvlvnvrvkdkkA 379
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1224026142 368 SGEINRVlddpQGALARVEAAYAPLGpaidrtdglsmefadwRFNLRSSNTEPVLRLNVESRgDAALMEaKTAELLA 444
Cdd:cd05802 380 LLENPRV----QAAIAEAEKELGGEG----------------RVLVRPSGTEPLIRVMVEGE-DEELVE-KLAEELA 434
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
11-444 |
4.49e-67 |
|
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: 221.03 E-value: 4.49e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 11 IRGRIPDELNDEVAYRIGRAYAQFL----QPGKVIVGRDVRLSSAGLCAALARGLTAGGADVIDIGLCGTEEVYFATFYS 86
Cdd:cd05803 7 IRGIVGEGLTPEVITRYVAAFATWQpertKGGKIVVGRDGRPSGPMLEKIVIGALLACGCDVIDLGIAPTPTVQVLVRQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 87 RADGGIMVTASHNPMDYNGMKLVREGSRPISGDSGlHEIRRLAEKGDFLPA--ERTGTIE-TTDMKVPYIRHLLGYID-- 161
Cdd:cd05803 87 QASGGIIITASHNPPQWNGLKFIGPDGEFLTPDEG-EEVLSCAEAGSAQKAgyDQLGEVTfSEDAIAEHIDKVLALVDvd 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 162 --ATRLRPLKIVVNAGNGCAGPVLDFLERQLPFEVFKICHEPDGTFPNgIPNPlLPENRDITSQAVLEHGAALGIAWDGD 239
Cdd:cd05803 166 viKIRERNFKVAVDSVNGAGGLLIPRLLEKLGCEVIVLNCEPTGLFPH-TPEP-LPENLTQLCAAVKESGADVGFAVDPD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 240 FDRCFLFDEQGRFIEGYYIVGLLAEAFLAREPGAKIIHDPRLTWNTIDMVHAAGGVPVM-SKTGHAFIKERMRLEDAAYG 318
Cdd:cd05803 244 ADRLALVDEDGRPIGEEYTLALAVDYVLKYGGRKGPVVVNLSTSRALEDIARKHGVPVFrSAVGEANVVEKMKEVDAVIG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 319 GE------MSAHHYFRDfAYcdSGMIpwlLVLELMCRKRKLLSELVGERMAKFPASGEINRVLDDPQGALARVEAAYApl 392
Cdd:cd05803 324 GEgnggviLPDVHYGRD-SL--VGIA---LVLQLLAASGKPLSEIVDELPQYYISKTKVTIAGEALERLLKKLEAYFK-- 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1224026142 393 GPAIDRTDGLSMEFADWRFNLRSSNTEPVLRLNVESRgdaalmEAKTAELLA 444
Cdd:cd05803 396 DAEASTLDGLRLDSEDSWVHVRPSNTEPIVRIIAEAP------TQDEAEALA 441
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
12-448 |
6.11e-52 |
|
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: 181.60 E-value: 6.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 12 RGRIPDELNDEVAYRIGRAYAQFLQ-----PGKVIVGRDVRLSSAGLCAALARGLTAGGADVIDI-GLCGTEEVYFATFY 85
Cdd:cd05800 9 RGIIAEDFTFENVRRVAQAIADYLKeegggGRGVVVGYDTRFLSEEFARAVAEVLAANGIDVYLSdRPVPTPAVSWAVKK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 86 SRADGGIMVTASHNPMDYNGMKLVREGSRPISgDSGLHEIRRLAEKGD--FLPAERTGTIETTDMKVPYIRHLLGYIDAT 163
Cdd:cd05800 89 LGAAGGVMITASHNPPEYNGVKVKPAFGGSAL-PEITAAIEARLASGEppGLEARAEGLIETIDPKPDYLEALRSLVDLE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 164 RLRP--LKIVVNAGNGCAGPVLDFLERQLPFEVFKICHEPDGTFPNGIPNPLlPENRDITSQAVLEHGAALGIAWDGDFD 241
Cdd:cd05800 168 AIREagLKVVVDPMYGAGAGYLEELLRGAGVDVEEIRAERDPLFGGIPPEPI-EKNLGELAEAVKEGGADLGLATDGDAD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 242 RCFLFDEQGRFIEGYYIVGLLAeAFLAREPG-----AKIIHdprlTWNTIDMVHAAGGVPVM-SKTGHAFIKERMRLEDA 315
Cdd:cd05800 247 RIGAVDEKGNFLDPNQILALLL-DYLLENKGlrgpvVKTVS----TTHLIDRIAEKHGLPVYeTPVGFKYIAEKMLEEDV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 316 AYGGEMSAHHYFRDFAYCDSGMIPWLLVLELMCRKRKLLSELVGERMAKFPAS--GEINRVLDDPQGA--LARVEAAYAP 391
Cdd:cd05800 322 LIGGEESGGLGIRGHIPERDGILAGLLLLEAVAKTGKPLSELVAELEEEYGPSyyDRIDLRLTPAQKEaiLEKLKNEPPL 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1224026142 392 LGPA-----IDRTDGLSMEFAD--WrFNLRSSNTEPVLRLNVesrgdaalmEAKTAELL-ALLDA 448
Cdd:cd05800 402 SIAGgkvdeVNTIDGVKLVLEDgsW-LLIRPSGTEPLLRIYA---------EAPSPEKVeALLDA 456
|
|
| PLN02371 |
PLN02371 |
phosphoglucosamine mutase family protein |
10-435 |
2.68e-48 |
|
phosphoglucosamine mutase family protein
Pssm-ID: 215211 [Multi-domain] Cd Length: 583 Bit Score: 174.09 E-value: 2.68e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 10 DIRG--------RIPDeLNDEVAYRIGRAYAQFL---------QPGKVIVGRDVRLSSAGLCAALARGLTAGGADVIDIG 72
Cdd:PLN02371 72 DIRGvavegvegEPVT-LTPPAVEAIGAAFAEWLlekkkadgsGELRVSVGRDPRISGPRLADAVFAGLASAGLDVVDMG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 73 LCGTEEVYFATFYSRADG--GIMVTASHNPMDYNGMKL-VREG--SRPISGDSGLHEIRRLAEKGDFLPAERTGTIETTD 147
Cdd:PLN02371 151 LATTPAMFMSTLTEREDYdaPIMITASHLPYNRNGLKFfTKDGglGKPDIKDILERAARIYKEWSDEGLLKSSSGASSVV 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 148 MKVPY-----------IRHLLGYIDA--TRLRPLKIVVNAGNGCAGPVLDFLERQLPFEVFKICH-EPDGTFPNGIPNPL 213
Cdd:PLN02371 231 CRVDFmstyakhlrdaIKEGVGHPTNyeTPLEGFKIVVDAGNGAGGFFAEKVLEPLGADTSGSLFlEPDGMFPNHIPNPE 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 214 LPENRDITSQAVLEHGAALGIAWDGDFDRCFLFDEQGRFIEGYYIVGLLAEAFLAREPGAKIIHDPRLTWNTIDMVHAAG 293
Cdd:PLN02371 311 DKAAMSATTQAVLANKADLGIIFDTDVDRSAVVDSSGREINRNRLIALMSAIVLEEHPGTTIVTDSVTSDGLTTFIEKKG 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 294 GVPVMSKTGHA-FIKERMRL----EDAAYGGEMSAH------HYFRDFAYCdsgMIPwllVLELMCRKRKL-----LSEL 357
Cdd:PLN02371 391 GKHHRFKRGYKnVIDKGVRLnsdgEETHLMIETSGHgalkenHFLDDGAYL---AVK---IIIELVRMRAAgagggLGDL 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 358 VgERMAKFPASGEIN-RVLDDPQGALARVEAAYAPLGPAIDRTDGLSMEFAD---WR-----------FNLRSSNTEPVL 422
Cdd:PLN02371 465 I-EDLEEPLEAVELRlKILDEGKDFKAYGEEVLEHLRNSIESDGKLEGAPVNyegVRvsdegegfggwFLLRQSLHDPVI 543
|
490
....*....|....*
gi 1224026142 423 RLNVES--RGDAALM 435
Cdd:PLN02371 544 PLNIESssPGGAQKM 558
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
6-440 |
4.76e-45 |
|
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: 160.21 E-value: 4.76e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 6 FKAYDIRGRIPDELNDEVAYRIGRAYaqflqpgkvivgrdvrlssaglcaalargltaggadvidiglcGTEevyfatfy 85
Cdd:cd03084 2 FGTSGVRGVVGDDITPETAVALGQAI-------------------------------------------GST-------- 30
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 86 sradGGIMVTASHNPMDYNGMKLVREGSRPISGDsglHE--IRRLAEKGD---FLPAERTGTIETTDMKVPYIRHLLGYI 160
Cdd:cd03084 31 ----GGIMITASHNPPEDNGIKFVDPDGEPIASE---EEkaIEDLAEKEDepsAVAYELGGSVKAVDILQRYFEALKKLF 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 161 D--ATRLRPLKIVVNAGNGCAGPVLDFLERQLPFEVFKICHEPDGTFPNGIPNPLLPENRDITSQAVLEHGAALGIAWDG 238
Cdd:cd03084 104 DvaALSNKKFKVVVDSVNGVGGPIAPQLLEKLGAEVIPLNCEPDGNFGNINPDPGSETNLKQLLAVVKAEKADFGVAFDG 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 239 DFDRCFLFDEQGRFIEGYYIVGLLA-EAFLAREPGAKIIHDPRLTWNTIDMVHAAGGVPVMSKTGHAFIKERMRLEDAAY 317
Cdd:cd03084 184 DADRLIVVDENGGFLDGDELLALLAvELFLTFNPRGGVVKTVVSSGALDKVAKKLGIKVIRTKTGFKWVGEAMQEGDVVL 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 318 GGEMSAHHYFRDFAYCDSGMIPWLLVLELMCRKRKLLSELVGErmakFPAsgeinrvlddpqgalarveaayaplgPAID 397
Cdd:cd03084 264 GGEESGGVIFPEFHPGRDGISAALLLLEILANLGKSLSELFSE----LPR--------------------------YYYI 313
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1224026142 398 RTDglsmefADWRFNLRSSNTEPVLRLNVESRGDAALMEAKTA 440
Cdd:cd03084 314 RLK------VRGWVLVRASGTEPAIRIYAEADTQEDVEQIKKE 350
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
6-135 |
1.57e-42 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 146.60 E-value: 1.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 6 FKAYDIRGRIP-DELNDEVAYRIGRAYAQFLQP----GKVIVGRDVRLSSAGLCAALARGLTAGGADVIDIGLCGTEEVY 80
Cdd:pfam02878 4 FGTSGIRGKVGvGELTPEFALKLGQAIASYLRAqgggGKVVVGRDTRYSSRELARALAAGLASNGVEVILLGLLPTPAVS 83
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1224026142 81 FATFYSRADGGIMVTASHNPMDYNGMKLVREGSRPISGDSgLHEIRRLAEKGDFL 135
Cdd:pfam02878 84 FATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEV-EKKIEAIIEKEDFY 137
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
254-365 |
1.49e-34 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 124.87 E-value: 1.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 254 EGYYIVGLLAEAFLAR---EPGAKIIHDPRLTWNTIDMVHAAGGVPVMSKTGHAFIKERMRLEDAAYGGEMSAHHYFRDF 330
Cdd:pfam02880 1 DGDQILALLAKYLLEQgklPPGAGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEGALFGGEESGHIIFLDH 80
|
90 100 110
....*....|....*....|....*....|....*
gi 1224026142 331 AYCDSGMIPWLLVLELMCRKRKLLSELVGERMAKF 365
Cdd:pfam02880 81 ATTKDGILAALLVLEILARTGKSLSELLEELPEKY 115
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
23-444 |
5.16e-31 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 123.71 E-value: 5.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 23 VAYRIGRAYAQFLQPgKVIVGRDVRLSSAGLCAALARGLTAGGADVIDIGLCGTEEVYFATFYSRADGGIMVTASHNPMD 102
Cdd:PRK10887 26 LGWAAGKVLARQGRP-KVLIGKDTRISGYMLESALEAGLAAAGVDVLLTGPMPTPAVAYLTRTLRAEAGIVISASHNPYY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 103 YNGMKLvregsrpISGDsglheirrlaekGDFLPAERTGTIET---TDMK-VPYirHLLG-----------YID------ 161
Cdd:PRK10887 105 DNGIKF-------FSAD------------GTKLPDEVELAIEAeldKPLTcVES--AELGkasrindaagrYIEfckstf 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 162 --ATRLRPLKIVVNAGNGC----AGPVLdfleRQLPFEVFKICHEPDGTFPN---GIPNPllpenrDITSQAVLEHGAAL 232
Cdd:PRK10887 164 pnELSLRGLKIVVDCANGAtyhiAPNVF----RELGAEVIAIGCEPNGLNINdecGATDP------EALQAAVLAEKADL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 233 GIAWDGDFDRCFLFDEQGRFIEGYYIVGLLAEAFLAREpgakiihdpRL------TWNT-IDMVHA--AGGVP-VMSKTG 302
Cdd:PRK10887 234 GIAFDGDGDRVIMVDHLGNLVDGDQLLYIIARDRLRRG---------QLrggvvgTLMSnMGLELAlkQLGIPfVRAKVG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 303 HAFIKERMRLEDAAYGGEMSAHHYFRDFAYCDSGMIPWLLVLELMCRKRKLLSELVgERMAKFP--------ASGEINRV 374
Cdd:PRK10887 305 DRYVLEKLQEKGWRLGGENSGHILCLDKTTTGDGIVAALQVLAAMVRSGMSLADLC-SGMKLFPqvlinvrfKPGADDPL 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1224026142 375 LDDP-QGALARVEAAYAPLGpaidrtdglsmefadwRFNLRSSNTEPVLRLNVESRgDAALMEAkTAELLA 444
Cdd:PRK10887 384 ESEAvKAALAEVEAELGGRG----------------RVLLRKSGTEPLIRVMVEGE-DEAQVTA-LAERIA 436
|
|
| MPG1_transferase |
cd05805 |
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose ... |
6-360 |
1.93e-27 |
|
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose pyrophosphorylase, is a bifunctional enzyme with both phosphomannose isomerase (PMI) activity and GDP-mannose phosphorylase (GMP) activity. The protein contains an N-terminal NTP transferase domain, an L-beta-H domain, and a C-terminal PGM-like domain that belongs to the alpha-D-phosphohexomutase superfamily. This subfamily is limited to bacteria and archaea. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Members of this group appear to lack conserved residues necessary for metal binding and catalytic activity. Other 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: 100097 Cd Length: 441 Bit Score: 113.50 E-value: 1.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 6 FKAYDIRGRIPDELNDEVAYRIGRAYAQFLQPG-KVIVGRDVRLSSAGLCAALARGLTAGGADVIDIGLCGTEEVYFATF 84
Cdd:cd05805 2 FGGRGVSGLINVDITPEFATRLGAAYGSTLPPGsTVTVSRDASRASRMLKRALISGLLSTGVNVRDLGALPLPVARYAIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 85 YSRADGGIMV-TASHNP-------MDYNGMKLVREGSRPISGDSGLHEIRRlAEKGDFLPaertgTIETTDMKVPYIRHL 156
Cdd:cd05805 82 FLGASGGIHVrTSPDDPdkveiefFDSRGLNISRAMERKIENAFFREDFRR-AHVDEIGD-----ITEPPDFVEYYIRGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 157 LGYIDATRLR--PLKIVVNAGNGCAGPVLDFLERQLPFEVfkichepdGTFPN----GIPNPLLPENRDIT--SQAVLEH 228
Cdd:cd05805 156 LRALDTSGLKksGLKVVIDYAYGVAGIVLPGLLSRLGCDV--------VILNArldeDAPRTDTERQRSLDrlGRIVKAL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 229 GAALGIAWDGDFDRCFLFDEQGRFIEGYYIVGLLAEAFLAREPGAKI---IHDPRLtwnTIDMVHAAGGVPVMSKTGHAF 305
Cdd:cd05805 228 GADFGVIIDPNGERLILVDEAGRVISDDLLTALVSLLVLKSEPGGTVvvpVTAPSV---IEQLAERYGGRVIRTKTSPQA 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1224026142 306 IKERMrLEDAAYGGEMSAHHYFRDFAYCDSGMIPWLLVLELMCRKRKLLSELVGE 360
Cdd:cd05805 305 LMEAA-LENVVLAGDGDGGFIFPEFHPGFDAIAALVKILEMLARTNISLSQIVDE 358
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
151-250 |
1.71e-24 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 96.98 E-value: 1.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 151 PYIRHLLGYIDATRL--RPLKIVVNAGNGCAGPVLDFLERQLPFEVFKICHEPDGTFPNGIPNPLLPENRDITSQAVLEH 228
Cdd:pfam02879 1 AYIDHLLELVDSEALkkRGLKVVYDPLHGVGGGYLPELLKRLGCDVVEENCEPDPDFPTRAPNPEEPEALALLIELVKSV 80
|
90 100
....*....|....*....|..
gi 1224026142 229 GAALGIAWDGDFDRCFLFDEQG 250
Cdd:pfam02879 81 GADLGIATDGDADRLGVVDERG 102
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
12-445 |
3.63e-19 |
|
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: 89.57 E-value: 3.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 12 RGRIPDeLNDEVAYRIGRAYAQFLQ---PG-KVIVGRDVRLSSAGLCAALARGLTAGGADVIDIGLCGTEEVyfaTFYSR 87
Cdd:cd03088 8 RGLVTD-LTDEVCYAYTRAFLQHLEskfPGdTVAVGRDLRPSSPRIAAACAAALRDAGFRVVDCGAVPTPAL---ALYAM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 88 ADG--GIMVTASHNPMDYNGMKLVREGSRpISGDSglhEIRRLAEKGDFLPA--ERTGTIETTDMKV--PYIRHLLGYID 161
Cdd:cd03088 84 KRGapAIMVTGSHIPADRNGLKFYRPDGE-ITKAD---EAAILAALVELPEAlfDPAGALLPPDTDAadAYIARYTDFFG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 162 ATRLRPLKIVVNAGNGCAGPVLDFLERQLPFEVfkICHEPDGTFpngIP---NPLLPENRDITSQAVLEHGAALGIAWDG 238
Cdd:cd03088 160 AGALKGLRIGVYQHSSVGRDLLVRILEALGAEV--VPLGRSDTF---IPvdtEAVRPEDRALAAAWAAEHGLDAIVSTDG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 239 DFDRCFLFDEQGRFIEGyYIVGLLAEAFLarepGAKIIHDPrLTWNTidMVHAAGGVPVMSKT--GHAFIKERMRLEDA- 315
Cdd:cd03088 235 DGDRPLVADETGEWLRG-DILGLLTARFL----GADTVVTP-VSSNS--AIELSGFFKRVVRTriGSPYVIAAMAEAAAa 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 316 ---------AYGGEMSAhhyfrDFAYCDSG----------MIPWLLVLELMCRKRKLLSELVGE---------RMAKFP- 366
Cdd:cd03088 307 gagrvvgyeANGGFLLG-----SDIERNGRtlkalptrdaVLPILAVLAAAKEAGIPLSELVASlparftasdRLQNFPt 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 367 -ASGE-INRVLDDPQGALARVEAAYAPLGpAIDRTDGLSMEFADWRF-NLRSSNTEPVLRLNVEsrgdaALMEAKTAELL 443
Cdd:cd03088 382 eKSQAlIARLSADPEARAAFFFALGGEVA-SIDTTDGLRMTFANGDIvHLRPSGNAPELRCYVE-----ADSEERARELL 455
|
..
gi 1224026142 444 AL 445
Cdd:cd03088 456 AR 457
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
11-444 |
5.14e-19 |
|
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The mammalian PGM2 is thought to be a phosphopentomutase that catalyzes the conversion of the nucleoside breakdown products, ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. PGM2L1 is thought to catalyze the 1,3-bisphosphoglycerate-dependent synthesis of glucose 1,6-bisphosphate and other aldose-bisphosphates that serve as cofactors for several sugar phosphomutases and possibly also as regulators of glycolytic enzymes. PGM2 and PGM2L1 belong 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 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: 100092 Cd Length: 487 Bit Score: 89.10 E-value: 5.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 11 IRGRI---PDELNDEVAYRIGRAYAQFL-------QPGKVIVGRDVRLSSAGLCAALARGLTAGGADVI--DiGLCGTEE 78
Cdd:cd05799 9 LRGKMgagTNRMNDYTVRQATQGLANYLkkkgpdaKNRGVVIGYDSRHNSREFAELTAAVLAANGIKVYlfD-DLRPTPL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 79 VYFATFYSRADGGIMVTASHNPMDYNGMKLVRE-GSRPISGDSGL--HEIRRLAE--KGDFLPAERTGTIETTDMKV--P 151
Cdd:cd05799 88 LSFAVRHLGADAGIMITASHNPKEYNGYKVYWEdGAQIIPPHDAEiaEEIEAVLEplDIKFEEALDSGLIKYIGEEIddA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 152 YI---RHLLGYIDATRLRPLKIVVNAGNGCAG-PVLDFLER---QLPFEVFKIChEPDGTFPN-GIPNPLLPENRDITSQ 223
Cdd:cd05799 168 YLeavKKLLVNPELNEGKDLKIVYTPLHGVGGkFVPRALKEagfTNVIVVEEQA-EPDPDFPTvKFPNPEEPGALDLAIE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 224 AVLEHGAALGIAWDGDFDRCFLF--DEQGRFIE----------GYYIVGLLAEAFLAREPGAkIIhdprltwNTI----- 286
Cdd:cd05799 247 LAKKVGADLILATDPDADRLGVAvkDKDGEWRLltgneigallADYLLEQRKEKGKLPKNPV-IV-------KTIvssel 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 287 --DMVHAAGGVPVMSKTGHAFIKERMR-LEDAAY----GGEMSAHHYFRDFAYCDSGMIPWLLVLELMC---RKRKLLSE 356
Cdd:cd05799 319 lrKIAKKYGVKVEETLTGFKWIGNKIEeLESGGKkflfGFEESIGYLVGPFVRDKDGISAAALLAEMAAylkAQGKTLLD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 357 LVGERMAKFP--ASGEINRVLDDPQGAlARVEAAYAPLgpaIDRTDGLSMEFADW-RFNLRSSNTEPVLRLNVESRG--D 431
Cdd:cd05799 399 RLDELYEKYGyyKEKTISITFEGKEGP-EKIKAIMDRL---RNNPNVLTFYLEDGsRVTVRPSGTEPKIKFYIEVVGkkT 474
|
490
....*....|...
gi 1224026142 432 AALMEAKTAELLA 444
Cdd:cd05799 475 LEEAEKKLDALKK 487
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
370-445 |
6.22e-09 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 52.27 E-value: 6.22e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1224026142 370 EINRVLDDPQgALARVEAAYAPL--GPAIDRTDGlsmefadWRFNLRSSNTEPVLRLNVESRGDAALMEAKTAELLAL 445
Cdd:pfam00408 1 LINVRVAEKK-KLAALAAILKVFadAEKILGEDG-------RRLDVRPSGTEPVLRVMVEGDSDEELARLADEIADLL 70
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
31-242 |
5.91e-07 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 51.61 E-value: 5.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 31 YAQFLQPGKVIVGRDVRLSSAGLCAALARGLTAGGADVIDIG-LCGTEEVYFATFYSRADGGIMVTASHNPMDYNGMKLV 109
Cdd:PTZ00150 83 FGQALKSRGVVIGYDGRYHSRRFAEITASVFLSKGFKVYLFGqTVPTPFVPYAVRKLKCLAGVMVTASHNPKEDNGYKVY 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 110 RE-GSRPISG-DSGLheirrlaekGDFLPAERT------GTIETTDMKVPYIRHLLGYIDATRLR---------PLKIVV 172
Cdd:PTZ00150 163 WSnGAQIIPPhDKNI---------SAKILSNLEpwssswEYLTETLVEDPLAEVSDAYFATLKSEynpaccdrsKVKIVY 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 173 NAGNGCAGPVLdflerQLPFEVFKICH--------EPDGTFPN-GIPNPllPENR---DITSQAVLEHGAALGIAWDGDF 240
Cdd:PTZ00150 234 TAMHGVGTRFV-----QKALHTVGLPNllsvaqqaEPDPEFPTvTFPNP--EEGKgalKLSMETAEAHGSTVVLANDPDA 306
|
..
gi 1224026142 241 DR 242
Cdd:PTZ00150 307 DR 308
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
36-263 |
4.82e-06 |
|
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: 48.74 E-value: 4.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 36 QPGKVIVGRDVRLSSAGLCAALARGLTAGGADVIDIGLCGTEEVYFATfYSRADGGIMVTASHnPMDYNgmKLVregsrp 115
Cdd:cd03086 101 VPANVFVGRDTRPSGPALLQALLDGLKALGGNVIDYGLVTTPQLHYLV-RAANTEGAYGEPTE-EGYYE--KLS------ 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 116 isgdSGLHEIRRLAEKGDflpaertgtiettdmkvpyirhllgyidatrLRPLKIVVNAGNGCAGPVLDFLERQLPFEV- 194
Cdd:cd03086 171 ----KAFNELYNLLQDGG-------------------------------DEPEKLVVDCANGVGALKLKELLKRLKKGLs 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1224026142 195 FKICHEPDGTfpngiPNPL--------------LPenRDITSQAVLEHGAALgiawDGDFDR--CFLFDEQGRF--IEGY 256
Cdd:cd03086 216 VKIINDGEEG-----PELLndgcgadyvktkqkPP--RGFELKPPGVRCCSF----DGDADRlvYFYPDSSNKFhlLDGD 284
|
....*..
gi 1224026142 257 YIVGLLA 263
Cdd:cd03086 285 KIATLFA 291
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
80-109 |
9.52e-06 |
|
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: 47.97 E-value: 9.52e-06
10 20 30
....*....|....*....|....*....|....
gi 1224026142 80 YFATFYSRADG----GIMVTASHNPMDYNGMKLV 109
Cdd:cd03086 23 ILAALRSKKLGgktiGVMITASHNPVEDNGVKIV 56
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
36-102 |
4.60e-04 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 42.70 E-value: 4.60e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1224026142 36 QPGKVIVGRDVRLSSAGLCAALARGLTAGGADVIDIGLCGTEEVYFatfysradggiMVTASHNPMD 102
Cdd:PLN02895 126 PPAEVLLGRDTRPSGPALLAAALKGVRAIGARAVDMGILTTPQLHW-----------MVRAANKGMK 181
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
91-109 |
6.57e-04 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 41.93 E-value: 6.57e-04
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
80-109 |
2.57e-03 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 40.02 E-value: 2.57e-03
10 20 30
....*....|....*....|....*....|
gi 1224026142 80 YFATFYSRADGGIMVTASHNPMDYNGMKLV 109
Cdd:PTZ00302 67 GKRAKRGNKSVGVMITASHNPIQDNGVKII 96
|
|
| |
