|
Name |
Accession |
Description |
Interval |
E-value |
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
12-451 |
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: 741.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 12 IFRAYDIRGVVGDTLTAETAYWIGRAIGSESLARGEPCVAVGRDGRLSGPELVKQLIQGLVDCGCQVSDVGMVPTPVLYY 91
Cdd:cd03089 1 IFRAYDIRGIAGEELTEEIAYAIGRAFGSWLLEKGAKKVVVGRDGRLSSPELAAALIEGLLAAGCDVIDIGLVPTPVLYF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 92 AANVLEGKSGVMLTGDHNPPDYNGFKIVVAGETLANEQIQALRERIEKNDLA--SGVGSVEQVDILPRYFKQIRDDIAMA 169
Cdd:cd03089 81 ATFHLDADGGVMITASHNPPEYNGFKIVIGGGPLSGEDIQALRERAEKGDFAaaTGRGSVEKVDILPDYIDRLLSDIKLG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 170 -KPMKVVVDCGNGVAGVIAPQLIEALGCSVIPLYCEVDGNFPNHHPDPGKPENLKDLIAKVKAENADLGLAFDGDGDRVG 248
Cdd:cd03089 161 kRPLKVVVDAGNGAAGPIAPQLLEALGCEVIPLFCEPDGTFPNHHPDPTDPENLEDLIAAVKENGADLGIAFDGDGDRLG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 249 VVTNTGTIIYPDRLLMLFAKDVVSRNPGADIIFDVKCTRRLIALISGYGGRPVMWKTGHSLIKKKMKETGALLAGEMSGH 328
Cdd:cd03089 241 VVDEKGEIIWGDRLLALFARDILKRNPGATIVYDVKCSRNLYDFIEEAGGKPIMWKTGHSFIKAKMKETGALLAGEMSGH 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 329 VFFKERWFGFDDGIYSAARLLEILSQDQRDSEHVFSAFPSDISTPEINITVTEDSKFAIIEALQRDAQWGEGNITTLDGV 408
Cdd:cd03089 321 IFFKDRWYGFDDGIYAALRLLELLSKSGKTLSELLADLPKYFSTPEIRIPVTEEDKFAVIERLKEHFEFPGAEIIDIDGV 400
|
410 420 430 440
....*....|....*....|....*....|....*....|...
2FKM_X 409 RVDYPKGWGLVRASNTTPVLVLRFEADTEEELERIKTVFRNQL 451
Cdd:cd03089 401 RVDFEDGWGLVRASNTEPVLVLRFEADTEEGLEEIKAELRKLL 443
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
9-454 |
0e+00 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 540.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 9 PASIFRAYDIRGVVGDTLTAETAYWIGRAIGSESLARGEPCVAVGRDGRLSGPELVKQLIQGLVDCGCQVSDVGMVPTPV 88
Cdd:COG1109 3 YKKLFGTDGIRGIVGEELTPEFVLKLGRAFGTYLKEKGGPKVVVGRDTRLSSPMLARALAAGLASAGIDVYDLGLVPTPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 89 LYYAANVLEGKSGVMLTGDHNPPDYNGFKIVVA-GETLANEQIQALRERIEKNDL----ASGVGSVEQV-DILPRYFKQI 162
Cdd:COG1109 83 LAFAVRHLGADGGIMITASHNPPEYNGIKFFDAdGGKLSPEEEKEIEALIEKEDFrraeAEEIGKVTRIeDVLEAYIEAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 163 RDDIAMA---KPMKVVVDCGNGVAGVIAPQLIEALGCSVIPLYCEVDGNFPNHHPDPgKPENLKDLIAKVKAENADLGLA 239
Cdd:COG1109 163 KSLVDEAlrlRGLKVVVDCGNGAAGGVAPRLLRELGAEVIVLNAEPDGNFPNHNPNP-EPENLEDLIEAVKETGADLGIA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 240 FDGDGDRVGVVTNTGTIIYPDRLLMLFAKDVVSRNPGADIIFDVKCTRRLIALISGYGGRPVMWKTGHSLIKKKMKETGA 319
Cdd:COG1109 242 FDGDADRLGVVDEKGRFLDGDQLLALLARYLLEKGPGGTVVVTVMSSLALEDIAEKHGGEVVRTKVGFKYIKEKMRETGA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 320 LLAGEMSGHVFFKErWFGFDDGIYSAARLLEILSQDQRDSEHVFSAFPsDISTPEINITVTEDSKF-AIIEALQRDAQWG 398
Cdd:COG1109 322 VLGGEESGGIIFPD-FVPTDDGILAALLLLELLAKQGKSLSELLAELP-RYPQPEINVRVPDEEKIgAVMEKLREAVEDK 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
2FKM_X 399 EgNITTLDGVRVDYP-KGWGLVRASNTTPVLVLRFEADTEEELERIKTVFRNQLKAV 454
Cdd:COG1109 400 E-ELDTIDGVKVDLEdGGWVLVRPSGTEPLLRVYAEAKDEEEAEELLAELAELVEEA 455
|
|
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
12-443 |
1.04e-132 |
|
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: 390.34 E-value: 1.04e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 12 IFRAYDIRGVVGDTLTAETAYWIGRAIGSeslARGEPCVAVGRDGRLSGPELVKQLIQGLVDCGCQVSDVGMVPTPVLYY 91
Cdd:TIGR03990 3 LFGTSGIRGIVGEELTPELALKVGKAFGT---YLRGGKVVVGRDTRTSGPMLENAVIAGLLSTGCDVVDLGIAPTPTLQY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 92 AANVLEGKSGVMLTGDHNPPDYNGFKIVVA-GETLANEQIQALRERIEKNDLA----SGVGSVEQV-DILPRYFKQI--- 162
Cdd:TIGR03990 80 AVRELGADGGIMITASHNPPEYNGIKLLNSdGTELSREQEEEIEEIAESGDFEradwDEIGTVTSDeDAIDDYIEAIldk 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 163 --RDDIAmAKPMKVVVDCGNGVAGVIAPQLIEALGCSVIPLYCEVDGNFPNHHPDPgKPENLKDLIAKVKAENADLGLAF 240
Cdd:TIGR03990 160 vdVEAIR-KKGFKVVVDCGNGAGSLTTPYLLRELGCKVITLNCQPDGTFPGRNPEP-TPENLKDLSALVKATGADLGIAH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 241 DGDGDRVGVVTNTGTIIYPDRLLMLFAKDVVsRNPGADIIFDVKCTRRLIALISGYGGRPVMWKTGHSLIKKKMKETGAL 320
Cdd:TIGR03990 238 DGDADRLVFIDEKGRFIGGDYTLALFAKYLL-EHGGGKVVTNVSSSRAVEDVAERHGGEVIRTKVGEVNVAEKMKEEGAV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 321 LAGEMSGHVFFKERWFGfDDGIYSAARLLEILSQDQRDSEHVFSAFPsDISTPEINITVTEDSKFAIIEALQRDAQwgEG 400
Cdd:TIGR03990 317 FGGEGNGGWIFPDHHYC-RDGLMAAALFLELLAEEGKPLSELLAELP-KYPMSKEKVELPDEDKEEVMEAVEEEFA--DA 392
|
410 420 430 440
....*....|....*....|....*....|....*....|...
2FKM_X 401 NITTLDGVRVDYPKGWGLVRASNTTPVLVLRFEADTEEELERI 443
Cdd:TIGR03990 393 EIDTIDGVRIDFEDGWVLVRPSGTEPIVRIYAEAKTEERAEEL 435
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
12-451 |
2.40e-129 |
|
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: 378.62 E-value: 2.40e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 12 IFRAYDIRGVVGDTLTAETAYWIGRAIGSESlargepcvavgrdgrlsgpelvkqliqglvdcgcqvsdvgmvptpvlyy 91
Cdd:cd03084 1 IFGTSGVRGVVGDDITPETAVALGQAIGSTG------------------------------------------------- 31
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 92 aanvlegksGVMLTGDHNPPDYNGFKIVVA-GETLANEQIQALRERIEKNDLASGV-----GSVEQVDILPRYFKQIRDD 165
Cdd:cd03084 32 ---------GIMITASHNPPEDNGIKFVDPdGEPIASEEEKAIEDLAEKEDEPSAVayelgGSVKAVDILQRYFEALKKL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 166 IAMA----KPMKVVVDCGNGVAGVIAPQLIEALGCSVIPLYCEVDGNFPNHHPDPGKPENLKDLIAKVKAENADLGLAFD 241
Cdd:cd03084 103 FDVAalsnKKFKVVVDSVNGVGGPIAPQLLEKLGAEVIPLNCEPDGNFGNINPDPGSETNLKQLLAVVKAEKADFGVAFD 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 242 GDGDRVGVVTNTGTIIYPDRLLMLFAKDVV-SRNPGADIIFDVKCTRRLIALISGYGGRPVMWKTGHSLIKKKMKETGAL 320
Cdd:cd03084 183 GDADRLIVVDENGGFLDGDELLALLAVELFlTFNPRGGVVKTVVSSGALDKVAKKLGIKVIRTKTGFKWVGEAMQEGDVV 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 321 LAGEMSGHVFFKERwFGFDDGIYSAARLLEILSQDQRDSEHVFSAFPSDISTpeinitvtedskfaiiealqrdaqwgeg 400
Cdd:cd03084 263 LGGEESGGVIFPEF-HPGRDGISAALLLLEILANLGKSLSELFSELPRYYYI---------------------------- 313
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
2FKM_X 401 nittldgvRVDYpKGWGLVRASNTTPVLVLRFEADTEEELERIKTVFRNQL 451
Cdd:cd03084 314 --------RLKV-RGWVLVRASGTEPAIRIYAEADTQEDVEQIKKEARELV 355
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
18-449 |
6.66e-108 |
|
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: 326.84 E-value: 6.66e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 18 IRGVVGDTLTAETAYWIGRAIGSeslARGEPCVAVGRDGRLSGPELVKQLIQGLVDCGCQVSDVGMVPTPVLYYAAnVLE 97
Cdd:cd03087 7 IRGVVGEELTPELALKVGKALGT---YLGGGTVVVGRDTRTSGPMLKNAVIAGLLSAGCDVIDIGIVPTPALQYAV-RKL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 98 GKSGVMLTGDHNPPDYNGFKIVVA-GETLANEQIQALRERIEKNDLA----SGVGSVEQVD-ILPRYFKQIRD--DIAMA 169
Cdd:cd03087 83 GDAGVMITASHNPPEYNGIKLVNPdGTEFSREQEEEIEEIIFSERFRrvawDEVGSVRREDsAIDEYIEAILDkvDIDGG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 170 KPMKVVVDCGNGVAGVIAPQLIEALGCSVIPLYCEVDGNFPNHHPDPgKPENLKDLIAKVKAENADLGLAFDGDGDRVGV 249
Cdd:cd03087 163 KGLKVVVDCGNGAGSLTTPYLLRELGCKVITLNANPDGFFPGRPPEP-TPENLSELMELVRATGADLGIAHDGDADRAVF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 250 VTNTGTIIYPDRLLMLFAKDVVSRNPGAdIIFDVKCTRRLIALISGYGGRpVMW-KTGHSLIKKKMKETGALLAGEMSGH 328
Cdd:cd03087 242 VDEKGRFIDGDKLLALLAKYLLEEGGGK-VVTPVDASMLVEDVVEEAGGE-VIRtPVGDVHVAEEMIENGAVFGGEPNGG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 329 VFFKErwFGF-DDGIYSAARLLEILSQDQRDSEhVFSAFPSDISTPEiNITVTEDSKFAIIEALQRDAQWGEGNITTLDG 407
Cdd:cd03087 320 WIFPD--HQLcRDGIMTAALLLELLAEEKPLSE-LLDELPKYPLLRE-KVECPDEKKEEVMEAVEEELSDADEDVDTIDG 395
|
410 420 430 440
....*....|....*....|....*....|....*....|..
2FKM_X 408 VRVDYPKGWGLVRASNTTPVLVLRFEADTEEELERIKTVFRN 449
Cdd:cd03087 396 VRIEYEDGWVLIRPSGTEPKIRITAEAKTEERAKELLEEGRS 437
|
|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
13-443 |
2.05e-95 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 294.97 E-value: 2.05e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 13 FRAYDIRGVVGDTLTAETAYWIGRAIGSESLARGEPCVAVGRDGRLSGPELVKQLIQGLVDCGCQVSDVGMVPTPVLYYA 92
Cdd:PRK09542 1 IKAYDVRGVVGEQIDEDLVRDVGAAFARLMRAEGATTVVIGHDMRDSSPELAAAFAEGVTAQGLDVVRIGLASTDQLYFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 93 ANVLEGkSGVMLTGDHNPPDYNGFKIVVAG------ET-LAneqiqALRERIEKN--DLASGVGSVEQVDILPRYFKQIR 163
Cdd:PRK09542 81 SGLLDC-PGAMFTASHNPAAYNGIKLCRAGakpvgqDTgLA-----AIRDDLIAGvpAYDGPPGTVTERDVLADYAAFLR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 164 D--DIAMAKPMKVVVDCGNGVAGVIAPQLIEALGCSVIPLYCEVDGNFPNHHPDPGKPENLKDLIAKVKAENADLGLAFD 241
Cdd:PRK09542 155 SlvDLSGIRPLKVAVDAGNGMGGHTVPAVLGGLPITLLPLYFELDGTFPNHEANPLDPANLVDLQAFVRETGADIGLAFD 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 242 GDGDRVGVVTNTGTIIYPDRLLMLFAKDVVSRNPGADIIFDVKCTRRLIALISGYGGRPVMWKTGHSLIKKKMKETGALL 321
Cdd:PRK09542 235 GDADRCFVVDERGQPVSPSAVTALVAARELAREPGATIIHNLITSRAVPELVAERGGTPVRTRVGHSFIKALMAETGAIF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 322 AGEMSGHVFFKERWfGFDDGIYSAARLLEILSQDQRDSEHVFSAFPSDISTPEINITVteDSKFAIIEALqRDAQWG-EG 400
Cdd:PRK09542 315 GGEHSAHYYFRDFW-GADSGMLAALHVLAALGEQDRPLSELMADYQRYAASGEINSTV--ADAPARMEAV-LKAFADrIV 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....
2FKM_X 401 NITTLDGVRVDYPKG-WGLVRASNTTPVLVLRFEADTEEELERI 443
Cdd:PRK09542 391 SVDHLDGVTVDLGDGsWFNLRASNTEPLLRLNVEARTEEEVDAL 434
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
18-441 |
2.85e-70 |
|
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: 229.50 E-value: 2.85e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 18 IRGVVGDTLTAETAYWIGRAIG-SESLARGEPCVAVGRDGRLSGPELVKQLIQGLVDCGCQVSDVGMVPTPVLYYAANVL 96
Cdd:cd05803 7 IRGIVGEGLTPEVITRYVAAFAtWQPERTKGGKIVVGRDGRPSGPMLEKIVIGALLACGCDVIDLGIAPTPTVQVLVRQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 97 EGKSGVMLTGDHNPPDYNGFKIVVA-GETLANEQIQALRERIEKNDLA----SGVGSVEQ-VDILPRYFKQI--RDDIAM 168
Cdd:cd05803 87 QASGGIIITASHNPPQWNGLKFIGPdGEFLTPDEGEEVLSCAEAGSAQkagyDQLGEVTFsEDAIAEHIDKVlaLVDVDV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 169 AKP----MKVVVDCGNGVAGVIAPQLIEALGCSVIPLYCEVDGNFPnHHPDPgKPENLKDLIAKVKAENADLGLAFDGDG 244
Cdd:cd05803 167 IKIrernFKVAVDSVNGAGGLLIPRLLEKLGCEVIVLNCEPTGLFP-HTPEP-LPENLTQLCAAVKESGADVGFAVDPDA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 245 DRVGVVTNTGTIIYPDRLLMLFAKDVVSRNPGADIIFDVKCTRRLIALISGYGGRPVMW-KTGHSLIKKKMKETGALLAG 323
Cdd:cd05803 245 DRLALVDEDGRPIGEEYTLALAVDYVLKYGGRKGPVVVNLSTSRALEDIARKHGVPVFRsAVGEANVVEKMKEVDAVIGG 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 324 EMSGHVFFKERWFGfDDGIYSAARLLEILSQDQRDSEHVFSAFPsDISTPEINITVTEDSKFAIIEALQrdAQWGEGNIT 403
Cdd:cd05803 325 EGNGGVILPDVHYG-RDSLVGIALVLQLLAASGKPLSEIVDELP-QYYISKTKVTIAGEALERLLKKLE--AYFKDAEAS 400
|
410 420 430
....*....|....*....|....*....|....*...
2FKM_X 404 TLDGVRVDYPKGWGLVRASNTTPVLVLRFEADTEEELE 441
Cdd:cd05803 401 TLDGLRLDSEDSWVHVRPSNTEPIVRIIAEAPTQDEAE 438
|
|
| PRK15414 |
PRK15414 |
phosphomannomutase; |
13-445 |
8.36e-68 |
|
phosphomannomutase;
Pssm-ID: 185312 Cd Length: 456 Bit Score: 223.67 E-value: 8.36e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 13 FRAYDIRGVVGDTLTAETAYWIGRAIGsESLArgEPCVAVGRDGRLSGPELVKQLIQGLVDCGCQVSDVGMVPTPVLYYA 92
Cdd:PRK15414 7 FKAYDIRGKLGEELNEDIAWRIGRAYG-EFLK--PKTIVLGGDVRLTSETLKLALAKGLQDAGVDVLDIGMSGTEEIYFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 93 ANVLEGKSGVMLTGDHNPPDYNGFKIV------VAGETlaneQIQALRERIEKNDL----ASGVGSVEQVDILPRYFKQI 162
Cdd:PRK15414 84 TFHLGVDGGIEVTASHNPMDYNGMKLVregarpISGDT----GLRDVQRLAEANDFppvdETKRGRYQQINLRDAYVDHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 163 RD--DIAMAKPMKVVVDCGNGVAGVIAPQL---IEALGCSV--IPLYCEVDGNFPNHHPDPGKPENLKDLIAKVKAENAD 235
Cdd:PRK15414 160 FGyiNVKNLTPLKLVINSGNGAAGPVVDAIearFKALGAPVelIKVHNTPDGNFPNGIPNPLLPECRDDTRNAVIKHGAD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 236 LGLAFDGDGDRVGVVTNTGTIIYPDRLLMLFAKDVVSRNPGADIIFDVKCTRRLIALISGYGGRPVMWKTGHSLIKKKMK 315
Cdd:PRK15414 240 MGIAFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKNPGAKIIHDPRLSWNTVDVVTAAGGTPVMSKTGHAFIKERMR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 316 ETGALLAGEMSGHVFFKErwFGF-DDGIYSAARLLEILS-QDQRDSEHV---FSAFPsdiSTPEINITVTEDSkfAIIEA 390
Cdd:PRK15414 320 KEDAIYGGEMSAHHYFRD--FAYcDSGMIPWLLVAELVClKGKTLGELVrdrMAAFP---ASGEINSKLAQPV--EAINR 392
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
2FKM_X 391 LQRDAQWGEGNITTLDGVRVDYPKGWGLVRASNTTPVLVLRFEADTEEELERIKT 445
Cdd:PRK15414 393 VEQHFSREALAVDRTDGISMTFADWRFNLRSSNTEPVVRLNVESRGDVPLMEART 447
|
|
| GlmM |
cd05802 |
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ... |
18-443 |
1.39e-66 |
|
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: 219.66 E-value: 1.39e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 18 IRGVVGDTLTAETAYWIGRAIGSeSLAR--GEPCVAVGRDGRLSGPELVKQLIQGLVDCGCQVSDVGMVPTPVLYYAANV 95
Cdd:cd05802 7 IRGVANEPLTPELALKLGRAAGK-VLGKggGRPKVLIGKDTRISGYMLESALAAGLTSAGVDVLLLGVIPTPAVAYLTRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 96 LEGKSGVMLTGDHNPPDYNGFKIVVA-GETLANE---QIQALRERIEKNDLAS-GVGSVEQVDILP-RYFKQIRD--DIA 167
Cdd:cd05802 86 LRADAGVVISASHNPFEDNGIKFFSSdGYKLPDEveeEIEALIDKELELPPTGeKIGRVYRIDDARgRYIEFLKStfPKD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 168 MAKPMKVVVDCGNGVAGVIAPQLIEALGCSVIPLYCEVDGNFPNH-----HPDPgkpenlkdLIAKVKAENADLGLAFDG 242
Cdd:cd05802 166 LLSGLKIVLDCANGAAYKVAPEVFRELGAEVIVINNAPDGLNINVncgstHPES--------LQKAVLENGADLGIAFDG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 243 DGDRVGVVTNTGTIIYPDRLLMLFAKD-----------VVS---RNPGadiiFDVKCTRRLIALI-SGYGGRPVMwktgh 307
Cdd:cd05802 238 DADRVIAVDEKGNIVDGDQILAICARDlkergrlkgntVVGtvmSNLG----LEKALKELGIKLVrTKVGDRYVL----- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 308 slikKKMKETGALLAGEMSGHVFFKERWF-GfdDGIYSAARLLEILSQ-DQRDSE--HVFSAFPSDIstpeINITVTEDS 383
Cdd:cd05802 309 ----EEMLKHGANLGGEQSGHIIFLDHSTtG--DGLLTALQLLAIMKRsGKSLSElaSDMKLYPQVL----VNVRVKDKK 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 384 KFAIIEALQRDAQWGEGNITtlDGVRVdypkgwgLVRASNTTPVLVLRFEADTEEELERI 443
Cdd:cd05802 379 ALLENPRVQAAIAEAEKELG--GEGRV-------LVRPSGTEPLIRVMVEGEDEELVEKL 429
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
19-443 |
1.24e-62 |
|
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: 210.10 E-value: 1.24e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 19 RGVVGDTLTAETAYWIGRAIGSESLAR--GEPCVAVGRDGRLSGPELVKQLIQGLVDCGCQV--SDvGMVPTPVLYYAAN 94
Cdd:cd05800 9 RGIIAEDFTFENVRRVAQAIADYLKEEggGGRGVVVGYDTRFLSEEFARAVAEVLAANGIDVylSD-RPVPTPAVSWAVK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 95 VLEGKSGVMLTGDHNPPDYNGFKIVVAGETLAN-EQIQALRERIEKNDLASGV----GSVEQVDILPRYFKQIRD--DIA 167
Cdd:cd05800 88 KLGAAGGVMITASHNPPEYNGVKVKPAFGGSALpEITAAIEARLASGEPPGLEaraeGLIETIDPKPDYLEALRSlvDLE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 168 MAKPM--KVVVDCGNGVAGVIAPQLIEALGCSVIPLYCEVDGNFPNHHPDPgKPENLKDLIAKVKAENADLGLAFDGDGD 245
Cdd:cd05800 168 AIREAglKVVVDPMYGAGAGYLEELLRGAGVDVEEIRAERDPLFGGIPPEP-IEKNLGELAEAVKEGGADLGLATDGDAD 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 246 RVGVVTNTGTIIYPDRLLMLFAKDVV-SRNPGADIIFDVKCTRRLIALISGYGGR----PVmwktGHSLIKKKMKETGAL 320
Cdd:cd05800 247 RIGAVDEKGNFLDPNQILALLLDYLLeNKGLRGPVVKTVSTTHLIDRIAEKHGLPvyetPV----GFKYIAEKMLEEDVL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 321 LAGEMSG------HVffKERwfgfdDGIYSAARLLEILSQDQRD-SEHV---FSAFpSDISTPEINITVTEDSKFAIIEA 390
Cdd:cd05800 323 IGGEESGglgirgHI--PER-----DGILAGLLLLEAVAKTGKPlSELVaelEEEY-GPSYYDRIDLRLTPAQKEAILEK 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
2FKM_X 391 LQRDAQWGEG-----NITTLDGVRVDY-PKGWGLVRASNTTPVLVLRFEADTEEELERI 443
Cdd:cd05800 395 LKNEPPLSIAggkvdEVNTIDGVKLVLeDGSWLLIRPSGTEPLLRIYAEAPSPEKVEAL 453
|
|
| PLN02371 |
PLN02371 |
phosphoglucosamine mutase family protein |
17-457 |
6.13e-58 |
|
phosphoglucosamine mutase family protein
Pssm-ID: 215211 [Multi-domain] Cd Length: 583 Bit Score: 200.67 E-value: 6.13e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 17 DIRGVVGD-------TLTAETAYWIGRAIGS------ESLARGEPCVAVGRDGRLSGPELVKQLIQGLVDCGCQVSDVGM 83
Cdd:PLN02371 72 DIRGVAVEgvegepvTLTPPAVEAIGAAFAEwllekkKADGSGELRVSVGRDPRISGPRLADAVFAGLASAGLDVVDMGL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 84 VPTPVLYYAAnVLEGKS---GVMLTGDHNPPDYNGFKIVVAGETLANEQIQALRER---IEKNDLASGV--------GSV 149
Cdd:PLN02371 152 ATTPAMFMST-LTEREDydaPIMITASHLPYNRNGLKFFTKDGGLGKPDIKDILERaarIYKEWSDEGLlksssgasSVV 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 150 EQVDILPRYFKQIRDDIAMA--------KP---MKVVVDCGNGVAGVIAPQLIEALGCSVI-PLYCEVDGNFPNHHPDPG 217
Cdd:PLN02371 231 CRVDFMSTYAKHLRDAIKEGvghptnyeTPlegFKIVVDAGNGAGGFFAEKVLEPLGADTSgSLFLEPDGMFPNHIPNPE 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 218 KPENLKDLIAKVKAENADLGLAFDGDGDRVGVVTNTGTIIYPDRLLMLFAKDVVSRNPGADIIFDVKCTRRLIALISGYG 297
Cdd:PLN02371 311 DKAAMSATTQAVLANKADLGIIFDTDVDRSAVVDSSGREINRNRLIALMSAIVLEEHPGTTIVTDSVTSDGLTTFIEKKG 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 298 GRPVMWKTGH-SLIKK--KMKETG--ALLAGEMSGHVFFKERWFgFDDGIYSAARLL-EILSQDQRDSEHVFSAFPSDIS 371
Cdd:PLN02371 391 GKHHRFKRGYkNVIDKgvRLNSDGeeTHLMIETSGHGALKENHF-LDDGAYLAVKIIiELVRMRAAGAGGGLGDLIEDLE 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 372 TP----EINITVTEDSKFA------IIEALQ----RDAQWgEGNITTLDGVRVDYPK----GWGLVRASNTTPVLVLRFE 433
Cdd:PLN02371 470 EPleavELRLKILDEGKDFkaygeeVLEHLRnsieSDGKL-EGAPVNYEGVRVSDEGegfgGWFLLRQSLHDPVIPLNIE 548
|
490 500
....*....|....*....|....*..
2FKM_X 434 ADTEEELERIKTVFRNQLK---AVDSS 457
Cdd:PLN02371 549 SSSPGGAQKMALVVLTWLKefaALDAS 575
|
|
| glmM |
TIGR01455 |
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ... |
18-443 |
2.02e-52 |
|
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also designated in MrsA and YhbF E. coli, UreC in Helicobacter pylori, and femR315 or FemD in Staphlococcus aureus. It converts glucosamine-6-phosphate to glucosamine-1-phosphate as part of the pathway toward UDP-N-acetylglucosamine for peptidoglycan and lipopolysaccharides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Central intermediary metabolism, Amino sugars]
Pssm-ID: 130522 Cd Length: 443 Bit Score: 182.57 E-value: 2.02e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 18 IRGVVGD-TLTAETAYWIGRAIGsESLARGEP---CVAVGRDGRLSGPELVKQLIQGLVDCGCQVSDVGMVPTPVLYYAA 93
Cdd:TIGR01455 6 VRGRAGQePLTAELALLLGAAAG-RVLRQGRDtapRVVIGKDTRLSGYMLENALAAGLNSAGVDVLLLGPLPTPAVAYLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 94 NVLEGKSGVMLTGDHNPPDYNGFKIVVA-GETLANEQIQALRERIEKNDL-----ASGVGSV-EQVDILPRYFKQIRDDI 166
Cdd:TIGR01455 85 RTLRADAGVMISASHNPYEDNGIKFFGPgGFKLDDATEAAIEALLDEADPlprpeSEGLGRVkRYPDAVGRYIEFLKSTL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 167 AMAKP---MKVVVDCGNGVAGVIAPQLIEALGCSVIPLYCEVDGNFPNHHPDPGKPENLKdliAKVKAENADLGLAFDGD 243
Cdd:TIGR01455 165 PRGLTlsgLKVVLDCANGAAYKVAPHVFRELGAEVIAIGVEPDGLNINDGCGSTHLDALQ---KAVREHGADLGIAFDGD 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 244 GDRVGVVTNTGTIIYPDRLLMLFAKDVVSRN--PGADIIFDVKCTRRLIALISGYGGRPVMWKTGHSLIKKKMKETGALL 321
Cdd:TIGR01455 242 ADRVLAVDANGRIVDGDQILYIIARALKESGelAGNTVVATVMSNLGLERALEKLGLTLIRTAVGDRYVLEEMRESGYNL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 322 AGEMSGHVFFKERWFGfDDGIYSAARLLEILSQDQRDSEHVFSAFpsdISTPEINITV-TEDSKFAI-----IEALQRDA 395
Cdd:TIGR01455 322 GGEQSGHIILLDYSTT-GDGIVSALQVLTIMKKSGSTLSELAAEF---VPYPQTLVNVrVADRKLAAaeapaVKAAIEDA 397
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
2FKM_X 396 QWGEGnittldgvrvdyPKGWGLVRASNTTPVLVLRFEADTEEELERI 443
Cdd:TIGR01455 398 EAELG------------GTGRILLRPSGTEPLIRVMVEAADEELVQQL 433
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
12-143 |
4.18e-43 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 148.53 E-value: 4.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 12 IFRAYDIRGVVG-DTLTAETAYWIGRAIGSESLAR-GEPCVAVGRDGRLSGPELVKQLIQGLVDCGCQVSDVGMVPTPVL 89
Cdd:pfam02878 3 LFGTSGIRGKVGvGELTPEFALKLGQAIASYLRAQgGGGKVVVGRDTRYSSRELARALAAGLASNGVEVILLGLLPTPAV 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
2FKM_X 90 YYAANVLEGKSGVMLTGDHNPPDYNGFKIVVA-GETLANEQIQALRERIEKNDLA 143
Cdd:pfam02878 83 SFATRKLKADGGIMITASHNPPEYNGIKVFDSnGGPIPPEVEKKIEAIIEKEDFY 137
|
|
| MPG1_transferase |
cd05805 |
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose ... |
12-443 |
7.16e-38 |
|
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: 143.16 E-value: 7.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 12 IFRAYDIRGVVGDTLTAETAYWIGRAIGSeSLARGEPcVAVGRDGRLSGPELVKQLIQGLVDCGCQVSDVGMVPTPVLYY 91
Cdd:cd05805 1 LFGGRGVSGLINVDITPEFATRLGAAYGS-TLPPGST-VTVSRDASRASRMLKRALISGLLSTGVNVRDLGALPLPVARY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 92 AANVLEGKSGVMLTGDHNPPDYngFKIVVAGETLANeqIQALRER-IE----KND----LASGVGSVEQVDILPRYFKQ- 161
Cdd:cd05805 79 AIRFLGASGGIHVRTSPDDPDK--VEIEFFDSRGLN--ISRAMERkIEnaffREDfrraHVDEIGDITEPPDFVEYYIRg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 162 ----IRDDIAMAKPMKVVVDCGNGVAGVIAPQLIEALGCSVIPLYCEVDGNfpNHHPDPGKPENLKDLIAKVKAENADLG 237
Cdd:cd05805 155 llraLDTSGLKKSGLKVVIDYAYGVAGIVLPGLLSRLGCDVVILNARLDED--APRTDTERQRSLDRLGRIVKALGADFG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 238 LAFDGDGDRVGVVTNTGTIIYPDRLLMLFAKDVVSRNPGADIIFDVKCTRRLIALISGYGGRPVMWKTGHSLIKKKMKEt 317
Cdd:cd05805 233 VIIDPNGERLILVDEAGRVISDDLLTALVSLLVLKSEPGGTVVVPVTAPSVIEQLAERYGGRVIRTKTSPQALMEAALE- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 318 GALLAGEMSGHVFFKERWFGFdDGIYSAARLLEILSQDQRDSEHVFSAFPsDISTPEINITVTEDSKFAIIEALQRDAQw 397
Cdd:cd05805 312 NVVLAGDGDGGFIFPEFHPGF-DAIAALVKILEMLARTNISLSQIVDELP-RFYVLHKEVPCPWEAKGRVMRRLIEEAP- 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
2FKM_X 398 gEGNITTLDGVRVDYPKGWGLVRASNTTPVLVLRFEADTEEELERI 443
Cdd:cd05805 389 -DKSIELIDGVKIYEDDGWVLVLPDADEPLCHIYAEGSDQERAEEL 433
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
158-254 |
1.04e-31 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 117.01 E-value: 1.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 158 YFKQIRDDIAMA----KPMKVVVDCGNGVAGVIAPQLIEALGCSVIPLYCEVDGNFPNHHPDPGKPENLKDLIAKVKAEN 233
Cdd:pfam02879 2 YIDHLLELVDSEalkkRGLKVVYDPLHGVGGGYLPELLKRLGCDVVEENCEPDPDFPTRAPNPEEPEALALLIELVKSVG 81
|
90 100
....*....|....*....|.
2FKM_X 234 ADLGLAFDGDGDRVGVVTNTG 254
Cdd:pfam02879 82 ADLGIATDGDADRLGVVDERG 102
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
18-450 |
9.95e-28 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 114.85 E-value: 9.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 18 IRGVVGDT-LTAETAYWIGRAIGSESLARGEPCVAVGRDGRLSGPELVKQLIQGLVDCGCQVSDVGMVPTPVLYYAANVL 96
Cdd:PRK10887 9 IRGKVGQApITPDFVLKLGWAAGKVLARQGRPKVLIGKDTRISGYMLESALEAGLAAAGVDVLLTGPMPTPAVAYLTRTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 97 EGKSGVMLTGDHNPPDYNGFKIVVA-GETLANEQIQALRERIEKnDLASgVGSVE------QVDILPRYfkqirddIAMA 169
Cdd:PRK10887 89 RAEAGIVISASHNPYYDNGIKFFSAdGTKLPDEVELAIEAELDK-PLTC-VESAElgkasrINDAAGRY-------IEFC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 170 K---P-------MKVVVDCGNGVAGVIAPQLIEALGCSVIPLYCEVDGNFPNHHPDPGKPENLKdliAKVKAENADLGLA 239
Cdd:PRK10887 160 KstfPnelslrgLKIVVDCANGATYHIAPNVFRELGAEVIAIGCEPNGLNINDECGATDPEALQ---AAVLAEKADLGIA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 240 FDGDGDRVGVVTNTGTIIYPDRLLMLFAKDVVSRN---PGA------DIIFDVKCTRRLIALI-SGYGGRPVMwktghsl 309
Cdd:PRK10887 237 FDGDGDRVIMVDHLGNLVDGDQLLYIIARDRLRRGqlrGGVvgtlmsNMGLELALKQLGIPFVrAKVGDRYVL------- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 310 ikKKMKETGALLAGEMSGHVFFkerwfgFD-----DGIYSAARLLEILSQDQRDSEHV---FSAFPSDIstpeINITVTE 381
Cdd:PRK10887 310 --EKLQEKGWRLGGENSGHILC------LDktttgDGIVAALQVLAAMVRSGMSLADLcsgMKLFPQVL----INVRFKP 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
2FKM_X 382 DSKFAI----IEALQRDAQwgegniTTLDGvrvdypKGWGLVRASNTTPVLVLRFEADTEEEL----ERIKTVFRNQ 450
Cdd:PRK10887 378 GADDPLeseaVKAALAEVE------AELGG------RGRVLLRKSGTEPLIRVMVEGEDEAQVtalaERIADAVKAA 442
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
259-367 |
1.73e-26 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 103.30 E-value: 1.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 259 PDRLLMLFAKDVVSR---NPGADIIFDVKCTRRLIALISGYGGRPVMWKTGHSLIKKKMKETGALLAGEMSGHVFFKERW 335
Cdd:pfam02880 2 GDQILALLAKYLLEQgklPPGAGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEGALFGGEESGHIIFLDHA 81
|
90 100 110
....*....|....*....|....*....|...
2FKM_X 336 FgFDDGIYSAARLLEILSQDQRD-SEHVFSAFP 367
Cdd:pfam02880 82 T-TKDGILAALLVLEILARTGKSlSELLEELPE 113
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
27-250 |
8.75e-25 |
|
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: 106.44 E-value: 8.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 27 TAETAYWIgRAIGSESLARGepcVAVGRDGRLSGPELVKQLIQGLVDCGCQV---SDvgMVPTPVLYYAANVLEGKSGVM 103
Cdd:cd05799 29 TQGLANYL-KKKGPDAKNRG---VVIGYDSRHNSREFAELTAAVLAANGIKVylfDD--LRPTPLLSFAVRHLGADAGIM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 104 LTGDHNPPDYNGFKivVAGETLAneQI-----QALRERIEKNDLASGVGSVEQV----------DILPRYFKQI-----R 163
Cdd:cd05799 103 ITASHNPKEYNGYK--VYWEDGA--QIipphdAEIAEEIEAVLEPLDIKFEEALdsglikyigeEIDDAYLEAVkkllvN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 164 DDIAMAKPMKVVVDCGNGVAGVIAPQLIEALGCS---VIPLYCEVDGNFPN-HHPDPGKPENLKDLIAKVKAENADLGLA 239
Cdd:cd05799 179 PELNEGKDLKIVYTPLHGVGGKFVPRALKEAGFTnviVVEEQAEPDPDFPTvKFPNPEEPGALDLAIELAKKVGADLILA 258
|
250
....*....|.
2FKM_X 240 FDGDGDRVGVV 250
Cdd:cd05799 259 TDPDADRLGVA 269
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
19-280 |
3.97e-15 |
|
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: 77.24 E-value: 3.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 19 RGVVGDtLTAETAYWIGRAIGS--ESLARGEPcVAVGRDGRLSGPELVKQLIQGLVDCGCQVSDVGMVPTPVLYYAAnVL 96
Cdd:cd03088 8 RGLVTD-LTDEVCYAYTRAFLQhlESKFPGDT-VAVGRDLRPSSPRIAAACAAALRDAGFRVVDCGAVPTPALALYA-MK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 97 EGKSGVMLTGDHNPPDYNGFKIVVA-GETL-ANEQ--IQALRERIEKNDLASGVGSVEQVDILPRYFKQIRDDIAMA--K 170
Cdd:cd03088 85 RGAPAIMVTGSHIPADRNGLKFYRPdGEITkADEAaiLAALVELPEALFDPAGALLPPDTDAADAYIARYTDFFGAGalK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 171 PMKVVVDCGNGVAGVIAPQLIEALGCSVIPL-----YCEVDgnfpnhhPDPGKPENLKDLIAKVKAENADLGLAFDGDGD 245
Cdd:cd03088 165 GLRIGVYQHSSVGRDLLVRILEALGAEVVPLgrsdtFIPVD-------TEAVRPEDRALAAAWAAEHGLDAIVSTDGDGD 237
|
250 260 270
....*....|....*....|....*....|....*
2FKM_X 246 RVGVVTNTGTIIYPDRLLMLFAKDVvsrnpGADII 280
Cdd:cd03088 238 RPLVADETGEWLRGDILGLLTARFL-----GADTV 267
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
374-452 |
1.44e-13 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 65.37 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 374 EINITVTEDSKFAIIEALQRDaqwgegnitTLDGVRVDYPKGWGL-VRASNTTPVLVLRFEADTEEELERIKTVFRNQLK 452
Cdd:pfam00408 1 LINVRVAEKKKLAALAAILKV---------FADAEKILGEDGRRLdVRPSGTEPVLRVMVEGDSDEELARLADEIADLLE 71
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
52-246 |
1.03e-10 |
|
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate (G-1-P) and glucose-6-phosphate (G-6-P) via a glucose 1,6-diphosphate intermediate, an important metabolic step in prokaryotes and eukaryotes. In one direction, G-1-P produced from sucrose catabolism is converted to G-6-P, the first intermediate in glycolysis. In the other direction, conversion of G-6-P to G-1-P generates a substrate for synthesis of UDP-glucose which is required for synthesis of a variety of cellular constituents including cell wall polymers and glycoproteins. The PGM1 family also includes a non-enzymatic PGM-related protein (PGM-RP) thought to play a structural role in eukaryotes, as well as pp63/parafusin, a phosphoglycoprotein that plays an important role in calcium-regulated exocytosis in ciliated protozoans. PGM1 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 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: 100087 [Multi-domain] Cd Length: 548 Bit Score: 63.78 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 52 VGRDGRLSGPELVKQLIQglVDCGCQVSDV-----GMVPTPVlyyAANVL---EGKSGVMLTGDHNP--PDyNGFKIVV- 120
Cdd:cd03085 54 VGGDGRYYNKEAIQIIIK--IAAANGVGKVvvgqnGLLSTPA---VSAVIrkrKATGGIILTASHNPggPE-GDFGIKYn 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 121 ------AGETLANeQIQALRERIEKNDLASG-------VGS---------VEQVDILPRY---------FKQIRDDIAmA 169
Cdd:cd03085 128 tsnggpAPESVTD-KIYEITKKITEYKIADDpdvdlskIGVtkfggkpftVEVIDSVEDYvelmkeifdFDAIKKLLS-R 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 170 KPMKVVVDCGNGVAGVIAPQL-IEALGC---SVipLYCEVDGNFPNHHPDPgkpeNL---KDLIAKVKAENADLGLAFDG 242
Cdd:cd03085 206 KGFKVRFDAMHGVTGPYAKKIfVEELGApesSV--VNCTPLPDFGGGHPDP----NLtyaKDLVELMKSGEPDFGAASDG 279
|
....
2FKM_X 243 DGDR 246
Cdd:cd03085 280 DGDR 283
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
83-296 |
1.26e-09 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 60.47 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 83 MVPTPVLYYAANVLEGKSGVMLTGDHNPPDYNGFKivVAGETLAneQIQA-----LRERIEKN-----DLASGVGSVEQV 152
Cdd:PTZ00150 126 TVPTPFVPYAVRKLKCLAGVMVTASHNPKEDNGYK--VYWSNGA--QIIPphdknISAKILSNlepwsSSWEYLTETLVE 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 153 DIL----PRYFKQIRDDIAMAK----PMKVVVDCGNGVAGVIAPQLIEALG---CSVIPLYCEVDGNFPN-HHPDPGKPE 220
Cdd:PTZ00150 202 DPLaevsDAYFATLKSEYNPACcdrsKVKIVYTAMHGVGTRFVQKALHTVGlpnLLSVAQQAEPDPEFPTvTFPNPEEGK 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 221 NLKDL-IAKVKAENADLGLAFDGDGDRVGVV---TNTGTIIYPDRLLMLFAKDVVSRNPGADI-------IFDVKCTRRL 289
Cdd:PTZ00150 282 GALKLsMETAEAHGSTVVLANDPDADRLAVAeklNNGWKIFTGNELGALLAWWAMKRYRRQGIdkskcffICTVVSSRML 361
|
....*....
2FKM_X 290 --IALISGY 296
Cdd:PTZ00150 362 kkMAEKEGF 370
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
50-268 |
5.17e-09 |
|
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: 58.37 E-value: 5.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 50 VAVGRDGRLSGPELVKQLIQGLVDCGCQVSDVGMVPTPVLYY---AANvLEGKSGVmltgdhnpPDYNGFKivvagETLA 126
Cdd:cd03086 105 VFVGRDTRPSGPALLQALLDGLKALGGNVIDYGLVTTPQLHYlvrAAN-TEGAYGE--------PTEEGYY-----EKLS 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 127 NEQIQALRERIEKNDlasgvgsveqvdilpryfkqirddiamaKPMKVVVDCGNGVAGVIAPQLIEALGCSVIPLYCevd 206
Cdd:cd03086 171 KAFNELYNLLQDGGD----------------------------EPEKLVVDCANGVGALKLKELLKRLKKGLSVKII--- 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 207 gNFPNHhpDPGK----------------PENLKDLIAKVKAenadlgLAFDGDGDRVgV---VTNTGT--IIYPDRLLML 265
Cdd:cd03086 220 -NDGEE--GPELlndgcgadyvktkqkpPRGFELKPPGVRC------CSFDGDADRL-VyfyPDSSNKfhLLDGDKIATL 289
|
...
2FKM_X 266 FAK 268
Cdd:cd03086 290 FAK 292
|
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
48-254 |
6.67e-08 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 54.76 E-value: 6.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 48 PCVaVGRDGR-LSGPELVKQL-------IQGLVdcgcqVSDVGMVPTPVLYYA---ANVLEGKS--GVMLTGDHNPPDYN 114
Cdd:PRK07564 78 PLF-VGGDTHaLSEPAIQSALevlaangVGVVI-----VGRGGYTPTPAVSHAilkYNGRGGGLadGIVITPSHNPPEDG 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 115 GFK------------IVVAGETLANEQIQA-LRE--RIEKNDLASGvGSVEQVDILPRY---------FKQIRddiamAK 170
Cdd:PRK07564 152 GIKynppnggpadtdVTDAIEARANELLAYgLKGvkRIPLDRALAS-MTVEVIDPVADYvedlenvfdFDAIR-----KA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 171 PMKVVVDCGNGVAGVIAPQLIEALGCSV-------------IPLycEVDGNfpnHHPDPGKPENLKDLIAKvkAENADLG 237
Cdd:PRK07564 226 GLRLGVDPLGGATGPYWKAIAERYGLDLtvvnapvdptfnfMPL--DDDGK---IRMDCSSPYAMAGLLAL--KDAFDLA 298
|
250
....*....|....*..
2FKM_X 238 LAFDGDGDRVGVVTNTG 254
Cdd:PRK07564 299 FANDPDGDRHGIVTPGG 315
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
49-268 |
8.52e-08 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 54.66 E-value: 8.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 49 CVAVGRDGRLSGPELVKQLIQGL-VDCGCQVSDVGMVPTPVLYYAanvlegksgVMLT-GDHNPPDYNGFKIVVAGETLA 126
Cdd:PTZ00302 154 KVHVGRDTRPSSPELVSALLRGLkLLIGSNVRNFGIVTTPQLHFL---------VAFAnGLGVDVVESSDELYYAYLLAA 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 127 NEQIQALRERIEKNDLASGVgsveqvdilpryfkqirddiamakPMKVVVDCGNGVAGVIAPQLIEAL---GCSVIPLYC 203
Cdd:PTZ00302 225 FKELYRTLQEGGPVDLTQNN------------------------SKILVVDCANGVGGYKIKRFFEALkqlGIEIIPINI 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 204 EVDGNFP-NH---------HPDPgkPENLKDLIAKVKAENAdlglAFDGDGDRV------GVVTNTGTIIYPDRLLMLFA 267
Cdd:PTZ00302 281 NCDEEELlNDkcgadyvqkTRKP--PRAMKEWPGDEETRVA----SFDGDADRLvyffpdKDGDDKWVLLDGDRIAILYA 354
|
.
2FKM_X 268 K 268
Cdd:PTZ00302 355 M 355
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
50-267 |
1.26e-06 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 50.79 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 50 VAVGRDGRLSGPELVKQLIQGLVDCGCQVSDVGMVPTPVLYY---AANvlegksgvmltgdhnppdyNGFKivvAGETLA 126
Cdd:PLN02895 130 VLLGRDTRPSGPALLAAALKGVRAIGARAVDMGILTTPQLHWmvrAAN-------------------KGMK---ATESDY 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 127 NEQIQ----ALRERIEKNDLASGVGSveqvdilpryfkqirddiamakpmKVVVDCGNGVAGVIAPQLIEALGCSVIPLY 202
Cdd:PLN02895 188 FEQLSssfrALLDLIPNGSGDDRADD------------------------KLVVDGANGVGAEKLETLKKALGGLDLEVR 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 203 cevdgnfpNHHPDPGKPEN--------LKDLIAKVKAENADLGL---AFDGDGDRVgV---VTNTGTIIY---PDRLLML 265
Cdd:PLN02895 244 --------NSGKEGEGVLNegvgadfvQKEKVPPTGFASKDVGLrcaSLDGDADRL-VyfyVSSAGSKIDlldGDKIASL 314
|
..
2FKM_X 266 FA 267
Cdd:PLN02895 315 FA 316
|
|
| PGM_like3 |
cd05801 |
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
48-263 |
7.08e-06 |
|
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily. 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 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: 100094 [Multi-domain] Cd Length: 522 Bit Score: 48.40 E-value: 7.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 48 PCVaVGRDGR-LSGPELVKQLiQGLVDCGCQV---SDVGMVPTPVLYYA-----ANVLEGKS-GVMLTGDHNPPDYNGFK 117
Cdd:cd05801 61 PLF-LGKDTHaLSEPAFISAL-EVLAANGVEViiqQNDGYTPTPVISHAiltynRGRTEGLAdGIVITPSHNPPEDGGFK 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 118 ------------IVVAGETLANEQIQALRERIEKNDLASGVGS--VEQVDILPRYFKQIRDDIAM----AKPMKVVVDCG 179
Cdd:cd05801 139 ynpphggpadtdITRWIEKRANALLANGLKGVKRIPLEAALASgyTHRHDFVTPYVADLGNVIDMdairKSGLRLGVDPL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 180 NGvAGVIAPQLIEAL-GCSVIPLYCEVDGNFPNHHPD--------PGKPENLKDLIAkvKAENADLGLAFDGDGDRVGVV 250
Cdd:cd05801 219 GG-ASVPYWQPIAEKyGLNLTVVNPKVDPTFRFMTLDhdgkirmdCSSPYAMAGLLK--LKDKFDLAFANDPDADRHGIV 295
|
250
....*....|...
2FKM_X 251 TNTGTIIYPDRLL 263
Cdd:cd05801 296 TPSAGLMNPNHYL 308
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
96-126 |
2.18e-04 |
|
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: 43.74 E-value: 2.18e-04
10 20 30
....*....|....*....|....*....|...
2FKM_X 96 LEGKS-GVMLTGDHNPPDYNGFKIV-VAGETLA 126
Cdd:cd03086 32 LGGKTiGVMITASHNPVEDNGVKIVdPDGEMLE 64
|
|
| PLN02307 |
PLN02307 |
phosphoglucomutase |
52-246 |
1.01e-03 |
|
phosphoglucomutase
Pssm-ID: 177942 [Multi-domain] Cd Length: 579 Bit Score: 41.56 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 52 VGRDGRLSGPELVKQLIQGLVDCGCQ---VSDVGMVPTP-VLYYAANVLEGKS--GVMLTGDHNP--PDYN-GFKIVV-- 120
Cdd:PLN02307 66 LGGDGRYFNKEAIQIIIKIAAANGVRrvwVGQNGLLSTPaVSAVIRERDGSKAngGFILTASHNPggPEEDfGIKYNYes 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 121 ---AGETLANE------QIQALR--ERIEKNDLAS-GVGS--------VEQVDILPRY---------FKQIRDDIAMAKp 171
Cdd:PLN02307 146 gqpAPESITDKiygntlTIKEYKmaEDIPDVDLSAvGVTKfggpedfdVEVIDPVEDYvklmksifdFELIKKLLSRPD- 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2FKM_X 172 MKVVVDCGNGVAGVIA-PQLIEALGC--SVIpLYCEVDGNFPNHHPDPgkpeNL---KDLIAKV------KAENA-DLGL 238
Cdd:PLN02307 225 FTFCFDAMHGVTGAYAkRIFVEELGApeSSL-LNCVPKEDFGGGHPDP----NLtyaKELVKRMglgktsYGDEPpEFGA 299
|
....*...
2FKM_X 239 AFDGDGDR 246
Cdd:PLN02307 300 ASDGDGDR 307
|
|
| |
