|
Name |
Accession |
Description |
Interval |
E-value |
| Arch_GlmM |
TIGR03990 |
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ... |
2-457 |
0e+00 |
|
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: 590.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 2 SLIKSISGIRGTIGgrpgEGLSPLDIVKFTAAYARFISGSTtrksrtIVVGRDARLSGPMVSDLVTATLTGMGFDVVNIG 81
Cdd:TIGR03990 1 MLLFGTSGIRGIVG----EELTPELALKVGKAFGTYLRGGK------VVVGRDTRTSGPMLENAVIAGLLSTGCDVVDLG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 82 LASTPTTELAVVMEKACGGIIITASHNPKQWNALKLLNENGEFLNDAQGKEVLAIAEADGYSFAEVDALGHVYSNETYNR 161
Cdd:TIGR03990 71 IAPTPTLQYAVRELGADGGIMITASHNPPEYNGIKLLNSDGTELSREQEEEIEEIAESGDFERADWDEIGTVTSDEDAID 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 162 RHIDSVlaLDLVDVDAIAKADFTVAVDAVNSVGGIVIPQLLRVLGVKnIIELNCEATGKF-AHTPELIPENLTQIADLMR 240
Cdd:TIGR03990 151 DYIEAI--LDKVDVEAIRKKGFKVVVDCGNGAGSLTTPYLLRELGCK-VITLNCQPDGTFpGRNPEPTPENLKDLSALVK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 241 DGKADVGFVVDPDVDRLAIVMENGEMFVEEYTLVAVADYVLSHTPGSTVSNLSSSRALRDVTRRHGCEYSAAAVGEVNVV 320
Cdd:TIGR03990 228 ATGADLGIAHDGDADRLVFIDEKGRFIGGDYTLALFAKYLLEHGGGKVVTNVSSSRAVEDVAERHGGEVIRTKVGEVNVA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 321 TKMKETGAVIGGEGNGGVIYPASHYGRDALVGVALFLTLLAKSGKKVSELKATYPEYAIAKNKIQLtPDIDVDAILEAVK 400
Cdd:TIGR03990 308 EKMKEEGAVFGGEGNGGWIFPDHHYCRDGLMAAALFLELLAEEGKPLSELLAELPKYPMSKEKVEL-PDEDKEEVMEAVE 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2530778051 401 KRYASETITDIDGVKIDFPDSWVHLRKSNTEPIIRIYSEASTMEKADALAQDIKSVI 457
Cdd:TIGR03990 387 EEFADAEIDTIDGVRIDFEDGWVLVRPSGTEPIVRIYAEAKTEERAEELLEEGRSLV 443
|
|
| PGM_like4 |
cd05803 |
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ... |
4-450 |
0e+00 |
|
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: 588.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 4 IKSISGIRGTIGgrpgEGLSPLDIVKFTAAYARFISGSTTRKsrTIVVGRDARLSGPMVSDLVTATLTGMGFDVVNIGLA 83
Cdd:cd05803 1 IISISGIRGIVG----EGLTPEVITRYVAAFATWQPERTKGG--KIVVGRDGRPSGPMLEKIVIGALLACGCDVIDLGIA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 84 STPTTELAVVMEKACGGIIITASHNPKQWNALKLLNENGEFLNDAQGKEVLAIAEADGYSFAEVDALGHVYSNETYNRRH 163
Cdd:cd05803 75 PTPTVQVLVRQSQASGGIIITASHNPPQWNGLKFIGPDGEFLTPDEGEEVLSCAEAGSAQKAGYDQLGEVTFSEDAIAEH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 164 IDSVLALDLVDVDAIAKADFTVAVDAVNSVGGIVIPQLLRVLGVKnIIELNCEATGKFAHTPELIPENLTQIADLMRDGK 243
Cdd:cd05803 155 IDKVLALVDVDVIKIRERNFKVAVDSVNGAGGLLIPRLLEKLGCE-VIVLNCEPTGLFPHTPEPLPENLTQLCAAVKESG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 244 ADVGFVVDPDVDRLAIVMENGEMFVEEYTLVAVADYVLS--HTPGSTVSNLSSSRALRDVTRRHGCEYSAAAVGEVNVVT 321
Cdd:cd05803 234 ADVGFAVDPDADRLALVDEDGRPIGEEYTLALAVDYVLKygGRKGPVVVNLSTSRALEDIARKHGVPVFRSAVGEANVVE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 322 KMKETGAVIGGEGNGGVIYPASHYGRDALVGVALFLTLLAKSGKKVSELKATYPEYAIAKNKIQLtPDIDVDAILEAVKK 401
Cdd:cd05803 314 KMKEVDAVIGGEGNGGVILPDVHYGRDSLVGIALVLQLLAASGKPLSEIVDELPQYYISKTKVTI-AGEALERLLKKLEA 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2530778051 402 RYASETITDIDGVKIDFPDSWVHLRKSNTEPIIRIYSEASTMEKADALA 450
Cdd:cd05803 393 YFKDAEASTLDGLRLDSEDSWVHVRPSNTEPIVRIIAEAPTQDEAEALA 441
|
|
| ManB |
COG1109 |
Phosphomannomutase [Carbohydrate transport and metabolism]; |
4-461 |
1.92e-151 |
|
Phosphomannomutase [Carbohydrate transport and metabolism];
Pssm-ID: 440726 [Multi-domain] Cd Length: 456 Bit Score: 438.48 E-value: 1.92e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 4 IKSISGIRGTIGgrpgEGLSPLDIVKFTAAYARFIsgsTTRKSRTIVVGRDARLSGPMVSDLVTATLTGMGFDVVNIGLA 83
Cdd:COG1109 6 LFGTDGIRGIVG----EELTPEFVLKLGRAFGTYL---KEKGGPKVVVGRDTRLSSPMLARALAAGLASAGIDVYDLGLV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 84 STPTTELAVVMEKACGGIIITASHNPKQWNALKLLNENGEFLNDAQGKEVLAIAEADGYSFAEVDALGHVYSNETYNRRH 163
Cdd:COG1109 79 PTPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKEDFRRAEAEEIGKVTRIEDVLEAY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 164 IDSVlaLDLVDvDAIAKADFTVAVDAVNSVGGIVIPQLLRVLGVKnIIELNCEATGKF-AHTPELIPENLTQIADLMRDG 242
Cdd:COG1109 159 IEAL--KSLVD-EALRLRGLKVVVDCGNGAAGGVAPRLLRELGAE-VIVLNAEPDGNFpNHNPNPEPENLEDLIEAVKET 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 243 KADVGFVVDPDVDRLAIVMENGEMFVEEYTLVAVADYVLSHTPGST-VSNLSSSRALRDVTRRHGCEYSAAAVGEVNVVT 321
Cdd:COG1109 235 GADLGIAFDGDADRLGVVDEKGRFLDGDQLLALLARYLLEKGPGGTvVVTVMSSLALEDIAEKHGGEVVRTKVGFKYIKE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 322 KMKETGAVIGGEGNGGVIYPASHYGRDALVGVALFLTLLAKSGKKVSELKATYPEYAIAKNKIQLTPDIDVDAILEAVKK 401
Cdd:COG1109 315 KMRETGAVLGGEESGGIIFPDFVPTDDGILAALLLLELLAKQGKSLSELLAELPRYPQPEINVRVPDEEKIGAVMEKLRE 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2530778051 402 RYAS-ETITDIDGVKIDFPD-SWVHLRKSNTEPIIRIYSEASTMEKADALAQDIKSVIASLA 461
Cdd:COG1109 395 AVEDkEELDTIDGVKVDLEDgGWVLVRPSGTEPLLRVYAEAKDEEEAEELLAELAELVEEAL 456
|
|
| PGM_like1 |
cd03087 |
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
8-457 |
1.59e-117 |
|
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: 351.10 E-value: 1.59e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 8 SGIRGtiggRPGEGLSPLDIVKFTAAYArfisgsTTRKSRTIVVGRDARLSGPMVSDLVTATLTGMGFDVVNIGLASTPT 87
Cdd:cd03087 5 SGIRG----VVGEELTPELALKVGKALG------TYLGGGTVVVGRDTRTSGPMLKNAVIAGLLSAGCDVIDIGIVPTPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 88 TELAVvMEKACGGIIITASHNPKQWNALKLLNENGEFLNDAQGKEVLAIAEADGYSFAEVDALGHVYSNETYNRRHIDSV 167
Cdd:cd03087 75 LQYAV-RKLGDAGVMITASHNPPEYNGIKLVNPDGTEFSREQEEEIEEIIFSERFRRVAWDEVGSVRREDSAIDEYIEAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 168 LAldlvDVDAIAKADFTVAVDAVNSVGGIVIPQLLRVLGVKnIIELNCEATGKF-AHTPELIPENLTQIADLMRDGKADV 246
Cdd:cd03087 154 LD----KVDIDGGKGLKVVVDCGNGAGSLTTPYLLRELGCK-VITLNANPDGFFpGRPPEPTPENLSELMELVRATGADL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 247 GFVVDPDVDRLAIVMENGEMFVEEYTLVAVADYVLSHTPGSTVSNLSSSRALRDVTRRHGCEYSAAAVGEVNVVTKMKET 326
Cdd:cd03087 229 GIAHDGDADRAVFVDEKGRFIDGDKLLALLAKYLLEEGGGKVVTPVDASMLVEDVVEEAGGEVIRTPVGDVHVAEEMIEN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 327 GAVIGGEGNGGVIYPASHYGRDALVGVALFLTLLAKSgKKVSELKATYPEYAIAKNKIQlTPDIDVDAILEAVKKRY--A 404
Cdd:cd03087 309 GAVFGGEPNGGWIFPDHQLCRDGIMTAALLLELLAEE-KPLSELLDELPKYPLLREKVE-CPDEKKEEVMEAVEEELsdA 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2530778051 405 SETITDIDGVKIDFPDSWVHLRKSNTEPIIRIYSEASTMEKADALAQDIKSVI 457
Cdd:cd03087 387 DEDVDTIDGVRIEYEDGWVLIRPSGTEPKIRITAEAKTEERAKELLEEGRSKV 439
|
|
| PMM_PGM |
cd03089 |
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ... |
10-457 |
4.57e-90 |
|
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: 280.94 E-value: 4.57e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 10 IRGTIGgrpgEGLSPLDIVKFTAAYARFISgstTRKSRTIVVGRDARLSGPMVSDLVTATLTGMGFDVVNIGLASTPTTE 89
Cdd:cd03089 7 IRGIAG----EELTEEIAYAIGRAFGSWLL---EKGAKKVVVGRDGRLSSPELAAALIEGLLAAGCDVIDIGLVPTPVLY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 90 LAVVMEKACGGIIITASHNPKQWNALKLLNeNGEFLNDAQGKEVLAIAEAdgYSFAEVDALGHVYSNETYNrRHIDsvla 169
Cdd:cd03089 80 FATFHLDADGGVMITASHNPPEYNGFKIVI-GGGPLSGEDIQALRERAEK--GDFAAATGRGSVEKVDILP-DYID---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 170 lDLVDVDAIAKADFTVAVDAVNSVGGIVIPQLLRVLGVkNIIELNCEATGKF-AHTPE-LIPENLTQIADLMRDGKADVG 247
Cdd:cd03089 152 -RLLSDIKLGKRPLKVVVDAGNGAAGPIAPQLLEALGC-EVIPLFCEPDGTFpNHHPDpTDPENLEDLIAAVKENGADLG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 248 FVVDPDVDRLAIVMENGEMFVEEYTLVAVADYVLSHTPGST-VSNLSSSRALRDVTRRHGCEYSAAAVGEVNVVTKMKET 326
Cdd:cd03089 230 IAFDGDGDRLGVVDEKGEIIWGDRLLALFARDILKRNPGATiVYDVKCSRNLYDFIEEAGGKPIMWKTGHSFIKAKMKET 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 327 GAVIGGEGNGGVIYPASHYG-RDALVGVALFLTLLAKSGKKVSELKATYPEYAIaknkiqlTPDI-------DVDAILEA 398
Cdd:cd03089 310 GALLAGEMSGHIFFKDRWYGfDDGIYAALRLLELLSKSGKTLSELLADLPKYFS-------TPEIripvteeDKFAVIER 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2530778051 399 VKKRYAS--ETITDIDGVKIDFPDSWVHLRKSNTEPIIRIYSEASTMEKADALAQDIKSVI 457
Cdd:cd03089 383 LKEHFEFpgAEIIDIDGVRVDFEDGWGLVRASNTEPVLVLRFEADTEEGLEEIKAELRKLL 443
|
|
| PGM_like2 |
cd05800 |
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ... |
8-457 |
6.48e-71 |
|
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: 231.67 E-value: 6.48e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 8 SGIRGTIGgrpgEGLSPLDIVKFTAAYARFIsGSTTRKSRTIVVGRDARLSGPMVSDLVTATLTGMGFDVVNI-GLASTP 86
Cdd:cd05800 6 DGWRGIIA----EDFTFENVRRVAQAIADYL-KEEGGGGRGVVVGYDTRFLSEEFARAVAEVLAANGIDVYLSdRPVPTP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 87 TTELAVVMEKACGGIIITASHNPKQWNALKLLNENGEFLNDAQGKEVLAIAEADGYSFAEVDALGHVysnETYNRR--HI 164
Cdd:cd05800 81 AVSWAVKKLGAAGGVMITASHNPPEYNGVKVKPAFGGSALPEITAAIEARLASGEPPGLEARAEGLI---ETIDPKpdYL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 165 DSVLalDLVDVDAIAKADFTVAVDAVNSVGGIVIPQLLRVLGVkNIIELNCEATGKF-AHTPELIPENLTQIADLMRDGK 243
Cdd:cd05800 158 EALR--SLVDLEAIREAGLKVVVDPMYGAGAGYLEELLRGAGV-DVEEIRAERDPLFgGIPPEPIEKNLGELAEAVKEGG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 244 ADVGFVVDPDVDRLAIVMENGEMFVEEYTLVAVADYVL--SHTPGSTVSNLSSSRALRDVTRRHGCEYSAAAVGEVNVVT 321
Cdd:cd05800 235 ADLGLATDGDADRIGAVDEKGNFLDPNQILALLLDYLLenKGLRGPVVKTVSTTHLIDRIAEKHGLPVYETPVGFKYIAE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 322 KMKETGAVIGGEGNGGVIYPASHYGRDALVGVALFLTLLAKSGKKVSEL-KATYPEY-AIAKNKIQLT-PDIDVDAILEA 398
Cdd:cd05800 315 KMLEEDVLIGGEESGGLGIRGHIPERDGILAGLLLLEAVAKTGKPLSELvAELEEEYgPSYYDRIDLRlTPAQKEAILEK 394
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2530778051 399 VKKR-------YASETITDIDGVKIDF-PDSWVHLRKSNTEPIIRIYSEASTMEKADALAQDIKSVI 457
Cdd:cd05800 395 LKNEpplsiagGKVDEVNTIDGVKLVLeDGSWLLIRPSGTEPLLRIYAEAPSPEKVEALLDAGKKLA 461
|
|
| phosphohexomutase |
cd03084 |
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ... |
99-449 |
1.41e-70 |
|
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: 227.62 E-value: 1.41e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 99 GGIIITASHNPKQWNALKLLNENGEFLNDAQGKEVLAIAEA-DGYSFAEVDALGHVYSnETYNRRHIDsvLALDLVDVDA 177
Cdd:cd03084 31 GGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKeDEPSAVAYELGGSVKA-VDILQRYFE--ALKKLFDVAA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 178 IAKADFTVAVDAVNSVGGIVIPQLLRVLGVkNIIELNCEATGKF--AHTPELIPENLTQIADLMRDGKADVGFVVDPDVD 255
Cdd:cd03084 108 LSNKKFKVVVDSVNGVGGPIAPQLLEKLGA-EVIPLNCEPDGNFgnINPDPGSETNLKQLLAVVKAEKADFGVAFDGDAD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 256 RLAIVMENGEMFVEEYTLVAVADYVLSHTP--GSTVSNLSSSRALRDVTRRHGCEYSAAAVGEVNVVTKMKETGAVIGGE 333
Cdd:cd03084 187 RLIVVDENGGFLDGDELLALLAVELFLTFNprGGVVKTVVSSGALDKVAKKLGIKVIRTKTGFKWVGEAMQEGDVVLGGE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 334 GNGGVIYPASHYGRDALVGVALFLTLLAKSGKKVSELKATYPEYAIAKNKIQltpdidvdaileavkkryasetitdidg 413
Cdd:cd03084 267 ESGGVIFPEFHPGRDGISAALLLLEILANLGKSLSELFSELPRYYYIRLKVR---------------------------- 318
|
330 340 350
....*....|....*....|....*....|....*.
gi 2530778051 414 vkidfpdSWVHLRKSNTEPIIRIYSEASTMEKADAL 449
Cdd:cd03084 319 -------GWVLVRASGTEPAIRIYAEADTQEDVEQI 347
|
|
| MPG1_transferase |
cd05805 |
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose ... |
21-457 |
5.55e-58 |
|
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: 197.08 E-value: 5.55e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 21 GLSPLDI-----VKFTAAYarfisGSTTRKSRTIVVGRDARLSGPMVSDLVTATLTGMGFDVVNIGLASTPTTELAVVME 95
Cdd:cd05805 9 GLINVDItpefaTRLGAAY-----GSTLPPGSTVTVSRDASRASRMLKRALISGLLSTGVNVRDLGALPLPVARYAIRFL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 96 KACGGIIITASHNPKQWNALKLLNENGEFLNDAQGKEVLAIAEADGYSFAEVDALGHVYSNETYNRRHIDSVLalDLVDV 175
Cdd:cd05805 84 GASGGIHVRTSPDDPDKVEIEFFDSRGLNISRAMERKIENAFFREDFRRAHVDEIGDITEPPDFVEYYIRGLL--RALDT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 176 DAIAKADFTVAVDAVNSVGGIVIPQLLRVLGVKNIIeLNCEATGKFAHTPELIPENLTQIADLMRDGKADVGFVVDPDVD 255
Cdd:cd05805 162 SGLKKSGLKVVIDYAYGVAGIVLPGLLSRLGCDVVI-LNARLDEDAPRTDTERQRSLDRLGRIVKALGADFGVIIDPNGE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 256 RLAIVMENGEMFVEEYTLVAVADYVLSHTPGSTVS-NLSSSRALRDVTRRHGCEYSAAAVGEVNVVTKMKEtGAVIGGEG 334
Cdd:cd05805 241 RLILVDEAGRVISDDLLTALVSLLVLKSEPGGTVVvPVTAPSVIEQLAERYGGRVIRTKTSPQALMEAALE-NVVLAGDG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 335 NGGVIYPASHYGRDALVGVALFLTLLAKSGKKVSELKATYPEYAIAKNKIQlTPDIDVDAILEAVKKRYASETITDIDGV 414
Cdd:cd05805 320 DGGFIFPEFHPGFDAIAALVKILEMLARTNISLSQIVDELPRFYVLHKEVP-CPWEAKGRVMRRLIEEAPDKSIELIDGV 398
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2530778051 415 KIDFPDSWVHLRKSNTEPIIRIYSEASTMEKADALAQDIKSVI 457
Cdd:cd05805 399 KIYEDDGWVLVLPDADEPLCHIYAEGSDQERAEELTEFYVEKV 441
|
|
| manB |
PRK09542 |
phosphomannomutase/phosphoglucomutase; Reviewed |
10-459 |
4.77e-50 |
|
phosphomannomutase/phosphoglucomutase; Reviewed
Pssm-ID: 236557 Cd Length: 445 Bit Score: 176.33 E-value: 4.77e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 10 IRGTIGgrpgEGLSPlDIVK-FTAAYARFISGSttrKSRTIVVGRDARLSGPMVSDLVTATLTGMGFDVVNIGLASTPTT 88
Cdd:PRK09542 6 VRGVVG----EQIDE-DLVRdVGAAFARLMRAE---GATTVVIGHDMRDSSPELAAAFAEGVTAQGLDVVRIGLASTDQL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 89 ELAV-VMEkaCGGIIITASHNPKQWNALKLL--------NENGefLNDAQGKEVLAIAEADGY--SFAEVDALGHvYSne 157
Cdd:PRK09542 78 YFASgLLD--CPGAMFTASHNPAAYNGIKLCragakpvgQDTG--LAAIRDDLIAGVPAYDGPpgTVTERDVLAD-YA-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 158 tynrRHIDSvlaldLVDVDAIAKadFTVAVDAVNSVGGIVIPQLLRVLGVKnIIELNCEATGKFAHTPE--LIPENLTQI 235
Cdd:PRK09542 151 ----AFLRS-----LVDLSGIRP--LKVAVDAGNGMGGHTVPAVLGGLPIT-LLPLYFELDGTFPNHEAnpLDPANLVDL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 236 ADLMRDGKADVGFVVDPDVDRLAIVMENGEMfVEEYTLVA-VADYVLSHTPGSTV-SNLSSSRALRDVTRRHGCEYSAAA 313
Cdd:PRK09542 219 QAFVRETGADIGLAFDGDADRCFVVDERGQP-VSPSAVTAlVAARELAREPGATIiHNLITSRAVPELVAERGGTPVRTR 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 314 VGEVNVVTKMKETGAVIGGEgnggviYPASHYGRD---ALVGVALFLTLLAKSG---KKVSELKATYPEYAiAKNKIQLT 387
Cdd:PRK09542 298 VGHSFIKALMAETGAIFGGE------HSAHYYFRDfwgADSGMLAALHVLAALGeqdRPLSELMADYQRYA-ASGEINST 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2530778051 388 PDiDVDAILEAVKKRYAS--ETITDIDGVKIDFPD-SWVHLRKSNTEPIIRIYSEASTMEKADALAQDIKSVIAS 459
Cdd:PRK09542 371 VA-DAPARMEAVLKAFADriVSVDHLDGVTVDLGDgSWFNLRASNTEPLLRLNVEARTEEEVDALVDEVLAIIRA 444
|
|
| PGM2 |
cd05799 |
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ... |
8-454 |
5.34e-37 |
|
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: 141.49 E-value: 5.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 8 SGIRGTIGgrPGE-GLSPLDIVKFTAAYARFI-SGSTTRKSRTIVVGRDARLSGPMVSDLVTATLTGMGFDV-VNIGLAS 84
Cdd:cd05799 7 AGLRGKMG--AGTnRMNDYTVRQATQGLANYLkKKGPDAKNRGVVIGYDSRHNSREFAELTAAVLAANGIKVyLFDDLRP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 85 TPTTELAVVMEKACGGIIITASHNPKQWNALKLLNENGeflndAQ---------GKEVLAIAEADGYSFAEVDALGHV-Y 154
Cdd:cd05799 85 TPLLSFAVRHLGADAGIMITASHNPKEYNGYKVYWEDG-----AQiipphdaeiAEEIEAVLEPLDIKFEEALDSGLIkY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 155 SNETYNRRHIDSVLALdLVDVDAIAKADFTVAVDAVNSVGGIVIPQLLRVLGVKNII--ELNCEATGKFAHT----PElI 228
Cdd:cd05799 160 IGEEIDDAYLEAVKKL-LVNPELNEGKDLKIVYTPLHGVGGKFVPRALKEAGFTNVIvvEEQAEPDPDFPTVkfpnPE-E 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 229 PENLTQIADLMRDGKADVGFVVDPDVDRLAIVMENGEmfvEEYTL-----VAV--ADYVLSH--------TPGSTVSNLS 293
Cdd:cd05799 238 PGALDLAIELAKKVGADLILATDPDADRLGVAVKDKD---GEWRLltgneIGAllADYLLEQrkekgklpKNPVIVKTIV 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 294 SSRALRDVTRRHGCEYsaaavgeVNVVTKMKETGAVIGG--EGNGGVI--------YPASHYGR--DALVGVALFLTL-- 359
Cdd:cd05799 315 SSELLRKIAKKYGVKV-------EETLTGFKWIGNKIEEleSGGKKFLfgfeesigYLVGPFVRdkDGISAAALLAEMaa 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 360 -LAKSGKKVSE-LKATYPEYAIAKNK-IQLTpdidvdaileaVKKRYASETITDI--------DGVKIDFPD-SWVHLRK 427
Cdd:cd05799 388 yLKAQGKTLLDrLDELYEKYGYYKEKtISIT-----------FEGKEGPEKIKAImdrlrnnpNVLTFYLEDgSRVTVRP 456
|
490 500 510
....*....|....*....|....*....|
gi 2530778051 428 SNTEPIIRIYSEA---STMEKADALAQDIK 454
Cdd:cd05799 457 SGTEPKIKFYIEVvgkKTLEEAEKKLDALK 486
|
|
| PRK15414 |
PRK15414 |
phosphomannomutase; |
14-459 |
1.46e-32 |
|
phosphomannomutase;
Pssm-ID: 185312 Cd Length: 456 Bit Score: 128.91 E-value: 1.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 14 IGGRPGEGLSPlDIV-KFTAAYARFIsgsttrKSRTIVVGRDARLSGPMVSDLVTATLTGMGFDVVNIGLASTPTTELAV 92
Cdd:PRK15414 12 IRGKLGEELNE-DIAwRIGRAYGEFL------KPKTIVLGGDVRLTSETLKLALAKGLQDAGVDVLDIGMSGTEEIYFAT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 93 VMEKACGGIIITASHNPKQWNALKLLNENGEFLNDAQG-KEVLAIAEADGYSFAEVDALGHvYSNETYNRRHIDSVLAld 171
Cdd:PRK15414 85 FHLGVDGGIEVTASHNPMDYNGMKLVREGARPISGDTGlRDVQRLAEANDFPPVDETKRGR-YQQINLRDAYVDHLFG-- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 172 LVDVDAIAKadFTVAVDAVNSVGGIVIPQL---LRVLGVK-NIIELNCEATGKFAH-TPE-LIPENLTQIADLMRDGKAD 245
Cdd:PRK15414 162 YINVKNLTP--LKLVINSGNGAAGPVVDAIearFKALGAPvELIKVHNTPDGNFPNgIPNpLLPECRDDTRNAVIKHGAD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 246 VGFVVDPDVDRLAIVMENGEmFVEEYTLVA-VADYVLSHTPGST-VSNLSSSRALRDVTRRHGCEYSAAAVGEVNVVTKM 323
Cdd:PRK15414 240 MGIAFDGDFDRCFLFDEKGQ-FIEGYYIVGlLAEAFLEKNPGAKiIHDPRLSWNTVDVVTAAGGTPVMSKTGHAFIKERM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 324 KETGAVIGGEgnggviYPASHYGRD------ALVGVALFLTLLAKSGKKVSEL----KATYPeyaiAKNKIQLTPDIDVD 393
Cdd:PRK15414 319 RKEDAIYGGE------MSAHHYFRDfaycdsGMIPWLLVAELVCLKGKTLGELvrdrMAAFP----ASGEINSKLAQPVE 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2530778051 394 AIlEAVKKRYASE--TITDIDGVKIDFPDSWVHLRKSNTEPIIRIYSEA-STMEKADALAQDIKSVIAS 459
Cdd:PRK15414 389 AI-NRVEQHFSREalAVDRTDGISMTFADWRFNLRSSNTEPVVRLNVESrGDVPLMEARTRTLLTLLNE 456
|
|
| PGM_PMM_I |
pfam02878 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I; |
8-140 |
6.02e-30 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
Pssm-ID: 427032 Cd Length: 138 Bit Score: 113.47 E-value: 6.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 8 SGIRGTIGGRPgegLSPLDIVKFTAAYARFISGstTRKSRTIVVGRDARLSGPMVSDLVTATLTGMGFDVVNIGLASTPT 87
Cdd:pfam02878 7 SGIRGKVGVGE---LTPEFALKLGQAIASYLRA--QGGGGKVVVGRDTRYSSRELARALAAGLASNGVEVILLGLLPTPA 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2530778051 88 TELAVVMEKACGGIIITASHNPKQWNALKLLNENGEFLNDAQGKEVLAIAEAD 140
Cdd:pfam02878 82 VSFATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEKE 134
|
|
| PLN02371 |
PLN02371 |
phosphoglucosamine mutase family protein |
8-459 |
3.55e-24 |
|
phosphoglucosamine mutase family protein
Pssm-ID: 215211 [Multi-domain] Cd Length: 583 Bit Score: 105.52 E-value: 3.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 8 SGIRGT-IGGRPGEG--LSPLDIVKFTAAYARF-ISGSTTRKSR--TIVVGRDARLSGPMVSDLVTATLTGMGFDVVNIG 81
Cdd:PLN02371 71 SDIRGVaVEGVEGEPvtLTPPAVEAIGAAFAEWlLEKKKADGSGelRVSVGRDPRISGPRLADAVFAGLASAGLDVVDMG 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 82 LASTPTTELAVVMEKACG--GIIITASHNPKQWNALKLLNENGEfLNDAQGKEVLAIAeADGYSfAEVDALGHVYSNETY 159
Cdd:PLN02371 151 LATTPAMFMSTLTEREDYdaPIMITASHLPYNRNGLKFFTKDGG-LGKPDIKDILERA-ARIYK-EWSDEGLLKSSSGAS 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 160 NRRH-ID--SVLALDLvdVDAIAKA------------DFTVAVDAVNSVGGIVIPQLLRVLGVKNIIELNCEATGKFA-H 223
Cdd:PLN02371 228 SVVCrVDfmSTYAKHL--RDAIKEGvghptnyetpleGFKIVVDAGNGAGGFFAEKVLEPLGADTSGSLFLEPDGMFPnH 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 224 TPEliPENLT---QIADLMRDGKADVGFVVDPDVDRLAIVMENGEMFVEEYTLVAVADYVLSHTPGST-VSNLSSSRAL- 298
Cdd:PLN02371 306 IPN--PEDKAamsATTQAVLANKADLGIIFDTDVDRSAVVDSSGREINRNRLIALMSAIVLEEHPGTTiVTDSVTSDGLt 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 299 RDVTRRHG--CEYSaaaVGEVNVVTKMKETGAVigGE---------GNGGViyPASHYGRD-ALVGVALFLTL----LAK 362
Cdd:PLN02371 384 TFIEKKGGkhHRFK---RGYKNVIDKGVRLNSD--GEethlmietsGHGAL--KENHFLDDgAYLAVKIIIELvrmrAAG 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 363 SGKKVSELKATYPEYAIAKN---KIQLTPDiDVDAILEAVKKRYASETITDID---------GVKI-DFPDS---WVHLR 426
Cdd:PLN02371 457 AGGGLGDLIEDLEEPLEAVElrlKILDEGK-DFKAYGEEVLEHLRNSIESDGKlegapvnyeGVRVsDEGEGfggWFLLR 535
|
490 500 510
....*....|....*....|....*....|...
gi 2530778051 427 KSNTEPIIRIYSEASTMEKADALAQDIKSVIAS 459
Cdd:PLN02371 536 QSLHDPVIPLNIESSSPGGAQKMALVVLTWLKE 568
|
|
| PGM_PMM_III |
pfam02880 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III; |
271-377 |
5.15e-22 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
Pssm-ID: 460733 Cd Length: 115 Bit Score: 90.59 E-value: 5.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 271 YTLVAVADYVLSHT---PGST-VSNLSSSRALRDVTRRHGCEYSAAAVGEVNVVTKMKETGAVIGGEGNGGVIYPASHYG 346
Cdd:pfam02880 4 QILALLAKYLLEQGklpPGAGvVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEGALFGGEESGHIIFLDHATT 83
|
90 100 110
....*....|....*....|....*....|..
gi 2530778051 347 RDALVGVALFLTLLAKSGKKVSEL-KATYPEY 377
Cdd:pfam02880 84 KDGILAALLVLEILARTGKSLSELlEELPEKY 115
|
|
| ManB |
cd03088 |
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ... |
8-451 |
6.81e-21 |
|
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: 94.96 E-value: 6.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 8 SGIRGTIggrpgEGLSPLDIVKFTAAYARFISgsTTRKSRTIVVGRDARLSGPMVSDLVTATLTGMGFDVVNIGlaSTPT 87
Cdd:cd03088 5 SGLRGLV-----TDLTDEVCYAYTRAFLQHLE--SKFPGDTVAVGRDLRPSSPRIAAACAAALRDAGFRVVDCG--AVPT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 88 TELAVV-MEKACGGIIITASHNPKQWNALKLLNENGEFLN-DAQGKEVLAIAEADGYSFAEVDALGHVYSNET-YNRRHI 164
Cdd:cd03088 76 PALALYaMKRGAPAIMVTGSHIPADRNGLKFYRPDGEITKaDEAAILAALVELPEALFDPAGALLPPDTDAADaYIARYT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 165 DSVLAldlvdvDAIAKAdfTVAVDAVNSVGGIVIPQLLRVLGVKnIIELncEATGKF------AHTPELIpenlTQIADL 238
Cdd:cd03088 156 DFFGA------GALKGL--RIGVYQHSSVGRDLLVRILEALGAE-VVPL--GRSDTFipvdteAVRPEDR----ALAAAW 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 239 MRDGKADVGFVVDPDVDRLAIVMENGEM------------FVEEYTLVavadyvlshTPGSTVSNLSSSRALRDVTR-RH 305
Cdd:cd03088 221 AAEHGLDAIVSTDGDGDRPLVADETGEWlrgdilglltarFLGADTVV---------TPVSSNSAIELSGFFKRVVRtRI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 306 GCEYSAAAVGEVNVvtkmKETGAVIGGEGNGGVI--YPASHYG--------RDALVGVALFLTLLAKSGKKVSELKATYP 375
Cdd:cd03088 292 GSPYVIAAMAEAAA----AGAGRVVGYEANGGFLlgSDIERNGrtlkalptRDAVLPILAVLAAAKEAGIPLSELVASLP 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 376 EYAIAKNKIQ--------------LTPDIDVDAILEAVKKRYASetITDIDGVKIDFPD-SWVHLRKSNTEPIIRIYSEA 440
Cdd:cd03088 368 ARFTASDRLQnfpteksqaliarlSADPEARAAFFFALGGEVAS--IDTTDGLRMTFANgDIVHLRPSGNAPELRCYVEA 445
|
490
....*....|.
gi 2530778051 441 STMEKADALAQ 451
Cdd:cd03088 446 DSEERARELLA 456
|
|
| glmM |
PRK10887 |
phosphoglucosamine mutase; Provisional |
44-461 |
1.45e-20 |
|
phosphoglucosamine mutase; Provisional
Pssm-ID: 236787 Cd Length: 443 Bit Score: 93.66 E-value: 1.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 44 RKSRTIVVGRDARLSGPMVSDLVTATLTGMGFDVVNIGLASTPttelAVVM----EKACGGIIITASHNPKQWNALKLLN 119
Cdd:PRK10887 37 QGRPKVLIGKDTRISGYMLESALEAGLAAAGVDVLLTGPMPTP----AVAYltrtLRAEAGIVISASHNPYYDNGIKFFS 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 120 ENGEFLNDAQGKEVLAIAEADgYSFAEVDALGHVYSNETYNRRHID----------SVLALDLVdVDAIAKADFTVAvda 189
Cdd:PRK10887 113 ADGTKLPDEVELAIEAELDKP-LTCVESAELGKASRINDAAGRYIEfckstfpnelSLRGLKIV-VDCANGATYHIA--- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 190 vnsvggiviPQLLRVLGVkNIIELNCEATG-----KFAHTPeliPENLTQIadlMRDGKADVGFVVDPDVDRLAIVMENG 264
Cdd:PRK10887 188 ---------PNVFRELGA-EVIAIGCEPNGlnindECGATD---PEALQAA---VLAEKADLGIAFDGDGDRVIMVDHLG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 265 EMFVEEYTLVAVADYVLSHTP------GSTVSNLSSSRALRdvtrRHGCEYSAAAVGEVNVVTKMKETGAVIGGEGNGGV 338
Cdd:PRK10887 252 NLVDGDQLLYIIARDRLRRGQlrggvvGTLMSNMGLELALK----QLGIPFVRAKVGDRYVLEKLQEKGWRLGGENSGHI 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 339 IYPASHYGRDALVGVALFLTLLAKSGKKVSELKAT---YPEYAI-------AKNKIQltpDIDVDAILEAVKKRYASEti 408
Cdd:PRK10887 328 LCLDKTTTGDGIVAALQVLAAMVRSGMSLADLCSGmklFPQVLInvrfkpgADDPLE---SEAVKAALAEVEAELGGR-- 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2530778051 409 tdidgvkidfpdSWVHLRKSNTEPIIRIYSEASTMEKADALAQDIKSVIASLA 461
Cdd:PRK10887 403 ------------GRVLLRKSGTEPLIRVMVEGEDEAQVTALAERIADAVKAAA 443
|
|
| PGM_PMM_II |
pfam02879 |
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II; |
163-264 |
3.44e-20 |
|
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
Pssm-ID: 427033 Cd Length: 102 Bit Score: 85.04 E-value: 3.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 163 HIDSVLALdlVDVDAIAKADFTVAVDAVNSVGGIVIPQLLRVLGVkNIIELNCEATGKF-AHTPELIP-ENLTQIADLMR 240
Cdd:pfam02879 2 YIDHLLEL--VDSEALKKRGLKVVYDPLHGVGGGYLPELLKRLGC-DVVEENCEPDPDFpTRAPNPEEpEALALLIELVK 78
|
90 100
....*....|....*....|....
gi 2530778051 241 DGKADVGFVVDPDVDRLAIVMENG 264
Cdd:pfam02879 79 SVGADLGIATDGDADRLGVVDERG 102
|
|
| PRK07564 |
PRK07564 |
phosphoglucomutase; Validated |
48-439 |
6.03e-15 |
|
phosphoglucomutase; Validated
Pssm-ID: 236050 Cd Length: 543 Bit Score: 77.10 E-value: 6.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 48 TIVVGRDAR-LSGPMvsdLVTAT--LTGMGFDVV---NIGLASTPTTELAVV-----MEKACGGIIITASHNPkqwnalk 116
Cdd:PRK07564 78 PLFVGGDTHaLSEPA---IQSALevLAANGVGVVivgRGGYTPTPAVSHAILkyngrGGGLADGIVITPSHNP------- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 117 llNENGEF-LNDAQG---------------KEVLA--IAEADGYSFAEVDALGHVysnetynrRHIDSV---LAL--DLV 173
Cdd:PRK07564 148 --PEDGGIkYNPPNGgpadtdvtdaiearaNELLAygLKGVKRIPLDRALASMTV--------EVIDPVadyVEDleNVF 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 174 DVDAIAKADFTVAVDAVNSVGGIVIPQLLRVLGVkNIIELNCEATGKFAHTPelIPE--------NLTQ-IADLM-RDGK 243
Cdd:PRK07564 218 DFDAIRKAGLRLGVDPLGGATGPYWKAIAERYGL-DLTVVNAPVDPTFNFMP--LDDdgkirmdcSSPYaMAGLLaLKDA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 244 ADVGFVVDPDVDRLAIVMENGEMFVEEYtLVAVADYVLSHTPG---------STVsnlsSSRALRDVTRRHGCEysaaaV 314
Cdd:PRK07564 295 FDLAFANDPDGDRHGIVTPGGLMNPNHY-LAVAIAYLFHHRPGwragagvgkTLV----SSAMIDRVAAKLGRK-----L 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 315 GEVNV-----VTKMKETGAVIGGEGNGGviypAS---HYGR------DALVGVALFLTLLAKSGKKVS----ELKATY-- 374
Cdd:PRK07564 365 YEVPVgfkwfVNGLDDGSLGFGGEESAG----ASflrRDGSvwttdkDGLIAVLLAAEILAVTGKSPSeiyrELWARFgr 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 375 PEY------AIAKNK---IQLTPDiDVDAileavkKRYASETIT-----------DIDGVKIDFPDSWVHLRKSNTEPII 434
Cdd:PRK07564 441 PYYsrhdapATPEQKaalRKLSPE-LVGA------TELAGDPIDaslteapgngaAIGGLKVVTENGWFAARPSGTETTY 513
|
....*
gi 2530778051 435 RIYSE 439
Cdd:PRK07564 514 KIYAE 518
|
|
| PTZ00150 |
PTZ00150 |
phosphoglucomutase-2-like protein; Provisional |
41-451 |
6.14e-12 |
|
phosphoglucomutase-2-like protein; Provisional
Pssm-ID: 240294 Cd Length: 584 Bit Score: 67.79 E-value: 6.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 41 STTRKSRTIVVGRDARLSGPMVSDLVTATLTGMGFDVVNIG-LASTPTTELAVVMEKACGGIIITASHNPKQWNALKLLN 119
Cdd:PTZ00150 84 GQALKSRGVVIGYDGRYHSRRFAEITASVFLSKGFKVYLFGqTVPTPFVPYAVRKLKCLAGVMVTASHNPKEDNGYKVYW 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 120 ENGEFLNDAQGKEVLA--------IAEADGYsFAE---VDALGHVYSNETYNRRHIDSVLALDLVDVdaiaKADFTvavd 188
Cdd:PTZ00150 164 SNGAQIIPPHDKNISAkilsnlepWSSSWEY-LTEtlvEDPLAEVSDAYFATLKSEYNPACCDRSKV----KIVYT---- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 189 AVNSVGGIVIPQLLRVLGVKNII--ELNCEATGKFAHTPELIPE------NLT-QIADlmrdgKADVGFVV--DPDVDRL 257
Cdd:PTZ00150 235 AMHGVGTRFVQKALHTVGLPNLLsvAQQAEPDPEFPTVTFPNPEegkgalKLSmETAE-----AHGSTVVLanDPDADRL 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 258 AIV--MENG-EMFVEEYTLVAVADYVL--------SHTPGSTVSNLSSSRALRDVTRRHGCEYSAAAVGEVNVVTKMKET 326
Cdd:PTZ00150 310 AVAekLNNGwKIFTGNELGALLAWWAMkryrrqgiDKSKCFFICTVVSSRMLKKMAEKEGFQYDETLTGFKWIGNKAIEL 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 327 GAVIGG-------EGNGGVIypaSHYGRD-----ALVGVALFLTLLAKSGKKVSE-LKATYPEYA--IAKNKIQLTPD-I 390
Cdd:PTZ00150 390 NAENGLttlfayeEAIGFML---GTRVRDkdgvtAAAVVAEMALYLYERGKTLVEhLESLYKQYGyhFTNNSYYICYDpS 466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 391 DVDAILEAVKK--RY----ASETITDI----DGVKIDFPD---------------------SWVHLRKSNTEPIIRIYSE 439
Cdd:PTZ00150 467 RIVSIFNDIRNngSYptklGGYPVTRIrdltTGYDTATPDgkpllpvsastqmitfyfengAIITIRGSGTEPKLKWYAE 546
|
490
....*....|..
gi 2530778051 440 ASTMEKADALAQ 451
Cdd:PTZ00150 547 LSGTKDEAVEKE 558
|
|
| PLN02307 |
PLN02307 |
phosphoglucomutase |
45-256 |
1.12e-07 |
|
phosphoglucomutase
Pssm-ID: 177942 [Multi-domain] Cd Length: 579 Bit Score: 54.28 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 45 KSRTIVVGRDARLSGPMVSDLVTATLTGMGFDVVNIG---LASTPTTElAVVME----KACGGIIITASHNP----KQWn 113
Cdd:PLN02307 60 KGATLVLGGDGRYFNKEAIQIIIKIAAANGVRRVWVGqngLLSTPAVS-AVIRErdgsKANGGFILTASHNPggpeEDF- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 114 ALKLLNENG----EFLNDAQGKEVLAIAE---ADGYSFAEVDALGHVY--SNETYNRRHIDSV-----LALDLVDVDAI- 178
Cdd:PLN02307 138 GIKYNYESGqpapESITDKIYGNTLTIKEykmAEDIPDVDLSAVGVTKfgGPEDFDVEVIDPVedyvkLMKSIFDFELIk 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 179 ---AKADFTVAVDAVNSVGG-IVIPQLLRVLGVKNIIELNCEATGKFAH---TPELI-PENLTQIADLMRDGKA----DV 246
Cdd:PLN02307 218 kllSRPDFTFCFDAMHGVTGaYAKRIFVEELGAPESSLLNCVPKEDFGGghpDPNLTyAKELVKRMGLGKTSYGdeppEF 297
|
250
....*....|
gi 2530778051 247 GFVVDPDVDR 256
Cdd:PLN02307 298 GAASDGDGDR 307
|
|
| PGM1 |
cd03085 |
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ... |
44-260 |
2.70e-07 |
|
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: 52.99 E-value: 2.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 44 RKSRTIVVGRDARLSGPMVSDLVTATLTGMGFDVVNIG---LASTPTTELAVVMEKACGGIIITASHNPKQWNA---LKL 117
Cdd:cd03085 47 LKGATLVVGGDGRYYNKEAIQIIIKIAAANGVGKVVVGqngLLSTPAVSAVIRKRKATGGIILTASHNPGGPEGdfgIKY 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 118 LNENG----EFLNDAQGKEVLAIAE---ADGysfAEVDaLGHVYSNEtYNRRH-----IDSV-----LALDLVDVDAIAK 180
Cdd:cd03085 127 NTSNGgpapESVTDKIYEITKKITEykiADD---PDVD-LSKIGVTK-FGGKPftvevIDSVedyveLMKEIFDFDAIKK 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 181 A----DFTVAVDAVNSVGG-----IVIPQllrvLGVKNIIELNCEATGKF-AHTPEliPeNLTQIADL---MRDGKADVG 247
Cdd:cd03085 202 LlsrkGFKVRFDAMHGVTGpyakkIFVEE----LGAPESSVVNCTPLPDFgGGHPD--P-NLTYAKDLvelMKSGEPDFG 274
|
250
....*....|...
gi 2530778051 248 FVVDPDVDRLAIV 260
Cdd:cd03085 275 AASDGDGDRNMIL 287
|
|
| PGM_PMM_IV |
pfam00408 |
Phosphoglucomutase/phosphomannomutase, C-terminal domain; |
396-458 |
2.96e-06 |
|
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
Pssm-ID: 425666 Cd Length: 71 Bit Score: 44.57 E-value: 2.96e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2530778051 396 LEAVKKRYAsetiTDIDGVKIDFPD-SWVHLRKSNTEPIIRIYSEASTMEKADALAQDIKSVIA 458
Cdd:pfam00408 12 LAALAAILK----VFADAEKILGEDgRRLDVRPSGTEPVLRVMVEGDSDEELARLADEIADLLE 71
|
|
| PGM3 |
cd03086 |
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ... |
48-457 |
1.82e-05 |
|
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: 46.82 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 48 TIVVGRDARLSGPMVSDLVTATLTGMGFDVVNIGLASTPTTELAVvmekacggiiitashnpkqwnalKLLNENGEFlnd 127
Cdd:cd03086 104 NVFVGRDTRPSGPALLQALLDGLKALGGNVIDYGLVTTPQLHYLV-----------------------RAANTEGAY--- 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 128 aqgkevlAIAEADGYSFAEVDALGHVYSNETYNRRHIDSVLaldlvdvdaiakadftvaVDAVNSVGGIVIPQLLRVLGV 207
Cdd:cd03086 158 -------GEPTEEGYYEKLSKAFNELYNLLQDGGDEPEKLV------------------VDCANGVGALKLKELLKRLKK 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 208 KNIIEL---NCEATGK--------FAHTPELIPENLTQIADLMR----DGKAD--VGFVVDP-------DVDRLAIVMEn 263
Cdd:cd03086 213 GLSVKIindGEEGPELlndgcgadYVKTKQKPPRGFELKPPGVRccsfDGDADrlVYFYPDSsnkfhllDGDKIATLFA- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 264 geMFVEEytLVAVADYVLSHTPG---STVSNLSSSRALRDVTR-RHGC-------------EYSAAAVGEVN----VVTK 322
Cdd:cd03086 292 --KFIKE--LLKKAGEELKLTIGvvqTAYANGASTKYLEDVLKvPVVCtptgvkhlhhaaeEFDIGVYFEANghgtVLFS 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 323 MKETGAVIGGEGNGGVIYPASH----YGR-------DALVGVALFLTLLAKSGKKVSELKATYPE--------YAIAKNK 383
Cdd:cd03086 368 ESALAKIEENSSLSDEQEKAAKtllaFSRlinqtvgDAISDMLAVELILAALGWSPQDWDNLYTDlpnrqlkvKVPDRSV 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2530778051 384 IQLTPDIDV--------DAILEAVKKryasetitdidgvkidFPDSWVHLRKSNTEPIIRIYSEASTMEKADALAQDIKS 455
Cdd:cd03086 448 IKTTDAERRlvepkglqDKIDAIVAK----------------YNNGRAFVRPSGTEDVVRVYAEAATQEEADELANEVAE 511
|
..
gi 2530778051 456 VI 457
Cdd:cd03086 512 LV 513
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
425-457 |
1.80e-04 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 43.87 E-value: 1.80e-04
10 20 30
....*....|....*....|....*....|...
gi 2530778051 425 LRKSNTEPIIRIYSEASTMEKADALAQDIKSVI 457
Cdd:PTZ00302 546 IRPSGTEPVVRVYAEAPTLEQADELANEVKGLV 578
|
|
| PLN02895 |
PLN02895 |
phosphoacetylglucosamine mutase |
426-461 |
1.10e-03 |
|
phosphoacetylglucosamine mutase
Pssm-ID: 215485 Cd Length: 562 Bit Score: 41.55 E-value: 1.10e-03
10 20 30
....*....|....*....|....*....|....*.
gi 2530778051 426 RKSNTEPIIRIYSEASTMEKADALAQDIKSVIASLA 461
Cdd:PLN02895 520 RPSGTEDVVRVYAEASTQEAADSLAREVARLVYDLL 555
|
|
| PTZ00302 |
PTZ00302 |
N-acetylglucosamine-phosphate mutase; Provisional |
100-126 |
1.17e-03 |
|
N-acetylglucosamine-phosphate mutase; Provisional
Pssm-ID: 240352 [Multi-domain] Cd Length: 585 Bit Score: 41.18 E-value: 1.17e-03
10 20
....*....|....*....|....*..
gi 2530778051 100 GIIITASHNPKQWNALKLLNENGEFLN 126
Cdd:PTZ00302 78 GVMITASHNPIQDNGVKIIDPDGGMLE 104
|
|
| |
