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Conserved domains on  [gi|1225985232|emb|SNU03343|]
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phosphomannomutase [Prevotellaceae bacterium MN60]

Protein Classification

phosphohexomutase domain-containing protein( domain architecture ID 1562470)

phosphohexomutase domain-containing protein catalyzes catalyzes the reversible conversion of 1-phospho to 6-phosphohexose, with various sugars including glucose, mannose, glucosamine, and N-acetylglucosamine

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
phosphohexomutase super family cl38939
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ...
 4-452 0e+00

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.


The actual alignment was detected with superfamily member cd05803:

Pssm-ID: 476822  Cd Length: 445  Bit Score: 581.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232   4 IKSISGIRGTIGGrtgdTLNPLDIVKFTTAYATFIPRKT--GRIVVGRDGRISGHMVRDIVCGTLVGMGYDVLDIGYAST 81
Cdd:cd05803     1 IISISGIRGIVGE----GLTPEVITRYVAAFATWQPERTkgGKIVVGRDGRPSGPMLEKIVIGALLACGCDVIDLGIAPT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232  82 PTTELAVRMSGADGGIIITASHNPRQWNALKLLNSEGEFLTAADGNKVLEIAEKEDFNYADVDQLGHVTIDNSYDDRHVQ 161
Cdd:cd05803    77 PTVQVLVRQSQASGGIIITASHNPPQWNGLKFIGPDGEFLTPDEGEEVLSCAEAGSAQKAGYDQLGEVTFSEDAIAEHID 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 162 SVLDLKLVDVEAIKKANFKVCVDSINSVGGLILPKLLDKLGVSYQFLNGEVTGDFAHNPEPLEKNLTGIMDEMKTGKYDL 241
Cdd:cd05803   157 KVLALVDVDVIKIRERNFKVAVDSVNGAGGLLIPRLLEKLGCEVIVLNCEPTGLFPHTPEPLPENLTQLCAAVKESGADV 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 242 GIVVDPDVDRLAFIREDGKMFGEEYTLVSVADYVLSQ--TKGNTVSNLSSTRALRDITEKHGGTYAAAAVGEVNVTTKMK 319
Cdd:cd05803   237 GFAVDPDADRLALVDEDGRPIGEEYTLALAVDYVLKYggRKGPVVVNLSTSRALEDIARKHGVPVFRSAVGEANVVEKMK 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 320 EVNAVIGGEGNGGVIYPESHYGRDALVGIALFLTSLAKKGCKVSELRKALPHYKIAKNRIDLTPEtDVDAILVKVKEMFA 399
Cdd:cd05803   317 EVDAVIGGEGNGGVILPDVHYGRDSLVGIALVLQLLAASGKPLSEIVDELPQYYISKTKVTIAGE-ALERLLKKLEAYFK 395

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1225985232 400 QdasAKVNDIDGVKIDFPDRWVHLRKSNTEPIIRVYSEAATMETADELGKKLM 452
Cdd:cd05803   396 D---AEASTLDGLRLDSEDSWVHVRPSNTEPIVRIIAEAPTQDEAEALADRFI 445
 
Name Accession Description Interval E-value
PGM_like4 cd05803
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ...
 4-452 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: 581.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232   4 IKSISGIRGTIGGrtgdTLNPLDIVKFTTAYATFIPRKT--GRIVVGRDGRISGHMVRDIVCGTLVGMGYDVLDIGYAST 81
Cdd:cd05803     1 IISISGIRGIVGE----GLTPEVITRYVAAFATWQPERTkgGKIVVGRDGRPSGPMLEKIVIGALLACGCDVIDLGIAPT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232  82 PTTELAVRMSGADGGIIITASHNPRQWNALKLLNSEGEFLTAADGNKVLEIAEKEDFNYADVDQLGHVTIDNSYDDRHVQ 161
Cdd:cd05803    77 PTVQVLVRQSQASGGIIITASHNPPQWNGLKFIGPDGEFLTPDEGEEVLSCAEAGSAQKAGYDQLGEVTFSEDAIAEHID 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 162 SVLDLKLVDVEAIKKANFKVCVDSINSVGGLILPKLLDKLGVSYQFLNGEVTGDFAHNPEPLEKNLTGIMDEMKTGKYDL 241
Cdd:cd05803   157 KVLALVDVDVIKIRERNFKVAVDSVNGAGGLLIPRLLEKLGCEVIVLNCEPTGLFPHTPEPLPENLTQLCAAVKESGADV 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 242 GIVVDPDVDRLAFIREDGKMFGEEYTLVSVADYVLSQ--TKGNTVSNLSSTRALRDITEKHGGTYAAAAVGEVNVTTKMK 319
Cdd:cd05803   237 GFAVDPDADRLALVDEDGRPIGEEYTLALAVDYVLKYggRKGPVVVNLSTSRALEDIARKHGVPVFRSAVGEANVVEKMK 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 320 EVNAVIGGEGNGGVIYPESHYGRDALVGIALFLTSLAKKGCKVSELRKALPHYKIAKNRIDLTPEtDVDAILVKVKEMFA 399
Cdd:cd05803   317 EVDAVIGGEGNGGVILPDVHYGRDSLVGIALVLQLLAASGKPLSEIVDELPQYYISKTKVTIAGE-ALERLLKKLEAYFK 395

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1225985232 400 QdasAKVNDIDGVKIDFPDRWVHLRKSNTEPIIRVYSEAATMETADELGKKLM 452
Cdd:cd05803   396 D---AEASTLDGLRLDSEDSWVHVRPSNTEPIVRIIAEAPTQDEAEALADRFI 445
Arch_GlmM TIGR03990
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ...
 2-455 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: 581.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232   2 TLIKSISGIRGTIGgrtgDTLNPLDIVKFTTAYATFIPRktGRIVVGRDGRISGHMVRDIVCGTLVGMGYDVLDIGYAST 81
Cdd:TIGR03990   1 MLLFGTSGIRGIVG----EELTPELALKVGKAFGTYLRG--GKVVVGRDTRTSGPMLENAVIAGLLSTGCDVVDLGIAPT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232  82 PTTELAVRMSGADGGIIITASHNPRQWNALKLLNSEGEFLTAADGNKVLEIAEKEDFNYADVDQLGHVTIDNSYDDRHVQ 161
Cdd:TIGR03990  75 PTLQYAVRELGADGGIMITASHNPPEYNGIKLLNSDGTELSREQEEEIEEIAESGDFERADWDEIGTVTSDEDAIDDYIE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 162 SVLDlkLVDVEAIKKANFKVCVDSINSVGGLILPKLLDKLGVSYQFLNGEVTGDF-AHNPEPLEKNLTGIMDEMKTGKYD 240
Cdd:TIGR03990 155 AILD--KVDVEAIRKKGFKVVVDCGNGAGSLTTPYLLRELGCKVITLNCQPDGTFpGRNPEPTPENLKDLSALVKATGAD 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 241 LGIVVDPDVDRLAFIREDGKMFGEEYTLVSVADYVLSQTKGNTVSNLSSTRALRDITEKHGGTYAAAAVGEVNVTTKMKE 320
Cdd:TIGR03990 233 LGIAHDGDADRLVFIDEKGRFIGGDYTLALFAKYLLEHGGGKVVTNVSSSRAVEDVAERHGGEVIRTKVGEVNVAEKMKE 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 321 VNAVIGGEGNGGVIYPESHYGRDALVGIALFLTSLAKKGCKVSELRKALPHYKIAKNRIDLtPETDVDAILVKVKEMFAQ 400
Cdd:TIGR03990 313 EGAVFGGEGNGGWIFPDHHYCRDGLMAAALFLELLAEEGKPLSELLAELPKYPMSKEKVEL-PDEDKEEVMEAVEEEFAD 391

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1225985232 401 dasAKVNDIDGVKIDFPDRWVHLRKSNTEPIIRVYSEAATMETADELGKKLMKVV 455
Cdd:TIGR03990 392 ---AEIDTIDGVRIDFEDGWVLVRPSGTEPIVRIYAEAKTEERAEELLEEGRSLV 443
ManB COG1109
Phosphomannomutase [Carbohydrate transport and metabolism];
4-455 1.74e-147

Phosphomannomutase [Carbohydrate transport and metabolism];


Pssm-ID: 440726 [Multi-domain]  Cd Length: 456  Bit Score: 428.08  E-value: 1.74e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232   4 IKSISGIRGTIGgrtgDTLNPLDIVKFTTAYATFIPRKTG-RIVVGRDGRISGHMVRDIVCGTLVGMGYDVLDIGYASTP 82
Cdd:COG1109     6 LFGTDGIRGIVG----EELTPEFVLKLGRAFGTYLKEKGGpKVVVGRDTRLSSPMLARALAAGLASAGIDVYDLGLVPTP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232  83 TTELAVRMSGADGGIIITASHNPRQWNALKLLNSEGEFLTAADGNKVLEIAEKEDFNYADVDQLGHVTIDNSYDDRHVQS 162
Cdd:COG1109    82 ALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKEDFRRAEAEEIGKVTRIEDVLEAYIEA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 163 VldLKLVDvEAIKKANFKVCVDSINSVGGLILPKLLDKLGVSYQFLNGEVTGDF-AHNPEPLEKNLTGIMDEMKTGKYDL 241
Cdd:COG1109   162 L--KSLVD-EALRLRGLKVVVDCGNGAAGGVAPRLLRELGAEVIVLNAEPDGNFpNHNPNPEPENLEDLIEAVKETGADL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 242 GIVVDPDVDRLAFIREDGKMFGEEYTLVSVADYVLSQTKGNT-VSNLSSTRALRDITEKHGGTYAAAAVGEVNVTTKMKE 320
Cdd:COG1109   239 GIAFDGDADRLGVVDEKGRFLDGDQLLALLARYLLEKGPGGTvVVTVMSSLALEDIAEKHGGEVVRTKVGFKYIKEKMRE 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 321 VNAVIGGEGNGGVIYPESHYGRDALVGIALFLTSLAKKGCKVSELRKALPHYKIAKNRIDLTPETDVDAILVKVKEMFAQ 400
Cdd:COG1109   319 TGAVLGGEESGGIIFPDFVPTDDGILAALLLLELLAKQGKSLSELLAELPRYPQPEINVRVPDEEKIGAVMEKLREAVED 398

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1225985232 401 DasAKVNDIDGVKIDFPDR-WVHLRKSNTEPIIRVYSEAATMETADELGKKLMKVV 455
Cdd:COG1109   399 K--EELDTIDGVKVDLEDGgWVLVRPSGTEPLLRVYAEAKDEEEAEELLAELAELV 452
PRK15414 PRK15414
phosphomannomutase;
14-438 2.78e-34

phosphomannomutase;


Pssm-ID: 185312  Cd Length: 456  Bit Score: 133.53  E-value: 2.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232  14 IGGRTGDTLNPlDIV-KFTTAYATFIPRKTgrIVVGRDGRISGHMVRDIVCGTLVGMGYDVLDIGYASTPTTELAVRMSG 92
Cdd:PRK15414   12 IRGKLGEELNE-DIAwRIGRAYGEFLKPKT--IVLGGDVRLTSETLKLALAKGLQDAGVDVLDIGMSGTEEIYFATFHLG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232  93 ADGGIIITASHNPRQWNALKLLNSEGEFLTAADG-NKVLEIAEKEDF---NYADVDQLGHVTIDNSYDDrHVQSVLDLKl 168
Cdd:PRK15414   89 VDGGIEVTASHNPMDYNGMKLVREGARPISGDTGlRDVQRLAEANDFppvDETKRGRYQQINLRDAYVD-HLFGYINVK- 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 169 vdveaiKKANFKVCVDSINSVGGLILPKL---LDKLGVSYQFLNGEVT--GDFAHN-PEPLeknLTGIMDEMKTG----K 238
Cdd:PRK15414  167 ------NLTPLKLVINSGNGAAGPVVDAIearFKALGAPVELIKVHNTpdGNFPNGiPNPL---LPECRDDTRNAvikhG 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 239 YDLGIVVDPDVDRLAFIREDGKmFGEEYTLVS-VADYVLSQTKG-NTVSNLSSTRALRDITEKHGGTYAAAAVGEVNVTT 316
Cdd:PRK15414  238 ADMGIAFDGDFDRCFLFDEKGQ-FIEGYYIVGlLAEAFLEKNPGaKIIHDPRLSWNTVDVVTAAGGTPVMSKTGHAFIKE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 317 KMKEVNAVIGGEGNGgviypeSHYGRD------ALVGIALFLTSLAKKGCKVSELRK----ALPhykiAKNRIDLTPETD 386
Cdd:PRK15414  317 RMRKEDAIYGGEMSA------HHYFRDfaycdsGMIPWLLVAELVCLKGKTLGELVRdrmaAFP----ASGEINSKLAQP 386

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1225985232 387 VDAIlVKVKEMFAQDASAkVNDIDGVKIDFPDRWVHLRKSNTEPIIRVYSEA 438
Cdd:PRK15414  387 VEAI-NRVEQHFSREALA-VDRTDGISMTFADWRFNLRSSNTEPVVRLNVES 436
PGM_PMM_I pfam02878
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
8-139 4.00e-31

Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;


Pssm-ID: 427032  Cd Length: 138  Bit Score: 116.55  E-value: 4.00e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232   8 SGIRGTIGGrtgDTLNPLDIVKFTTAYATFIP--RKTGRIVVGRDGRISGHMVRDIVCGTLVGMGYDVLDIGYASTPTTE 85
Cdd:pfam02878   7 SGIRGKVGV---GELTPEFALKLGQAIASYLRaqGGGGKVVVGRDTRYSSRELARALAAGLASNGVEVILLGLLPTPAVS 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1225985232  86 LAVRMSGADGGIIITASHNPRQWNALKLLNSEGEFLTAADGNKVLEIAEKEDFN 139
Cdd:pfam02878  84 FATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEKEDFY 137
 
Name Accession Description Interval E-value
PGM_like4 cd05803
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ...
 4-452 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: 581.96  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232   4 IKSISGIRGTIGGrtgdTLNPLDIVKFTTAYATFIPRKT--GRIVVGRDGRISGHMVRDIVCGTLVGMGYDVLDIGYAST 81
Cdd:cd05803     1 IISISGIRGIVGE----GLTPEVITRYVAAFATWQPERTkgGKIVVGRDGRPSGPMLEKIVIGALLACGCDVIDLGIAPT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232  82 PTTELAVRMSGADGGIIITASHNPRQWNALKLLNSEGEFLTAADGNKVLEIAEKEDFNYADVDQLGHVTIDNSYDDRHVQ 161
Cdd:cd05803    77 PTVQVLVRQSQASGGIIITASHNPPQWNGLKFIGPDGEFLTPDEGEEVLSCAEAGSAQKAGYDQLGEVTFSEDAIAEHID 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 162 SVLDLKLVDVEAIKKANFKVCVDSINSVGGLILPKLLDKLGVSYQFLNGEVTGDFAHNPEPLEKNLTGIMDEMKTGKYDL 241
Cdd:cd05803   157 KVLALVDVDVIKIRERNFKVAVDSVNGAGGLLIPRLLEKLGCEVIVLNCEPTGLFPHTPEPLPENLTQLCAAVKESGADV 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 242 GIVVDPDVDRLAFIREDGKMFGEEYTLVSVADYVLSQ--TKGNTVSNLSSTRALRDITEKHGGTYAAAAVGEVNVTTKMK 319
Cdd:cd05803   237 GFAVDPDADRLALVDEDGRPIGEEYTLALAVDYVLKYggRKGPVVVNLSTSRALEDIARKHGVPVFRSAVGEANVVEKMK 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 320 EVNAVIGGEGNGGVIYPESHYGRDALVGIALFLTSLAKKGCKVSELRKALPHYKIAKNRIDLTPEtDVDAILVKVKEMFA 399
Cdd:cd05803   317 EVDAVIGGEGNGGVILPDVHYGRDSLVGIALVLQLLAASGKPLSEIVDELPQYYISKTKVTIAGE-ALERLLKKLEAYFK 395

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1225985232 400 QdasAKVNDIDGVKIDFPDRWVHLRKSNTEPIIRVYSEAATMETADELGKKLM 452
Cdd:cd05803   396 D---AEASTLDGLRLDSEDSWVHVRPSNTEPIVRIIAEAPTQDEAEALADRFI 445
Arch_GlmM TIGR03990
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ...
 2-455 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: 581.39  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232   2 TLIKSISGIRGTIGgrtgDTLNPLDIVKFTTAYATFIPRktGRIVVGRDGRISGHMVRDIVCGTLVGMGYDVLDIGYAST 81
Cdd:TIGR03990   1 MLLFGTSGIRGIVG----EELTPELALKVGKAFGTYLRG--GKVVVGRDTRTSGPMLENAVIAGLLSTGCDVVDLGIAPT 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232  82 PTTELAVRMSGADGGIIITASHNPRQWNALKLLNSEGEFLTAADGNKVLEIAEKEDFNYADVDQLGHVTIDNSYDDRHVQ 161
Cdd:TIGR03990  75 PTLQYAVRELGADGGIMITASHNPPEYNGIKLLNSDGTELSREQEEEIEEIAESGDFERADWDEIGTVTSDEDAIDDYIE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 162 SVLDlkLVDVEAIKKANFKVCVDSINSVGGLILPKLLDKLGVSYQFLNGEVTGDF-AHNPEPLEKNLTGIMDEMKTGKYD 240
Cdd:TIGR03990 155 AILD--KVDVEAIRKKGFKVVVDCGNGAGSLTTPYLLRELGCKVITLNCQPDGTFpGRNPEPTPENLKDLSALVKATGAD 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 241 LGIVVDPDVDRLAFIREDGKMFGEEYTLVSVADYVLSQTKGNTVSNLSSTRALRDITEKHGGTYAAAAVGEVNVTTKMKE 320
Cdd:TIGR03990 233 LGIAHDGDADRLVFIDEKGRFIGGDYTLALFAKYLLEHGGGKVVTNVSSSRAVEDVAERHGGEVIRTKVGEVNVAEKMKE 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 321 VNAVIGGEGNGGVIYPESHYGRDALVGIALFLTSLAKKGCKVSELRKALPHYKIAKNRIDLtPETDVDAILVKVKEMFAQ 400
Cdd:TIGR03990 313 EGAVFGGEGNGGWIFPDHHYCRDGLMAAALFLELLAEEGKPLSELLAELPKYPMSKEKVEL-PDEDKEEVMEAVEEEFAD 391

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1225985232 401 dasAKVNDIDGVKIDFPDRWVHLRKSNTEPIIRVYSEAATMETADELGKKLMKVV 455
Cdd:TIGR03990 392 ---AEIDTIDGVRIDFEDGWVLVRPSGTEPIVRIYAEAKTEERAEELLEEGRSLV 443
ManB COG1109
Phosphomannomutase [Carbohydrate transport and metabolism];
4-455 1.74e-147

Phosphomannomutase [Carbohydrate transport and metabolism];


Pssm-ID: 440726 [Multi-domain]  Cd Length: 456  Bit Score: 428.08  E-value: 1.74e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232   4 IKSISGIRGTIGgrtgDTLNPLDIVKFTTAYATFIPRKTG-RIVVGRDGRISGHMVRDIVCGTLVGMGYDVLDIGYASTP 82
Cdd:COG1109     6 LFGTDGIRGIVG----EELTPEFVLKLGRAFGTYLKEKGGpKVVVGRDTRLSSPMLARALAAGLASAGIDVYDLGLVPTP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232  83 TTELAVRMSGADGGIIITASHNPRQWNALKLLNSEGEFLTAADGNKVLEIAEKEDFNYADVDQLGHVTIDNSYDDRHVQS 162
Cdd:COG1109    82 ALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADGGKLSPEEEKEIEALIEKEDFRRAEAEEIGKVTRIEDVLEAYIEA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 163 VldLKLVDvEAIKKANFKVCVDSINSVGGLILPKLLDKLGVSYQFLNGEVTGDF-AHNPEPLEKNLTGIMDEMKTGKYDL 241
Cdd:COG1109   162 L--KSLVD-EALRLRGLKVVVDCGNGAAGGVAPRLLRELGAEVIVLNAEPDGNFpNHNPNPEPENLEDLIEAVKETGADL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 242 GIVVDPDVDRLAFIREDGKMFGEEYTLVSVADYVLSQTKGNT-VSNLSSTRALRDITEKHGGTYAAAAVGEVNVTTKMKE 320
Cdd:COG1109   239 GIAFDGDADRLGVVDEKGRFLDGDQLLALLARYLLEKGPGGTvVVTVMSSLALEDIAEKHGGEVVRTKVGFKYIKEKMRE 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 321 VNAVIGGEGNGGVIYPESHYGRDALVGIALFLTSLAKKGCKVSELRKALPHYKIAKNRIDLTPETDVDAILVKVKEMFAQ 400
Cdd:COG1109   319 TGAVLGGEESGGIIFPDFVPTDDGILAALLLLELLAKQGKSLSELLAELPRYPQPEINVRVPDEEKIGAVMEKLREAVED 398

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1225985232 401 DasAKVNDIDGVKIDFPDR-WVHLRKSNTEPIIRVYSEAATMETADELGKKLMKVV 455
Cdd:COG1109   399 K--EELDTIDGVKVDLEDGgWVLVRPSGTEPLLRVYAEAKDEEEAEELLAELAELV 452
PGM_like1 cd03087
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ...
 8-455 5.97e-114

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: 341.86  E-value: 5.97e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232   8 SGIRGtiggRTGDTLNPLDIVKFTTAYATFipRKTGRIVVGRDGRISGHMVRDIVCGTLVGMGYDVLDIGYASTPTTELA 87
Cdd:cd03087     5 SGIRG----VVGEELTPELALKVGKALGTY--LGGGTVVVGRDTRTSGPMLKNAVIAGLLSAGCDVIDIGIVPTPALQYA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232  88 VRMSGaDGGIIITASHNPRQWNALKLLNSEGEFLTAADGNKVLEIAEKEDFNYADVDQLGHVTIDNSYDDRHVQSVLDlk 167
Cdd:cd03087    79 VRKLG-DAGVMITASHNPPEYNGIKLVNPDGTEFSREQEEEIEEIIFSERFRRVAWDEVGSVRREDSAIDEYIEAILD-- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 168 lvDVEAIKKANFKVCVDSINSVGGLILPKLLDKLGVSYQFLNGEVTGDF-AHNPEPLEKNLTGIMDEMKTGKYDLGIVVD 246
Cdd:cd03087   156 --KVDIDGGKGLKVVVDCGNGAGSLTTPYLLRELGCKVITLNANPDGFFpGRPPEPTPENLSELMELVRATGADLGIAHD 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 247 PDVDRLAFIREDGKMFGEEYTLVSVADYVLSQTKGNTVSNLSSTRALRDITEKHGGTYAAAAVGEVNVTTKMKEVNAVIG 326
Cdd:cd03087   234 GDADRAVFVDEKGRFIDGDKLLALLAKYLLEEGGGKVVTPVDASMLVEDVVEEAGGEVIRTPVGDVHVAEEMIENGAVFG 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 327 GEGNGGVIYPESHYGRDALVGIALFLTSLAKKGcKVSELRKALPHYKIAKNRIDLTPEtDVDAILVKVKEMFaQDASAKV 406
Cdd:cd03087   314 GEPNGGWIFPDHQLCRDGIMTAALLLELLAEEK-PLSELLDELPKYPLLREKVECPDE-KKEEVMEAVEEEL-SDADEDV 390

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1225985232 407 NDIDGVKIDFPDRWVHLRKSNTEPIIRVYSEAATMETADELGKKLMKVV 455
Cdd:cd03087   391 DTIDGVRIEYEDGWVLIRPSGTEPKIRITAEAKTEERAKELLEEGRSKV 439
PMM_PGM cd03089
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ...
 14-451 2.06e-83

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: 263.60  E-value: 2.06e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232  14 IGGRTGDTLNPLDIVKFTTAYATFIPRKTG-RIVVGRDGRISGHMVRDIVCGTLVGMGYDVLDIGYASTPTTELAVRMSG 92
Cdd:cd03089     7 IRGIAGEELTEEIAYAIGRAFGSWLLEKGAkKVVVGRDGRLSSPELAAALIEGLLAAGCDVIDIGLVPTPVLYFATFHLD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232  93 ADGGIIITASHNPRQWNALKL-LNSEGefLTAADGNKVLEIAEKEDFnyADVDQLGHVT---IDNSYDDRhvqsvldlkL 168
Cdd:cd03089    87 ADGGVMITASHNPPEYNGFKIvIGGGP--LSGEDIQALRERAEKGDF--AAATGRGSVEkvdILPDYIDR---------L 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 169 VDVEAIKKANFKVCVDSINSVGGLILPKLLDKLGVSYQFLNGEVTGDF-AHNPEPL-EKNLTGIMDEMKTGKYDLGIVVD 246
Cdd:cd03089   154 LSDIKLGKRPLKVVVDAGNGAAGPIAPQLLEALGCEVIPLFCEPDGTFpNHHPDPTdPENLEDLIAAVKENGADLGIAFD 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 247 PDVDRLAFIREDGKMFGEEYTLVSVADYVLSQTKGNT-VSNLSSTRALRDITEKHGGTYAAAAVGEVNVTTKMKEVNAVI 325
Cdd:cd03089   234 GDGDRLGVVDEKGEIIWGDRLLALFARDILKRNPGATiVYDVKCSRNLYDFIEEAGGKPIMWKTGHSFIKAKMKETGALL 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 326 GGEGNGGVIYPESHYG-RDALVGIALFLTSLAKKGCKVSELRKALPHYKIAKN-RIDLTpETDVDAILVKVKEmFAQDAS 403
Cdd:cd03089   314 AGEMSGHIFFKDRWYGfDDGIYAALRLLELLSKSGKTLSELLADLPKYFSTPEiRIPVT-EEDKFAVIERLKE-HFEFPG 391

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1225985232 404 AKVNDIDGVKIDFPDRWVHLRKSNTEPIIRVYSEAATMETADELGKKL 451
Cdd:cd03089   392 AEIIDIDGVRVDFEDGWGLVRASNTEPVLVLRFEADTEEGLEEIKAEL 439
PGM_like2 cd05800
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ...
 8-451 1.27e-72

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: 236.29  E-value: 1.27e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232   8 SGIRGTIGgrtgDTLNPLDIVKFTTAYATFIPRKTG---RIVVGRDGR-ISGHMVRDiVCGTLVGMGYDVLDI-GYASTP 82
Cdd:cd05800     6 DGWRGIIA----EDFTFENVRRVAQAIADYLKEEGGggrGVVVGYDTRfLSEEFARA-VAEVLAANGIDVYLSdRPVPTP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232  83 TTELAVRMSGADGGIIITASHNPRQWNALKLLNSEGEFLTAADGNKVLEIAEKEDFNYADVDQLGHVTIDNSYDDrHVQS 162
Cdd:cd05800    81 AVSWAVKKLGAAGGVMITASHNPPEYNGVKVKPAFGGSALPEITAAIEARLASGEPPGLEARAEGLIETIDPKPD-YLEA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 163 VLdlKLVDVEAIKKANFKVCVDSINSVGGLILPKLLDKLGVSYQFLNGEVTGDF-AHNPEPLEKNLTGIMDEMKTGKYDL 241
Cdd:cd05800   160 LR--SLVDLEAIREAGLKVVVDPMYGAGAGYLEELLRGAGVDVEEIRAERDPLFgGIPPEPIEKNLGELAEAVKEGGADL 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 242 GIVVDPDVDRLAFIREDGKMFGEEYTLVSVADYvLSQTKGNT---VSNLSSTRALRDITEKHGGTYAAAAVGEVNVTTKM 318
Cdd:cd05800   238 GLATDGDADRIGAVDEKGNFLDPNQILALLLDY-LLENKGLRgpvVKTVSTTHLIDRIAEKHGLPVYETPVGFKYIAEKM 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 319 KEVNAVIGGEGNGGVIYPESHYGRDALVGIALFLTSLAKKGCKVSELRKAL-----PHYkiaKNRIDLT-PETDVDAILV 392
Cdd:cd05800   317 LEEDVLIGGEESGGLGIRGHIPERDGILAGLLLLEAVAKTGKPLSELVAELeeeygPSY---YDRIDLRlTPAQKEAILE 393

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1225985232 393 KVKEmFAQDASA-----KVNDIDGVKIDF-PDRWVHLRKSNTEPIIRVYSEAATMETADEL---GKKL 451
Cdd:cd05800   394 KLKN-EPPLSIAggkvdEVNTIDGVKLVLeDGSWLLIRPSGTEPLLRIYAEAPSPEKVEALldaGKKL 460
phosphohexomutase cd03084
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ...
 76-455 1.02e-71

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: 230.71  E-value: 1.02e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232  76 IGYASTPTTELAVRMS-GADGGIIITASHNPRQWNALKLLNSEGEFLTAADGNKVLEIAEKEDFNYA-DVDQLGHVTIDn 153
Cdd:cd03084    11 VGDDITPETAVALGQAiGSTGGIMITASHNPPEDNGIKFVDPDGEPIASEEEKAIEDLAEKEDEPSAvAYELGGSVKAV- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 154 SYDDRHVQSVldLKLVDVEAIKKANFKVCVDSINSVGGLILPKLLDKLGVSYQFLNGEVTGDF-AHNPEP-LEKNLTGIM 231
Cdd:cd03084    90 DILQRYFEAL--KKLFDVAALSNKKFKVVVDSVNGVGGPIAPQLLEKLGAEVIPLNCEPDGNFgNINPDPgSETNLKQLL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 232 DEMKTGKYDLGIVVDPDVDRLAFIREDGKMF-GEEYTLVsVADYVLSQTKGNT--VSNLSSTRALRDITEKHGGTYAAAA 308
Cdd:cd03084   168 AVVKAEKADFGVAFDGDADRLIVVDENGGFLdGDELLAL-LAVELFLTFNPRGgvVKTVVSSGALDKVAKKLGIKVIRTK 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 309 VGEVNVTTKMKEVNAVIGGEGNGGVIYPESHYGRDALVGIALFLTSLAKKGCKVSELRKALPHYKIaknridltpetdvd 388
Cdd:cd03084   247 TGFKWVGEAMQEGDVVLGGEESGGVIFPEFHPGRDGISAALLLLEILANLGKSLSELFSELPRYYY-------------- 312

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1225985232 389 aILVKVKEmfaqdasakvndidgvkidfpdrWVHLRKSNTEPIIRVYSEAATMETADELGKKLMKVV 455
Cdd:cd03084   313 -IRLKVRG-----------------------WVLVRASGTEPAIRIYAEADTQEDVEQIKKEARELV 355
MPG1_transferase cd05805
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose ...
 9-455 1.89e-60

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: 203.63  E-value: 1.89e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232   9 GIRGtIGGRTGDTLNPLDIVKFTTAYATFIPRKTgRIVVGRDGRISGHMVRDIVCGTLVGMGYDVLDIGYASTPTTELAV 88
Cdd:cd05805     3 GGRG-VSGLINVDITPEFATRLGAAYGSTLPPGS-TVTVSRDASRASRMLKRALISGLLSTGVNVRDLGALPLPVARYAI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232  89 RMSGADGGIIITASHNPRQWNALKLLNSEGEFLTAADGNKVLEIAEKEDFNYADVDQLGHVTIDNSYDDRHVQSVLDLkl 168
Cdd:cd05805    81 RFLGASGGIHVRTSPDDPDKVEIEFFDSRGLNISRAMERKIENAFFREDFRRAHVDEIGDITEPPDFVEYYIRGLLRA-- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 169 VDVEAIKKANFKVCVDSINSVGGLILPKLLDKLGVSYQFLNGEVTGDFAHNPEPLEKNLTGIMDEMKTGKYDLGIVVDPD 248
Cdd:cd05805   159 LDTSGLKKSGLKVVIDYAYGVAGIVLPGLLSRLGCDVVILNARLDEDAPRTDTERQRSLDRLGRIVKALGADFGVIIDPN 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 249 VDRLAFIREDGKMFGEEYTLVSVADYVLSQTKGNTVS-NLSSTRALRDITEKHGGTYAAAAVGEVNVTTKMKEvNAVIGG 327
Cdd:cd05805   239 GERLILVDEAGRVISDDLLTALVSLLVLKSEPGGTVVvPVTAPSVIEQLAERYGGRVIRTKTSPQALMEAALE-NVVLAG 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 328 EGNGGVIYPESHYGRDALVGIALFLTSLAKKGCKVSELRKALPHYKIAKNRIDlTPETDVDAILVKVKEMFAQDasaKVN 407
Cdd:cd05805   318 DGDGGFIFPEFHPGFDAIAALVKILEMLARTNISLSQIVDELPRFYVLHKEVP-CPWEAKGRVMRRLIEEAPDK---SIE 393

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1225985232 408 DIDGVKIDFPDRWVHLRKSNTEPIIRVYSEAATMETADELGKKLMKVV 455
Cdd:cd05805   394 LIDGVKIYEDDGWVLVLPDADEPLCHIYAEGSDQERAEELTEFYVEKV 441
GlmM cd05802
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ...
 9-451 2.63e-49

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: 173.82  E-value: 2.63e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232   9 GIRGtiggRTGDTLNPLDIVKFTTAYATFIPR--KTGRIVVGRDGRISGHMVRDIVCGTLVGMGYDVLDIGYASTPTTEL 86
Cdd:cd05802     6 GIRG----VANEPLTPELALKLGRAAGKVLGKggGRPKVLIGKDTRISGYMLESALAAGLTSAGVDVLLLGVIPTPAVAY 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232  87 AVRMSGADGGIIITASHNPRQWNALKLLNSEGEFLTAADGNKVLEIAEKEDFNYADVDQLGHVTIDNSYDDR---HVQSV 163
Cdd:cd05802    82 LTRKLRADAGVVISASHNPFEDNGIKFFSSDGYKLPDEVEEEIEALIDKELELPPTGEKIGRVYRIDDARGRyieFLKST 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 164 LDLKLVDveaikkaNFKVCVDSINSVGGLILPKLLDKLGVSYQFLNGEVTGDF------AHNPEPLEKnltgimdEMKTG 237
Cdd:cd05802   162 FPKDLLS-------GLKIVLDCANGAAYKVAPEVFRELGAEVIVINNAPDGLNinvncgSTHPESLQK-------AVLEN 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 238 KYDLGIVVDPDVDRLAFIREDGKMFGEEYTLVSVADYVLSQT--KGNTV-----SNLSSTRALRditeKHGGTYAAAAVG 310
Cdd:cd05802   228 GADLGIAFDGDADRVIAVDEKGNIVDGDQILAICARDLKERGrlKGNTVvgtvmSNLGLEKALK----ELGIKLVRTKVG 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 311 EVNVTTKMKEVNAVIGGEGNGGVIYPESHYGRDALVGIALFLTSLAKKGCKVSELRKALPHYkiaknridltPETDVDai 390
Cdd:cd05802   304 DRYVLEEMLKHGANLGGEQSGHIIFLDHSTTGDGLLTALQLLAIMKRSGKSLSELASDMKLY----------PQVLVN-- 371

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1225985232 391 lVKVKEMFAQDASAKVND-IDGVKIDFPDRW-VHLRKSNTEPIIRVYSEAATMETADELGKKL 451
Cdd:cd05802   372 -VRVKDKKALLENPRVQAaIAEAEKELGGEGrVLVRPSGTEPLIRVMVEGEDEELVEKLAEEL 433
PRK15414 PRK15414
phosphomannomutase;
14-438 2.78e-34

phosphomannomutase;


Pssm-ID: 185312  Cd Length: 456  Bit Score: 133.53  E-value: 2.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232  14 IGGRTGDTLNPlDIV-KFTTAYATFIPRKTgrIVVGRDGRISGHMVRDIVCGTLVGMGYDVLDIGYASTPTTELAVRMSG 92
Cdd:PRK15414   12 IRGKLGEELNE-DIAwRIGRAYGEFLKPKT--IVLGGDVRLTSETLKLALAKGLQDAGVDVLDIGMSGTEEIYFATFHLG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232  93 ADGGIIITASHNPRQWNALKLLNSEGEFLTAADG-NKVLEIAEKEDF---NYADVDQLGHVTIDNSYDDrHVQSVLDLKl 168
Cdd:PRK15414   89 VDGGIEVTASHNPMDYNGMKLVREGARPISGDTGlRDVQRLAEANDFppvDETKRGRYQQINLRDAYVD-HLFGYINVK- 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 169 vdveaiKKANFKVCVDSINSVGGLILPKL---LDKLGVSYQFLNGEVT--GDFAHN-PEPLeknLTGIMDEMKTG----K 238
Cdd:PRK15414  167 ------NLTPLKLVINSGNGAAGPVVDAIearFKALGAPVELIKVHNTpdGNFPNGiPNPL---LPECRDDTRNAvikhG 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 239 YDLGIVVDPDVDRLAFIREDGKmFGEEYTLVS-VADYVLSQTKG-NTVSNLSSTRALRDITEKHGGTYAAAAVGEVNVTT 316
Cdd:PRK15414  238 ADMGIAFDGDFDRCFLFDEKGQ-FIEGYYIVGlLAEAFLEKNPGaKIIHDPRLSWNTVDVVTAAGGTPVMSKTGHAFIKE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 317 KMKEVNAVIGGEGNGgviypeSHYGRD------ALVGIALFLTSLAKKGCKVSELRK----ALPhykiAKNRIDLTPETD 386
Cdd:PRK15414  317 RMRKEDAIYGGEMSA------HHYFRDfaycdsGMIPWLLVAELVCLKGKTLGELVRdrmaAFP----ASGEINSKLAQP 386

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1225985232 387 VDAIlVKVKEMFAQDASAkVNDIDGVKIDFPDRWVHLRKSNTEPIIRVYSEA 438
Cdd:PRK15414  387 VEAI-NRVEQHFSREALA-VDRTDGISMTFADWRFNLRSSNTEPVVRLNVES 436
PGM2 cd05799
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ...
 8-455 5.04e-32

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: 127.62  E-value: 5.04e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232   8 SGIRGTIGGRTGdTLNPLDIVKFTTAYATFI-----PRKTGRIVVGRDGRisgHMVRD---IVCGTLVGMGYDVLdIGYA 79
Cdd:cd05799     7 AGLRGKMGAGTN-RMNDYTVRQATQGLANYLkkkgpDAKNRGVVIGYDSR---HNSREfaeLTAAVLAANGIKVY-LFDD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232  80 STPTTEL--AVRMSGADGGIIITASHNPRQWNALKLLNSEGEFLT--AADG-----NKVLEIAEKEdFNYADVDQLGHVt 150
Cdd:cd05799    82 LRPTPLLsfAVRHLGADAGIMITASHNPKEYNGYKVYWEDGAQIIppHDAEiaeeiEAVLEPLDIK-FEEALDSGLIKY- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 151 IDNSYDDRHVQSVLDLkLVDVEAIKKANFKVCVDSINSVGGLILPKLLDKLG------VSYQFlngEVTGDFAH----NP 220
Cdd:cd05799   160 IGEEIDDAYLEAVKKL-LVNPELNEGKDLKIVYTPLHGVGGKFVPRALKEAGftnvivVEEQA---EPDPDFPTvkfpNP 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 221 EPlEKNLTGIMDEMKTGKYDLGIVVDPDVDRLAF-IREDGKmfgeEYTLVS-------VADYVLSQTK--------GNTV 284
Cdd:cd05799   236 EE-PGALDLAIELAKKVGADLILATDPDADRLGVaVKDKDG----EWRLLTgneigalLADYLLEQRKekgklpknPVIV 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 285 SNLSSTRALRDITEKHGGTYAAAAVGEVNVTTKMKEVNaviggEGNGGVI--YPESH------YGR--DALVGIALFLT- 353
Cdd:cd05799   311 KTIVSSELLRKIAKKYGVKVEETLTGFKWIGNKIEELE-----SGGKKFLfgFEESIgylvgpFVRdkDGISAAALLAEm 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 354 --SLAKKGCKVSELRKAL----------PHYKIAKNRIDLTpetdvdailvKVKEMFaqdasAKV-NDIDGVKIDFPDR- 419
Cdd:cd05799   386 aaYLKAQGKTLLDRLDELyekygyykekTISITFEGKEGPE----------KIKAIM-----DRLrNNPNVLTFYLEDGs 450

                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 1225985232 420 WVHLRKSNTEPIIRVYSEAATMETADELGKKLMKVV 455
Cdd:cd05799   451 RVTVRPSGTEPKIKFYIEVVGKKTLEEAEKKLDALK 486
manB PRK09542
phosphomannomutase/phosphoglucomutase; Reviewed
 10-455 3.00e-31

phosphomannomutase/phosphoglucomutase; Reviewed


Pssm-ID: 236557  Cd Length: 445  Bit Score: 124.71  E-value: 3.00e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232  10 IRGTIGgrtgDTLNPlDIVK-FTTAYATFI-PRKTGRIVVGRDGRISGHMVRDIVCGTLVGMGYDVLDIGYASTPTTELA 87
Cdd:PRK09542    6 VRGVVG----EQIDE-DLVRdVGAAFARLMrAEGATTVVIGHDMRDSSPELAAAFAEGVTAQGLDVVRIGLASTDQLYFA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232  88 vrmSGADG--GIIITASHNPRQWNALKLLNSEGEFLTAADGnkVLEIAEKEDFNYADVD-QLGHVTIDNSYDD--RHVQS 162
Cdd:PRK09542   81 ---SGLLDcpGAMFTASHNPAAYNGIKLCRAGAKPVGQDTG--LAAIRDDLIAGVPAYDgPPGTVTERDVLADyaAFLRS 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 163 vldlkLVDVEAIKKanFKVCVDSINSVGGLILPKLLDKLGVSYQFLNGEVTGDFA-HNPEPLE-KNLTGIMDEMKTGKYD 240
Cdd:PRK09542  156 -----LVDLSGIRP--LKVAVDAGNGMGGHTVPAVLGGLPITLLPLYFELDGTFPnHEANPLDpANLVDLQAFVRETGAD 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 241 LGIVVDPDVDRLAFIREDGKMFGEEYTLVSVADYVLSQTKGNTV-SNLSSTRALRDITEKHGGTYAAAAVGEVNVTTKMK 319
Cdd:PRK09542  229 IGLAFDGDADRCFVVDERGQPVSPSAVTALVAARELAREPGATIiHNLITSRAVPELVAERGGTPVRTRVGHSFIKALMA 308

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 320 EVNAVIGGEGNGgviypeSHYGRD---ALVGI--ALF-LTSLAKKGCKVSELRKALPHYkIAKNRIDLTPEtDVDAILVK 393
Cdd:PRK09542  309 ETGAIFGGEHSA------HYYFRDfwgADSGMlaALHvLAALGEQDRPLSELMADYQRY-AASGEINSTVA-DAPARMEA 380

                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1225985232 394 VKEMFAqDASAKVNDIDGVKIDFPD-RWVHLRKSNTEPIIRVYSEAATMETADELGKKLMKVV 455
Cdd:PRK09542  381 VLKAFA-DRIVSVDHLDGVTVDLGDgSWFNLRASNTEPLLRLNVEARTEEEVDALVDEVLAII 442
PGM_PMM_I pfam02878
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
8-139 4.00e-31

Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;


Pssm-ID: 427032  Cd Length: 138  Bit Score: 116.55  E-value: 4.00e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232   8 SGIRGTIGGrtgDTLNPLDIVKFTTAYATFIP--RKTGRIVVGRDGRISGHMVRDIVCGTLVGMGYDVLDIGYASTPTTE 85
Cdd:pfam02878   7 SGIRGKVGV---GELTPEFALKLGQAIASYLRaqGGGGKVVVGRDTRYSSRELARALAAGLASNGVEVILLGLLPTPAVS 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1225985232  86 LAVRMSGADGGIIITASHNPRQWNALKLLNSEGEFLTAADGNKVLEIAEKEDFN 139
Cdd:pfam02878  84 FATRKLKADGGIMITASHNPPEYNGIKVFDSNGGPIPPEVEKKIEAIIEKEDFY 137
PLN02371 PLN02371
phosphoglucosamine mutase family protein
 8-457 6.87e-29

phosphoglucosamine mutase family protein


Pssm-ID: 215211 [Multi-domain]  Cd Length: 583  Bit Score: 119.39  E-value: 6.87e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232   8 SGIRGT-IGGRTGD--TLNPLDIVKFTTAYATFIPRKTG-------RIVVGRDGRISGHMVRDIVCGTLVGMGYDVLDIG 77
Cdd:PLN02371   71 SDIRGVaVEGVEGEpvTLTPPAVEAIGAAFAEWLLEKKKadgsgelRVSVGRDPRISGPRLADAVFAGLASAGLDVVDMG 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232  78 YASTPTTELAVRMSGADG--GIIITASHNPRQWNALKLLNSEGEfLTAADGNKVLEIAEKEDFNYADVDQLGHVTIDNSy 155
Cdd:PLN02371  151 LATTPAMFMSTLTEREDYdaPIMITASHLPYNRNGLKFFTKDGG-LGKPDIKDILERAARIYKEWSDEGLLKSSSGASS- 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 156 ddrhvqsvlDLKLVD---------VEAIKKA------------NFKVCVDSINSVGGLILPKLLDKLG--VSY-QFLNGE 211
Cdd:PLN02371  229 ---------VVCRVDfmstyakhlRDAIKEGvghptnyetpleGFKIVVDAGNGAGGFFAEKVLEPLGadTSGsLFLEPD 299

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 212 vtGDFA-HNPEPLEKNLTG-IMDEMKTGKYDLGIVVDPDVDRLAFIREDGKMFGEEYTLVSVADYVLSQTKGNTVSNLSS 289
Cdd:PLN02371  300 --GMFPnHIPNPEDKAAMSaTTQAVLANKADLGIIFDTDVDRSAVVDSSGREINRNRLIALMSAIVLEEHPGTTIVTDSV 377

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 290 TR-ALRDITEKHGGTYAAAAVGEVNVTTKMKEVNAVigGE---------GNGGViyPESHYGRDAL-----VGIALFLTS 354
Cdd:PLN02371  378 TSdGLTTFIEKKGGKHHRFKRGYKNVIDKGVRLNSD--GEethlmietsGHGAL--KENHFLDDGAylavkIIIELVRMR 453

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 355 LAKKGCKVSELRKALPHYKIAKN-RIDLT-PETDVDAILVKVKEMFAQDAS-------AKVNDiDGVKI-DFPDR---WV 421
Cdd:PLN02371  454 AAGAGGGLGDLIEDLEEPLEAVElRLKILdEGKDFKAYGEEVLEHLRNSIEsdgklegAPVNY-EGVRVsDEGEGfggWF 532

                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 1225985232 422 HLRKSNTEPIIRVYSEAATMETADELGKKLMKVVYD 457
Cdd:PLN02371  533 LLRQSLHDPVIPLNIESSSPGGAQKMALVVLTWLKE 568
PGM_PMM_II pfam02879
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
166-259 1.04e-19

Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;


Pssm-ID: 427033  Cd Length: 102  Bit Score: 83.88  E-value: 1.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 166 LKLVDVEAIKKANFKVCVDSINSVGGLILPKLLDKLGVSYQFLNGEVTGDF-AHNPEPLEK-NLTGIMDEMKTGKYDLGI 243
Cdd:pfam02879   7 LELVDSEALKKRGLKVVYDPLHGVGGGYLPELLKRLGCDVVEENCEPDPDFpTRAPNPEEPeALALLIELVKSVGADLGI 86

                          90
                  ....*....|....*.
gi 1225985232 244 VVDPDVDRLAFIREDG 259
Cdd:pfam02879  87 ATDGDADRLGVVDERG 102
PGM_PMM_III pfam02880
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
266-371 5.14e-19

Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;


Pssm-ID: 460733  Cd Length: 115  Bit Score: 82.50  E-value: 5.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 266 YTLVSVADYVLSQ--TKGNT--VSNLSSTRALRDITEKHGGTYAAAAVGEVNVTTKMKEVNAVIGGEGNGGVIYPESHYG 341
Cdd:pfam02880   4 QILALLAKYLLEQgkLPPGAgvVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEGALFGGEESGHIIFLDHATT 83

                          90       100       110
                  ....*....|....*....|....*....|
gi 1225985232 342 RDALVGIALFLTSLAKKGCKVSELRKALPH 371
Cdd:pfam02880  84 KDGILAALLVLEILARTGKSLSELLEELPE 113
glmM PRK10887
phosphoglucosamine mutase; Provisional
 40-455 1.74e-17

phosphoglucosamine mutase; Provisional


Pssm-ID: 236787  Cd Length: 443  Bit Score: 84.42  E-value: 1.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232  40 RKTGRIVVGRDGRISGHMVRDIVCGTLVGMGYDVLDIGYASTPttelAV----RMSGADGGIIITASHNPRQWNALKLLN 115
Cdd:PRK10887   37 QGRPKVLIGKDTRISGYMLESALEAGLAAAGVDVLLTGPMPTP----AVayltRTLRAEAGIVISASHNPYYDNGIKFFS 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 116 SEGEFLTAADGNKVlEIAEKEDFNYADVDQLGHVT-IDNS------YDDRHVQSVLDLKlvdveaikkaNFKVCVDSINS 188
Cdd:PRK10887  113 ADGTKLPDEVELAI-EAELDKPLTCVESAELGKASrINDAagryieFCKSTFPNELSLR----------GLKIVVDCANG 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 189 VGGLILPKLLDKLGvsyqflnGEVT--GDfahNPEPLEKN-------LTGIMDEMKTGKYDLGIVVDPDVDRLAFIREDG 259
Cdd:PRK10887  182 ATYHIAPNVFRELG-------AEVIaiGC---EPNGLNINdecgatdPEALQAAVLAEKADLGIAFDGDGDRVIMVDHLG 251

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 260 KMF-GEEYTLVSVADYVLSQTKGNTV-----SNLSSTRALRditeKHGGTYAAAAVGEVNVTTKMKEVNAVIGGEGNGGV 333
Cdd:PRK10887  252 NLVdGDQLLYIIARDRLRRGQLRGGVvgtlmSNMGLELALK----QLGIPFVRAKVGDRYVLEKLQEKGWRLGGENSGHI 327

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 334 IYPESHYGRDALVGIALFLTSLAKKGCKVSELRKALPHY-------KIAKNRIDLTPETDVDAILVKVKEMFAQDAsakv 406
Cdd:PRK10887  328 LCLDKTTTGDGIVAALQVLAAMVRSGMSLADLCSGMKLFpqvlinvRFKPGADDPLESEAVKAALAEVEAELGGRG---- 403

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*....
gi 1225985232 407 ndidgvkidfpdRwVHLRKSNTEPIIRVYSEAATMETADELGKKLMKVV 455
Cdd:PRK10887  404 ------------R-VLLRKSGTEPLIRVMVEGEDEAQVTALAERIADAV 439
PRK07564 PRK07564
phosphoglucomutase; Validated
 42-437 1.47e-13

phosphoglucomutase; Validated


Pssm-ID: 236050  Cd Length: 543  Bit Score: 72.48  E-value: 1.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232  42 TGRIVVGRDGRISGHMVRDIVCGTLVGMGYDVL---DIGYASTPTTELAVR-----MSGADGGIIITASHNPRQWNALKL 113
Cdd:PRK07564   76 TGPLFVGGDTHALSEPAIQSALEVLAANGVGVVivgRGGYTPTPAVSHAILkyngrGGGLADGIVITPSHNPPEDGGIKY 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 114 LNSEG----EFLT---AADGNKVLE--IAEKEDFNYADVDQLGHVT-ID--NSYddrhvqsVLDL-KLVDVEAIKKANFK 180
Cdd:PRK07564  156 NPPNGgpadTDVTdaiEARANELLAygLKGVKRIPLDRALASMTVEvIDpvADY-------VEDLeNVFDFDAIRKAGLR 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 181 VCVDSINSVGGLILPKLLDKLGVSYQFLNGEVtgDFAHNPEPLEKNLTGIMD-----------EMKtGKYDLGIVVDPDV 249
Cdd:PRK07564  229 LGVDPLGGATGPYWKAIAERYGLDLTVVNAPV--DPTFNFMPLDDDGKIRMDcsspyamagllALK-DAFDLAFANDPDG 305

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 250 DRLAFIREDGkmfgeeytLVSVADY--VLsqtkgntVSNLSSTRALrditekhggtYAA-AAVGEVNVTTKM-------- 318
Cdd:PRK07564  306 DRHGIVTPGG--------LMNPNHYlaVA-------IAYLFHHRPG----------WRAgAGVGKTLVSSAMidrvaakl 360

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 319 ----KEV--------------NAVIGGEgnggviypES-------HYGR------DALVGIALFLTSLAKKGCKVSELRK 367
Cdd:PRK07564  361 grklYEVpvgfkwfvnglddgSLGFGGE--------ESagasflrRDGSvwttdkDGLIAVLLAAEILAVTGKSPSEIYR 432

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 368 AL------PHYkiakNRIDLtPETDVD-AILVKV------KEMFAQD--------ASAKVNDIDGVKIDFPDRWVHLRKS 426
Cdd:PRK07564  433 ELwarfgrPYY----SRHDA-PATPEQkAALRKLspelvgATELAGDpidaslteAPGNGAAIGGLKVVTENGWFAARPS 507

                         490
                  ....*....|.
gi 1225985232 427 NTEPIIRVYSE 437
Cdd:PRK07564  508 GTETTYKIYAE 518
PGM1 cd03085
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ...
 40-251 4.08e-13

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: 71.10  E-value: 4.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232  40 RKTGRIVVGRDGRISGHMVRDIVCGTLVGMGYDVLDIG---YASTPTTELAVRMSGADGGIIITASHNPRQWNA---LKL 113
Cdd:cd03085    47 LKGATLVVGGDGRYYNKEAIQIIIKIAAANGVGKVVVGqngLLSTPAVSAVIRKRKATGGIILTASHNPGGPEGdfgIKY 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 114 LNSEG----EFLTaadgNKVLEIAEK-EDFNYA-----DVDQLGhvtiDNSYDDRH-----VQSVLDL-----KLVDVEA 173
Cdd:cd03085   127 NTSNGgpapESVT----DKIYEITKKiTEYKIAddpdvDLSKIG----VTKFGGKPftvevIDSVEDYvelmkEIFDFDA 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 174 IKKA----NFKVCVDSINSVGGLILPKLL-DKLGVSYQ-FLNGEVTGDF-AHNPEPlekNLT---GIMDEMKTGKYDLGI 243
Cdd:cd03085   199 IKKLlsrkGFKVRFDAMHGVTGPYAKKIFvEELGAPESsVVNCTPLPDFgGGHPDP---NLTyakDLVELMKSGEPDFGA 275


                  ....*...
gi 1225985232 244 VVDPDVDR 251
Cdd:cd03085   276 ASDGDGDR 283
ManB cd03088
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ...
 8-447 6.21e-13

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: 70.31  E-value: 6.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232   8 SGIRGTIGGRTGDTlnpldIVKFTTAYATFIPRKT--GRIVVGRDGRISGHMVRDIVCGTLVGMGYDVLDIGYASTPTTE 85
Cdd:cd03088     5 SGLRGLVTDLTDEV-----CYAYTRAFLQHLESKFpgDTVAVGRDLRPSSPRIAAACAAALRDAGFRVVDCGAVPTPALA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232  86 LAVRMSGAdGGIIITASHNPRQWNALKLLNSEGEFlTAADGNKVLEIAEKEDfnyADVDQLGHVTIDNSYD--DRHVQSV 163
Cdd:cd03088    80 LYAMKRGA-PAIMVTGSHIPADRNGLKFYRPDGEI-TKADEAAILAALVELP---EALFDPAGALLPPDTDaaDAYIARY 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 164 LDLklVDVEAIKkaNFKVCVDSINSVGGLILPKLLDKLGvsyqflnGEVTG-----DF------AHNPEPLEKnltgimd 232
Cdd:cd03088   155 TDF--FGAGALK--GLRIGVYQHSSVGRDLLVRILEALG-------AEVVPlgrsdTFipvdteAVRPEDRAL------- 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 233 eMKT--GKYDLGIVV--DPDVDRLAFIREDG-------------KMFGeeytlvsvADYVLSQTKGNTVSNLSStRALRD 295
Cdd:cd03088   217 -AAAwaAEHGLDAIVstDGDGDRPLVADETGewlrgdilglltaRFLG--------ADTVVTPVSSNSAIELSG-FFKRV 286

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 296 ITEKHGGTYAAAAVGEVNVTTKmkevNAVIGGEGNGGVIYP---ESHYG-------RDALVGIALFLTSLAKKGCKVSEL 365
Cdd:cd03088   287 VRTRIGSPYVIAAMAEAAAAGA----GRVVGYEANGGFLLGsdiERNGRtlkalptRDAVLPILAVLAAAKEAGIPLSEL 362

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 366 RKALPHYKIAKNRIDLTPETDVDAILVKVKE-------MFAQDAS--AKVNDIDGVKIDFPD-RWVHLRKSNTEPIIRVY 435
Cdd:cd03088   363 VASLPARFTASDRLQNFPTEKSQALIARLSAdpearaaFFFALGGevASIDTTDGLRMTFANgDIVHLRPSGNAPELRCY 442

                         490
                  ....*....|..
gi 1225985232 436 SEAATMETADEL 447
Cdd:cd03088   443 VEADSEERAREL 454
PTZ00150 PTZ00150
phosphoglucomutase-2-like protein; Provisional
 9-455 4.39e-11

phosphoglucomutase-2-like protein; Provisional


Pssm-ID: 240294  Cd Length: 584  Bit Score: 65.09  E-value: 4.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232   9 GIRGTIGgrTG-DTLNPLDIVKFTTAYATFI------PRKTGRIVVGRDGRISGHMVRDIVCGTLVGMGYDVLDIGY-AS 80
Cdd:PTZ00150   51 GLRGKMG--AGfNCMNDLTVQQTAQGLCAYVietfgqALKSRGVVIGYDGRYHSRRFAEITASVFLSKGFKVYLFGQtVP 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232  81 TPTTELAVRMSGADGGIIITASHNPRQWNALKLLNSEG-EFLTAADGN---KVLEIAEKEDFNYADVDQLGHVTIDNSYD 156
Cdd:PTZ00150  129 TPFVPYAVRKLKCLAGVMVTASHNPKEDNGYKVYWSNGaQIIPPHDKNisaKILSNLEPWSSSWEYLTETLVEDPLAEVS 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 157 DRHVQsvlDLKL-VDVEAIKKANFKVCVDSINSVGGLILPKLLDKLG------VSYQflnGEVTGDFAH----NPEPLEK 225
Cdd:PTZ00150  209 DAYFA---TLKSeYNPACCDRSKVKIVYTAMHGVGTRFVQKALHTVGlpnllsVAQQ---AEPDPEFPTvtfpNPEEGKG 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 226 NLTGIMDEmkTGKYDLGIVV--DPDVDRLAF-IREDG--KMF-GEEYTLVsVADYVLSQ--TKGNTVSN------LSSTR 291
Cdd:PTZ00150  283 ALKLSMET--AEAHGSTVVLanDPDADRLAVaEKLNNgwKIFtGNELGAL-LAWWAMKRyrRQGIDKSKcffictVVSSR 359

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 292 ALRDITEKHGGTYAAAAVGEVNVTTKMKEVNA------VIGGEGNGGVIYPESHYGRD---ALVGIALFLTSLAKKGCKV 362
Cdd:PTZ00150  360 MLKKMAEKEGFQYDETLTGFKWIGNKAIELNAenglttLFAYEEAIGFMLGTRVRDKDgvtAAAVVAEMALYLYERGKTL 439

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 363 SE----LRKALpHYKIAKNRIDLTPE-TDVDAILVKVK---EMFAQDASAKVNDI----DGVKIDFPDR----------- 419
Cdd:PTZ00150  440 VEhlesLYKQY-GYHFTNNSYYICYDpSRIVSIFNDIRnngSYPTKLGGYPVTRIrdltTGYDTATPDGkpllpvsastq 518

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 1225985232 420 ----------WVHLRKSNTEPIIRVYSEaaTMETADELGKK-LMKVV 455
Cdd:PTZ00150  519 mitfyfengaIITIRGSGTEPKLKWYAE--LSGTKDEAVEKeLAALV 563
PLN02307 PLN02307
phosphoglucomutase
 41-251 1.77e-10

phosphoglucomutase


Pssm-ID: 177942 [Multi-domain]  Cd Length: 579  Bit Score: 63.13  E-value: 1.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232  41 KTGRIVVGRDGRISGHMVRDIVCGTLVGMGYDVLDIG---YASTPTTELAVR---MSGADGGIIITASHNP----RQWnA 110
Cdd:PLN02307   60 KGATLVLGGDGRYFNKEAIQIIIKIAAANGVRRVWVGqngLLSTPAVSAVIRerdGSKANGGFILTASHNPggpeEDF-G 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 111 LKLLNSEG----EFLTAADGNKVLEIAE---KEDFNYADVDQLGHVTI--DNSYDDRHVQSVLD-LKLV----DVEAIKK 176
Cdd:PLN02307  139 IKYNYESGqpapESITDKIYGNTLTIKEykmAEDIPDVDLSAVGVTKFggPEDFDVEVIDPVEDyVKLMksifDFELIKK 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 177 ----ANFKVCVDSINSVGG-LILPKLLDKLGVSYQ-FLNGEVTGDFAH-NPEP---LEKNLTGIMDEMKTGKY----DLG 242
Cdd:PLN02307  219 llsrPDFTFCFDAMHGVTGaYAKRIFVEELGAPESsLLNCVPKEDFGGgHPDPnltYAKELVKRMGLGKTSYGdeppEFG 298


                  ....*....
gi 1225985232 243 IVVDPDVDR 251
Cdd:PLN02307  299 AASDGDGDR 307
PGM_PMM_IV pfam00408
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
392-455 4.77e-08

Phosphoglucomutase/phosphomannomutase, C-terminal domain;


Pssm-ID: 425666  Cd Length: 71  Bit Score: 49.96  E-value: 4.77e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1225985232 392 VKVKEMFAQDASAKVND--IDGVKIDFPD-RWVHLRKSNTEPIIRVYSEAATMETADELGKKLMKVV 455
Cdd:pfam00408   4 VRVAEKKKLAALAAILKvfADAEKILGEDgRRLDVRPSGTEPVLRVMVEGDSDEELARLADEIADLL 70
PLN02895 PLN02895
phosphoacetylglucosamine mutase
 343-458 3.83e-07

phosphoacetylglucosamine mutase


Pssm-ID: 215485  Cd Length: 562  Bit Score: 52.33  E-value: 3.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 343 DALVGIALFLTSLAKKGCKVSE---LRKALPHYKIAKNRIDLTPETDVDAILVKVKEMFAQDAsakvndIDGVKIDFPDR 419
Cdd:PLN02895  442 DALSGLLLVEAILQYRGWSLAEwnaLYQDLPSRQLKVKVADRTAITTTDAETVVVRPAGLQDA------IDAEVAKYPRG 515

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1225985232 420 WVHLRKSNTEPIIRVYSEAATMETADELGKKLMKVVYDM 458
Cdd:PLN02895  516 RAFVRPSGTEDVVRVYAEASTQEAADSLAREVARLVYDL 554
PGM3 cd03086
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ...
 96-455 1.19e-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: 47.59  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232  96 GIIITASHNPRQWNALKLLNSEGEFL------------TAADGN---KVLEIAEKEDFNYaDVDQLGHVTIdnSYDDRH- 159
Cdd:cd03086    38 GVMITASHNPVEDNGVKIVDPDGEMLeeswepyatqlaNASDDEllvLVLMLISVKELNI-DLSVPANVFV--GRDTRPs 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 160 ----VQSVLD-LKLVDVEAI-------------------------------------------------KKANFKVCVDS 185
Cdd:cd03086   115 gpalLQALLDgLKALGGNVIdyglvttpqlhylvraantegaygepteegyyeklskafnelynllqdgGDEPEKLVVDC 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 186 INSVGGLILPKLLD--KLGVSYQFLNGEVTG----------DFAHNPEPLEKNLTgimdemKTGKYDLGIVVDPDVDRLA 253
Cdd:cd03086   195 ANGVGALKLKELLKrlKKGLSVKIINDGEEGpellndgcgaDYVKTKQKPPRGFE------LKPPGVRCCSFDGDADRLV 268

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 254 F--IREDGKMF---GEEY---------TLVSVADYVLS------QTkgnTVSNLSSTRALRDitekhggtyaaaaVGEVN 313
Cdd:cd03086   269 YfyPDSSNKFHlldGDKIatlfakfikELLKKAGEELKltigvvQT---AYANGASTKYLED-------------VLKVP 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 314 VT---TKMK---------------EVNaviggeGNGGVIYPESHYGR------------------------------DAL 345
Cdd:cd03086   333 VVctpTGVKhlhhaaeefdigvyfEAN------GHGTVLFSESALAKieensslsdeqekaaktllafsrlinqtvgDAI 406

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1225985232 346 VGIALFLTSLAKKGCKVSELRKA---LPH----YKIAKNRIDLTpeTDVDAILVKVKEMfaQDAsakvndIDGVKIDFPD 418
Cdd:cd03086   407 SDMLAVELILAALGWSPQDWDNLytdLPNrqlkVKVPDRSVIKT--TDAERRLVEPKGL--QDK------IDAIVAKYNN 476

                         490       500       510
                  ....*....|....*....|....*....|....*..
gi 1225985232 419 RWVHLRKSNTEPIIRVYSEAATMETADELGKKLMKVV 455
Cdd:cd03086   477 GRAFVRPSGTEDVVRVYAEAATQEEADELANEVAELV 513
PTZ00302 PTZ00302
N-acetylglucosamine-phosphate mutase; Provisional
 423-447 6.29e-04

N-acetylglucosamine-phosphate mutase; Provisional


Pssm-ID: 240352 [Multi-domain]  Cd Length: 585  Bit Score: 42.33  E-value: 6.29e-04
                          10        20
                  ....*....|....*....|....*
gi 1225985232 423 LRKSNTEPIIRVYSEAATMETADEL 447
Cdd:PTZ00302  546 IRPSGTEPVVRVYAEAPTLEQADEL 570
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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