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Conserved domains on  [gi|1733551951|dbj|GER01371|]
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phosphomannomutase [Iodidimonas gelatinilytica]

Protein Classification

phosphomannomutase/phosphoglucomutase( domain architecture ID 10122997)

phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the reversible conversion of 1-phospho to 6-phospho-sugars via a bisphosphorylated sugar intermediate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PMM_PGM cd03089
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ...
 4-373 0e+00

The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the reversible conversion of 1-phospho to 6-phospho-sugars (e.g. between mannose-1-phosphate and mannose-6-phosphate or glucose-1-phosphate and glucose-6-phosphate) via a bisphosphorylated sugar intermediate. The reaction involves two phosphoryl transfers, with an intervening 180 degree reorientation of the reaction intermediate during catalysis. Reorientation of the intermediate occurs without dissociation from the active site of the enzyme and is thus, a simple example of processivity, as defined by multiple rounds of catalysis without release of substrate. Glucose-6-phosphate and glucose-1-phosphate are known to be utilized for energy metabolism and cell surface construction, respectively. PMM/PGM belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the phosphoglucomutases (PGM1 and PGM2). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


:

Pssm-ID: 100091  Cd Length: 443  Bit Score: 529.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951   4 IGLGPTPMVYYAVHELKADGGLMITGSHNPPDYNGIKMMMGKAPVFGEQIKALGALAASGDFE--QGSGTLETVPVFDRY 81
Cdd:cd03089    70 IGLVPTPVLYFATFHLDADGGVMITASHNPPEYNGFKIVIGGGPLSGEDIQALRERAEKGDFAaaTGRGSVEKVDILPDY 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951  82 IHRLLRDFTGAT--MAVAWDPGNGAAGDAVTALVKRLPGRHIVINADIDGRFPNHHPDPTVEENLEQLKQVVIREGMDLG 159
Cdd:cd03089   150 IDRLLSDIKLGKrpLKVVVDAGNGAAGPIAPQLLEALGCEVIPLFCEPDGTFPNHHPDPTDPENLEDLIAAVKENGADLG 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 160 LAFDGDGDRIGAVDRTGHVVWGDQILLILARHLLKEQKGATIIADVKASQVFFDGVVQAGGKAEMWKTGHSLIKSRMAET 239
Cdd:cd03089   230 IAFDGDGDRLGVVDEKGEIIWGDRLLALFARDILKRNPGATIVYDVKCSRNLYDFIEEAGGKPIMWKTGHSFIKAKMKET 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 240 GAPLAGEMSGHIFYKDRFYGHDDGLYAAIRFLNAIWAQGGDLARLRQEMPHVLNTPELRFPCAEDRKMPVIEGVRDRLSQ 319
Cdd:cd03089   310 GALLAGEMSGHIFFKDRWYGFDDGIYAALRLLELLSKSGKTLSELLADLPKYFSTPEIRIPVTEEDKFAVIERLKEHFEF 389

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1733551951 320 SGAQVIDVDGVRVLTEDGWWLLRASNTQDVLVARVEARDEEGLTRLKDLLRGQL 373
Cdd:cd03089   390 PGAEIIDIDGVRVDFEDGWGLVRASNTEPVLVLRFEADTEEGLEEIKAELRKLL 443
 
Name Accession Description Interval E-value
PMM_PGM cd03089
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ...
 4-373 0e+00

The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the reversible conversion of 1-phospho to 6-phospho-sugars (e.g. between mannose-1-phosphate and mannose-6-phosphate or glucose-1-phosphate and glucose-6-phosphate) via a bisphosphorylated sugar intermediate. The reaction involves two phosphoryl transfers, with an intervening 180 degree reorientation of the reaction intermediate during catalysis. Reorientation of the intermediate occurs without dissociation from the active site of the enzyme and is thus, a simple example of processivity, as defined by multiple rounds of catalysis without release of substrate. Glucose-6-phosphate and glucose-1-phosphate are known to be utilized for energy metabolism and cell surface construction, respectively. PMM/PGM belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the phosphoglucomutases (PGM1 and PGM2). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


Pssm-ID: 100091  Cd Length: 443  Bit Score: 529.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951   4 IGLGPTPMVYYAVHELKADGGLMITGSHNPPDYNGIKMMMGKAPVFGEQIKALGALAASGDFE--QGSGTLETVPVFDRY 81
Cdd:cd03089    70 IGLVPTPVLYFATFHLDADGGVMITASHNPPEYNGFKIVIGGGPLSGEDIQALRERAEKGDFAaaTGRGSVEKVDILPDY 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951  82 IHRLLRDFTGAT--MAVAWDPGNGAAGDAVTALVKRLPGRHIVINADIDGRFPNHHPDPTVEENLEQLKQVVIREGMDLG 159
Cdd:cd03089   150 IDRLLSDIKLGKrpLKVVVDAGNGAAGPIAPQLLEALGCEVIPLFCEPDGTFPNHHPDPTDPENLEDLIAAVKENGADLG 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 160 LAFDGDGDRIGAVDRTGHVVWGDQILLILARHLLKEQKGATIIADVKASQVFFDGVVQAGGKAEMWKTGHSLIKSRMAET 239
Cdd:cd03089   230 IAFDGDGDRLGVVDEKGEIIWGDRLLALFARDILKRNPGATIVYDVKCSRNLYDFIEEAGGKPIMWKTGHSFIKAKMKET 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 240 GAPLAGEMSGHIFYKDRFYGHDDGLYAAIRFLNAIWAQGGDLARLRQEMPHVLNTPELRFPCAEDRKMPVIEGVRDRLSQ 319
Cdd:cd03089   310 GALLAGEMSGHIFFKDRWYGFDDGIYAALRLLELLSKSGKTLSELLADLPKYFSTPEIRIPVTEEDKFAVIERLKEHFEF 389

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1733551951 320 SGAQVIDVDGVRVLTEDGWWLLRASNTQDVLVARVEARDEEGLTRLKDLLRGQL 373
Cdd:cd03089   390 PGAEIIDIDGVRVDFEDGWGLVRASNTEPVLVLRFEADTEEGLEEIKAELRKLL 443
ManB COG1109
Phosphomannomutase [Carbohydrate transport and metabolism];
4-376 9.98e-139

Phosphomannomutase [Carbohydrate transport and metabolism];


Pssm-ID: 440726 [Multi-domain]  Cd Length: 456  Bit Score: 403.04  E-value: 9.98e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951   4 IGLGPTPMVYYAVHELKADGGLMITGSHNPPDYNGIKMMMGK-APVFGEQIKALGALAASGDFE----QGSGTLETVP-V 77
Cdd:COG1109    75 LGLVPTPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADgGKLSPEEEKEIEALIEKEDFRraeaEEIGKVTRIEdV 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951  78 FDRYIHRLLRDFTGAT----MAVAWDPGNGAAGDAVTALVKRLPGRHIVINADIDGRFPNHHPDPTvEENLEQLKQVVIR 153
Cdd:COG1109   155 LEAYIEALKSLVDEALrlrgLKVVVDCGNGAAGGVAPRLLRELGAEVIVLNAEPDGNFPNHNPNPE-PENLEDLIEAVKE 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 154 EGMDLGLAFDGDGDRIGAVDRTGHVVWGDQILLILARHLLKEQKGATIIADVKASQVFFDGVVQAGGKAEMWKTGHSLIK 233
Cdd:COG1109   234 TGADLGIAFDGDADRLGVVDEKGRFLDGDQLLALLARYLLEKGPGGTVVVTVMSSLALEDIAEKHGGEVVRTKVGFKYIK 313

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 234 SRMAETGAPLAGEMSGHIFYKDrFYGHDDGLYAAIRFLNAIWAQGGDLARLRQEMPHVLnTPELRFPCAEDRKMP-VIEG 312
Cdd:COG1109   314 EKMRETGAVLGGEESGGIIFPD-FVPTDDGILAALLLLELLAKQGKSLSELLAELPRYP-QPEINVRVPDEEKIGaVMEK 391

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1733551951 313 VRDRLsQSGAQVIDVDGVRVLTEDG-WWLLRASNTQDVLVARVEARDEEGLTRLKDLLRGQLKQA 376
Cdd:COG1109   392 LREAV-EDKEELDTIDGVKVDLEDGgWVLVRPSGTEPLLRVYAEAKDEEEAEELLAELAELVEEA 455
Arch_GlmM TIGR03990
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ...
 4-367 2.42e-92

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: 284.02  E-value: 2.42e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951   4 IGLGPTPMVYYAVHELKADGGLMITGSHNPPDYNGIKMMMGKAPVFG-EQIKALGALAASGDFEQ----GSGTLETVP-V 77
Cdd:TIGR03990  69 LGIAPTPTLQYAVRELGADGGIMITASHNPPEYNGIKLLNSDGTELSrEQEEEIEEIAESGDFERadwdEIGTVTSDEdA 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951  78 FDRYIHRLLRDFTGATMA-----VAWDPGNGAAGDAVTALVKRLPGRHIVINADIDGRFPNHHPDPTvEENLEQLKQVVI 152
Cdd:TIGR03990 149 IDDYIEAILDKVDVEAIRkkgfkVVVDCGNGAGSLTTPYLLRELGCKVITLNCQPDGTFPGRNPEPT-PENLKDLSALVK 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 153 REGMDLGLAFDGDGDRIGAVDRTGHVVWGDQILLILARHLLkEQKGATIIADVKASQVFFDGVVQAGGKAEMWKTGHSLI 232
Cdd:TIGR03990 228 ATGADLGIAHDGDADRLVFIDEKGRFIGGDYTLALFAKYLL-EHGGGKVVTNVSSSRAVEDVAERHGGEVIRTKVGEVNV 306

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 233 KSRMAETGAPLAGEMSGHIFYKDRFYGhDDGLYAAIRFLNAIWAQGGDLARLRQEMPHvLNTPELRFPCAEDRKMPVIEG 312
Cdd:TIGR03990 307 AEKMKEEGAVFGGEGNGGWIFPDHHYC-RDGLMAAALFLELLAEEGKPLSELLAELPK-YPMSKEKVELPDEDKEEVMEA 384

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1733551951 313 VRDRLsqSGAQVIDVDGVRVLTEDGWWLLRASNTQDVLVARVEARDEEGLTRLKD 367
Cdd:TIGR03990 385 VEEEF--ADAEIDTIDGVRIDFEDGWVLVRPSGTEPIVRIYAEAKTEERAEELLE 437
manB PRK09542
phosphomannomutase/phosphoglucomutase; Reviewed
 3-367 3.58e-60

phosphomannomutase/phosphoglucomutase; Reviewed


Pssm-ID: 236557  Cd Length: 445  Bit Score: 200.98  E-value: 3.58e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951   3 AIGLGPTPMVYYAVHELKADGGlMITGSHNPPDYNGIKM-MMGKAPVFGE----QIKALgALAASGDFEQGSGTLETVPV 77
Cdd:PRK09542   68 RIGLASTDQLYFASGLLDCPGA-MFTASHNPAAYNGIKLcRAGAKPVGQDtglaAIRDD-LIAGVPAYDGPPGTVTERDV 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951  78 FDRYIHRL--LRDFTGA-TMAVAWDPGNGAAGDAVTALVKRLPGRHIVINADIDGRFPNHHPDPTVEENLEQLKQVVIRE 154
Cdd:PRK09542  146 LADYAAFLrsLVDLSGIrPLKVAVDAGNGMGGHTVPAVLGGLPITLLPLYFELDGTFPNHEANPLDPANLVDLQAFVRET 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 155 GMDLGLAFDGDGDRIGAVDRTGHVVWGDQILLILARHLLKEQKGATIIADVKASQVFFDGVVQAGGKAEMWKTGHSLIKS 234
Cdd:PRK09542  226 GADIGLAFDGDADRCFVVDERGQPVSPSAVTALVAARELAREPGATIIHNLITSRAVPELVAERGGTPVRTRVGHSFIKA 305

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 235 RMAETGAPLAGEMSGHIFYKDrFYGHDDGLYAAIRFLNAIWAQGGDLARLRQEMPHVLNTPELRFPCA--EDRKMPVIEG 312
Cdd:PRK09542  306 LMAETGAIFGGEHSAHYYFRD-FWGADSGMLAALHVLAALGEQDRPLSELMADYQRYAASGEINSTVAdaPARMEAVLKA 384

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1733551951 313 VRDRlsqsGAQVIDVDGVRV-LTEDGWWLLRASNTQDVLVARVEARDEEGLTRLKD 367
Cdd:PRK09542  385 FADR----IVSVDHLDGVTVdLGDGSWFNLRASNTEPLLRLNVEARTEEEVDALVD 436
PGM_PMM_III pfam02880
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
180-290 6.22e-26

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


Pssm-ID: 460733  Cd Length: 115  Bit Score: 100.60  E-value: 6.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 180 WGDQILLILARHLLKEQ---KGATIIADVKASQVFFDGVVQAGGKAEMWKTGHSLIKSRMAETGAPLAGEMSGHIFYKDR 256
Cdd:pfam02880   1 DGDQILALLAKYLLEQGklpPGAGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEGALFGGEESGHIIFLDH 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1733551951 257 FYGhDDGLYAAIRFLNAIWAQGGDLARLRQEMPH 290
Cdd:pfam02880  81 ATT-KDGILAALLVLEILARTGKSLSELLEELPE 113
 
Name Accession Description Interval E-value
PMM_PGM cd03089
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ...
 4-373 0e+00

The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the reversible conversion of 1-phospho to 6-phospho-sugars (e.g. between mannose-1-phosphate and mannose-6-phosphate or glucose-1-phosphate and glucose-6-phosphate) via a bisphosphorylated sugar intermediate. The reaction involves two phosphoryl transfers, with an intervening 180 degree reorientation of the reaction intermediate during catalysis. Reorientation of the intermediate occurs without dissociation from the active site of the enzyme and is thus, a simple example of processivity, as defined by multiple rounds of catalysis without release of substrate. Glucose-6-phosphate and glucose-1-phosphate are known to be utilized for energy metabolism and cell surface construction, respectively. PMM/PGM belongs to the alpha-D-phosphohexomutase superfamily which includes several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the phosphoglucomutases (PGM1 and PGM2). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


Pssm-ID: 100091  Cd Length: 443  Bit Score: 529.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951   4 IGLGPTPMVYYAVHELKADGGLMITGSHNPPDYNGIKMMMGKAPVFGEQIKALGALAASGDFE--QGSGTLETVPVFDRY 81
Cdd:cd03089    70 IGLVPTPVLYFATFHLDADGGVMITASHNPPEYNGFKIVIGGGPLSGEDIQALRERAEKGDFAaaTGRGSVEKVDILPDY 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951  82 IHRLLRDFTGAT--MAVAWDPGNGAAGDAVTALVKRLPGRHIVINADIDGRFPNHHPDPTVEENLEQLKQVVIREGMDLG 159
Cdd:cd03089   150 IDRLLSDIKLGKrpLKVVVDAGNGAAGPIAPQLLEALGCEVIPLFCEPDGTFPNHHPDPTDPENLEDLIAAVKENGADLG 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 160 LAFDGDGDRIGAVDRTGHVVWGDQILLILARHLLKEQKGATIIADVKASQVFFDGVVQAGGKAEMWKTGHSLIKSRMAET 239
Cdd:cd03089   230 IAFDGDGDRLGVVDEKGEIIWGDRLLALFARDILKRNPGATIVYDVKCSRNLYDFIEEAGGKPIMWKTGHSFIKAKMKET 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 240 GAPLAGEMSGHIFYKDRFYGHDDGLYAAIRFLNAIWAQGGDLARLRQEMPHVLNTPELRFPCAEDRKMPVIEGVRDRLSQ 319
Cdd:cd03089   310 GALLAGEMSGHIFFKDRWYGFDDGIYAALRLLELLSKSGKTLSELLADLPKYFSTPEIRIPVTEEDKFAVIERLKEHFEF 389

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1733551951 320 SGAQVIDVDGVRVLTEDGWWLLRASNTQDVLVARVEARDEEGLTRLKDLLRGQL 373
Cdd:cd03089   390 PGAEIIDIDGVRVDFEDGWGLVRASNTEPVLVLRFEADTEEGLEEIKAELRKLL 443
ManB COG1109
Phosphomannomutase [Carbohydrate transport and metabolism];
4-376 9.98e-139

Phosphomannomutase [Carbohydrate transport and metabolism];


Pssm-ID: 440726 [Multi-domain]  Cd Length: 456  Bit Score: 403.04  E-value: 9.98e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951   4 IGLGPTPMVYYAVHELKADGGLMITGSHNPPDYNGIKMMMGK-APVFGEQIKALGALAASGDFE----QGSGTLETVP-V 77
Cdd:COG1109    75 LGLVPTPALAFAVRHLGADGGIMITASHNPPEYNGIKFFDADgGKLSPEEEKEIEALIEKEDFRraeaEEIGKVTRIEdV 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951  78 FDRYIHRLLRDFTGAT----MAVAWDPGNGAAGDAVTALVKRLPGRHIVINADIDGRFPNHHPDPTvEENLEQLKQVVIR 153
Cdd:COG1109   155 LEAYIEALKSLVDEALrlrgLKVVVDCGNGAAGGVAPRLLRELGAEVIVLNAEPDGNFPNHNPNPE-PENLEDLIEAVKE 233

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 154 EGMDLGLAFDGDGDRIGAVDRTGHVVWGDQILLILARHLLKEQKGATIIADVKASQVFFDGVVQAGGKAEMWKTGHSLIK 233
Cdd:COG1109   234 TGADLGIAFDGDADRLGVVDEKGRFLDGDQLLALLARYLLEKGPGGTVVVTVMSSLALEDIAEKHGGEVVRTKVGFKYIK 313

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 234 SRMAETGAPLAGEMSGHIFYKDrFYGHDDGLYAAIRFLNAIWAQGGDLARLRQEMPHVLnTPELRFPCAEDRKMP-VIEG 312
Cdd:COG1109   314 EKMRETGAVLGGEESGGIIFPD-FVPTDDGILAALLLLELLAKQGKSLSELLAELPRYP-QPEINVRVPDEEKIGaVMEK 391

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1733551951 313 VRDRLsQSGAQVIDVDGVRVLTEDG-WWLLRASNTQDVLVARVEARDEEGLTRLKDLLRGQLKQA 376
Cdd:COG1109   392 LREAV-EDKEELDTIDGVKVDLEDGgWVLVRPSGTEPLLRVYAEAKDEEEAEELLAELAELVEEA 455
Arch_GlmM TIGR03990
phosphoglucosamine mutase; The MMP1680 protein from Methanococcus maripaludis has been ...
 4-367 2.42e-92

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: 284.02  E-value: 2.42e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951   4 IGLGPTPMVYYAVHELKADGGLMITGSHNPPDYNGIKMMMGKAPVFG-EQIKALGALAASGDFEQ----GSGTLETVP-V 77
Cdd:TIGR03990  69 LGIAPTPTLQYAVRELGADGGIMITASHNPPEYNGIKLLNSDGTELSrEQEEEIEEIAESGDFERadwdEIGTVTSDEdA 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951  78 FDRYIHRLLRDFTGATMA-----VAWDPGNGAAGDAVTALVKRLPGRHIVINADIDGRFPNHHPDPTvEENLEQLKQVVI 152
Cdd:TIGR03990 149 IDDYIEAILDKVDVEAIRkkgfkVVVDCGNGAGSLTTPYLLRELGCKVITLNCQPDGTFPGRNPEPT-PENLKDLSALVK 227

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 153 REGMDLGLAFDGDGDRIGAVDRTGHVVWGDQILLILARHLLkEQKGATIIADVKASQVFFDGVVQAGGKAEMWKTGHSLI 232
Cdd:TIGR03990 228 ATGADLGIAHDGDADRLVFIDEKGRFIGGDYTLALFAKYLL-EHGGGKVVTNVSSSRAVEDVAERHGGEVIRTKVGEVNV 306

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 233 KSRMAETGAPLAGEMSGHIFYKDRFYGhDDGLYAAIRFLNAIWAQGGDLARLRQEMPHvLNTPELRFPCAEDRKMPVIEG 312
Cdd:TIGR03990 307 AEKMKEEGAVFGGEGNGGWIFPDHHYC-RDGLMAAALFLELLAEEGKPLSELLAELPK-YPMSKEKVELPDEDKEEVMEA 384

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1733551951 313 VRDRLsqSGAQVIDVDGVRVLTEDGWWLLRASNTQDVLVARVEARDEEGLTRLKD 367
Cdd:TIGR03990 385 VEEEF--ADAEIDTIDGVRIDFEDGWVLVRPSGTEPIVRIYAEAKTEERAEELLE 437
PGM_like1 cd03087
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ...
 4-369 7.60e-77

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: 244.02  E-value: 7.60e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951   4 IGLGPTPMVYYAVHELkADGGLMITGSHNPPDYNGIKMMMGKAPVFG-EQIKALGALAASGDFEQGS----GTLETVP-V 77
Cdd:cd03087    67 IGIVPTPALQYAVRKL-GDAGVMITASHNPPEYNGIKLVNPDGTEFSrEQEEEIEEIIFSERFRRVAwdevGSVRREDsA 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951  78 FDRYIHRLLR---DFTGATMAVAWDPGNGAAGdAVTALVKRLPGRHIV-INADIDGRFPNHHPDPTvEENLEQLKQVVIR 153
Cdd:cd03087   146 IDEYIEAILDkvdIDGGKGLKVVVDCGNGAGS-LTTPYLLRELGCKVItLNANPDGFFPGRPPEPT-PENLSELMELVRA 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 154 EGMDLGLAFDGDGDRIGAVDRTGHVVWGDQILLILARHLLKEQKGaTIIADVKASQVFFDGVVQAGGKAEMWKTGHSLIK 233
Cdd:cd03087   224 TGADLGIAHDGDADRAVFVDEKGRFIDGDKLLALLAKYLLEEGGG-KVVTPVDASMLVEDVVEEAGGEVIRTPVGDVHVA 302

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 234 SRMAETGAPLAGEMSGHIFYKDRFYGHdDGLYAAIRFLnAIWAQGGDLARLRQEMPHVLNTPElRFPCAEDRKMPVIEGV 313
Cdd:cd03087   303 EEMIENGAVFGGEPNGGWIFPDHQLCR-DGIMTAALLL-ELLAEEKPLSELLDELPKYPLLRE-KVECPDEKKEEVMEAV 379

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1733551951 314 RDRLSQSGAQVIDVDGVRVLTEDGWWLLRASNTQDVLVARVEARDEEgltRLKDLL 369
Cdd:cd03087   380 EEELSDADEDVDTIDGVRIEYEDGWVLIRPSGTEPKIRITAEAKTEE---RAKELL 432
manB PRK09542
phosphomannomutase/phosphoglucomutase; Reviewed
 3-367 3.58e-60

phosphomannomutase/phosphoglucomutase; Reviewed


Pssm-ID: 236557  Cd Length: 445  Bit Score: 200.98  E-value: 3.58e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951   3 AIGLGPTPMVYYAVHELKADGGlMITGSHNPPDYNGIKM-MMGKAPVFGE----QIKALgALAASGDFEQGSGTLETVPV 77
Cdd:PRK09542   68 RIGLASTDQLYFASGLLDCPGA-MFTASHNPAAYNGIKLcRAGAKPVGQDtglaAIRDD-LIAGVPAYDGPPGTVTERDV 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951  78 FDRYIHRL--LRDFTGA-TMAVAWDPGNGAAGDAVTALVKRLPGRHIVINADIDGRFPNHHPDPTVEENLEQLKQVVIRE 154
Cdd:PRK09542  146 LADYAAFLrsLVDLSGIrPLKVAVDAGNGMGGHTVPAVLGGLPITLLPLYFELDGTFPNHEANPLDPANLVDLQAFVRET 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 155 GMDLGLAFDGDGDRIGAVDRTGHVVWGDQILLILARHLLKEQKGATIIADVKASQVFFDGVVQAGGKAEMWKTGHSLIKS 234
Cdd:PRK09542  226 GADIGLAFDGDADRCFVVDERGQPVSPSAVTALVAARELAREPGATIIHNLITSRAVPELVAERGGTPVRTRVGHSFIKA 305

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 235 RMAETGAPLAGEMSGHIFYKDrFYGHDDGLYAAIRFLNAIWAQGGDLARLRQEMPHVLNTPELRFPCA--EDRKMPVIEG 312
Cdd:PRK09542  306 LMAETGAIFGGEHSAHYYFRD-FWGADSGMLAALHVLAALGEQDRPLSELMADYQRYAASGEINSTVAdaPARMEAVLKA 384

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1733551951 313 VRDRlsqsGAQVIDVDGVRV-LTEDGWWLLRASNTQDVLVARVEARDEEGLTRLKD 367
Cdd:PRK09542  385 FADR----IVSVDHLDGVTVdLGDGSWFNLRASNTEPLLRLNVEARTEEEVDALVD 436
phosphohexomutase cd03084
The alpha-D-phosphohexomutase superfamily includes several related enzymes that catalyze a ...
 23-373 1.79e-58

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: 193.73  E-value: 1.79e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951  23 GGLMITGSHNPPDYNGIKMMMGK-APVFGEQIKALGALA-----ASGDFEQGSGTLETVPVFDRYIHRLLRDF-----TG 91
Cdd:cd03084    31 GGIMITASHNPPEDNGIKFVDPDgEPIASEEEKAIEDLAekedePSAVAYELGGSVKAVDILQRYFEALKKLFdvaalSN 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951  92 ATMAVAWDPGNGAAGDAVTALVKRLPGRHIVINADIDGRFPNHHPDPTVEENLEQLKQVVIREGMDLGLAFDGDGDRIGA 171
Cdd:cd03084   111 KKFKVVVDSVNGVGGPIAPQLLEKLGAEVIPLNCEPDGNFGNINPDPGSETNLKQLLAVVKAEKADFGVAFDGDADRLIV 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 172 VDRTGHVVWGDQILLILARHLLKE-QKGATIIADVKASQVFFDGVVQAGGKAEMWKTGHSLIKSRMAETGAPLAGEMSGH 250
Cdd:cd03084   191 VDENGGFLDGDELLALLAVELFLTfNPRGGVVKTVVSSGALDKVAKKLGIKVIRTKTGFKWVGEAMQEGDVVLGGEESGG 270

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 251 IFYKDRFYGhDDGLYAAIRFLNAIWAQGGDLARLRQEMPHVLNTPelrfpcaedrkmpviegvrdrlsqsgaqvidvdgv 330
Cdd:cd03084   271 VIFPEFHPG-RDGISAALLLLEILANLGKSLSELFSELPRYYYIR----------------------------------- 314

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1733551951 331 rvLTEDGWWLLRASNTQDVLVARVEARDEEGLTRLKDLLRGQL 373
Cdd:cd03084   315 --LKVRGWVLVRASGTEPAIRIYAEADTQEDVEQIKKEARELV 355
PGM_like2 cd05800
This PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ...
 8-365 3.47e-58

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: 195.85  E-value: 3.47e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951   8 PTPMVYYAVHELKADGGLMITGSHNPPDYNGIKMMMGKA-PVFGEQIKALGALAASGD----FEQGSGTLETVPVFDRYI 82
Cdd:cd05800    78 PTPAVSWAVKKLGAAGGVMITASHNPPEYNGVKVKPAFGgSALPEITAAIEARLASGEppglEARAEGLIETIDPKPDYL 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951  83 HRLLR--DFT---GATMAVAWDPGNGAAGDAVTALVKRLPGRHIVINADIDGRFPNHHPDPTvEENLEQLKQVVIREGMD 157
Cdd:cd05800   158 EALRSlvDLEairEAGLKVVVDPMYGAGAGYLEELLRGAGVDVEEIRAERDPLFGGIPPEPI-EKNLGELAEAVKEGGAD 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 158 LGLAFDGDGDRIGAVDRTGHVVWGDQILLILARHLLKEQKGATIIADVKASQVFFDGVVQAGG-KAEMWKTGHSLIKSRM 236
Cdd:cd05800   237 LGLATDGDADRIGAVDEKGNFLDPNQILALLLDYLLENKGLRGPVVKTVSTTHLIDRIAEKHGlPVYETPVGFKYIAEKM 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 237 AETGAPLAGEMSGHIFYKdrfyGH---DDGLYAAIRFLNAIWAQGGDLARLRQEM-----PHVLNtpELRFPCAEDRKMP 308
Cdd:cd05800   317 LEEDVLIGGEESGGLGIR----GHipeRDGILAGLLLLEAVAKTGKPLSELVAELeeeygPSYYD--RIDLRLTPAQKEA 390

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1733551951 309 VIEGVRDRLSQSGA-----QVIDVDGVRVLTEDGWWLL-RASNTQDVLVARVEARDEEGLTRL 365
Cdd:cd05800   391 ILEKLKNEPPLSIAggkvdEVNTIDGVKLVLEDGSWLLiRPSGTEPLLRIYAEAPSPEKVEAL 453
PRK15414 PRK15414
phosphomannomutase;
4-369 1.19e-54

phosphomannomutase;


Pssm-ID: 185312  Cd Length: 456  Bit Score: 186.69  E-value: 1.19e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951   4 IGLGPTPMVYYAVHELKADGGLMITGSHNPPDYNGIKMMM-GKAPVFGEQ-IKALGALAASGDF----EQGSGTLETVPV 77
Cdd:PRK15414   72 IGMSGTEEIYFATFHLGVDGGIEVTASHNPMDYNGMKLVReGARPISGDTgLRDVQRLAEANDFppvdETKRGRYQQINL 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951  78 FDRYIHRLL-----RDFTgaTMAVAWDPGNGAAGDAVTALVKRL-----PGRHIVINADIDGRFPNHHPDPTVEENLEQL 147
Cdd:PRK15414  152 RDAYVDHLFgyinvKNLT--PLKLVINSGNGAAGPVVDAIEARFkalgaPVELIKVHNTPDGNFPNGIPNPLLPECRDDT 229

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 148 KQVVIREGMDLGLAFDGDGDRIGAVDRTGHVVWGDQILLILARHLLKEQKGATIIADVKASQVFFDGVVQAGGKAEMWKT 227
Cdd:PRK15414  230 RNAVIKHGADMGIAFDGDFDRCFLFDEKGQFIEGYYIVGLLAEAFLEKNPGAKIIHDPRLSWNTVDVVTAAGGTPVMSKT 309

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 228 GHSLIKSRMAETGAPLAGEMSGHIFYKDRFYGhDDGLYAAIRFLNAIWAQGGDLARL-RQEMPHVLNTPELRFPCAEDRK 306
Cdd:PRK15414  310 GHAFIKERMRKEDAIYGGEMSAHHYFRDFAYC-DSGMIPWLLVAELVCLKGKTLGELvRDRMAAFPASGEINSKLAQPVE 388

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1733551951 307 mpVIEGVRDRLSQSGAQVIDVDGVRVLTEDGWWLLRASNTQDVLVARVEARDEEGL--TRLKDLL 369
Cdd:PRK15414  389 --AINRVEQHFSREALAVDRTDGISMTFADWRFNLRSSNTEPVVRLNVESRGDVPLmeARTRTLL 451
GlmM cd05802
GlmM is a bacterial phosphoglucosamine mutase (PNGM) that belongs to the ...
 4-360 7.56e-46

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: 162.65  E-value: 7.56e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951   4 IGLGPTPMVYYAVHELKADGGLMITGSHNPPDYNGIKmmmgkapVFG-----------EQIKALgALAASGDFEQGSG-- 70
Cdd:cd05802    71 LGVIPTPAVAYLTRKLRADAGVVISASHNPFEDNGIK-------FFSsdgyklpdeveEEIEAL-IDKELELPPTGEKig 142

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951  71 -TLETVPVFDRYIHRLL-----RDFTGatMAVAWDPGNGAAGDAVTALVKRLPGRHIVINADIDGRFPNHHPDPTveeNL 144
Cdd:cd05802   143 rVYRIDDARGRYIEFLKstfpkDLLSG--LKIVLDCANGAAYKVAPEVFRELGAEVIVINNAPDGLNINVNCGST---HP 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 145 EQLKQVVIREGMDLGLAFDGDGDRIGAVDRTGHVVWGDQILLILARHLLKEQ--KGATIIADVKASQVFFDGVVQAGGKA 222
Cdd:cd05802   218 ESLQKAVLENGADLGIAFDGDADRVIAVDEKGNIVDGDQILAICARDLKERGrlKGNTVVGTVMSNLGLEKALKELGIKL 297

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 223 EMWKTGHSLIKSRMAETGAPLAGEMSGHIFYKDrfygHD---DGLYAAIRFLNAIWAQGGDLARLRQEM---PHVL-NTP 295
Cdd:cd05802   298 VRTKVGDRYVLEEMLKHGANLGGEQSGHIIFLD----HSttgDGLLTALQLLAIMKRSGKSLSELASDMklyPQVLvNVR 373

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1733551951 296 -ELRFPCAED-RKMPVIEGVRDRLSQSGaqvidvdgvRVltedgwwLLRASNTQDVLVARVEARDEE 360
Cdd:cd05802   374 vKDKKALLENpRVQAAIAEAEKELGGEG---------RV-------LVRPSGTEPLIRVMVEGEDEE 424
glmM TIGR01455
phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also ...
 4-369 1.14e-44

phosphoglucosamine mutase; This model describes GlmM, phosphoglucosamine mutase, also designated in MrsA and YhbF E. coli, UreC in Helicobacter pylori, and femR315 or FemD in Staphlococcus aureus. It converts glucosamine-6-phosphate to glucosamine-1-phosphate as part of the pathway toward UDP-N-acetylglucosamine for peptidoglycan and lipopolysaccharides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan, Central intermediary metabolism, Amino sugars]


Pssm-ID: 130522  Cd Length: 443  Bit Score: 159.84  E-value: 1.14e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951   4 IGLGPTPMVYYAVHELKADGGLMITGSHNPPDYNGIKM---MMGKAP-VFGEQIKALGALAASGDFEQGSG---TLETVP 76
Cdd:TIGR01455  72 LGPLPTPAVAYLTRTLRADAGVMISASHNPYEDNGIKFfgpGGFKLDdATEAAIEALLDEADPLPRPESEGlgrVKRYPD 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951  77 VFDRYIHRLLRDFTGAT----MAVAWDPGNGAAGDAVTALVKRLPGRHIVINADIDGRFPNHHPDPTveeNLEQLKQVVI 152
Cdd:TIGR01455 152 AVGRYIEFLKSTLPRGLtlsgLKVVLDCANGAAYKVAPHVFRELGAEVIAIGVEPDGLNINDGCGST---HLDALQKAVR 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 153 REGMDLGLAFDGDGDRIGAVDRTGHVVWGDQILLILARHLLK--EQKGATIIADVKASQVFFDGVVQAGGKAEMWKTGHS 230
Cdd:TIGR01455 229 EHGADLGIAFDGDADRVLAVDANGRIVDGDQILYIIARALKEsgELAGNTVVATVMSNLGLERALEKLGLTLIRTAVGDR 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 231 LIKSRMAETGAPLAGEMSGHIFYKDRFYGhDDGLYAAIRFLNAIWAQGGDLARLRQEMPHVLNTpeLRFPCAEDRKMPVI 310
Cdd:TIGR01455 309 YVLEEMRESGYNLGGEQSGHIILLDYSTT-GDGIVSALQVLTIMKKSGSTLSELAAEFVPYPQT--LVNVRVADRKLAAA 385

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1733551951 311 E--GVRDRLSQSGAQvidvdgvrvLTEDGWWLLRASNTQDVLVARVEARDEEGLTRLKDLL 369
Cdd:TIGR01455 386 EapAVKAAIEDAEAE---------LGGTGRILLRPSGTEPLIRVMVEAADEELVQQLADTL 437
PGM_like4 cd05803
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ...
 4-367 1.37e-41

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: 151.69  E-value: 1.37e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951   4 IGLGPTPMVYYAVHELKADGGLMITGSHNPPDYNGIKMMMGKAPVF-GEQIKALGALAASGDFE----QGSGTLETVP-V 77
Cdd:cd05803    71 LGIAPTPTVQVLVRQSQASGGIIITASHNPPQWNGLKFIGPDGEFLtPDEGEEVLSCAEAGSAQkagyDQLGEVTFSEdA 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951  78 FDRYIHRLL------------RDFTgatmaVAWDPGNGAAGDAVTALVKRLPGRHIVINADIDGRFPnHHPDPTvEENLE 145
Cdd:cd05803   151 IAEHIDKVLalvdvdvikireRNFK-----VAVDSVNGAGGLLIPRLLEKLGCEVIVLNCEPTGLFP-HTPEPL-PENLT 223

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 146 QLKQVVIREGMDLGLAFDGDGDRIGAVDRTGHVVwGDQILLILA-RHLLKEQ-KGATIIADVKASQVFFDGVVQAGGKAE 223
Cdd:cd05803   224 QLCAAVKESGADVGFAVDPDADRLALVDEDGRPI-GEEYTLALAvDYVLKYGgRKGPVVVNLSTSRALEDIARKHGVPVF 302

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 224 MWKTGHSLIKSRMAETGAPLAGEMSGHIFYKDRFYGHdDGLYAAIRFLNAIWAQGGDLARLRQEMPHVLNTpELRFPCAE 303
Cdd:cd05803   303 RSAVGEANVVEKMKEVDAVIGGEGNGGVILPDVHYGR-DSLVGIALVLQLLAASGKPLSEIVDELPQYYIS-KTKVTIAG 380

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1733551951 304 drkmPVIEGVRDRLSQ--SGAQVIDVDGVRVLTEDGWWLLRASNTQDVLVARVEARDEEGLTRLKD 367
Cdd:cd05803   381 ----EALERLLKKLEAyfKDAEASTLDGLRLDSEDSWVHVRPSNTEPIVRIIAEAPTQDEAEALAD 442
PGM_PMM_III pfam02880
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
180-290 6.22e-26

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


Pssm-ID: 460733  Cd Length: 115  Bit Score: 100.60  E-value: 6.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 180 WGDQILLILARHLLKEQ---KGATIIADVKASQVFFDGVVQAGGKAEMWKTGHSLIKSRMAETGAPLAGEMSGHIFYKDR 256
Cdd:pfam02880   1 DGDQILALLAKYLLEQGklpPGAGVVKTVMSSLGLDRVAKKLGGKLVRTPVGDKYVKEKMREEGALFGGEESGHIIFLDH 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1733551951 257 FYGhDDGLYAAIRFLNAIWAQGGDLARLRQEMPH 290
Cdd:pfam02880  81 ATT-KDGILAALLVLEILARTGKSLSELLEELPE 113
glmM PRK10887
phosphoglucosamine mutase; Provisional
 8-377 5.64e-25

phosphoglucosamine mutase; Provisional


Pssm-ID: 236787  Cd Length: 443  Bit Score: 105.60  E-value: 5.64e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951   8 PTPMVYYAVHELKADGGLMITGSHNPPDYNGIKMmmgkapvFG-----------EQIKALgalaasgdFEQgsgTLETVP 76
Cdd:PRK10887   77 PTPAVAYLTRTLRAEAGIVISASHNPYYDNGIKF-------FSadgtklpdeveLAIEAE--------LDK---PLTCVE 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951  77 ---------VFD---RYIH----RLLRDFTGATMAVAWDPGNGAAGDAVTALVKRLPGRHIVINADIDGRFPNHHPDPTv 140
Cdd:PRK10887  139 saelgkasrINDaagRYIEfcksTFPNELSLRGLKIVVDCANGATYHIAPNVFRELGAEVIAIGCEPNGLNINDECGAT- 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 141 eeNLEQLKQVVIREGMDLGLAFDGDGDRIGAVDRTGHVVWGDQILLILARHLLKEQKGAtiiadvkasqvffDGVV---- 216
Cdd:PRK10887  218 --DPEALQAAVLAEKADLGIAFDGDGDRVIMVDHLGNLVDGDQLLYIIARDRLRRGQLR-------------GGVVgtlm 282

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 217 ----------QAGGKAEMWKTGHSLIKSRMAETGAPLAGEMSGHIFYKDRfygHD--DGLYAAIRFLNAIWAQGGDLARL 284
Cdd:PRK10887  283 snmglelalkQLGIPFVRAKVGDRYVLEKLQEKGWRLGGENSGHILCLDK---TTtgDGIVAALQVLAAMVRSGMSLADL 359

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 285 RQEM---PHVL-NtpeLRFPCAEDRKMP------VIEGVRDRLSQSGaqvidvdgvRVltedgwwLLRASNTQDVLVARV 354
Cdd:PRK10887  360 CSGMklfPQVLiN---VRFKPGADDPLEseavkaALAEVEAELGGRG---------RV-------LLRKSGTEPLIRVMV 420

                         410       420
                  ....*....|....*....|...
gi 1733551951 355 EARDEEGLTRLKDLLRGQLKQAG 377
Cdd:PRK10887  421 EGEDEAQVTALAERIADAVKAAA 443
PLN02371 PLN02371
phosphoglucosamine mutase family protein
 5-374 1.67e-24

phosphoglucosamine mutase family protein


Pssm-ID: 215211 [Multi-domain]  Cd Length: 583  Bit Score: 105.14  E-value: 1.67e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951   5 GLGPTPMVYYAV--HELKADGGLMITGSHNPPDYNGIKMMMGKAPVFGEQIKALGALAASGDFEQGSGTLETV------- 75
Cdd:PLN02371  150 GLATTPAMFMSTltEREDYDAPIMITASHLPYNRNGLKFFTKDGGLGKPDIKDILERAARIYKEWSDEGLLKSssgassv 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951  76 -------PVFDRYIHRLLRDFTGAT---------MAVAWDPGNGAAGDAVTALVKRLpgrhiviNADI--------DGRF 131
Cdd:PLN02371  230 vcrvdfmSTYAKHLRDAIKEGVGHPtnyetplegFKIVVDAGNGAGGFFAEKVLEPL-------GADTsgslflepDGMF 302

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 132 PNHHPDPTVEENLEQLKQVVIREGMDLGLAFDGDGDRIGAVDRTGHVVWGDQILLILARHLLKEQKGATIIADVKASQVF 211
Cdd:PLN02371  303 PNHIPNPEDKAAMSATTQAVLANKADLGIIFDTDVDRSAVVDSSGREINRNRLIALMSAIVLEEHPGTTIVTDSVTSDGL 382

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 212 FDGVVQAGGKAEMWKTGH-SLIKS--RMAETG--APLAGEMSGHIFYKDRFYgHDDGLYAAIRFLNAIWA-----QGGDL 281
Cdd:PLN02371  383 TTFIEKKGGKHHRFKRGYkNVIDKgvRLNSDGeeTHLMIETSGHGALKENHF-LDDGAYLAVKIIIELVRmraagAGGGL 461

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 282 ARLRQEMPHVLNTPELRFPCAEDRK------MPVIEGVRDRLSQSGAQVIDVD---GVRVLTED----GWWLLRASNTQD 348
Cdd:PLN02371  462 GDLIEDLEEPLEAVELRLKILDEGKdfkaygEEVLEHLRNSIESDGKLEGAPVnyeGVRVSDEGegfgGWFLLRQSLHDP 541

                         410       420
                  ....*....|....*....|....*.
gi 1733551951 349 VLVARVEARDEEGLTRLKDLLRGQLK 374
Cdd:PLN02371  542 VIPLNIESSSPGGAQKMALVVLTWLK 567
PGM2 cd05799
This CD includes PGM2 (phosphoglucomutase 2) and PGM2L1 (phosphoglucomutase 2-like 1). The ...
 8-197 2.14e-22

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: 98.35  E-value: 2.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951   8 PTPMVYYAVHELKADGGLMITGSHNPPDYNGIKmmmgkapVFGE---QI-------------KALGALAASGDFEQGSGT 71
Cdd:cd05799    84 PTPLLSFAVRHLGADAGIMITASHNPKEYNGYK-------VYWEdgaQIipphdaeiaeeieAVLEPLDIKFEEALDSGL 156

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951  72 LETVP--VFDRYIHRLLR------DFTGATMAVAWDPGNGAAGDAVTALVKRLPGRHIVI---NADIDGRFPN-HHPDPT 139
Cdd:cd05799   157 IKYIGeeIDDAYLEAVKKllvnpeLNEGKDLKIVYTPLHGVGGKFVPRALKEAGFTNVIVveeQAEPDPDFPTvKFPNPE 236

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1733551951 140 VEENLEQLKQVVIREGMDLGLAFDGDGDRIGAVDRTGHVVW----GDQILLILARHLLKEQK 197
Cdd:cd05799   237 EPGALDLAIELAKKVGADLILATDPDADRLGVAVKDKDGEWrlltGNEIGALLADYLLEQRK 298
MPG1_transferase cd05805
GTP-mannose-1-phosphate guanyltransferase (MPG1 transferase), also known as GDP-mannose ...
 4-360 1.56e-21

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: 95.39  E-value: 1.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951   4 IGLGPTPMVYYAVHELKADGGLMITGSHNPPDYNGIKMMMGK-APVFGEQIKALGALAASGDF----EQGSGTLETVPVF 78
Cdd:cd05805    68 LGALPLPVARYAIRFLGASGGIHVRTSPDDPDKVEIEFFDSRgLNISRAMERKIENAFFREDFrrahVDEIGDITEPPDF 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951  79 -DRYIHRLLR-----DFTGATMAVAWDPGNGAAGDAVTALVKRLPGRHIVINADIDGRfpNHHPDPTVEENLEQLKQVVI 152
Cdd:cd05805   148 vEYYIRGLLRaldtsGLKKSGLKVVIDYAYGVAGIVLPGLLSRLGCDVVILNARLDED--APRTDTERQRSLDRLGRIVK 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 153 REGMDLGLAFDGDGDRIGAVDRTGHVVWGDQILLILARHLLKEQKGATIIADVKASQVFFDGVVQAGGKAEMWKTGHSLI 232
Cdd:cd05805   226 ALGADFGVIIDPNGERLILVDEAGRVISDDLLTALVSLLVLKSEPGGTVVVPVTAPSVIEQLAERYGGRVIRTKTSPQAL 305

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 233 KSRMAEtGAPLAGEMSGHIFYKdRFYGHDDGLYAAIRFLNAIWAQGGDLARLRQEMP--HVLNTpelRFPCAEDRKMPVI 310
Cdd:cd05805   306 MEAALE-NVVLAGDGDGGFIFP-EFHPGFDAIAALVKILEMLARTNISLSQIVDELPrfYVLHK---EVPCPWEAKGRVM 380

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1733551951 311 egvRDRLSQSGAQVID-VDGVRVLTEDGWWLLRASNTQDVLVARVEARDEE 360
Cdd:cd05805   381 ---RRLIEEAPDKSIElIDGVKIYEDDGWVLVLPDADEPLCHIYAEGSDQE 428
PGM_PMM_II pfam02879
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II;
81-176 2.19e-20

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


Pssm-ID: 427033  Cd Length: 102  Bit Score: 85.04  E-value: 2.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951  81 YIHRLLRDF-----TGATMAVAWDPGNGAAGDAVTALVKRLPGRHIVINADIDGRFPNHHPDPTVEENLEQLKQVVIREG 155
Cdd:pfam02879   2 YIDHLLELVdsealKKRGLKVVYDPLHGVGGGYLPELLKRLGCDVVEENCEPDPDFPTRAPNPEEPEALALLIELVKSVG 81

                          90       100
                  ....*....|....*....|.
gi 1733551951 156 MDLGLAFDGDGDRIGAVDRTG 176
Cdd:pfam02879  82 ADLGIATDGDADRLGVVDERG 102
PGM_PMM_I pfam02878
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain I;
4-65 7.21e-19

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


Pssm-ID: 427032  Cd Length: 138  Bit Score: 82.27  E-value: 7.21e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1733551951   4 IGLGPTPMVYYAVHELKADGGLMITGSHNPPDYNGIKMMMGK-APVFGEQIKALGALAASGDF 65
Cdd:pfam02878  74 LGLLPTPAVSFATRKLKADGGIMITASHNPPEYNGIKVFDSNgGPIPPEVEKKIEAIIEKEDF 136
PGM_PMM_IV pfam00408
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
296-374 8.82e-12

Phosphoglucomutase/phosphomannomutase, C-terminal domain;


Pssm-ID: 425666  Cd Length: 71  Bit Score: 59.98  E-value: 8.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 296 ELRFPCAEDRKMPVIEGVRDRLSqsgaqvidvDGVRVLTEDGWWL-LRASNTQDVLVARVEARDEEGLTRLKDLLRGQLK 374
Cdd:pfam00408   1 LINVRVAEKKKLAALAAILKVFA---------DAEKILGEDGRRLdVRPSGTEPVLRVMVEGDSDEELARLADEIADLLE 71
PGM1 cd03085
Phosphoglucomutase 1 (PGM1) catalyzes the bidirectional interconversion of glucose-1-phosphate ...
 5-168 1.30e-08

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: 56.46  E-value: 1.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951   5 GLGPTPMVYYAVHELKADGGLMITGSHNP--PDYN-GIKMMM---GKAP------VFGE-----QIKALGA----LAASG 63
Cdd:cd03085    87 GLLSTPAVSAVIRKRKATGGIILTASHNPggPEGDfGIKYNTsngGPAPesvtdkIYEItkkitEYKIADDpdvdLSKIG 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951  64 DFEQGSGTLeTVPVFDR---YIhRLLR---DF-------TGATMAVAWDPGNGAAGD-AVTALVKRL--PgRHIVINADI 127
Cdd:cd03085   167 VTKFGGKPF-TVEVIDSvedYV-ELMKeifDFdaikkllSRKGFKVRFDAMHGVTGPyAKKIFVEELgaP-ESSVVNCTP 243

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1733551951 128 DGRFPNHHPDPtveeNL---EQLKQVVIREGMDLGLAFDGDGDR 168
Cdd:cd03085   244 LPDFGGGHPDP----NLtyaKDLVELMKSGEPDFGAASDGDGDR 283
ManB cd03088
ManB is a bacterial phosphomannomutase (PMM) that catalyzes the conversion of mannose ...
 1-203 1.06e-07

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: 53.36  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951   1 MRAIGLG--PTPMVYYAVHELKAdGGLMITGSHNPPDYNGIKmmmgkapvF----GE-------QIKALGALAASGDFEQ 67
Cdd:cd03088    65 FRVVDCGavPTPALALYAMKRGA-PAIMVTGSHIPADRNGLK--------FyrpdGEitkadeaAILAALVELPEALFDP 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951  68 GSGTLETVP-VFDRYIHRLLRDFTGATMA---VAWDPGNGAAGDAVTALVKRLPGRHIVInadidGRFPNHHPDPT---V 140
Cdd:cd03088   136 AGALLPPDTdAADAYIARYTDFFGAGALKglrIGVYQHSSVGRDLLVRILEALGAEVVPL-----GRSDTFIPVDTeavR 210

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1733551951 141 EENLEQLKQVVIREGMDLGLAFDGDGDRIGAVDRTGHVVWGDQILLILARHLlkeqkGATIIA 203
Cdd:cd03088   211 PEDRALAAAWAAEHGLDAIVSTDGDGDRPLVADETGEWLRGDILGLLTARFL-----GADTVV 268
PTZ00150 PTZ00150
phosphoglucomutase-2-like protein; Provisional
 8-194 2.08e-07

phosphoglucomutase-2-like protein; Provisional


Pssm-ID: 240294  Cd Length: 584  Bit Score: 52.76  E-value: 2.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951   8 PTPMVYYAVHELKADGGLMITGSHNPPDYNGIKmmmgkapVF---GEQIKA-------------LGALAASGDFEQGSGT 71
Cdd:PTZ00150  128 PTPFVPYAVRKLKCLAGVMVTASHNPKEDNGYK-------VYwsnGAQIIPphdknisakilsnLEPWSSSWEYLTETLV 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951  72 LETV-PVFDRYIHRLLRDFTGAT-----MAVAWDPGNGAAGDAVTALVK--RLPGrHIVINADI--DGRFPN-HHPDPtv 140
Cdd:PTZ00150  201 EDPLaEVSDAYFATLKSEYNPACcdrskVKIVYTAMHGVGTRFVQKALHtvGLPN-LLSVAQQAepDPEFPTvTFPNP-- 277

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951 141 EENLEQLK---QVVIREGMDLGLAFDGDGDRIGAVDRTG---HVVWGDQILLILARHLLK 194
Cdd:PTZ00150  278 EEGKGALKlsmETAEAHGSTVVLANDPDADRLAVAEKLNngwKIFTGNELGALLAWWAMK 337
PGM3 cd03086
PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 ...
 24-41 1.57e-04

PGM3 (phosphoglucomutase 3), also known as PAGM (phosphoacetylglucosamine mutase) and AGM1 (N-acetylglucosamine-phosphate mutase), is an essential enzyme found in eukaryotes that reversibly catalyzes the conversion of GlcNAc-6-phosphate into GlcNAc-1-phosphate as part of the UDP-N-acetylglucosamine (UDP-GlcNAc) biosynthetic pathway. UDP-GlcNAc is an essential metabolite that serves as the biosynthetic precursor of many glycoproteins and mucopolysaccharides. AGM1 is a member of the alpha-D-phosphohexomutase superfamily, which catalyzes the intramolecular phosphoryl transfer of sugar substrates. The alpha-D-phosphohexomutases have four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


Pssm-ID: 100088  Cd Length: 513  Bit Score: 43.74  E-value: 1.57e-04
                          10
                  ....*....|....*...
gi 1733551951  24 GLMITGSHNPPDYNGIKM 41
Cdd:cd03086    38 GVMITASHNPVEDNGVKI 55
PGM_like3 cd05801
This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ...
 8-40 1.68e-04

This bacterial PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the alpha-D-phosphohexomutase superfamily. The alpha-D-phosphohexomutases include several related enzymes that catalyze a reversible intramolecular phosphoryl transfer on their sugar substrates. Other members of this superfamily include phosphoglucosamine mutase (PNGM), phosphoacetylglucosamine mutase (PAGM), the bacterial phosphomannomutase ManB, the bacterial phosphoglucosamine mutase GlmM, and the bifunctional phosphomannomutase/phosphoglucomutase (PMM/PGM). Each of these enzymes has four domains with a centrally located active site formed by four loops, one from each domain. All four domains are included in this alignment model.


Pssm-ID: 100094 [Multi-domain]  Cd Length: 522  Bit Score: 43.39  E-value: 1.68e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1733551951   8 PTPMVYYAV-------HELKADGgLMITGSHNPPDYNGIK 40
Cdd:cd05801   100 PTPVISHAIltynrgrTEGLADG-IVITPSHNPPEDGGFK 138
PRK07564 PRK07564
phosphoglucomutase; Validated
 5-176 1.83e-04

phosphoglucomutase; Validated


Pssm-ID: 236050  Cd Length: 543  Bit Score: 43.59  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951   5 GLGPTPMVYYAV-----HELKADGGLMITGSHNPPDYNGIKMMM---GKAPvfgEQI-----KALGALAASG-------D 64
Cdd:PRK07564  114 GYTPTPAVSHAIlkyngRGGGLADGIVITPSHNPPEDGGIKYNPpngGPAD---TDVtdaieARANELLAYGlkgvkriP 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1733551951  65 FEQgSGTLETVPVFD---RYIhRLLR---DF-----TGATMAVawDPGNGAAGDAVTALVKRLPGRHIVINADIDGRFP- 132
Cdd:PRK07564  191 LDR-ALASMTVEVIDpvaDYV-EDLEnvfDFdairkAGLRLGV--DPLGGATGPYWKAIAERYGLDLTVVNAPVDPTFNf 266

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1733551951 133 -------NHHPDPTVEENLEQLkqVVIREGMDLGLAFDGDGDRIGAVDRTG 176
Cdd:PRK07564  267 mpldddgKIRMDCSSPYAMAGL--LALKDAFDLAFANDPDGDRHGIVTPGG 315
 
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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