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Conserved domains on  [gi|1104065078|emb|SFX28180|]
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Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III, partial [Klebsiella quasipneumoniae]

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 ...
 1-139 8.17e-82

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 PRK15414:

Pssm-ID: 476822  Cd Length: 456  Bit Score: 247.55  E-value: 8.17e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104065078   1 MRQEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVAELLCLKNSSLKSLVADRQAAFPASGEINRKLGNAVEAIARIRAQY 80
Cdd:PRK15414  318 MRKEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVAELVCLKGKTLGELVRDRMAAFPASGEINSKLAQPVEAINRVEQHF 397

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1104065078  81 EPAAAHIDTTDGISIEYPEWRFNLRTSNTEPVVRLNVESRADTALMNEKTAELLNLLKE 139
Cdd:PRK15414  398 SREALAVDRTDGISMTFADWRFNLRSSNTEPVVRLNVESRGDVPLMEARTRTLLTLLNE 456
 
Name Accession Description Interval E-value
PRK15414 PRK15414
phosphomannomutase;
1-139 8.17e-82

phosphomannomutase;


Pssm-ID: 185312  Cd Length: 456  Bit Score: 247.55  E-value: 8.17e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104065078   1 MRQEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVAELLCLKNSSLKSLVADRQAAFPASGEINRKLGNAVEAIARIRAQY 80
Cdd:PRK15414  318 MRKEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVAELVCLKGKTLGELVRDRMAAFPASGEINSKLAQPVEAINRVEQHF 397

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1104065078  81 EPAAAHIDTTDGISIEYPEWRFNLRTSNTEPVVRLNVESRADTALMNEKTAELLNLLKE 139
Cdd:PRK15414  398 SREALAVDRTDGISMTFADWRFNLRSSNTEPVVRLNVESRGDVPLMEARTRTLLTLLNE 456
PMM_PGM cd03089
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ...
 1-137 3.37e-46

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: 154.98  E-value: 3.37e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104065078   1 MRQEDAIYGGEMSAHHYFRD-FAYCDSGMIPWLLVAELLCLKNSSLKSLVADRQAaFPASGEINRKL--GNAVEAIARIR 77
Cdd:cd03089   306 MKETGALLAGEMSGHIFFKDrWYGFDDGIYAALRLLELLSKSGKTLSELLADLPK-YFSTPEIRIPVteEDKFAVIERLK 384

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104065078  78 AQYEPAAAHIDTTDGISIEYPEWRFNLRTSNTEPVVRLNVESRADtALMNEKTAELLNLL 137
Cdd:cd03089   385 EHFEFPGAEIIDIDGVRVDFEDGWGLVRASNTEPVLVLRFEADTE-EGLEEIKAELRKLL 443
ManB COG1109
Phosphomannomutase [Carbohydrate transport and metabolism];
1-140 1.60e-35

Phosphomannomutase [Carbohydrate transport and metabolism];


Pssm-ID: 440726 [Multi-domain]  Cd Length: 456  Bit Score: 127.24  E-value: 1.60e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104065078   1 MRQEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVAELLCLKNSSLKSLVADRQAAFpaSGEINRKLGNAV---EAIARIR 77
Cdd:COG1109   316 MRETGAVLGGEESGGIIFPDFVPTDDGILAALLLLELLAKQGKSLSELLAELPRYP--QPEINVRVPDEEkigAVMEKLR 393

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1104065078  78 AQYEpAAAHIDTTDGISIEYPEW-RFNLRTSNTEPVVRLNVESRaDTALMNEKTAELLNLLKEE 140
Cdd:COG1109   394 EAVE-DKEELDTIDGVKVDLEDGgWVLVRPSGTEPLLRVYAEAK-DEEEAEELLAELAELVEEA 455
PGM_PMM_III pfam02880
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
1-56 2.06e-17

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


Pssm-ID: 460733  Cd Length: 115  Bit Score: 72.48  E-value: 2.06e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1104065078   1 MRQEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVAELLCLKNSSLKSLVADRQAAF 56
Cdd:pfam02880  60 MREEGALFGGEESGHIIFLDHATTKDGILAALLVLEILARTGKSLSELLEELPEKY 115
 
Name Accession Description Interval E-value
PRK15414 PRK15414
phosphomannomutase;
1-139 8.17e-82

phosphomannomutase;


Pssm-ID: 185312  Cd Length: 456  Bit Score: 247.55  E-value: 8.17e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104065078   1 MRQEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVAELLCLKNSSLKSLVADRQAAFPASGEINRKLGNAVEAIARIRAQY 80
Cdd:PRK15414  318 MRKEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVAELVCLKGKTLGELVRDRMAAFPASGEINSKLAQPVEAINRVEQHF 397

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1104065078  81 EPAAAHIDTTDGISIEYPEWRFNLRTSNTEPVVRLNVESRADTALMNEKTAELLNLLKE 139
Cdd:PRK15414  398 SREALAVDRTDGISMTFADWRFNLRSSNTEPVVRLNVESRGDVPLMEARTRTLLTLLNE 456
PMM_PGM cd03089
The phosphomannomutase/phosphoglucomutase (PMM/PGM) bifunctional enzyme catalyzes the ...
 1-137 3.37e-46

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: 154.98  E-value: 3.37e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104065078   1 MRQEDAIYGGEMSAHHYFRD-FAYCDSGMIPWLLVAELLCLKNSSLKSLVADRQAaFPASGEINRKL--GNAVEAIARIR 77
Cdd:cd03089   306 MKETGALLAGEMSGHIFFKDrWYGFDDGIYAALRLLELLSKSGKTLSELLADLPK-YFSTPEIRIPVteEDKFAVIERLK 384

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104065078  78 AQYEPAAAHIDTTDGISIEYPEWRFNLRTSNTEPVVRLNVESRADtALMNEKTAELLNLL 137
Cdd:cd03089   385 EHFEFPGAEIIDIDGVRVDFEDGWGLVRASNTEPVLVLRFEADTE-EGLEEIKAELRKLL 443
ManB COG1109
Phosphomannomutase [Carbohydrate transport and metabolism];
1-140 1.60e-35

Phosphomannomutase [Carbohydrate transport and metabolism];


Pssm-ID: 440726 [Multi-domain]  Cd Length: 456  Bit Score: 127.24  E-value: 1.60e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104065078   1 MRQEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVAELLCLKNSSLKSLVADRQAAFpaSGEINRKLGNAV---EAIARIR 77
Cdd:COG1109   316 MRETGAVLGGEESGGIIFPDFVPTDDGILAALLLLELLAKQGKSLSELLAELPRYP--QPEINVRVPDEEkigAVMEKLR 393

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1104065078  78 AQYEpAAAHIDTTDGISIEYPEW-RFNLRTSNTEPVVRLNVESRaDTALMNEKTAELLNLLKEE 140
Cdd:COG1109   394 EAVE-DKEELDTIDGVKVDLEDGgWVLVRPSGTEPLLRVYAEAK-DEEEAEELLAELAELVEEA 455
manB PRK09542
phosphomannomutase/phosphoglucomutase; Reviewed
 1-134 3.09e-33

phosphomannomutase/phosphoglucomutase; Reviewed


Pssm-ID: 236557  Cd Length: 445  Bit Score: 120.86  E-value: 3.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104065078   1 MRQEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVAELLCLKNSSLKSLVADRQaAFPASGEINRKLGNAVEAIARIRAQY 80
Cdd:PRK09542  307 MAETGAIFGGEHSAHYYFRDFWGADSGMLAALHVLAALGEQDRPLSELMADYQ-RYAASGEINSTVADAPARMEAVLKAF 385

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1104065078  81 EPAAAHIDTTDGISIEYPE--WrFNLRTSNTEPVVRLNVESRaDTALMNEKTAELL 134
Cdd:PRK09542  386 ADRIVSVDHLDGVTVDLGDgsW-FNLRASNTEPLLRLNVEAR-TEEEVDALVDEVL 439
PGM_PMM_III pfam02880
Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain III;
1-56 2.06e-17

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


Pssm-ID: 460733  Cd Length: 115  Bit Score: 72.48  E-value: 2.06e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1104065078   1 MRQEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVAELLCLKNSSLKSLVADRQAAF 56
Cdd:pfam02880  60 MREEGALFGGEESGHIIFLDHATTKDGILAALLVLEILARTGKSLSELLEELPEKY 115
PGM_like1 cd03087
This archaeal PGM-like (phosphoglucomutase-like) protein of unknown function belongs to the ...
 1-120 1.46e-14

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: 69.14  E-value: 1.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104065078   1 MRQEDAIYGGEMSAHHYFRDFAYCDSGMIPWLLVAELLClKNSSLKSLVADRQAAFPASGEINRKLGNAVEAIARIRAQY 80
Cdd:cd03087   305 MIENGAVFGGEPNGGWIFPDHQLCRDGIMTAALLLELLA-EEKPLSELLDELPKYPLLREKVECPDEKKEEVMEAVEEEL 383

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1104065078  81 EPAAAHIDTTDGISIEYPEWRFNLRTSNTEPVVRLNVESR 120
Cdd:cd03087   384 SDADEDVDTIDGVRIEYEDGWVLIRPSGTEPKIRITAEAK 423
PGM_like4 cd05803
This PGM-like (phosphoglucomutase-like) domain is located C-terminal to a mannose-1-phosphate ...
 1-124 9.40e-13

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: 63.87  E-value: 9.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104065078   1 MRQEDAIYGGE------MSAHHYFRDfAYcdSGMIpwlLVAELLCLKNSSLKSLVADrqaaFPASGEINRKLGNAVEAIA 74
Cdd:cd05803   315 MKEVDAVIGGEgnggviLPDVHYGRD-SL--VGIA---LVLQLLAASGKPLSEIVDE----LPQYYISKTKVTIAGEALE 384

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1104065078  75 RIRAQYEPAA--AHIDTTDGISIEYPEWRFNLRTSNTEPVVRLNVESRA-DTA 124
Cdd:cd05803   385 RLLKKLEAYFkdAEASTLDGLRLDSEDSWVHVRPSNTEPIVRIIAEAPTqDEA 437
PGM_PMM_IV pfam00408
Phosphoglucomutase/phosphomannomutase, C-terminal domain;
61-138 2.26e-08

Phosphoglucomutase/phosphomannomutase, C-terminal domain;


Pssm-ID: 425666  Cd Length: 71  Bit Score: 48.03  E-value: 2.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1104065078  61 EINRKLGN--AVEAIARIRAQyEPAAAHIDTTDGisieypeWRFNLRTSNTEPVVRLNVESRaDTALMNEKTAELLNLLK 138
Cdd:pfam00408   1 LINVRVAEkkKLAALAAILKV-FADAEKILGEDG-------RRLDVRPSGTEPVLRVMVEGD-SDEELARLADEIADLLE 71
 
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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