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Conserved domains on  [gi|568960661|ref|XP_006510834|]
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mannose-6-phosphate isomerase isoform X1 [Mus musculus]

Protein Classification

class I mannose-6-phosphate isomerase( domain architecture ID 14401463)

mannose-6-phosphate isomerase, class I, catalyzes the reversible isomerization of fructose-6-phosphate (F6P) and mannose-6-phosphate (M6P), the first committed step in the synthesis of mannosylated glycoproteins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cupin_PMI_type_I_N cd07011
type I phosphomannose isomerase in eukaryotes and bacteria, N-terminal cupin domain; This ...
 2-125 1.49e-59

type I phosphomannose isomerase in eukaryotes and bacteria, N-terminal cupin domain; This subfamily contains type I phosphomannose isomerase (PMI; E.C. 5.3.1.8; also known as mannose-6-phosphate isomerase) found in eukaryotes and some bacteria such as Salmonella enterica. PMI catalyzes the reversible isomerization of fructose-6-phosphate (F6P) and mannose-6-phosphate (M6P), the first committed step in the synthesis of mannosylated glycoproteins. The active site, located within the N-terminal jelly roll-like beta-barrel cupin fold, contains a single essential zinc atom and forms a deep, open cavity large enough to contain M6P or F6P. PMI type I also has a C-terminal beta-barrel fold which has diverged considerably from the N-terminal domain and is not included here. This subfamily contains an alpha helical domain that is found in eukaryotic and some prokaryotic PMIs but is not present in their archaeal counterparts. F6P is a substrate for glycolysis and gluconeogenesis, while M6P is a substrate for production of activated mannose donor guanosine 5'-diphosphate D-mannose, an important precursor of mannosylated biomolecules such as glycoproteins, bacterial exopolysaccharides and fungal cell wall components. PMI is also essential for survival, virulence and possibly pathogenicity of some bacteria and protozoan parasites, as well as for cell wall integrity of certain yeasts. Thus, PMI is a potential target against fungal infections causing serious illness or death.


:

Pssm-ID: 380414 [Multi-domain]  Cd Length: 247  Bit Score: 187.76  E-value: 1.49e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960661   2 ASALRNCFSHLMKSEKkvVVEQLNLLVKRISQQVFDGnnMEDIYGKLLLQLHQQHPGDIGCFAIYFLNLLTLKPGEAMFL 81
Cdd:cd07011  128 KEGLKALFSALLTLDS--DEEALAALVARLRARPKSE--ELDEAEELVLRLAEQYPGDPGVFAALLLNLVTLKPGEAIFL 203

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 568960661  82 DANVPHAYLKGDCVECMACSDNTVRAGLTPKFIDVPTLCEMLNY 125
Cdd:cd07011  204 PAGEPHAYLSGDGVECMANSDNVVRAGLTPKHVDVDELLRMLDY 247
cupin_RmlC-like super family cl40423
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 68-214 2.51e-28

RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP (deoxythymidine diphosphates)-4-dehydrorhamnose 3,5-epimerase)-like cupins. RmlC is a dTDP-sugar isomerase involved in the synthesis of L-rhamnose, a saccharide required for the virulence of some pathogenic bacteria. Cupins are a functionally diverse superfamily originally discovered based on the highly conserved motif found in germin and germin-like proteins. This conserved motif forms a beta-barrel fold found in all of the cupins, giving rise to the name cupin ('cupa' is the Latin term for small barrel). The active site of members of this superfamily is generally located at the center of a conserved barrel and usually includes a metal ion. The different functional classes in this superfamily include single domain bacterial isomerases and epimerases involved in the modification of cell wall carbohydrates, two domain bicupins such as the desiccation-tolerant seed storage globulins, and multidomain nuclear transcription factors involved in legume root nodulation.


The actual alignment was detected with superfamily member TIGR00218:

Pssm-ID: 477354 [Multi-domain]  Cd Length: 302  Bit Score: 108.68  E-value: 2.51e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960661   68 LNLLTLKPGEAMFLDANVPHAYLKGDCVECMACSDNTVRAGLTPKFIDVPTLCEMLNYTPSPSNnrlFAPAQSQDDPYLS 147
Cdd:TIGR00218 150 LNRIKLKPGDFFYVPSGTPHAYKGGLVLEVMQNSDNVYRAGDTDKYLDIEKLVEVLTFPHVPEF---HLKGQPQKNGAEI 226

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568960661  148 IYDPPVPDFTVMKMEVPSSVTeykVSTLDSASILLMVQGtvTAIIPSAHAEIPLYRGGVLFIAANES 214
Cdd:TIGR00218 227 VFMVPTEYFSVYKWDISGKAE---FIQQQSALILSVLEG--SGRIKSGGKTLPLKKGESFFIPAHLG 288
 
Name Accession Description Interval E-value
cupin_PMI_type_I_N cd07011
type I phosphomannose isomerase in eukaryotes and bacteria, N-terminal cupin domain; This ...
 2-125 1.49e-59

type I phosphomannose isomerase in eukaryotes and bacteria, N-terminal cupin domain; This subfamily contains type I phosphomannose isomerase (PMI; E.C. 5.3.1.8; also known as mannose-6-phosphate isomerase) found in eukaryotes and some bacteria such as Salmonella enterica. PMI catalyzes the reversible isomerization of fructose-6-phosphate (F6P) and mannose-6-phosphate (M6P), the first committed step in the synthesis of mannosylated glycoproteins. The active site, located within the N-terminal jelly roll-like beta-barrel cupin fold, contains a single essential zinc atom and forms a deep, open cavity large enough to contain M6P or F6P. PMI type I also has a C-terminal beta-barrel fold which has diverged considerably from the N-terminal domain and is not included here. This subfamily contains an alpha helical domain that is found in eukaryotic and some prokaryotic PMIs but is not present in their archaeal counterparts. F6P is a substrate for glycolysis and gluconeogenesis, while M6P is a substrate for production of activated mannose donor guanosine 5'-diphosphate D-mannose, an important precursor of mannosylated biomolecules such as glycoproteins, bacterial exopolysaccharides and fungal cell wall components. PMI is also essential for survival, virulence and possibly pathogenicity of some bacteria and protozoan parasites, as well as for cell wall integrity of certain yeasts. Thus, PMI is a potential target against fungal infections causing serious illness or death.


Pssm-ID: 380414 [Multi-domain]  Cd Length: 247  Bit Score: 187.76  E-value: 1.49e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960661   2 ASALRNCFSHLMKSEKkvVVEQLNLLVKRISQQVFDGnnMEDIYGKLLLQLHQQHPGDIGCFAIYFLNLLTLKPGEAMFL 81
Cdd:cd07011  128 KEGLKALFSALLTLDS--DEEALAALVARLRARPKSE--ELDEAEELVLRLAEQYPGDPGVFAALLLNLVTLKPGEAIFL 203

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 568960661  82 DANVPHAYLKGDCVECMACSDNTVRAGLTPKFIDVPTLCEMLNY 125
Cdd:cd07011  204 PAGEPHAYLSGDGVECMANSDNVVRAGLTPKHVDVDELLRMLDY 247
PLN02288 PLN02288
mannose-6-phosphate isomerase
 3-215 8.04e-57

mannose-6-phosphate isomerase


Pssm-ID: 215162 [Multi-domain]  Cd Length: 394  Bit Score: 185.26  E-value: 8.04e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960661   3 SALRNCFSHLMKSEKKVVVEQLNLLVKR--ISQQVFDGNNMEDiygkLLLQLHQQHPGDIGCFAIYFLNLLTLKPGEAMF 80
Cdd:PLN02288 187 SVLRSAFTALMTASKDVVTEAVSKLKARlhAESQARELTDKEE----LVLRLEKQYPGDVGVLSAFFLNYVKLNPGEALY 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960661  81 LDANVPHAYLKGDCVECMACSDNTVRAGLTPKFIDVPTLCEMLNYtpspsnnRLFAPAQSQD---DPYLSIYDPPVPDFT 157
Cdd:PLN02288 263 LGANEPHAYLSGECIECMATSDNVVRAGLTPKFRDVQTLCSMLTY-------KQGFPEILTGvpvDPYTTRYLPPFDEFE 335

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568960661 158 VMKMEVPSSvTEYKVSTLDSASILLMVQGTVTAIIPSAHAEIPLYRGGVLFIAANESV 215
Cdd:PLN02288 336 VDHCDVPPG-ASVVFPAVPGPSVFLVIEGEGVLSTGSSEDGTAAKRGDVFFVPAGTEI 392
manA TIGR00218
mannose-6-phosphate isomerase, class I; The names phosphomannose isomerase and ...
 68-214 2.51e-28

mannose-6-phosphate isomerase, class I; The names phosphomannose isomerase and mannose-6-phosphate isomerase are synonomous. This family contains two rather deeply branched groups. One group contains an experimentally determined phosphomannose isomerase of Streptococcus mutans as well as three uncharacterized paralogous proteins of Bacillus subtilis, all at more than 50 % identity to each other, plus a more distant homolog from Archaeoglobus fulgidus. The other group contains members from E. coli, budding yeast, Borrelia burgdorferi, etc. [Energy metabolism, Sugars]


Pssm-ID: 272966 [Multi-domain]  Cd Length: 302  Bit Score: 108.68  E-value: 2.51e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960661   68 LNLLTLKPGEAMFLDANVPHAYLKGDCVECMACSDNTVRAGLTPKFIDVPTLCEMLNYTPSPSNnrlFAPAQSQDDPYLS 147
Cdd:TIGR00218 150 LNRIKLKPGDFFYVPSGTPHAYKGGLVLEVMQNSDNVYRAGDTDKYLDIEKLVEVLTFPHVPEF---HLKGQPQKNGAEI 226

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568960661  148 IYDPPVPDFTVMKMEVPSSVTeykVSTLDSASILLMVQGtvTAIIPSAHAEIPLYRGGVLFIAANES 214
Cdd:TIGR00218 227 VFMVPTEYFSVYKWDISGKAE---FIQQQSALILSVLEG--SGRIKSGGKTLPLKKGESFFIPAHLG 288
PMI_typeI_hel pfam20512
Phosphomannose isomerase type I, helical insertion domain; This entry represents the ...
 2-68 2.17e-22

Phosphomannose isomerase type I, helical insertion domain; This entry represents the alpha-helical insertion domain of Phosphomannose isomerase type I enzymes (EC 5.3.1.8), in which the helices are packed closely, connected by short turns and loops. This domain packs closely against the catalytic domain, interrupting it.


Pssm-ID: 466661 [Multi-domain]  Cd Length: 88  Bit Score: 87.52  E-value: 2.17e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568960661    2 ASALRNCFSHLMKSEKKVVVEQLNLLVKRISQQVfDGNNMEDIYGKLLLQLHQQHPGDIGCFAIYFL 68
Cdd:pfam20512  23 QKLLQKLFSSLMNSQKEKIKIQLAKLVERIQSQP-SEFNKTDALPELIQRLNEQYPGDIGLFAPLFL 88
PMI_typeI_C pfam01238
Phosphomannose isomerase type I C-terminal; This is the C-terminal domain of Phosphomannose ...
 148-192 6.95e-09

Phosphomannose isomerase type I C-terminal; This is the C-terminal domain of Phosphomannose isomerase type I enzymes (EC 5.3.1.8), which contains antiparallel beta-strands in an extended jelly roll topology with short loops connecting the strands.


Pssm-ID: 460127 [Multi-domain]  Cd Length: 48  Bit Score: 50.45  E-value: 6.95e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568960661  148 IYDPPVPDFTVMkmEVPSSVTEYKVSTLDSASILLMVQGTVTAII 192
Cdd:pfam01238   3 LYDPPIDEFAVL--QTKLPKGDHTILPLTSPSILICTEGTGTIIA 45
 
Name Accession Description Interval E-value
cupin_PMI_type_I_N cd07011
type I phosphomannose isomerase in eukaryotes and bacteria, N-terminal cupin domain; This ...
 2-125 1.49e-59

type I phosphomannose isomerase in eukaryotes and bacteria, N-terminal cupin domain; This subfamily contains type I phosphomannose isomerase (PMI; E.C. 5.3.1.8; also known as mannose-6-phosphate isomerase) found in eukaryotes and some bacteria such as Salmonella enterica. PMI catalyzes the reversible isomerization of fructose-6-phosphate (F6P) and mannose-6-phosphate (M6P), the first committed step in the synthesis of mannosylated glycoproteins. The active site, located within the N-terminal jelly roll-like beta-barrel cupin fold, contains a single essential zinc atom and forms a deep, open cavity large enough to contain M6P or F6P. PMI type I also has a C-terminal beta-barrel fold which has diverged considerably from the N-terminal domain and is not included here. This subfamily contains an alpha helical domain that is found in eukaryotic and some prokaryotic PMIs but is not present in their archaeal counterparts. F6P is a substrate for glycolysis and gluconeogenesis, while M6P is a substrate for production of activated mannose donor guanosine 5'-diphosphate D-mannose, an important precursor of mannosylated biomolecules such as glycoproteins, bacterial exopolysaccharides and fungal cell wall components. PMI is also essential for survival, virulence and possibly pathogenicity of some bacteria and protozoan parasites, as well as for cell wall integrity of certain yeasts. Thus, PMI is a potential target against fungal infections causing serious illness or death.


Pssm-ID: 380414 [Multi-domain]  Cd Length: 247  Bit Score: 187.76  E-value: 1.49e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960661   2 ASALRNCFSHLMKSEKkvVVEQLNLLVKRISQQVFDGnnMEDIYGKLLLQLHQQHPGDIGCFAIYFLNLLTLKPGEAMFL 81
Cdd:cd07011  128 KEGLKALFSALLTLDS--DEEALAALVARLRARPKSE--ELDEAEELVLRLAEQYPGDPGVFAALLLNLVTLKPGEAIFL 203

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 568960661  82 DANVPHAYLKGDCVECMACSDNTVRAGLTPKFIDVPTLCEMLNY 125
Cdd:cd07011  204 PAGEPHAYLSGDGVECMANSDNVVRAGLTPKHVDVDELLRMLDY 247
PLN02288 PLN02288
mannose-6-phosphate isomerase
 3-215 8.04e-57

mannose-6-phosphate isomerase


Pssm-ID: 215162 [Multi-domain]  Cd Length: 394  Bit Score: 185.26  E-value: 8.04e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960661   3 SALRNCFSHLMKSEKKVVVEQLNLLVKR--ISQQVFDGNNMEDiygkLLLQLHQQHPGDIGCFAIYFLNLLTLKPGEAMF 80
Cdd:PLN02288 187 SVLRSAFTALMTASKDVVTEAVSKLKARlhAESQARELTDKEE----LVLRLEKQYPGDVGVLSAFFLNYVKLNPGEALY 262

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960661  81 LDANVPHAYLKGDCVECMACSDNTVRAGLTPKFIDVPTLCEMLNYtpspsnnRLFAPAQSQD---DPYLSIYDPPVPDFT 157
Cdd:PLN02288 263 LGANEPHAYLSGECIECMATSDNVVRAGLTPKFRDVQTLCSMLTY-------KQGFPEILTGvpvDPYTTRYLPPFDEFE 335

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 568960661 158 VMKMEVPSSvTEYKVSTLDSASILLMVQGTVTAIIPSAHAEIPLYRGGVLFIAANESV 215
Cdd:PLN02288 336 VDHCDVPPG-ASVVFPAVPGPSVFLVIEGEGVLSTGSSEDGTAAKRGDVFFVPAGTEI 392
PRK15131 PRK15131
mannose-6-phosphate isomerase; Provisional
 56-214 2.86e-36

mannose-6-phosphate isomerase; Provisional


Pssm-ID: 185085 [Multi-domain]  Cd Length: 389  Bit Score: 131.63  E-value: 2.86e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960661  56 HPGDIGCFAIYFLNLLTLKPGEAMFLDANVPHAYLKGDCVECMACSDNTVRAGLTPKFIDVPTLCEMLNYTPSPSNNRLF 135
Cdd:PRK15131 224 YPDDSGLFSPLLLNVVKLNPGEAMFLFAETPHAYLQGVALEVMANSDNVLRAGLTPKYIDIPELVANVKFEAKPANQLLT 303

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960661 136 APAQSQDDPYLSIydpPVPD--FTVMKM-EVPSSVTEykvstlDSASILLMVQGtvTAIIPSAHAEIPLYRGGVLFIAAN 212
Cdd:PRK15131 304 QPVKQGAELDFPI---PVDDfaFSLHDLsDQPTTLSQ------QSAAILFCVEG--EAVLWKGEQQLTLKPGESAFIAAN 372


                 ..
gi 568960661 213 ES 214
Cdd:PRK15131 373 ES 374
manA TIGR00218
mannose-6-phosphate isomerase, class I; The names phosphomannose isomerase and ...
 68-214 2.51e-28

mannose-6-phosphate isomerase, class I; The names phosphomannose isomerase and mannose-6-phosphate isomerase are synonomous. This family contains two rather deeply branched groups. One group contains an experimentally determined phosphomannose isomerase of Streptococcus mutans as well as three uncharacterized paralogous proteins of Bacillus subtilis, all at more than 50 % identity to each other, plus a more distant homolog from Archaeoglobus fulgidus. The other group contains members from E. coli, budding yeast, Borrelia burgdorferi, etc. [Energy metabolism, Sugars]


Pssm-ID: 272966 [Multi-domain]  Cd Length: 302  Bit Score: 108.68  E-value: 2.51e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568960661   68 LNLLTLKPGEAMFLDANVPHAYLKGDCVECMACSDNTVRAGLTPKFIDVPTLCEMLNYTPSPSNnrlFAPAQSQDDPYLS 147
Cdd:TIGR00218 150 LNRIKLKPGDFFYVPSGTPHAYKGGLVLEVMQNSDNVYRAGDTDKYLDIEKLVEVLTFPHVPEF---HLKGQPQKNGAEI 226

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568960661  148 IYDPPVPDFTVMKMEVPSSVTeykVSTLDSASILLMVQGtvTAIIPSAHAEIPLYRGGVLFIAANES 214
Cdd:TIGR00218 227 VFMVPTEYFSVYKWDISGKAE---FIQQQSALILSVLEG--SGRIKSGGKTLPLKKGESFFIPAHLG 288
PMI_typeI_hel pfam20512
Phosphomannose isomerase type I, helical insertion domain; This entry represents the ...
 2-68 2.17e-22

Phosphomannose isomerase type I, helical insertion domain; This entry represents the alpha-helical insertion domain of Phosphomannose isomerase type I enzymes (EC 5.3.1.8), in which the helices are packed closely, connected by short turns and loops. This domain packs closely against the catalytic domain, interrupting it.


Pssm-ID: 466661 [Multi-domain]  Cd Length: 88  Bit Score: 87.52  E-value: 2.17e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568960661    2 ASALRNCFSHLMKSEKKVVVEQLNLLVKRISQQVfDGNNMEDIYGKLLLQLHQQHPGDIGCFAIYFL 68
Cdd:pfam20512  23 QKLLQKLFSSLMNSQKEKIKIQLAKLVERIQSQP-SEFNKTDALPELIQRLNEQYPGDIGLFAPLFL 88
PMI_typeI_C pfam01238
Phosphomannose isomerase type I C-terminal; This is the C-terminal domain of Phosphomannose ...
 148-192 6.95e-09

Phosphomannose isomerase type I C-terminal; This is the C-terminal domain of Phosphomannose isomerase type I enzymes (EC 5.3.1.8), which contains antiparallel beta-strands in an extended jelly roll topology with short loops connecting the strands.


Pssm-ID: 460127 [Multi-domain]  Cd Length: 48  Bit Score: 50.45  E-value: 6.95e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 568960661  148 IYDPPVPDFTVMkmEVPSSVTEYKVSTLDSASILLMVQGTVTAII 192
Cdd:pfam01238   3 LYDPPIDEFAVL--QTKLPKGDHTILPLTSPSILICTEGTGTIIA 45
 
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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