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Conserved domains on  [gi|1731094880|ref|WP_148359924|]
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type I phosphomannose isomerase catalytic subunit [Bacteroides clarus]

Protein Classification

class I mannose-6-phosphate isomerase( domain architecture ID 11445218)

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

CATH:  2.60.120.10
EC:  5.3.1.8
Gene Ontology:  GO:0004476|GO:0009298|GO:0008270
PubMed:  19478949|14697267|9507048
SCOP:  3001825

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ManA COG1482
Mannose-6-phosphate isomerase, class I [Carbohydrate transport and metabolism];
1-324 8.10e-152

Mannose-6-phosphate isomerase, class I [Carbohydrate transport and metabolism];


:

Pssm-ID: 441091 [Multi-domain]  Cd Length: 324  Bit Score: 428.82  E-value: 8.10e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731094880   1 MYPLKFEPILKQTLWGGDKIIPFKHLDETLPNVGESWEVSAVEGSESVVANGADKGYTLPEMVRKYKDELVGEANYARFG 80
Cdd:COG1482     2 MYPLRFKPIFKEKIWGGRRLKEVFGKDLPEGKIGESWEISAHPNGVSVVANGPLAGKTLDELVEEHPEELLGEKVYARFG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731094880  81 SKFPLLIKFIDAKLDLSIQVHPGDELAKKRH-NSFGKNEMWYVIAADKGAKLISGFSEEITPKEYKDRVHNGTFAEVLQT 159
Cdd:COG1482    82 DEFPLLIKFLDAKDDLSVQVHPDDEYAKEHEgGSYGKTEMWYILDAEPGAEIYLGFKEGVTKEEFREALENGDIEDLLNR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731094880 160 CTIEPGDVFYVPAGRVHGIGAGAFVAEIQQTSDITYRIFDYNRKDKDGKSRDLHTSQAMDAINFS--DVQDDFRTEYERI 237
Cdd:COG1482   162 VPVKKGDFFLIPAGTVHAIGAGILVLEIQQTSDITYRVYDYDRLDLDGKPRELHIEKALDVIDFErkPDEVVQPTVVEEE 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731094880 238 QNEPVEMVASPYFTTSVYDMTEEITCDysELDSFVIFICVEGSCRLTDDNqNEITLRAGETVLLPATVQEVTIVpegGRV 317
Cdd:COG1482   242 GNREERLVECPYFTVERLELDGEVTLD--TEDSFHILSVVEGEGTIESDG-EPYELKKGETFLLPAAVGEYTIR---GEA 315


                  ....*..
gi 1731094880 318 KLLETYV 324
Cdd:COG1482   316 KLLKSYV 322
 
Name Accession Description Interval E-value
ManA COG1482
Mannose-6-phosphate isomerase, class I [Carbohydrate transport and metabolism];
1-324 8.10e-152

Mannose-6-phosphate isomerase, class I [Carbohydrate transport and metabolism];


Pssm-ID: 441091 [Multi-domain]  Cd Length: 324  Bit Score: 428.82  E-value: 8.10e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731094880   1 MYPLKFEPILKQTLWGGDKIIPFKHLDETLPNVGESWEVSAVEGSESVVANGADKGYTLPEMVRKYKDELVGEANYARFG 80
Cdd:COG1482     2 MYPLRFKPIFKEKIWGGRRLKEVFGKDLPEGKIGESWEISAHPNGVSVVANGPLAGKTLDELVEEHPEELLGEKVYARFG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731094880  81 SKFPLLIKFIDAKLDLSIQVHPGDELAKKRH-NSFGKNEMWYVIAADKGAKLISGFSEEITPKEYKDRVHNGTFAEVLQT 159
Cdd:COG1482    82 DEFPLLIKFLDAKDDLSVQVHPDDEYAKEHEgGSYGKTEMWYILDAEPGAEIYLGFKEGVTKEEFREALENGDIEDLLNR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731094880 160 CTIEPGDVFYVPAGRVHGIGAGAFVAEIQQTSDITYRIFDYNRKDKDGKSRDLHTSQAMDAINFS--DVQDDFRTEYERI 237
Cdd:COG1482   162 VPVKKGDFFLIPAGTVHAIGAGILVLEIQQTSDITYRVYDYDRLDLDGKPRELHIEKALDVIDFErkPDEVVQPTVVEEE 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731094880 238 QNEPVEMVASPYFTTSVYDMTEEITCDysELDSFVIFICVEGSCRLTDDNqNEITLRAGETVLLPATVQEVTIVpegGRV 317
Cdd:COG1482   242 GNREERLVECPYFTVERLELDGEVTLD--TEDSFHILSVVEGEGTIESDG-EPYELKKGETFLLPAAVGEYTIR---GEA 315


                  ....*..
gi 1731094880 318 KLLETYV 324
Cdd:COG1482   316 KLLKSYV 322
cupin_PMI_type_I_N_bac cd07010
Phosphomannose isomerase in bacteria and archaea, N-terminal cupin domain; This subfamily ...
 8-222 1.12e-79

Phosphomannose isomerase in bacteria and archaea, 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 many bacteria (e.g. Bacillus subtilis) and archaea. 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 does not contain an alpha helical domain that exists in eukaryotic and some prokaryotic PMIs. 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: 380413  Cd Length: 173  Bit Score: 239.74  E-value: 1.12e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731094880   8 PILKQTLWGGDKIIPFKHLDETLPNVGESWEVSavegsesvvangadkgytlpemvrkykdelvgeanyarfgskfPLLI 87
Cdd:cd07010     1 PILKERVWGGRRLKELFGKPPPDEPIGESWEVS-------------------------------------------PLLV 37

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731094880  88 KFIDAKLDLSIQVHPGDELAKKRHNS-FGKNEMWYVIAADKGAKLISGFSEEITPKEYKDRVHNGTFAEVLQTCTIEPGD 166
Cdd:cd07010    38 KLLDAAERLSVQVHPDDEYARKHENEpFGKTEAWYILDAEPGAKIYLGFKEGVTREEFEKAIDDGDIEELLNKVPVKPGD 117

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1731094880 167 VFYVPAGRVHGIGAGAFVAEIQQTSDITYRIFDYNRKDKDGKSRDLHTSQAMDAIN 222
Cdd:cd07010   118 FFYIPAGTVHAIGAGILVLEIQQNSDITYRLYDWGRLDLDGKPRELHLEKALDVID 173
manA TIGR00218
mannose-6-phosphate isomerase, class I; The names phosphomannose isomerase and ...
 3-317 2.94e-57

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: 187.26  E-value: 2.94e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731094880   3 PLKFEPILKQTLWGGDKIIPFKHLDETLPNVGESWEVSAVEGSESVVANGADKGYTLPEMVRKYKdELVGEANyarfGSK 82
Cdd:TIGR00218   1 PLFIFPVFKERDWGGTALADLFGYSIPSQQTGECWAGSAHPKGPSTVLNGPYKGVSLIDLWEKHR-ELLGRAD----GDR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731094880  83 FPLLIKFIDAKLDLSIQVHPGDELAKKRHNS-FGKNEMWYVIAADKGAKLISGFSeEITPKEYKDRVHNGTFAEVLQTCT 161
Cdd:TIGR00218  76 FPFLFKVLDAAKPLSIQVHPDDKYAEIHEEGeLGKTECWYIIDCDEAAEIIKGHL-KNSKEELWTMIEDGLFKLLLNRIK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731094880 162 IEPGDVFYVPAGRVHGiGAGAFVAEIQQTSDITYRIFDYNrkdkdgksRDLHTSQAMDAINFSDVQDDFRTEYERIQN-E 240
Cdd:TIGR00218 155 LKPGDFFYVPSGTPHA-YKGGLVLEVMQNSDNVYRAGDTD--------KYLDIEKLVEVLTFPHVPEFHLKGQPQKNGaE 225

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1731094880 241 PVEMVASPYFTTSVYDMTEEITCdySELDSFVIFICVEGSCRLTDDNQnEITLRAGETVLLPATVQEVTIVPEGGRV 317
Cdd:TIGR00218 226 IVFMVPTEYFSVYKWDISGKAEF--IQQQSALILSVLEGSGRIKSGGK-TLPLKKGESFFIPAHLGPFTIEGECEAI 299
PMI_typeI_cat pfam20511
Phosphomannose isomerase type I, catalytic domain; This entry represents the catalytic domain ...
 4-117 3.04e-11

Phosphomannose isomerase type I, catalytic domain; This entry represents the catalytic domain of Phosphomannose isomerase type I enzymes (EC 5.3.1.8) which contains a zinc-binding site. It is composed of beta-strands connected by long loops in a jelly roll conformation.


Pssm-ID: 466660 [Multi-domain]  Cd Length: 143  Bit Score: 60.27  E-value: 3.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731094880   4 LKFEPILKQTLWG--GDKIIPFKHLDETLPNV------GESWEVSAVEGSeSVVANGADKGYTLPEMVrkykdELVGEAN 75
Cdd:pfam20511   2 FRLQCGVQNYAWGkiGSNSALAKLFAYSIPSIdedkpyAELWMGTHPKGP-SKVLNGQLRDVTLDELS-----AELGELF 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1731094880  76 YARFGSKFPLLIKFIDAKLDLSIQVHPGDELAKKRHNSFGKN 117
Cdd:pfam20511  76 GKRFGGNLPFLFKVLSVEKPLSIQVHPDKELGEILHAADPKN 117
PLN02288 PLN02288
mannose-6-phosphate isomerase
 47-113 1.69e-04

mannose-6-phosphate isomerase


Pssm-ID: 215162 [Multi-domain]  Cd Length: 394  Bit Score: 43.12  E-value: 1.69e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1731094880  47 SVVANGADKGYTLPEMVRKYKdELVGEANYARFGSKFPLLIKFIDAKLDLSIQVHPGDELAKKRHNS 113
Cdd:PLN02288   53 SFVVATGKGSVLLKEWIAENP-AALGDRVVERWGGDLPFLFKVLSVAKALSIQAHPDKKLAEKLHAE 118
 
Name Accession Description Interval E-value
ManA COG1482
Mannose-6-phosphate isomerase, class I [Carbohydrate transport and metabolism];
1-324 8.10e-152

Mannose-6-phosphate isomerase, class I [Carbohydrate transport and metabolism];


Pssm-ID: 441091 [Multi-domain]  Cd Length: 324  Bit Score: 428.82  E-value: 8.10e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731094880   1 MYPLKFEPILKQTLWGGDKIIPFKHLDETLPNVGESWEVSAVEGSESVVANGADKGYTLPEMVRKYKDELVGEANYARFG 80
Cdd:COG1482     2 MYPLRFKPIFKEKIWGGRRLKEVFGKDLPEGKIGESWEISAHPNGVSVVANGPLAGKTLDELVEEHPEELLGEKVYARFG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731094880  81 SKFPLLIKFIDAKLDLSIQVHPGDELAKKRH-NSFGKNEMWYVIAADKGAKLISGFSEEITPKEYKDRVHNGTFAEVLQT 159
Cdd:COG1482    82 DEFPLLIKFLDAKDDLSVQVHPDDEYAKEHEgGSYGKTEMWYILDAEPGAEIYLGFKEGVTKEEFREALENGDIEDLLNR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731094880 160 CTIEPGDVFYVPAGRVHGIGAGAFVAEIQQTSDITYRIFDYNRKDKDGKSRDLHTSQAMDAINFS--DVQDDFRTEYERI 237
Cdd:COG1482   162 VPVKKGDFFLIPAGTVHAIGAGILVLEIQQTSDITYRVYDYDRLDLDGKPRELHIEKALDVIDFErkPDEVVQPTVVEEE 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731094880 238 QNEPVEMVASPYFTTSVYDMTEEITCDysELDSFVIFICVEGSCRLTDDNqNEITLRAGETVLLPATVQEVTIVpegGRV 317
Cdd:COG1482   242 GNREERLVECPYFTVERLELDGEVTLD--TEDSFHILSVVEGEGTIESDG-EPYELKKGETFLLPAAVGEYTIR---GEA 315


                  ....*..
gi 1731094880 318 KLLETYV 324
Cdd:COG1482   316 KLLKSYV 322
cupin_PMI_type_I_N_bac cd07010
Phosphomannose isomerase in bacteria and archaea, N-terminal cupin domain; This subfamily ...
 8-222 1.12e-79

Phosphomannose isomerase in bacteria and archaea, 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 many bacteria (e.g. Bacillus subtilis) and archaea. 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 does not contain an alpha helical domain that exists in eukaryotic and some prokaryotic PMIs. 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: 380413  Cd Length: 173  Bit Score: 239.74  E-value: 1.12e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731094880   8 PILKQTLWGGDKIIPFKHLDETLPNVGESWEVSavegsesvvangadkgytlpemvrkykdelvgeanyarfgskfPLLI 87
Cdd:cd07010     1 PILKERVWGGRRLKELFGKPPPDEPIGESWEVS-------------------------------------------PLLV 37

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731094880  88 KFIDAKLDLSIQVHPGDELAKKRHNS-FGKNEMWYVIAADKGAKLISGFSEEITPKEYKDRVHNGTFAEVLQTCTIEPGD 166
Cdd:cd07010    38 KLLDAAERLSVQVHPDDEYARKHENEpFGKTEAWYILDAEPGAKIYLGFKEGVTREEFEKAIDDGDIEELLNKVPVKPGD 117

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1731094880 167 VFYVPAGRVHGIGAGAFVAEIQQTSDITYRIFDYNRKDKDGKSRDLHTSQAMDAIN 222
Cdd:cd07010   118 FFYIPAGTVHAIGAGILVLEIQQNSDITYRLYDWGRLDLDGKPRELHLEKALDVID 173
manA TIGR00218
mannose-6-phosphate isomerase, class I; The names phosphomannose isomerase and ...
 3-317 2.94e-57

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: 187.26  E-value: 2.94e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731094880   3 PLKFEPILKQTLWGGDKIIPFKHLDETLPNVGESWEVSAVEGSESVVANGADKGYTLPEMVRKYKdELVGEANyarfGSK 82
Cdd:TIGR00218   1 PLFIFPVFKERDWGGTALADLFGYSIPSQQTGECWAGSAHPKGPSTVLNGPYKGVSLIDLWEKHR-ELLGRAD----GDR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731094880  83 FPLLIKFIDAKLDLSIQVHPGDELAKKRHNS-FGKNEMWYVIAADKGAKLISGFSeEITPKEYKDRVHNGTFAEVLQTCT 161
Cdd:TIGR00218  76 FPFLFKVLDAAKPLSIQVHPDDKYAEIHEEGeLGKTECWYIIDCDEAAEIIKGHL-KNSKEELWTMIEDGLFKLLLNRIK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731094880 162 IEPGDVFYVPAGRVHGiGAGAFVAEIQQTSDITYRIFDYNrkdkdgksRDLHTSQAMDAINFSDVQDDFRTEYERIQN-E 240
Cdd:TIGR00218 155 LKPGDFFYVPSGTPHA-YKGGLVLEVMQNSDNVYRAGDTD--------KYLDIEKLVEVLTFPHVPEFHLKGQPQKNGaE 225

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1731094880 241 PVEMVASPYFTTSVYDMTEEITCdySELDSFVIFICVEGSCRLTDDNQnEITLRAGETVLLPATVQEVTIVPEGGRV 317
Cdd:TIGR00218 226 IVFMVPTEYFSVYKWDISGKAEF--IQQQSALILSVLEGSGRIKSGGK-TLPLKKGESFFIPAHLGPFTIEGECEAI 299
PMI_typeI_cat pfam20511
Phosphomannose isomerase type I, catalytic domain; This entry represents the catalytic domain ...
 4-117 3.04e-11

Phosphomannose isomerase type I, catalytic domain; This entry represents the catalytic domain of Phosphomannose isomerase type I enzymes (EC 5.3.1.8) which contains a zinc-binding site. It is composed of beta-strands connected by long loops in a jelly roll conformation.


Pssm-ID: 466660 [Multi-domain]  Cd Length: 143  Bit Score: 60.27  E-value: 3.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731094880   4 LKFEPILKQTLWG--GDKIIPFKHLDETLPNV------GESWEVSAVEGSeSVVANGADKGYTLPEMVrkykdELVGEAN 75
Cdd:pfam20511   2 FRLQCGVQNYAWGkiGSNSALAKLFAYSIPSIdedkpyAELWMGTHPKGP-SKVLNGQLRDVTLDELS-----AELGELF 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1731094880  76 YARFGSKFPLLIKFIDAKLDLSIQVHPGDELAKKRHNSFGKN 117
Cdd:pfam20511  76 GKRFGGNLPFLFKVLSVEKPLSIQVHPDKELGEILHAADPKN 117
ABD cd12213
Alpha-Mannosidase Binding Domain of Atg19/34; These proteins are related to the ...
 180-297 7.45e-09

Alpha-Mannosidase Binding Domain of Atg19/34; These proteins are related to the Alpha-mannosidase (Ams1) Binding Domain of Atg19/Atg34, a key component in the targeting pathway that directs alpha-mannosidase and aminopeptidase I to the vacuole, either through cytoplasm-to-vacuole trafficking or via autophagy in starvation conditions. Autophagy in a eukaryotic mechanism in which cytoplasm is enclosed in double-membraned autophagosomes which fuse with a vacuole for transport into the lumen. In Saccharomyces cerevisiae, alpha-mannosidase is selectively directed to the vacuole via the direct interaction with Atg19 (and paralog Atg34) in the Cvt pathway. Ams1 binding domains (ABD) Atg19/34 have a immunoglobulin fold with eight beta-strands. The ABD is responsible for Ams1 recognition, but its deletion does not affect the fusion of Atg19 with prApe1, and the transport of prApe1 to the vacuole. The Atg19 N-terminal region is a distinct coiled-coil domain.


Pssm-ID: 213406 [Multi-domain]  Cd Length: 112  Bit Score: 52.75  E-value: 7.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1731094880 180 AGAFVAEIQQ-TSDITYRIFDYNRKDKDGKSRDLHTSQAMDAINFsDVQDDFRTEYERIQNEPVEMVASPYFTTSVyDMT 258
Cdd:cd12213     1 AGSLLVEVNQrDNDLTFRLYNRGDSALPGNLKLVFQYQADDTANP-VTVSIYMGPHELQPNGSKKLLNFPYFGSII-LLE 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1731094880 259 EEITCDYSELDSFVIFICVEGScrltdDNQNEITLRAGE 297
Cdd:cd12213    79 GPCKIDLVNQDGEVIYTGKNSS-----SPKSEFSLKPPN 112
PLN02288 PLN02288
mannose-6-phosphate isomerase
 47-113 1.69e-04

mannose-6-phosphate isomerase


Pssm-ID: 215162 [Multi-domain]  Cd Length: 394  Bit Score: 43.12  E-value: 1.69e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1731094880  47 SVVANGADKGYTLPEMVRKYKdELVGEANYARFGSKFPLLIKFIDAKLDLSIQVHPGDELAKKRHNS 113
Cdd:PLN02288   53 SFVVATGKGSVLLKEWIAENP-AALGDRVVERWGGDLPFLFKVLSVAKALSIQAHPDKKLAEKLHAE 118
PRK15131 PRK15131
mannose-6-phosphate isomerase; Provisional
 45-102 5.06e-04

mannose-6-phosphate isomerase; Provisional


Pssm-ID: 185085 [Multi-domain]  Cd Length: 389  Bit Score: 41.50  E-value: 5.06e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1731094880  45 SESVVANGADKGYTLPEMVRKYKDELVGEANYARFGsKFPLLIKFIDAKLDLSIQVHP 102
Cdd:PRK15131   44 SSSRVQDANGDIVSLRDVIESDKSALLGEAVAKRFG-ELPFLFKVLCAAQPLSIQVHP 100
cupin_PMI_type_I_N cd07011
type I phosphomannose isomerase in eukaryotes and bacteria, N-terminal cupin domain; This ...
 79-121 7.67e-04

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: 40.23  E-value: 7.67e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1731094880  79 FGSKFPLLIKFIDAKLDLSIQVHPGDELAKKRHNSF--------GKNEMWY 121
Cdd:cd07011    37 MGTHLPFLFKVLSAAKPLSIQAHPDKEQAEKLFAREpenykdpnHKPEMAI 87
COG3450 COG3450
Predicted enzyme of the cupin superfamily [General function prediction only];
250-303 1.20e-03

Predicted enzyme of the cupin superfamily [General function prediction only];


Pssm-ID: 442673  Cd Length: 108  Bit Score: 38.04  E-value: 1.20e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1731094880 250 FTTSVYDMTE-EITCDYSELDSFVIficVEGSCRLTDDNQNEITLRAGETVLLPA 303
Cdd:COG3450    38 VSAGVWECTPgKFRWDYDEDEFCYI---LEGRVTVTDDDGEPVEFGAGDSFVFPA 89
 
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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