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Conserved domains on  [gi|574584836|ref|NP_001276084|]
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mannose-6-phosphate isomerase isoform 2 [Homo sapiens]

Protein Classification

cupin domain-containing protein( domain architecture ID 1562428)

cupin domain-containing protein, part of a functionally diverse superfamily with the active site generally located at the center of a conserved domain forming a beta-barrel fold

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cupin_RmlC-like super family cl40423
RmlC-like cupin superfamily; This superfamily contains proteins similar to the RmlC (dTDP ...
 9-281 1.74e-111

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 PLN02288:

Pssm-ID: 477354 [Multi-domain]  Cd Length: 394  Bit Score: 327.40  E-value: 1.74e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584836   9 LSCAVQQYAWGKMGSNSEVARLLASSDPlAQIAEDKPYAELWMGTHPRGDAKILDNRISQKTLSQWIAENQDSLGSKVKD 88
Cdd:PLN02288   4 LRCAVQNYDWGRIGSESEVARLAAANSG-SDVDPDKPYAELWMGTHPSGPSFVVATGKGSVLLKEWIAENPAALGDRVVE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584836  89 TFNGNLPFLFKVLSVETPLSIQAHPNKELAEKLHLQAPQHYPDANHKPEMAIALTPFQGLCGFRPVEEIVTFLKKVPEFQ 168
Cdd:PLN02288  83 RWGGDLPFLFKVLSVAKALSIQAHPDKKLAEKLHAEQPNVYKDDNHKPEMALALTEFEALCGFVTIQELKAVLRTVPELR 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584836 169 FLIGDEAATHLKQTMSHDSQA-VASSLQSCFSHLMKSEKKVVVEQLNLLVKRISQQAAAGNNMEDifGELLLQLHQQYPG 247
Cdd:PLN02288 163 ELVGSEAADQLLALPEHDGEEdVKSVLRSAFTALMTASKDVVTEAVSKLKARLHAESQARELTDK--EELVLRLEKQYPG 240

                        250       260       270
                 ....*....|....*....|....*....|....
gi 574584836 248 DIGCFAIYFLNLLTLKPGEAMFLEANVPHAYLKG 281
Cdd:PLN02288 241 DVGVLSAFFLNYVKLNPGEALYLGANEPHAYLSG 274
 
Name Accession Description Interval E-value
PLN02288 PLN02288
mannose-6-phosphate isomerase
 9-281 1.74e-111

mannose-6-phosphate isomerase


Pssm-ID: 215162 [Multi-domain]  Cd Length: 394  Bit Score: 327.40  E-value: 1.74e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584836   9 LSCAVQQYAWGKMGSNSEVARLLASSDPlAQIAEDKPYAELWMGTHPRGDAKILDNRISQKTLSQWIAENQDSLGSKVKD 88
Cdd:PLN02288   4 LRCAVQNYDWGRIGSESEVARLAAANSG-SDVDPDKPYAELWMGTHPSGPSFVVATGKGSVLLKEWIAENPAALGDRVVE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584836  89 TFNGNLPFLFKVLSVETPLSIQAHPNKELAEKLHLQAPQHYPDANHKPEMAIALTPFQGLCGFRPVEEIVTFLKKVPEFQ 168
Cdd:PLN02288  83 RWGGDLPFLFKVLSVAKALSIQAHPDKKLAEKLHAEQPNVYKDDNHKPEMALALTEFEALCGFVTIQELKAVLRTVPELR 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584836 169 FLIGDEAATHLKQTMSHDSQA-VASSLQSCFSHLMKSEKKVVVEQLNLLVKRISQQAAAGNNMEDifGELLLQLHQQYPG 247
Cdd:PLN02288 163 ELVGSEAADQLLALPEHDGEEdVKSVLRSAFTALMTASKDVVTEAVSKLKARLHAESQARELTDK--EELVLRLEKQYPG 240

                        250       260       270
                 ....*....|....*....|....*....|....
gi 574584836 248 DIGCFAIYFLNLLTLKPGEAMFLEANVPHAYLKG 281
Cdd:PLN02288 241 DVGVLSAFFLNYVKLNPGEALYLGANEPHAYLSG 274
cupin_PMI_type_I_N cd07011
type I phosphomannose isomerase in eukaryotes and bacteria, N-terminal cupin domain; This ...
 9-281 4.52e-105

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: 305.63  E-value: 4.52e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584836   9 LSCAVQQYAWGKMGSNSEVARllassdPLAQIAEDKPYAELWMGTHprgdakildnrisqktlsqwiaenqdslgskvkd 88
Cdd:cd07011    1 LKNAVQNYAWGSKGAISLLAR------GGGKIPEGKPYAELWMGTH---------------------------------- 40

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584836  89 tfngnLPFLFKVLSVETPLSIQAHPNKELAEKLHLQAPQHYPDANHKPEMAIALTPFQGLCGFRPVEEIVTFLKKV-PEF 167
Cdd:cd07011   41 -----LPFLFKVLSAAKPLSIQAHPDKEQAEKLFAREPENYKDPNHKPEMAIALTPFEALCGFRPLEEILALLERVpPEL 115

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584836 168 QFLIGDEAATHLKQTmshdsqavassLQSCFSHLMKSEKkvVVEQLNLLVKRISQQAAAGnnMEDIFGELLLQLHQQYPG 247
Cdd:cd07011  116 RELLGQEDAEQSKEG-----------LKALFSALLTLDS--DEEALAALVARLRARPKSE--ELDEAEELVLRLAEQYPG 180

                        250       260       270
                 ....*....|....*....|....*....|....
gi 574584836 248 DIGCFAIYFLNLLTLKPGEAMFLEANVPHAYLKG 281
Cdd:cd07011  181 DPGVFAALLLNLVTLKPGEAIFLPAGEPHAYLSG 214
PMI_typeI_cat pfam20511
Phosphomannose isomerase type I, catalytic domain; This entry represents the catalytic domain ...
 6-154 2.97e-82

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: 244.01  E-value: 2.97e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584836    6 VFPLSCAVQQYAWGKMGSNSEVARLLASSDPLaqIAEDKPYAELWMGTHPRGDAKILDNRISQKTLSQWIAENQDSLGsk 85
Cdd:pfam20511   1 LFRLQCGVQNYAWGKIGSNSALAKLFAYSIPS--IDEDKPYAELWMGTHPKGPSKVLNGQLRDVTLDELSAELGELFG-- 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 574584836   86 vkDTFNGNLPFLFKVLSVETPLSIQAHPNKELAEKLHLQAPQHYPDANHKPEMAIALTPFQGLCGFRPV 154
Cdd:pfam20511  77 --KRFGGNLPFLFKVLSVEKPLSIQVHPDKELGEILHAADPKNYPDDNHKPELAIALTPFEGLCGFRPL 143
manA TIGR00218
mannose-6-phosphate isomerase, class I; The names phosphomannose isomerase and ...
 15-119 1.68e-19

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: 86.33  E-value: 1.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584836   15 QYAWGKmgsnSEVARLLASSDPlaqiaeDKPYAELWMG-THPRGDAKILDNRISQKTLSQWIAENQDSLGSKVKDtfngN 93
Cdd:TIGR00218  10 ERDWGG----TALADLFGYSIP------SQQTGECWAGsAHPKGPSTVLNGPYKGVSLIDLWEKHRELLGRADGD----R 75

                          90       100
                  ....*....|....*....|....*.
gi 574584836   94 LPFLFKVLSVETPLSIQAHPNKELAE 119
Cdd:TIGR00218  76 FPFLFKVLDAAKPLSIQVHPDDKYAE 101
ManA COG1482
Mannose-6-phosphate isomerase, class I [Carbohydrate transport and metabolism];
43-138 4.42e-11

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


Pssm-ID: 441091 [Multi-domain]  Cd Length: 324  Bit Score: 62.50  E-value: 4.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584836  43 DKPYAELWMG-THPRGDAKILDNRISQKTLSQWIAENQDSL-GSKVKDTFNGNLPFLFKVLSVETPLSIQAHPNKELAEK 120
Cdd:COG1482   31 EGKIGESWEIsAHPNGVSVVANGPLAGKTLDELVEEHPEELlGEKVYARFGDEFPLLIKFLDAKDDLSVQVHPDDEYAKE 110

                         90
                 ....*....|....*...
gi 574584836 121 LHlqapqhyPDANHKPEM 138
Cdd:COG1482  111 HE-------GGSYGKTEM 121
 
Name Accession Description Interval E-value
PLN02288 PLN02288
mannose-6-phosphate isomerase
 9-281 1.74e-111

mannose-6-phosphate isomerase


Pssm-ID: 215162 [Multi-domain]  Cd Length: 394  Bit Score: 327.40  E-value: 1.74e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584836   9 LSCAVQQYAWGKMGSNSEVARLLASSDPlAQIAEDKPYAELWMGTHPRGDAKILDNRISQKTLSQWIAENQDSLGSKVKD 88
Cdd:PLN02288   4 LRCAVQNYDWGRIGSESEVARLAAANSG-SDVDPDKPYAELWMGTHPSGPSFVVATGKGSVLLKEWIAENPAALGDRVVE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584836  89 TFNGNLPFLFKVLSVETPLSIQAHPNKELAEKLHLQAPQHYPDANHKPEMAIALTPFQGLCGFRPVEEIVTFLKKVPEFQ 168
Cdd:PLN02288  83 RWGGDLPFLFKVLSVAKALSIQAHPDKKLAEKLHAEQPNVYKDDNHKPEMALALTEFEALCGFVTIQELKAVLRTVPELR 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584836 169 FLIGDEAATHLKQTMSHDSQA-VASSLQSCFSHLMKSEKKVVVEQLNLLVKRISQQAAAGNNMEDifGELLLQLHQQYPG 247
Cdd:PLN02288 163 ELVGSEAADQLLALPEHDGEEdVKSVLRSAFTALMTASKDVVTEAVSKLKARLHAESQARELTDK--EELVLRLEKQYPG 240

                        250       260       270
                 ....*....|....*....|....*....|....
gi 574584836 248 DIGCFAIYFLNLLTLKPGEAMFLEANVPHAYLKG 281
Cdd:PLN02288 241 DVGVLSAFFLNYVKLNPGEALYLGANEPHAYLSG 274
cupin_PMI_type_I_N cd07011
type I phosphomannose isomerase in eukaryotes and bacteria, N-terminal cupin domain; This ...
 9-281 4.52e-105

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: 305.63  E-value: 4.52e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584836   9 LSCAVQQYAWGKMGSNSEVARllassdPLAQIAEDKPYAELWMGTHprgdakildnrisqktlsqwiaenqdslgskvkd 88
Cdd:cd07011    1 LKNAVQNYAWGSKGAISLLAR------GGGKIPEGKPYAELWMGTH---------------------------------- 40

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584836  89 tfngnLPFLFKVLSVETPLSIQAHPNKELAEKLHLQAPQHYPDANHKPEMAIALTPFQGLCGFRPVEEIVTFLKKV-PEF 167
Cdd:cd07011   41 -----LPFLFKVLSAAKPLSIQAHPDKEQAEKLFAREPENYKDPNHKPEMAIALTPFEALCGFRPLEEILALLERVpPEL 115

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584836 168 QFLIGDEAATHLKQTmshdsqavassLQSCFSHLMKSEKkvVVEQLNLLVKRISQQAAAGnnMEDIFGELLLQLHQQYPG 247
Cdd:cd07011  116 RELLGQEDAEQSKEG-----------LKALFSALLTLDS--DEEALAALVARLRARPKSE--ELDEAEELVLRLAEQYPG 180

                        250       260       270
                 ....*....|....*....|....*....|....
gi 574584836 248 DIGCFAIYFLNLLTLKPGEAMFLEANVPHAYLKG 281
Cdd:cd07011  181 DPGVFAALLLNLVTLKPGEAIFLPAGEPHAYLSG 214
PMI_typeI_cat pfam20511
Phosphomannose isomerase type I, catalytic domain; This entry represents the catalytic domain ...
 6-154 2.97e-82

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: 244.01  E-value: 2.97e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584836    6 VFPLSCAVQQYAWGKMGSNSEVARLLASSDPLaqIAEDKPYAELWMGTHPRGDAKILDNRISQKTLSQWIAENQDSLGsk 85
Cdd:pfam20511   1 LFRLQCGVQNYAWGKIGSNSALAKLFAYSIPS--IDEDKPYAELWMGTHPKGPSKVLNGQLRDVTLDELSAELGELFG-- 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 574584836   86 vkDTFNGNLPFLFKVLSVETPLSIQAHPNKELAEKLHLQAPQHYPDANHKPEMAIALTPFQGLCGFRPV 154
Cdd:pfam20511  77 --KRFGGNLPFLFKVLSVEKPLSIQVHPDKELGEILHAADPKNYPDDNHKPELAIALTPFEGLCGFRPL 143
PRK15131 PRK15131
mannose-6-phosphate isomerase; Provisional
 12-281 2.60e-57

mannose-6-phosphate isomerase; Provisional


Pssm-ID: 185085 [Multi-domain]  Cd Length: 389  Bit Score: 188.64  E-value: 2.60e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584836  12 AVQQYAWGkmgSNSEVARLLASSDPlaqiaEDKPYAELWMGTHPRGDAKILDNRISQKTLSQWIAENQDS-LGSKVKDTF 90
Cdd:PRK15131   7 SVQNYAWG---SKTALTELYGIANP-----DNQPMAELWMGAHPKSSSRVQDANGDIVSLRDVIESDKSAlLGEAVAKRF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584836  91 nGNLPFLFKVLSVETPLSIQAHPNKELAEK---------LHLQAPQ-HYPDANHKPEMAIALTPFQGLCGFRPVEEIVTF 160
Cdd:PRK15131  79 -GELPFLFKVLCAAQPLSIQVHPNKRAAEIgfakenaagIPLDAAErNYKDPNHKPELVFALTPFLAMNAFREFSEIVSL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584836 161 LKKV----PEFQFLIGDEAATHLKQtmshdsqaVASSLQScfshlMKSEKKvvveQLNLLVKRisqqaAAGNNMEDIFGE 236
Cdd:PRK15131 158 LQPVagahPAIAHFLQQPDAERLSE--------LFASLLN-----MQGEEK----SRALAVLK-----SALNSQQGEPWQ 215

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 574584836 237 LLLQLHQQYPGDIGCFAIYFLNLLTLKPGEAMFLEANVPHAYLKG 281
Cdd:PRK15131 216 TIRLISEFYPDDSGLFSPLLLNVVKLNPGEAMFLFAETPHAYLQG 260
PMI_typeI_hel pfam20512
Phosphomannose isomerase type I, helical insertion domain; This entry represents the ...
 170-257 6.69e-34

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: 118.72  E-value: 6.69e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584836  170 LIGDEAATHLKQTMSHDS-QAVASSLQSCFSHLMKSEKKVVVEQLNLLVKRISQQAAaGNNMEDIFGELLLQLHQQYPGD 248
Cdd:pfam20512   1 LIGEEAATHFISAISLQEpDAEQKLLQKLFSSLMNSQKEKIKIQLAKLVERIQSQPS-EFNKTDALPELIQRLNEQYPGD 79


                  ....*....
gi 574584836  249 IGCFAIYFL 257
Cdd:pfam20512  80 IGLFAPLFL 88
manA TIGR00218
mannose-6-phosphate isomerase, class I; The names phosphomannose isomerase and ...
 15-119 1.68e-19

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: 86.33  E-value: 1.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584836   15 QYAWGKmgsnSEVARLLASSDPlaqiaeDKPYAELWMG-THPRGDAKILDNRISQKTLSQWIAENQDSLGSKVKDtfngN 93
Cdd:TIGR00218  10 ERDWGG----TALADLFGYSIP------SQQTGECWAGsAHPKGPSTVLNGPYKGVSLIDLWEKHRELLGRADGD----R 75

                          90       100
                  ....*....|....*....|....*.
gi 574584836   94 LPFLFKVLSVETPLSIQAHPNKELAE 119
Cdd:TIGR00218  76 FPFLFKVLDAAKPLSIQVHPDDKYAE 101
ManA COG1482
Mannose-6-phosphate isomerase, class I [Carbohydrate transport and metabolism];
43-138 4.42e-11

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


Pssm-ID: 441091 [Multi-domain]  Cd Length: 324  Bit Score: 62.50  E-value: 4.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584836  43 DKPYAELWMG-THPRGDAKILDNRISQKTLSQWIAENQDSL-GSKVKDTFNGNLPFLFKVLSVETPLSIQAHPNKELAEK 120
Cdd:COG1482   31 EGKIGESWEIsAHPNGVSVVANGPLAGKTLDELVEEHPEELlGEKVYARFGDEFPLLIKFLDAKDDLSVQVHPDDEYAKE 110

                         90
                 ....*....|....*...
gi 574584836 121 LHlqapqhyPDANHKPEM 138
Cdd:COG1482  111 HE-------GGSYGKTEM 121
cupin_PMI_type_I_N_bac cd07010
Phosphomannose isomerase in bacteria and archaea, N-terminal cupin domain; This subfamily ...
 95-165 1.40e-04

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: 41.74  E-value: 1.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 574584836  95 PFLFKVLSVETPLSIQAHPNKELAEKlhlqapqHYPDANHKPEMAIALTPFQG---LCGFRP------------VEEIVT 159
Cdd:cd07010   34 PLLVKLLDAAERLSVQVHPDDEYARK-------HENEPFGKTEAWYILDAEPGakiYLGFKEgvtreefekaidDGDIEE 106


                 ....*.
gi 574584836 160 FLKKVP 165
Cdd:cd07010  107 LLNKVP 112
 
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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