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Conserved domains on  [gi|165978410|gb|ABY76624|]
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manose-6-phosphate isomerase, partial [Rhogeessa tumida]

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 ...
 1-80 2.59e-16

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: 71.24  E-value: 2.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165978410   1 MAIALTSFQGLCGFRPIEEIVTFLTKVPEFQFLVGDNATAQLKQSLSHDSQAMA-SALQSGFSHLMESKQQLVVEQLNLL 79
Cdd:PLN02288 132 MALALTEFEALCGFVTIQELKAVLRTVPELRELVGSEAADQLLALPEHDGEEDVkSVLRSAFTALMTASKDVVTEAVSKL 211


                 .
gi 165978410  80 V 80
Cdd:PLN02288 212 K 212
 
Name Accession Description Interval E-value
PLN02288 PLN02288
mannose-6-phosphate isomerase
 1-80 2.59e-16

mannose-6-phosphate isomerase


Pssm-ID: 215162 [Multi-domain]  Cd Length: 394  Bit Score: 71.24  E-value: 2.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165978410   1 MAIALTSFQGLCGFRPIEEIVTFLTKVPEFQFLVGDNATAQLKQSLSHDSQAMA-SALQSGFSHLMESKQQLVVEQLNLL 79
Cdd:PLN02288 132 MALALTEFEALCGFVTIQELKAVLRTVPELRELVGSEAADQLLALPEHDGEEDVkSVLRSAFTALMTASKDVVTEAVSKL 211


                 .
gi 165978410  80 V 80
Cdd:PLN02288 212 K 212
cupin_PMI_type_I_N cd07011
type I phosphomannose isomerase in eukaryotes and bacteria, N-terminal cupin domain; This ...
 1-80 1.00e-13

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: 63.34  E-value: 1.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165978410   1 MAIALTSFQGLCGFRPIEEIVTFLTKV-PEFQFLVGDnataqlkqslsHDSQAMASALQSGFSHLMesKQQLVVEQLNLL 79
Cdd:cd07011   85 MAIALTPFEALCGFRPLEEILALLERVpPELRELLGQ-----------EDAEQSKEGLKALFSALL--TLDSDEEALAAL 151


                 .
gi 165978410  80 V 80
Cdd:cd07011  152 V 152
PMI_typeI_hel pfam20512
Phosphomannose isomerase type I, helical insertion domain; This entry represents the ...
 33-80 9.29e-05

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: 37.06  E-value: 9.29e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 165978410  33 LVGDNATAQLKQSLSHDS-QAMASALQSGFSHLMESKQQLVVEQLNLLV 80
Cdd:pfam20512  1 LIGEEAATHFISAISLQEpDAEQKLLQKLFSSLMNSQKEKIKIQLAKLV 49
 
Name Accession Description Interval E-value
PLN02288 PLN02288
mannose-6-phosphate isomerase
 1-80 2.59e-16

mannose-6-phosphate isomerase


Pssm-ID: 215162 [Multi-domain]  Cd Length: 394  Bit Score: 71.24  E-value: 2.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165978410   1 MAIALTSFQGLCGFRPIEEIVTFLTKVPEFQFLVGDNATAQLKQSLSHDSQAMA-SALQSGFSHLMESKQQLVVEQLNLL 79
Cdd:PLN02288 132 MALALTEFEALCGFVTIQELKAVLRTVPELRELVGSEAADQLLALPEHDGEEDVkSVLRSAFTALMTASKDVVTEAVSKL 211


                 .
gi 165978410  80 V 80
Cdd:PLN02288 212 K 212
cupin_PMI_type_I_N cd07011
type I phosphomannose isomerase in eukaryotes and bacteria, N-terminal cupin domain; This ...
 1-80 1.00e-13

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: 63.34  E-value: 1.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 165978410   1 MAIALTSFQGLCGFRPIEEIVTFLTKV-PEFQFLVGDnataqlkqslsHDSQAMASALQSGFSHLMesKQQLVVEQLNLL 79
Cdd:cd07011   85 MAIALTPFEALCGFRPLEEILALLERVpPELRELLGQ-----------EDAEQSKEGLKALFSALL--TLDSDEEALAAL 151


                 .
gi 165978410  80 V 80
Cdd:cd07011  152 V 152
PMI_typeI_hel pfam20512
Phosphomannose isomerase type I, helical insertion domain; This entry represents the ...
 33-80 9.29e-05

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: 37.06  E-value: 9.29e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 165978410  33 LVGDNATAQLKQSLSHDS-QAMASALQSGFSHLMESKQQLVVEQLNLLV 80
Cdd:pfam20512  1 LIGEEAATHFISAISLQEpDAEQKLLQKLFSSLMNSQKEKIKIQLAKLV 49
PMI_typeI_cat pfam20511
Phosphomannose isomerase type I, catalytic domain; This entry represents the catalytic domain ...
 1-17 2.82e-04

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: 36.78  E-value: 2.82e-04
                          10
                  ....*....|....*..
gi 165978410    1 MAIALTSFQGLCGFRPI 17
Cdd:pfam20511 127 LAIALTPFEGLCGFRPL 143
PRK15131 PRK15131
mannose-6-phosphate isomerase; Provisional
 4-27 8.32e-03

mannose-6-phosphate isomerase; Provisional


Pssm-ID: 185085 [Multi-domain]  Cd Length: 389  Bit Score: 33.02  E-value: 8.32e-03
                         10        20
                 ....*....|....*....|....
gi 165978410   4 ALTSFQGLCGFRPIEEIVTFLTKV 27
Cdd:PRK15131 138 ALTPFLAMNAFREFSEIVSLLQPV 161
 
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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