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Conserved domains on  [gi|291391686|ref|XP_002712216|]
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glucose-6-phosphatase 2 isoform X2 [Oryctolagus cuniculus]

Protein Classification

glucose-6-phosphatase( domain architecture ID 10130180)

glucose-6-phosphatase is a type 2 phosphatidic acid phosphatase (PAP2) family protein that catalyzes the hydrolysis of glucose-6-phosphate to glucose and phosphate

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PAP2_glucose_6_phosphatase cd03381
PAP2_like proteins, glucose-6-phosphatase subfamily. Glucose-6-phosphatase converts ...
38-278 7.89e-107

PAP2_like proteins, glucose-6-phosphatase subfamily. Glucose-6-phosphatase converts glucose-6-phosphate into free glucose and is active in the lumen of the endoplasmic reticulum, where it is bound to the membrane. The generation of free glucose is an important control point in metabolism, and stands at the end of gluconeogenesis and the release of glucose from glycogen. Deficiency of glucose-6-phosphatase leads to von Gierke's disease.


:

Pssm-ID: 239476  Cd Length: 235  Bit Score: 312.39  E-value: 7.89e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391686  38 IFSIYFPLWFQLNQTVGTKMIWVAVIGDWFNLIFKWILFGHRPYWWVQETQIYPNHSSPCLEQFPTTCETGPGSPSGHAM 117
Cdd:cd03381    1 LFLIVFPLCGHLSQSVGIKLLWVAVIGDWLNLVFKWILFGQRPYWWVHETDYYSNSSVPKIEQFPLTCETGPGSPSGHAM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391686 118 GSSCVWYVMVTAALSHTVSRMDkfsvtlHRLTWSFLWSLFWLIQISVCISRVFIATHFPHQVILGVIGGMLVAEAFEHTP 197
Cdd:cd03381   81 GTTAVLLVMVTALLSHLAGRKR------SRFLRVMLWLVFWGVQLAVCLSRIYLAAHFPHQVIAGVISGIAVAETFSHIR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391686 198 GIQTASLSTYLKTNLFLFLFALGFYLLLRLLDIDLLWSVPIAKKWCANPDWIHIDTTPFAGLVRNLGVLFGLGFAINSEM 277
Cdd:cd03381  155 YIYSASLKRYVLITFFLFGFALGFYLLLKWLGVDLLWSLEKAFKWCERPEWVHIDTTPFASLLRNLGTLLGLGLALNSSM 234

                 .
gi 291391686 278 F 278
Cdd:cd03381  235 Y 235
 
Name Accession Description Interval E-value
PAP2_glucose_6_phosphatase cd03381
PAP2_like proteins, glucose-6-phosphatase subfamily. Glucose-6-phosphatase converts ...
38-278 7.89e-107

PAP2_like proteins, glucose-6-phosphatase subfamily. Glucose-6-phosphatase converts glucose-6-phosphate into free glucose and is active in the lumen of the endoplasmic reticulum, where it is bound to the membrane. The generation of free glucose is an important control point in metabolism, and stands at the end of gluconeogenesis and the release of glucose from glycogen. Deficiency of glucose-6-phosphatase leads to von Gierke's disease.


Pssm-ID: 239476  Cd Length: 235  Bit Score: 312.39  E-value: 7.89e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391686  38 IFSIYFPLWFQLNQTVGTKMIWVAVIGDWFNLIFKWILFGHRPYWWVQETQIYPNHSSPCLEQFPTTCETGPGSPSGHAM 117
Cdd:cd03381    1 LFLIVFPLCGHLSQSVGIKLLWVAVIGDWLNLVFKWILFGQRPYWWVHETDYYSNSSVPKIEQFPLTCETGPGSPSGHAM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391686 118 GSSCVWYVMVTAALSHTVSRMDkfsvtlHRLTWSFLWSLFWLIQISVCISRVFIATHFPHQVILGVIGGMLVAEAFEHTP 197
Cdd:cd03381   81 GTTAVLLVMVTALLSHLAGRKR------SRFLRVMLWLVFWGVQLAVCLSRIYLAAHFPHQVIAGVISGIAVAETFSHIR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391686 198 GIQTASLSTYLKTNLFLFLFALGFYLLLRLLDIDLLWSVPIAKKWCANPDWIHIDTTPFAGLVRNLGVLFGLGFAINSEM 277
Cdd:cd03381  155 YIYSASLKRYVLITFFLFGFALGFYLLLKWLGVDLLWSLEKAFKWCERPEWVHIDTTPFASLLRNLGTLLGLGLALNSSM 234

                 .
gi 291391686 278 F 278
Cdd:cd03381  235 Y 235
acidPPc smart00014
Acid phosphatase homologues;
59-193 3.78e-18

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 79.31  E-value: 3.78e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391686    59 WVAVIGDWFNLIFKWILFGHRPYWWVqetqiypNHSSPCLEQFPTTCETGPGSPSGHAMGSSCVWYVMVTAALShtvsrm 138
Cdd:smart00014   2 LLAVVSQLFNGVIKNYFGRPRPFFLS-------IGDACCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYLPA------ 68
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 291391686   139 dkfsvtlhRLTWSFLWSLFWLIQISVCISRVFIATHFPHQVILGVIGGMLVAEAF 193
Cdd:smart00014  69 --------RAGRKLLIFLLLLLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVL 115
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
57-190 9.76e-08

PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), Glucose-6-phosphatase EC:3.1.3.9, Phosphatidylglycerophosphatase B EC:3.1.3.27 and bacterial acid phosphatase EC:3.1.3.2. The family also includes a variety of haloperoxidases that function by oxidising halides in the presence of hydrogen peroxide to form the corresponding hypohalous acids.


Pssm-ID: 426329 [Multi-domain]  Cd Length: 124  Bit Score: 50.11  E-value: 9.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391686   57 MIWVAVIGDWFNLIFKWILFGHRPYWWVQETQIYPNHSspcleqfpTTCETGPGSPSGHAMGSSCVWYVmvtaaLSHTVS 136
Cdd:pfam01569   2 LLLALALAGLLSSVLKDYFGRPRPFFLLLEGGLVPAPS--------TLPGLGYSFPSGHSATAFALALL-----LALLLR 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 291391686  137 RMDKFSVTLhrltwsfLWSLFWLIQISVCISRVFIATHFPHQVILGVIGGMLVA 190
Cdd:pfam01569  69 RLRKIVRVL-------LALLLLVLALLVGLSRLYLGVHFPSDVLAGALIGILLA 115
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
104-193 5.87e-03

Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; Membrane-associated phospholipid phosphatase is part of the Pathway/BioSystem: Phospholipid biosynthesis


Pssm-ID: 440435 [Multi-domain]  Cd Length: 189  Bit Score: 37.33  E-value: 5.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391686 104 TCETGPGSPSGHAMGSSCVWYVMVTAALSHtvsrmdkfsvtlhrltwsFLWSLFWLIQISVCISRVFIATHFPHQVILGV 183
Cdd:COG0671  112 GTAGGYSFPSGHAAAAFALALVLALLLPRR------------------WLAALLLALALLVGLSRVYLGVHYPSDVLAGA 173
                         90
                 ....*....|
gi 291391686 184 IGGMLVAEAF 193
Cdd:COG0671  174 LLGLAIALLL 183
 
Name Accession Description Interval E-value
PAP2_glucose_6_phosphatase cd03381
PAP2_like proteins, glucose-6-phosphatase subfamily. Glucose-6-phosphatase converts ...
38-278 7.89e-107

PAP2_like proteins, glucose-6-phosphatase subfamily. Glucose-6-phosphatase converts glucose-6-phosphate into free glucose and is active in the lumen of the endoplasmic reticulum, where it is bound to the membrane. The generation of free glucose is an important control point in metabolism, and stands at the end of gluconeogenesis and the release of glucose from glycogen. Deficiency of glucose-6-phosphatase leads to von Gierke's disease.


Pssm-ID: 239476  Cd Length: 235  Bit Score: 312.39  E-value: 7.89e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391686  38 IFSIYFPLWFQLNQTVGTKMIWVAVIGDWFNLIFKWILFGHRPYWWVQETQIYPNHSSPCLEQFPTTCETGPGSPSGHAM 117
Cdd:cd03381    1 LFLIVFPLCGHLSQSVGIKLLWVAVIGDWLNLVFKWILFGQRPYWWVHETDYYSNSSVPKIEQFPLTCETGPGSPSGHAM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391686 118 GSSCVWYVMVTAALSHTVSRMDkfsvtlHRLTWSFLWSLFWLIQISVCISRVFIATHFPHQVILGVIGGMLVAEAFEHTP 197
Cdd:cd03381   81 GTTAVLLVMVTALLSHLAGRKR------SRFLRVMLWLVFWGVQLAVCLSRIYLAAHFPHQVIAGVISGIAVAETFSHIR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391686 198 GIQTASLSTYLKTNLFLFLFALGFYLLLRLLDIDLLWSVPIAKKWCANPDWIHIDTTPFAGLVRNLGVLFGLGFAINSEM 277
Cdd:cd03381  155 YIYSASLKRYVLITFFLFGFALGFYLLLKWLGVDLLWSLEKAFKWCERPEWVHIDTTPFASLLRNLGTLLGLGLALNSSM 234

                 .
gi 291391686 278 F 278
Cdd:cd03381  235 Y 235
acidPPc smart00014
Acid phosphatase homologues;
59-193 3.78e-18

Acid phosphatase homologues;


Pssm-ID: 214471 [Multi-domain]  Cd Length: 116  Bit Score: 79.31  E-value: 3.78e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391686    59 WVAVIGDWFNLIFKWILFGHRPYWWVqetqiypNHSSPCLEQFPTTCETGPGSPSGHAMGSSCVWYVMVTAALShtvsrm 138
Cdd:smart00014   2 LLAVVSQLFNGVIKNYFGRPRPFFLS-------IGDACCTPNFLLTLEAGYSFPSGHTAFAFAFALFLLLYLPA------ 68
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 291391686   139 dkfsvtlhRLTWSFLWSLFWLIQISVCISRVFIATHFPHQVILGVIGGMLVAEAF 193
Cdd:smart00014  69 --------RAGRKLLIFLLLLLALVVGFSRVYLGAHWPSDVLAGSLLGILIAAVL 115
PAP2_like cd01610
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ...
57-193 5.71e-14

PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, includes type 2 phosphatidic acid phosphatase or lipid phosphate phosphatase (LPP), Glucose-6-phosphatase, Phosphatidylglycerophosphatase B and bacterial acid phosphatase, vanadium chloroperoxidases, vanadium bromoperoxidases, and several other mostly uncharacterized subfamilies. Several members of this superfamily have been predicted to be transmembrane proteins.


Pssm-ID: 238813 [Multi-domain]  Cd Length: 122  Bit Score: 67.87  E-value: 5.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391686  57 MIWVAVIGDWFNLIFKWILFGHRPYWWVQETQIYpnhsspcleQFPTTCETGPGSPSGHAMGSSCVWYVMvtaalshtvs 136
Cdd:cd01610    8 LLLALLAGLLLTGVLKYLFGRPRPYFLLRCGPDG---------DPLLLTEGGYSFPSGHAAFAFALALFL---------- 68
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 291391686 137 rmdkFSVTLHRLTWSFLWSLFWLIQISVCISRVFIATHFPHQVILGVIGGMLVAEAF 193
Cdd:cd01610   69 ----ALLLPRRLLRLLLGLLLLLLALLVGLSRVYLGVHYPSDVLAGALLGILVALLV 121
PAP2 pfam01569
PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), ...
57-190 9.76e-08

PAP2 superfamily; This family includes the enzyme type 2 phosphatidic acid phosphatase (PAP2), Glucose-6-phosphatase EC:3.1.3.9, Phosphatidylglycerophosphatase B EC:3.1.3.27 and bacterial acid phosphatase EC:3.1.3.2. The family also includes a variety of haloperoxidases that function by oxidising halides in the presence of hydrogen peroxide to form the corresponding hypohalous acids.


Pssm-ID: 426329 [Multi-domain]  Cd Length: 124  Bit Score: 50.11  E-value: 9.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391686   57 MIWVAVIGDWFNLIFKWILFGHRPYWWVQETQIYPNHSspcleqfpTTCETGPGSPSGHAMGSSCVWYVmvtaaLSHTVS 136
Cdd:pfam01569   2 LLLALALAGLLSSVLKDYFGRPRPFFLLLEGGLVPAPS--------TLPGLGYSFPSGHSATAFALALL-----LALLLR 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 291391686  137 RMDKFSVTLhrltwsfLWSLFWLIQISVCISRVFIATHFPHQVILGVIGGMLVA 190
Cdd:pfam01569  69 RLRKIVRVL-------LALLLLVLALLVGLSRLYLGVHFPSDVLAGALIGILLA 115
PgpB COG0671
Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; ...
104-193 5.87e-03

Membrane-associated phospholipid phosphatase [Lipid transport and metabolism]; Membrane-associated phospholipid phosphatase is part of the Pathway/BioSystem: Phospholipid biosynthesis


Pssm-ID: 440435 [Multi-domain]  Cd Length: 189  Bit Score: 37.33  E-value: 5.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391686 104 TCETGPGSPSGHAMGSSCVWYVMVTAALSHtvsrmdkfsvtlhrltwsFLWSLFWLIQISVCISRVFIATHFPHQVILGV 183
Cdd:COG0671  112 GTAGGYSFPSGHAAAAFALALVLALLLPRR------------------WLAALLLALALLVGLSRVYLGVHYPSDVLAGA 173
                         90
                 ....*....|
gi 291391686 184 IGGMLVAEAF 193
Cdd:COG0671  174 LLGLAIALLL 183
PAP2_like_2 cd03392
PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This ...
106-190 9.13e-03

PAP2_like_2 proteins. PAP2 is a super-family of phosphatases and haloperoxidases. This subgroup, which is specific to bacteria, lacks functional characterization and may act as a membrane-associated lipid phosphatase.


Pssm-ID: 239486  Cd Length: 182  Bit Score: 36.82  E-value: 9.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 291391686 106 ETGPGSPSGHAMGSSCVwYVMVTAALSHTVSRmdkfsvTLHRLTWSFLWSLFWLiqiSVCISRVFIATHFPHQVILGVIG 185
Cdd:cd03392   98 EGGYSFPSGHAMGATVL-YGFLAYLLARRLPR------RRVRILLLILAAILIL---LVGLSRLYLGVHYPSDVLAGWLL 167

                 ....*
gi 291391686 186 GMLVA 190
Cdd:cd03392  168 GLAWL 172
 
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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