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Conserved domains on  [gi|312717|emb|CAA51778|]
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glucose-1-phosphate adenylyltransferase, partial [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02241 super family cl33437
glucose-1-phosphate adenylyltransferase
 1-184 1.40e-127

glucose-1-phosphate adenylyltransferase


The actual alignment was detected with superfamily member PLN02241:

Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 365.33  E-value: 1.40e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312717      1 YPYIAGMGVYVFRKEGLLKLLRSSYPTSNDFGSEII-RARRKLHNVQAFLFNDYWEDIGTIGSFFDANLALTEQPPKFQF 79
Cdd:PLN02241 210 KPYIASMGIYVFKKDVLLKLLRWRFPTANDFGSEIIpGAIKEGYNVQAYLFDGYWEDIGTIKSFYEANLALTKQPPKFSF 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312717     80 YDQKTPFFTSPRFLPPTKVDKCRILDSIVSHGCFLRECSVQHSIVGIRSRLESGVELQDTMMMGADFYQTEAEIASLLAE 159
Cdd:PLN02241 290 YDPDAPIYTSPRFLPPSKIEDCRITDSIISHGCFLRECKIEHSVVGLRSRIGEGVEIEDTVMMGADYYETEEEIASLLAE 369

                        170       180
                 ....*....|....*....|....*
gi 312717    160 GKVPVGVGQNTRIKNCIIDINARIG 184
Cdd:PLN02241 370 GKVPIGIGENTKIRNAIIDKNARIG 394
 
Name Accession Description Interval E-value
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 1-184 1.40e-127

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 365.33  E-value: 1.40e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312717      1 YPYIAGMGVYVFRKEGLLKLLRSSYPTSNDFGSEII-RARRKLHNVQAFLFNDYWEDIGTIGSFFDANLALTEQPPKFQF 79
Cdd:PLN02241 210 KPYIASMGIYVFKKDVLLKLLRWRFPTANDFGSEIIpGAIKEGYNVQAYLFDGYWEDIGTIKSFYEANLALTKQPPKFSF 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312717     80 YDQKTPFFTSPRFLPPTKVDKCRILDSIVSHGCFLRECSVQHSIVGIRSRLESGVELQDTMMMGADFYQTEAEIASLLAE 159
Cdd:PLN02241 290 YDPDAPIYTSPRFLPPSKIEDCRITDSIISHGCFLRECKIEHSVVGLRSRIGEGVEIEDTVMMGADYYETEEEIASLLAE 369

                        170       180
                 ....*....|....*....|....*
gi 312717    160 GKVPVGVGQNTRIKNCIIDINARIG 184
Cdd:PLN02241 370 GKVPIGIGENTKIRNAIIDKNARIG 394
glgC TIGR02091
glucose-1-phosphate adenylyltransferase; This enzyme, glucose-1-phosphate adenylyltransferase, ...
 2-184 1.72e-66

glucose-1-phosphate adenylyltransferase; This enzyme, glucose-1-phosphate adenylyltransferase, is also called ADP-glucose pyrophosphorylase. The plant form is an alpha2,beta2 heterodimer, allosterically regulated in plants. Both subunits are homologous and included in this model. In bacteria, both homomeric forms of GlgC and more active heterodimers of GlgC and GlgD have been described. This model describes the GlgC subunit only. This enzyme appears in variants of glycogen synthesis pathways that use ADP-glucose, rather than UDP-glucose as in animals. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 273965 [Multi-domain]  Cd Length: 361  Bit Score: 207.11  E-value: 1.72e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312717       2 PYIAGMGVYVFRKEGLLKLLR---SSYPTSNDFGSEIIRARRKLHNVQAFLFNDYWEDIGTIGSFFDANLALTEQPPKFQ 78
Cdd:TIGR02091 186 FALASMGIYIFDKDVLKELLEedaDDPESSHDFGKDIIPRALEEGSVQAYLFSGYWRDVGTIDSFWEANMDLVSVVPPFD 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312717      79 FYDQKTPFFTSPRFLPPTKV--DKCRILDSIVSHGCFLRECSVQHSIVGIRSRLESGVELQDTMMMGAdfyqteaeiasl 156
Cdd:TIGR02091 266 LYDRKWPIYTYNEFLPPAKFvdSDAQVVDSLVSEGCIISGATVSHSVLGIRVRIGSGSTVEDSVIMGD------------ 333

                         170       180
                  ....*....|....*....|....*...
gi 312717     157 laegkvpVGVGQNTRIKNCIIDINARIG 184
Cdd:TIGR02091 334 -------VGIGRGAVIRNAIIDKNVRIG 354
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 2-184 4.56e-54

Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 175.65  E-value: 4.56e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312717     2 PYIAGMGVYVFRKEGLLKLLRSSYPTS-NDFGSEIIRARRKLHNVQAFLFNDYWEDIGTIGSFFDANLALTEQPPKFQFY 80
Cdd:COG0448 183 SALASMGIYVFNKDVLIELLEEDAPNSsHDFGKDIIPRLLDRGKVYAYEFDGYWRDVGTIDSYYEANMDLLDPEPEFNLY 262

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312717    81 DQKTPFFTSPRFLPPTK-VDKCRILDSIVSHGCFLrECSVQHSIVGIRSRLESGVELQDTMMMGAdfyqteaeiasllae 159
Cdd:COG0448 263 DPEWPIYTKQKDLPPAKfVRGGKVKNSLVSNGCII-SGTVENSVLFRGVRVESGAVVENSVIMPG--------------- 326

                       170       180
                ....*....|....*....|....*
gi 312717   160 gkvpVGVGQNTRIKNCIIDINARIG 184
Cdd:COG0448 327 ----VVIGEGAVIENAIIDKNVVIP 347
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 94-184 4.73e-21

Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Glucose-1-phosphate adenylyltransferase is also known as ADP-glucose synthase or ADP-glucose pyrophosphorylase. It catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for regulation of storage polysaccharide accumulation in plants and bacteria. The enzyme is a homotetramer, with each subunit containing an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain with at 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The LbH domain is involved in cooperative allosteric regulation and oligomerization.


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 82.90  E-value: 4.73e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312717    94 PPTKVDKCRILDSIVSHGCFLRECSVQHSIVGIRSRLESGVELQDTMMMGAdfyqteaeiasllaegkvpVGVGQNTRIK 173
Cdd:cd04651   1 PPYIGRRGEVKNSLVSEGCIISGGTVENSVLFRGVRVGSGSVVEDSVIMPN-------------------VGIGRNAVIR 61

                        90
                ....*....|.
gi 312717   174 NCIIDINARIG 184
Cdd:cd04651  62 RAIIDKNVVIP 72
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-71 2.60e-12

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 63.04  E-value: 2.60e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312717       2 PYIAGMGVYVFRKEGLLKLLR--SSYPTSNDFGSEIIR-ARRKLHNVQAFLFNDY-WEDIGTIGSFFDANLALT 71
Cdd:pfam00483 170 SNYASMGIYIFNSGVLDFLAKylEELKRGEDEITDILPkALEDGKLAYAFIFKGYaWLDVGTWDSLWEANLFLL 243
 
Name Accession Description Interval E-value
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 1-184 1.40e-127

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 365.33  E-value: 1.40e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312717      1 YPYIAGMGVYVFRKEGLLKLLRSSYPTSNDFGSEII-RARRKLHNVQAFLFNDYWEDIGTIGSFFDANLALTEQPPKFQF 79
Cdd:PLN02241 210 KPYIASMGIYVFKKDVLLKLLRWRFPTANDFGSEIIpGAIKEGYNVQAYLFDGYWEDIGTIKSFYEANLALTKQPPKFSF 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312717     80 YDQKTPFFTSPRFLPPTKVDKCRILDSIVSHGCFLRECSVQHSIVGIRSRLESGVELQDTMMMGADFYQTEAEIASLLAE 159
Cdd:PLN02241 290 YDPDAPIYTSPRFLPPSKIEDCRITDSIISHGCFLRECKIEHSVVGLRSRIGEGVEIEDTVMMGADYYETEEEIASLLAE 369

                        170       180
                 ....*....|....*....|....*
gi 312717    160 GKVPVGVGQNTRIKNCIIDINARIG 184
Cdd:PLN02241 370 GKVPIGIGENTKIRNAIIDKNARIG 394
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 2-184 1.25e-97

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 289.09  E-value: 1.25e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312717      2 PYIAGMGVYVFRKEGLLKLLRSSyPTSNDFGSEIIRARRKLHNVQAFLFNDYWEDIGTIGSFFDANLALTEQP-PKFQFY 80
Cdd:PRK02862 205 PYLASMGIYVFSRDVLFDLLNKN-PEYTDFGKEIIPEAIRDYKVQSYLFDGYWEDIGTIEAFYEANLALTQQPnPPFSFY 283

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312717     81 DQKTPFFTSPRFLPPTKVDKCRILDSIVSHGCFLRECSVQHSIVGIRSRLESGVELQDTMMMGADFYQTEAEIASLLAEG 160
Cdd:PRK02862 284 DEKAPIYTRARYLPPSKLLDATITESIIAEGCIIKNCSIHHSVLGIRSRIESGCTIEDTLVMGADFYESSEEREELRKEG 363

                        170       180
                 ....*....|....*....|....
gi 312717    161 KVPVGVGQNTRIKNCIIDINARIG 184
Cdd:PRK02862 364 KPPLGIGEGTTIKRAIIDKNARIG 387
glgC TIGR02091
glucose-1-phosphate adenylyltransferase; This enzyme, glucose-1-phosphate adenylyltransferase, ...
 2-184 1.72e-66

glucose-1-phosphate adenylyltransferase; This enzyme, glucose-1-phosphate adenylyltransferase, is also called ADP-glucose pyrophosphorylase. The plant form is an alpha2,beta2 heterodimer, allosterically regulated in plants. Both subunits are homologous and included in this model. In bacteria, both homomeric forms of GlgC and more active heterodimers of GlgC and GlgD have been described. This model describes the GlgC subunit only. This enzyme appears in variants of glycogen synthesis pathways that use ADP-glucose, rather than UDP-glucose as in animals. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 273965 [Multi-domain]  Cd Length: 361  Bit Score: 207.11  E-value: 1.72e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312717       2 PYIAGMGVYVFRKEGLLKLLR---SSYPTSNDFGSEIIRARRKLHNVQAFLFNDYWEDIGTIGSFFDANLALTEQPPKFQ 78
Cdd:TIGR02091 186 FALASMGIYIFDKDVLKELLEedaDDPESSHDFGKDIIPRALEEGSVQAYLFSGYWRDVGTIDSFWEANMDLVSVVPPFD 265

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312717      79 FYDQKTPFFTSPRFLPPTKV--DKCRILDSIVSHGCFLRECSVQHSIVGIRSRLESGVELQDTMMMGAdfyqteaeiasl 156
Cdd:TIGR02091 266 LYDRKWPIYTYNEFLPPAKFvdSDAQVVDSLVSEGCIISGATVSHSVLGIRVRIGSGSTVEDSVIMGD------------ 333

                         170       180
                  ....*....|....*....|....*...
gi 312717     157 laegkvpVGVGQNTRIKNCIIDINARIG 184
Cdd:TIGR02091 334 -------VGIGRGAVIRNAIIDKNVRIG 354
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 2-184 4.56e-54

Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 175.65  E-value: 4.56e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312717     2 PYIAGMGVYVFRKEGLLKLLRSSYPTS-NDFGSEIIRARRKLHNVQAFLFNDYWEDIGTIGSFFDANLALTEQPPKFQFY 80
Cdd:COG0448 183 SALASMGIYVFNKDVLIELLEEDAPNSsHDFGKDIIPRLLDRGKVYAYEFDGYWRDVGTIDSYYEANMDLLDPEPEFNLY 262

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312717    81 DQKTPFFTSPRFLPPTK-VDKCRILDSIVSHGCFLrECSVQHSIVGIRSRLESGVELQDTMMMGAdfyqteaeiasllae 159
Cdd:COG0448 263 DPEWPIYTKQKDLPPAKfVRGGKVKNSLVSNGCII-SGTVENSVLFRGVRVESGAVVENSVIMPG--------------- 326

                       170       180
                ....*....|....*....|....*
gi 312717   160 gkvpVGVGQNTRIKNCIIDINARIG 184
Cdd:COG0448 327 ----VVIGEGAVIENAIIDKNVVIP 347
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 5-184 8.48e-30

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 112.61  E-value: 8.48e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312717      5 AGMGVYVFRKEGLLKLLR---SSYPTSNDFGSEIIRARRKLHNVQAFLFND------------YWEDIGTIGSFFDANLA 69
Cdd:PRK00844 195 ASMGNYVFTTDALVDALRrdaADEDSSHDMGGDIIPRLVERGRAYVYDFSTnevpgaterdrgYWRDVGTIDAYYDAHMD 274

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312717     70 LTEQPPKFQFYDQKTPFFTSPRFLPPTKV-----DKCRILDSIVSHGCFLRECSVQHSIVGIRSRLESGVELQDTMMMGA 144
Cdd:PRK00844 275 LLSVHPVFNLYNREWPIYTSSPNLPPAKFvdgggRVGSAQDSLVSAGSIISGATVRNSVLSPNVVVESGAEVEDSVLMDG 354

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 312717    145 dfyqteaeiasllaegkvpVGVGQNTRIKNCIIDIN------ARIG 184
Cdd:PRK00844 355 -------------------VRIGRGAVVRRAILDKNvvvppgATIG 381
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 5-183 2.35e-29

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 111.86  E-value: 2.35e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312717      5 AGMGVYVFRKEGLLKLLR---SSYPTSNDFGSEIIRARRKLHNVQAFLFND-----------YWEDIGTIGSFFDANLAL 70
Cdd:PRK00725 207 ASMGIYVFNADYLYELLEedaEDPNSSHDFGKDIIPKIVEEGKVYAHPFSDscvrsdpeeepYWRDVGTLDAYWQANLDL 286

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312717     71 TEQPPKFQFYDQKTPFFTSPRFLPPTK----VDKCR--ILDSIVSHGCFLRECSVQHSIVGIRSRLESGVELQDTMMMga 144
Cdd:PRK00725 287 ASVTPELDLYDRNWPIWTYQEQLPPAKfvfdRSGRRgmAINSLVSGGCIISGAVVRRSVLFSRVRVNSFSNVEDSVLL-- 364

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 312717    145 dfyqteaeiasllaegkvP-VGVGQNTRIKNCIIDINARI 183
Cdd:PRK00725 365 ------------------PdVNVGRSCRLRRCVIDRGCVI 386
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 5-184 1.14e-24

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 98.40  E-value: 1.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312717      5 AGMGVYVFRKEGLLKLLRSSYPT---SNDFGSEII-RARRKLHNVQAFLFNDYWEDIGTIGSFFDANLALTEQPPKFQFY 80
Cdd:PRK05293 188 ASMGIYIFNWKRLKEYLIEDEKNpnsSHDFGKNVIpLYLEEGEKLYAYPFKGYWKDVGTIESLWEANMELLRPENPLNLF 267

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312717     81 DQKTPFFTSPRFLPPTKV-DKCRILDSIVSHGCFLrECSVQHSIVGIRSRLESGVELQDTMMMgadfyqTEAEIasllae 159
Cdd:PRK05293 268 DRNWRIYSVNPNLPPQYIaENAKVKNSLVVEGCVV-YGTVEHSVLFQGVQVGEGSVVKDSVIM------PGAKI------ 334

                        170       180
                 ....*....|....*....|....*
gi 312717    160 gkvpvgvGQNTRIKNCIIDINARIG 184
Cdd:PRK05293 335 -------GENVVIERAIIGENAVIG 352
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 94-184 4.73e-21

Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Glucose-1-phosphate adenylyltransferase is also known as ADP-glucose synthase or ADP-glucose pyrophosphorylase. It catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for regulation of storage polysaccharide accumulation in plants and bacteria. The enzyme is a homotetramer, with each subunit containing an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain with at 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The LbH domain is involved in cooperative allosteric regulation and oligomerization.


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 82.90  E-value: 4.73e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 312717    94 PPTKVDKCRILDSIVSHGCFLRECSVQHSIVGIRSRLESGVELQDTMMMGAdfyqteaeiasllaegkvpVGVGQNTRIK 173
Cdd:cd04651   1 PPYIGRRGEVKNSLVSEGCIISGGTVENSVLFRGVRVGSGSVVEDSVIMPN-------------------VGIGRNAVIR 61

                        90
                ....*....|.
gi 312717   174 NCIIDINARIG 184
Cdd:cd04651  62 RAIIDKNVVIP 72
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 3-57 6.51e-14

ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ADP-glucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase) catalyzes a very important step in the biosynthesis of alpha 1,4-glucans (glycogen or starch) in bacteria and plants: synthesis of the activated glucosyl donor, ADP-glucose, from glucose-1-phosphate and ATP. ADP-glucose pyrophosphorylase is a tetrameric allosterically regulated enzyme. While a homotetramer in bacteria, in plant chloroplasts and amyloplasts, it is a heterotetramer of two different, yet evolutionary related, subunits. There are a number of conserved regions in the sequence of bacterial and plant ADP-glucose pyrophosphorylase subunits. It is a subfamily of a very diverse glycosy transferase family 2.


Pssm-ID: 133002 [Multi-domain]  Cd Length: 200  Bit Score: 66.80  E-value: 6.51e-14
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 312717     3 YIAGMGVYVFRKEGLLKLLRSSY-PTSNDFGSEIIRARRKLHNVQAFLFNDYWEDI 57
Cdd:cd02508 145 YKASMGIYIFSKDLLIELLEEDAaDGSHDFGKDIIPAMLKKLKIYAYEFNGYWADI 200
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-71 2.60e-12

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 63.04  E-value: 2.60e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 312717       2 PYIAGMGVYVFRKEGLLKLLR--SSYPTSNDFGSEIIR-ARRKLHNVQAFLFNDY-WEDIGTIGSFFDANLALT 71
Cdd:pfam00483 170 SNYASMGIYIFNSGVLDFLAKylEELKRGEDEITDILPkALEDGKLAYAFIFKGYaWLDVGTWDSLWEANLFLL 243
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-58 4.17e-06

NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 45.26  E-value: 4.17e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 312717     3 YIAGMGVYVFRKEgLLKLLRSSYPTSNDFGSEIIRARRKLHNVQAFLFNDYWEDIG 58
Cdd:cd04181 163 NLANAGIYIFEPE-ILDYIPEILPRGEDELTDAIPLLIEEGKVYGYPVDGYWLDIG 217
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 117-184 3.50e-04

Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 37.61  E-value: 3.50e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 312717   117 CSVQHSIVGIRSRLESGVELQDTMMMGAdfyqteaeiasllaegkvpVGVGQNTRIKNCIIDINARIG 184
Cdd:cd03356  12 AIIKNSVIGDNVRIGDGVTITNSILMDN-------------------VTIGANSVIVDSIIGDNAVIG 60
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 7-70 3.16e-03

NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 37.05  E-value: 3.16e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 312717     7 MGVYVFRKEgLLKLLrssyPTSNDFG-SEIIRARRKLHNVQAFLFNDYWEDIGTIGSFFDANLAL 70
Cdd:COG1208 168 AGIYVLEPE-IFDYI----PEGEPFDlEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALL 227
 
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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