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Conserved domains on  [gi|520910452|ref|WP_020330228|]
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glucose-1-phosphate adenylyltransferase [Vibrio fluvialis]

Protein Classification

glucose-1-phosphate adenylyltransferase( domain architecture ID 11479259)

glucose-1-phosphate adenylyltransferase catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria

CATH:  3.90.550.10|2.160.10.10
EC:  2.7.7.27
Gene Ontology:  GO:0008878|GO:0005978|GO:0005524

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 1-403 0e+00

glucose-1-phosphate adenylyltransferase; Provisional


:

Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 761.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452   1 MTGVLGMILAGGEGSRLMPLTESRTKPAVPFGGSYRLIDFALNNFVNADLMRIYVLTQFKSQSLYLHMKKGWNVSSIRDR 80
Cdd:PRK00844   3 MPKVLAIVLAGGEGKRLMPLTADRAKPAVPFGGSYRLIDFVLSNLVNSGYLRIYVLTQYKSHSLDRHISQTWRLSGLLGN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  81 FIDCIPAQMRDGKRWYEGTADAIYQNLRFVEISEADQVCIFGSDHIYKMDIRQMLDYHRRKEARLTVSALRMPLSQASQF 160
Cdd:PRK00844  83 YITPVPAQQRLGKRWYLGSADAIYQSLNLIEDEDPDYVVVFGADHVYRMDPRQMVDFHIESGAGVTVAAIRVPREEASAF 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 161 GVIEVDDEGRMVGFEEKPKNPKAIPGDPEWALVSMGNYIFETETLCEELREDAALENSSHDFGKDIIPKMFPQGGVYVYD 240
Cdd:PRK00844 163 GVIEVDPDGRIRGFLEKPADPPGLPDDPDEALASMGNYVFTTDALVDALRRDAADEDSSHDMGGDIIPRLVERGRAYVYD 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 241 FSTNKIKG--EKESTYWRDVGTIESYWAAHMDLLEKEPPFSLYNRSWPLHTYYPPLPPATFIDVGDKKVTITDSLVSGGS 318
Cdd:PRK00844 243 FSTNEVPGatERDRGYWRDVGTIDAYYDAHMDLLSVHPVFNLYNREWPIYTSSPNLPPAKFVDGGGRVGSAQDSLVSAGS 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 319 YIQGVKIYKSILGFRSNIAAGSLISESVILGDVKIGAGCTIKRAIIDKNVEIAPGTIIGEDLELDRQRFHVSDEGIVVIA 398
Cdd:PRK00844 323 IISGATVRNSVLSPNVVVESGAEVEDSVLMDGVRIGRGAVVRRAILDKNVVVPPGATIGVDLEEDRRRFTVSEGGIVVVP 402


                 ....*
gi 520910452 399 KGTKV 403
Cdd:PRK00844 403 KGQRV 407
 
Name Accession Description Interval E-value
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 1-403 0e+00

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 761.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452   1 MTGVLGMILAGGEGSRLMPLTESRTKPAVPFGGSYRLIDFALNNFVNADLMRIYVLTQFKSQSLYLHMKKGWNVSSIRDR 80
Cdd:PRK00844   3 MPKVLAIVLAGGEGKRLMPLTADRAKPAVPFGGSYRLIDFVLSNLVNSGYLRIYVLTQYKSHSLDRHISQTWRLSGLLGN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  81 FIDCIPAQMRDGKRWYEGTADAIYQNLRFVEISEADQVCIFGSDHIYKMDIRQMLDYHRRKEARLTVSALRMPLSQASQF 160
Cdd:PRK00844  83 YITPVPAQQRLGKRWYLGSADAIYQSLNLIEDEDPDYVVVFGADHVYRMDPRQMVDFHIESGAGVTVAAIRVPREEASAF 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 161 GVIEVDDEGRMVGFEEKPKNPKAIPGDPEWALVSMGNYIFETETLCEELREDAALENSSHDFGKDIIPKMFPQGGVYVYD 240
Cdd:PRK00844 163 GVIEVDPDGRIRGFLEKPADPPGLPDDPDEALASMGNYVFTTDALVDALRRDAADEDSSHDMGGDIIPRLVERGRAYVYD 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 241 FSTNKIKG--EKESTYWRDVGTIESYWAAHMDLLEKEPPFSLYNRSWPLHTYYPPLPPATFIDVGDKKVTITDSLVSGGS 318
Cdd:PRK00844 243 FSTNEVPGatERDRGYWRDVGTIDAYYDAHMDLLSVHPVFNLYNREWPIYTSSPNLPPAKFVDGGGRVGSAQDSLVSAGS 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 319 YIQGVKIYKSILGFRSNIAAGSLISESVILGDVKIGAGCTIKRAIIDKNVEIAPGTIIGEDLELDRQRFHVSDEGIVVIA 398
Cdd:PRK00844 323 IISGATVRNSVLSPNVVVESGAEVEDSVLMDGVRIGRGAVVRRAILDKNVVVPPGATIGVDLEEDRRRFTVSEGGIVVVP 402


                 ....*
gi 520910452 399 KGTKV 403
Cdd:PRK00844 403 KGQRV 407
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 4-401 0e+00

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 568.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452   4 VLGMILAGGEGSRLMPLTESRTKPAVPFGGSYRLIDFALNNFVNADLMRIYVLTQFKSQSLYLHMKKG--WNVSSIRDrF 81
Cdd:COG0448    2 VLAIILAGGRGSRLGPLTKDRAKPAVPFGGKYRIIDFPLSNCVNSGIRRVGVLTQYKSHSLNDHIGSGkpWDLDRKRG-G 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  82 IDCIPA-QMRDGKRWYEGTADAIYQNLRFVEISEADQVCIFGSDHIYKMDIRQMLDYHRRKEARLTVSALRMPLSQASQF 160
Cdd:COG0448   81 VFILPPyQQREGEDWYQGTADAVYQNLDFIERSDPDYVLILSGDHIYKMDYRQMLDFHIESGADITVACIEVPREEASRF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 161 GVIEVDDEGRMVGFEEKPKNPKaipgdpeWALVSMGNYIFETETLCEELREDAalENSSHDFGKDIIPKMFPQGGVYVYD 240
Cdd:COG0448  161 GVMEVDEDGRITEFEEKPKDPK-------SALASMGIYVFNKDVLIELLEEDA--PNSSHDFGKDIIPRLLDRGKVYAYE 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 241 FstnkiKGekestYWRDVGTIESYWAAHMDLLEKEPPFSLYNRSWPLHTYYPPLPPATFIDVGdkkvTITDSLVSGGSYI 320
Cdd:COG0448  232 F-----DG-----YWRDVGTIDSYYEANMDLLDPEPEFNLYDPEWPIYTKQKDLPPAKFVRGG----KVKNSLVSNGCII 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 321 QGvKIYKSILGFRSNIAAGSLISESVILGDVKIGAGCTIKRAIIDKNVEIAPGTIIGEDLELDRQRFHVSDeGIVVIAKG 400
Cdd:COG0448  298 SG-TVENSVLFRGVRVESGAVVENSVIMPGVVIGEGAVIENAIIDKNVVIPPGVVIGEDPEEDRKRFTVSS-GIVVVGKG 375


                 .
gi 520910452 401 T 401
Cdd:COG0448  376 A 376
glgC TIGR02091
glucose-1-phosphate adenylyltransferase; This enzyme, glucose-1-phosphate adenylyltransferase, ...
 6-378 0e+00

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: 553.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452    6 GMILAGGEGSRLMPLTESRTKPAVPFGGSYRLIDFALNNFVNADLMRIYVLTQFKSQSLYLHMKKGWNVSSIRDRFIDCI 85
Cdd:TIGR02091   1 AMVLAGGRGSRLSPLTKRRAKPAVPFGGKYRIIDFPLSNCINSGIRRIGVLTQYKSHSLNRHIQRGWDFDGFIDGFVTLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452   86 PAQMR-DGKRWYEGTADAIYQNLRFVEISEADQVCIFGSDHIYKMDIRQMLDYHRRKEARLTVSALRMPLSQASQFGVIE 164
Cdd:TIGR02091  81 PAQQReSGTDWYQGTADAVYQNLDLIEDYDPEYVLILSGDHIYKMDYEKMLDYHIESGADVTIACIPVPRKEASRFGVMQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  165 VDDEGRMVGFEEKPKNPKAIPGDPEWALVSMGNYIFETETLCEELREDAALENSSHDFGKDIIPKMFPQGGVYVYDFstn 244
Cdd:TIGR02091 161 VDEDGRIVDFEEKPANPPSIPGMPDFALASMGIYIFDKDVLKELLEEDADDPESSHDFGKDIIPRALEEGSVQAYLF--- 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  245 kikgekeSTYWRDVGTIESYWAAHMDLLEKEPPFSLYNRSWPLHTYYPPLPPATFIDVGDKkvtITDSLVSGGSYIQGVK 324
Cdd:TIGR02091 238 -------SGYWRDVGTIDSFWEANMDLVSVVPPFDLYDRKWPIYTYNEFLPPAKFVDSDAQ---VVDSLVSEGCIISGAT 307

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 520910452  325 IYKSILGFRSNIAAGSLISESVILGDVKIGAGCTIKRAIIDKNVEIAPGTIIGE 378
Cdd:TIGR02091 308 VSHSVLGIRVRIGSGSTVEDSVIMGDVGIGRGAVIRNAIIDKNVRIGEGVVIGN 361
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 6-258 5.17e-87

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: 262.48  E-value: 5.17e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452   6 GMILAGGEGSRLMPLTESRTKPAVPFGGSYRLIDFALNNFVNADLMRIYVLTQFKSQSLYLHMKKGWNVSSIR-DRFIDC 84
Cdd:cd02508    1 AIILAGGEGTRLSPLTKKRAKPAVPFGGRYRLIDFPLSNMVNSGIRNVGVLTQYKSRSLNDHLGSGKEWDLDRkNGGLFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  85 IPAQMRDGKRWYEGTADAIYQNLRFVEISEADQVCIFGSDHIYKMDIRQMLDYHRRKEARLTVSalrmplsqasqfgvie 164
Cdd:cd02508   81 LPPQQRKGGDWYRGTADAIYQNLDYIERSDPEYVLILSGDHIYNMDYREMLDFHIESGADITVV---------------- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 165 vddegrmvgfeekpknpkaipgdpewALVSMGNYIFETETLCEELREDAAleNSSHDFGKDIIPKMFPQGGVYVYDFstn 244
Cdd:cd02508  145 --------------------------YKASMGIYIFSKDLLIELLEEDAA--DGSHDFGKDIIPAMLKKLKIYAYEF--- 193

                        250
                 ....*....|....
gi 520910452 245 kikgekeSTYWRDV 258
Cdd:cd02508  194 -------NGYWADI 200
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 5-272 1.85e-64

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: 206.34  E-value: 1.85e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452    5 LGMILAGGEGSRLMPLTESRTKPAVPFGGSYRLIDFALNNFVNADLMR-IYVLTQFKSQSLYLHMKKGWNVSsirdrfID 83
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKYPLIDYPLSRLANAGIREiIVILTQEHRFMLNELLGDGSKFG------VQ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452   84 CIPAQMRDGKrwyeGTADAIYQNLRFVEiSEADQVCIFGSDHIYKMDIRQMLDYHRRKEARLTVSALRMPLSQASQFGVI 163
Cdd:pfam00483  75 ITYALQPEGK----GTAPAVALAADFLG-DEKSDVLVLGGDHIYRMDLEQAVKFHIEKAADATVTFGIVPVEPPTGYGVV 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  164 EVDDEGRMVGFEEKPKNPKAIpgdpewALVSMGNYIFETETLcEELREDAALENSSHDFGKDIIPKMFPQGGVYVYDFst 243
Cdd:pfam00483 150 EFDDNGRVIRFVEKPKLPKAS------NYASMGIYIFNSGVL-DFLAKYLEELKRGEDEITDILPKALEDGKLAYAFI-- 220

                         250       260
                  ....*....|....*....|....*....
gi 520910452  244 nkikgeKESTYWRDVGTIESYWAAHMDLL 272
Cdd:pfam00483 221 ------FKGYAWLDVGTWDSLWEANLFLL 243
 
Name Accession Description Interval E-value
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 1-403 0e+00

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 761.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452   1 MTGVLGMILAGGEGSRLMPLTESRTKPAVPFGGSYRLIDFALNNFVNADLMRIYVLTQFKSQSLYLHMKKGWNVSSIRDR 80
Cdd:PRK00844   3 MPKVLAIVLAGGEGKRLMPLTADRAKPAVPFGGSYRLIDFVLSNLVNSGYLRIYVLTQYKSHSLDRHISQTWRLSGLLGN 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  81 FIDCIPAQMRDGKRWYEGTADAIYQNLRFVEISEADQVCIFGSDHIYKMDIRQMLDYHRRKEARLTVSALRMPLSQASQF 160
Cdd:PRK00844  83 YITPVPAQQRLGKRWYLGSADAIYQSLNLIEDEDPDYVVVFGADHVYRMDPRQMVDFHIESGAGVTVAAIRVPREEASAF 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 161 GVIEVDDEGRMVGFEEKPKNPKAIPGDPEWALVSMGNYIFETETLCEELREDAALENSSHDFGKDIIPKMFPQGGVYVYD 240
Cdd:PRK00844 163 GVIEVDPDGRIRGFLEKPADPPGLPDDPDEALASMGNYVFTTDALVDALRRDAADEDSSHDMGGDIIPRLVERGRAYVYD 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 241 FSTNKIKG--EKESTYWRDVGTIESYWAAHMDLLEKEPPFSLYNRSWPLHTYYPPLPPATFIDVGDKKVTITDSLVSGGS 318
Cdd:PRK00844 243 FSTNEVPGatERDRGYWRDVGTIDAYYDAHMDLLSVHPVFNLYNREWPIYTSSPNLPPAKFVDGGGRVGSAQDSLVSAGS 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 319 YIQGVKIYKSILGFRSNIAAGSLISESVILGDVKIGAGCTIKRAIIDKNVEIAPGTIIGEDLELDRQRFHVSDEGIVVIA 398
Cdd:PRK00844 323 IISGATVRNSVLSPNVVVESGAEVEDSVLMDGVRIGRGAVVRRAILDKNVVVPPGATIGVDLEEDRRRFTVSEGGIVVVP 402


                 ....*
gi 520910452 399 KGTKV 403
Cdd:PRK00844 403 KGQRV 407
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 4-401 0e+00

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 568.17  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452   4 VLGMILAGGEGSRLMPLTESRTKPAVPFGGSYRLIDFALNNFVNADLMRIYVLTQFKSQSLYLHMKKG--WNVSSIRDrF 81
Cdd:COG0448    2 VLAIILAGGRGSRLGPLTKDRAKPAVPFGGKYRIIDFPLSNCVNSGIRRVGVLTQYKSHSLNDHIGSGkpWDLDRKRG-G 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  82 IDCIPA-QMRDGKRWYEGTADAIYQNLRFVEISEADQVCIFGSDHIYKMDIRQMLDYHRRKEARLTVSALRMPLSQASQF 160
Cdd:COG0448   81 VFILPPyQQREGEDWYQGTADAVYQNLDFIERSDPDYVLILSGDHIYKMDYRQMLDFHIESGADITVACIEVPREEASRF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 161 GVIEVDDEGRMVGFEEKPKNPKaipgdpeWALVSMGNYIFETETLCEELREDAalENSSHDFGKDIIPKMFPQGGVYVYD 240
Cdd:COG0448  161 GVMEVDEDGRITEFEEKPKDPK-------SALASMGIYVFNKDVLIELLEEDA--PNSSHDFGKDIIPRLLDRGKVYAYE 231

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 241 FstnkiKGekestYWRDVGTIESYWAAHMDLLEKEPPFSLYNRSWPLHTYYPPLPPATFIDVGdkkvTITDSLVSGGSYI 320
Cdd:COG0448  232 F-----DG-----YWRDVGTIDSYYEANMDLLDPEPEFNLYDPEWPIYTKQKDLPPAKFVRGG----KVKNSLVSNGCII 297

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 321 QGvKIYKSILGFRSNIAAGSLISESVILGDVKIGAGCTIKRAIIDKNVEIAPGTIIGEDLELDRQRFHVSDeGIVVIAKG 400
Cdd:COG0448  298 SG-TVENSVLFRGVRVESGAVVENSVIMPGVVIGEGAVIENAIIDKNVVIPPGVVIGEDPEEDRKRFTVSS-GIVVVGKG 375


                 .
gi 520910452 401 T 401
Cdd:COG0448  376 A 376
glgC TIGR02091
glucose-1-phosphate adenylyltransferase; This enzyme, glucose-1-phosphate adenylyltransferase, ...
 6-378 0e+00

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: 553.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452    6 GMILAGGEGSRLMPLTESRTKPAVPFGGSYRLIDFALNNFVNADLMRIYVLTQFKSQSLYLHMKKGWNVSSIRDRFIDCI 85
Cdd:TIGR02091   1 AMVLAGGRGSRLSPLTKRRAKPAVPFGGKYRIIDFPLSNCINSGIRRIGVLTQYKSHSLNRHIQRGWDFDGFIDGFVTLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452   86 PAQMR-DGKRWYEGTADAIYQNLRFVEISEADQVCIFGSDHIYKMDIRQMLDYHRRKEARLTVSALRMPLSQASQFGVIE 164
Cdd:TIGR02091  81 PAQQReSGTDWYQGTADAVYQNLDLIEDYDPEYVLILSGDHIYKMDYEKMLDYHIESGADVTIACIPVPRKEASRFGVMQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  165 VDDEGRMVGFEEKPKNPKAIPGDPEWALVSMGNYIFETETLCEELREDAALENSSHDFGKDIIPKMFPQGGVYVYDFstn 244
Cdd:TIGR02091 161 VDEDGRIVDFEEKPANPPSIPGMPDFALASMGIYIFDKDVLKELLEEDADDPESSHDFGKDIIPRALEEGSVQAYLF--- 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  245 kikgekeSTYWRDVGTIESYWAAHMDLLEKEPPFSLYNRSWPLHTYYPPLPPATFIDVGDKkvtITDSLVSGGSYIQGVK 324
Cdd:TIGR02091 238 -------SGYWRDVGTIDSFWEANMDLVSVVPPFDLYDRKWPIYTYNEFLPPAKFVDSDAQ---VVDSLVSEGCIISGAT 307

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 520910452  325 IYKSILGFRSNIAAGSLISESVILGDVKIGAGCTIKRAIIDKNVEIAPGTIIGE 378
Cdd:TIGR02091 308 VSHSVLGIRVRIGSGSTVEDSVIMGDVGIGRGAVIRNAIIDKNVRIGEGVVIGN 361
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 5-397 0e+00

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 552.52  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452   5 LGMILAGGEGSRLMPLTESRTKPAVPFGGSYRLIDFALNNFVNADLMRIYVLTQFKSQSLYLHMKKGWN-VSSIRDRFID 83
Cdd:PRK00725  17 LALILAGGRGSRLKELTDKRAKPAVYFGGKFRIIDFALSNCINSGIRRIGVLTQYKAHSLIRHIQRGWSfFREELGEFVD 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  84 CIPAQMR-DGKRWYEGTADAIYQNLRFVEISEADQVCIFGSDHIYKMDIRQMLDYHRRKEARLTVSALRMPLSQASQFGV 162
Cdd:PRK00725  97 LLPAQQRvDEENWYRGTADAVYQNLDIIRRYDPKYVVILAGDHIYKMDYSRMLADHVESGADCTVACLEVPREEASAFGV 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 163 IEVDDEGRMVGFEEKPKNPKAIPGDPEWALVSMGNYIFETETLCEELREDAALENSSHDFGKDIIPKMFPQGGVYVYDFS 242
Cdd:PRK00725 177 MAVDENDRITAFVEKPANPPAMPGDPDKSLASMGIYVFNADYLYELLEEDAEDPNSSHDFGKDIIPKIVEEGKVYAHPFS 256

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 243 TNKIKGEKEST-YWRDVGTIESYWAAHMDLLEKEPPFSLYNRSWPLHTYYPPLPPATFI-DVGDKKVTITDSLVSGGSYI 320
Cdd:PRK00725 257 DSCVRSDPEEEpYWRDVGTLDAYWQANLDLASVTPELDLYDRNWPIWTYQEQLPPAKFVfDRSGRRGMAINSLVSGGCII 336

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 520910452 321 QGVKIYKSILGFRSNIAAGSLISESVILGDVKIGAGCTIKRAIIDKNVEIAPGTIIGEDLELDRQRFHVSDEGIVVI 397
Cdd:PRK00725 337 SGAVVRRSVLFSRVRVNSFSNVEDSVLLPDVNVGRSCRLRRCVIDRGCVIPEGMVIGEDPEEDAKRFRRSEEGIVLV 413
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 1-404 4.32e-134

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 389.23  E-value: 4.32e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452   1 MTGVLGMILAGGEGSRLMPLTESRTKPAVPFGGSYRLIDFALNNFVNADLMRIYVLTQFKSQSLYLHMKKG--WNvssir 78
Cdd:PRK05293   1 KKEMLAMILAGGQGTRLGKLTKNIAKPAVPFGGKYRIIDFTLSNCANSGIDTVGVLTQYQPLELNNHIGIGspWD----- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  79 drfIDCI--------PAQMRDGKRWYEGTADAIYQNLRFVEISEADQVCIFGSDHIYKMDIRQMLDYHRRKEARLTVSAL 150
Cdd:PRK05293  76 ---LDRInggvtilpPYSESEGGKWYKGTAHAIYQNIDYIDQYDPEYVLILSGDHIYKMDYDKMLDYHKEKEADVTIAVI 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 151 RMPLSQASQFGVIEVDDEGRMVGFEEKPKNPKAipgdpewALVSMGNYIFETETLCEELREDAALENSSHDFGKDIIPKM 230
Cdd:PRK05293 153 EVPWEEASRFGIMNTDENMRIVEFEEKPKNPKS-------NLASMGIYIFNWKRLKEYLIEDEKNPNSSHDFGKNVIPLY 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 231 FPQGG-VYVYDFstnkiKGekestYWRDVGTIESYWAAHMDLLEKEPPFSLYNRSWPLHTYYPPLPPAtFIDVGDKkvtI 309
Cdd:PRK05293 226 LEEGEkLYAYPF-----KG-----YWKDVGTIESLWEANMELLRPENPLNLFDRNWRIYSVNPNLPPQ-YIAENAK---V 291

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 310 TDSLVSGGSYIQGvKIYKSILGFRSNIAAGSLISESVILGDVKIGAGCTIKRAIIDKNVEIAPGTIIGEdleldrqrfhv 389
Cdd:PRK05293 292 KNSLVVEGCVVYG-TVEHSVLFQGVQVGEGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVIIGG----------- 359

                        410
                 ....*....|....*
gi 520910452 390 SDEGIVVIAKGTKVG 404
Cdd:PRK05293 360 GKEVITVIGENEVIG 374
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 1-401 1.22e-115

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 343.79  E-value: 1.22e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452   1 MTGVLGMILAGGEGSRLMPLTESRTKPAVPFGGSYRLIDFALNNFVNADLMRIYVLTQFKSQSLYLHMKKGWNVSSIRDR 80
Cdd:PRK02862   1 MKRVLAIILGGGAGTRLYPLTKLRAKPAVPLAGKYRLIDIPISNCINSGINKIYVLTQFNSASLNRHISQTYNFDGFSGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  81 FIDCIPA-QMRDGKRWYEGTADAIYQNLRFVEISEADQVCIFGSDHIYKMDIRQMLDYHRRKEARLTVSALRMPLSQASQ 159
Cdd:PRK02862  81 FVEVLAAqQTPENPSWFQGTADAVRKYLWHFQEWDVDEYLILSGDQLYRMDYRLFVQHHRETGADITLAVLPVDEKDASG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 160 FGVIEVDDEGRMVGFEEKPK---------NPKAIPGDPEWA-----LVSMGNYIFETETLCEELREDAalenSSHDFGKD 225
Cdd:PRK02862 161 FGLMKTDDDGRITEFSEKPKgdelkamavDTSRLGLSPEEAkgkpyLASMGIYVFSRDVLFDLLNKNP----EYTDFGKE 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 226 IIPKMFPQGGVYVYDFstnkikgekeSTYWRDVGTIESYWAAHMDL-LEKEPPFSLYNRSWPLHTYYPPLPPATFIDvgd 304
Cdd:PRK02862 237 IIPEAIRDYKVQSYLF----------DGYWEDIGTIEAFYEANLALtQQPNPPFSFYDEKAPIYTRARYLPPSKLLD--- 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 305 kkVTITDSLVSGGSYIQGVKIYKSILGFRSNIAAGSLISESVILG-------------------DVKIGAGCTIKRAIID 365
Cdd:PRK02862 304 --ATITESIIAEGCIIKNCSIHHSVLGIRSRIESGCTIEDTLVMGadfyesseereelrkegkpPLGIGEGTTIKRAIID 381

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|.
gi 520910452 366 KNVEIAPG-TIIGEDL--ELDR--QRFHVSDeGIVVIAKGT 401
Cdd:PRK02862 382 KNARIGNNvRIVNKDNveEADRedQGFYIRD-GIVVVVKNA 421
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 1-401 4.80e-107

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 322.19  E-value: 4.80e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452   1 MTGVLGMILAGGEGSRLMPLTESRTKPAVPFGGSYRLIDFALNNFVNADLMRIYVLTQFKSQSLYLHMKKGWNVSS---I 77
Cdd:PLN02241   1 PKSVAAIILGGGAGTRLFPLTKRRAKPAVPIGGNYRLIDIPMSNCINSGINKIYVLTQFNSASLNRHLSRAYNFGNggnF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  78 RDRFIDCIPA-QMRDGKRWYEGTADAIYQ--------NLRFVEIseadqVCIFGSDHIYKMDIRQMLDYHRRKEARLTVS 148
Cdd:PLN02241  81 GDGFVEVLAAtQTPGEKGWFQGTADAVRQflwlfedaKNKNVEE-----VLILSGDHLYRMDYMDFVQKHRESGADITIA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 149 ALRMPLSQASQFGVIEVDDEGRMVGFEEKPKNP--------KAIPG-DPEWA-----LVSMGNYIFETETLCEELREDaa 214
Cdd:PLN02241 156 CLPVDESRASDFGLMKIDDTGRIIEFSEKPKGDelkamqvdTTVLGlSPEEAkekpyIASMGIYVFKKDVLLKLLRWR-- 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 215 lENSSHDFGKDIIPKMFPQG-GVYVYDFstnkikgekeSTYWRDVGTIESYWAAHMDLLEKEPPFSLYNRSWPLHTYYPP 293
Cdd:PLN02241 234 -FPTANDFGSEIIPGAIKEGyNVQAYLF----------DGYWEDIGTIKSFYEANLALTKQPPKFSFYDPDAPIYTSPRF 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 294 LPPATFIDvgdkkVTITDSLVSGGSYIQGVKIYKSILGFRSNIAAGSLISESVILGD-------------------VKIG 354
Cdd:PLN02241 303 LPPSKIED-----CRITDSIISHGCFLRECKIEHSVVGLRSRIGEGVEIEDTVMMGAdyyeteeeiasllaegkvpIGIG 377

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|..
gi 520910452 355 AGCTIKRAIIDKNVEIAPG-TIIGED--LELDR--QRFHVSDeGIVVIAKGT 401
Cdd:PLN02241 378 ENTKIRNAIIDKNARIGKNvVIINKDgvQEADReeEGYYIRS-GIVVILKNA 428
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 6-258 5.17e-87

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: 262.48  E-value: 5.17e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452   6 GMILAGGEGSRLMPLTESRTKPAVPFGGSYRLIDFALNNFVNADLMRIYVLTQFKSQSLYLHMKKGWNVSSIR-DRFIDC 84
Cdd:cd02508    1 AIILAGGEGTRLSPLTKKRAKPAVPFGGRYRLIDFPLSNMVNSGIRNVGVLTQYKSRSLNDHLGSGKEWDLDRkNGGLFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  85 IPAQMRDGKRWYEGTADAIYQNLRFVEISEADQVCIFGSDHIYKMDIRQMLDYHRRKEARLTVSalrmplsqasqfgvie 164
Cdd:cd02508   81 LPPQQRKGGDWYRGTADAIYQNLDYIERSDPEYVLILSGDHIYNMDYREMLDFHIESGADITVV---------------- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 165 vddegrmvgfeekpknpkaipgdpewALVSMGNYIFETETLCEELREDAAleNSSHDFGKDIIPKMFPQGGVYVYDFstn 244
Cdd:cd02508  145 --------------------------YKASMGIYIFSKDLLIELLEEDAA--DGSHDFGKDIIPAMLKKLKIYAYEF--- 193

                        250
                 ....*....|....
gi 520910452 245 kikgekeSTYWRDV 258
Cdd:cd02508  194 -------NGYWADI 200
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 5-272 1.85e-64

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: 206.34  E-value: 1.85e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452    5 LGMILAGGEGSRLMPLTESRTKPAVPFGGSYRLIDFALNNFVNADLMR-IYVLTQFKSQSLYLHMKKGWNVSsirdrfID 83
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKYPLIDYPLSRLANAGIREiIVILTQEHRFMLNELLGDGSKFG------VQ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452   84 CIPAQMRDGKrwyeGTADAIYQNLRFVEiSEADQVCIFGSDHIYKMDIRQMLDYHRRKEARLTVSALRMPLSQASQFGVI 163
Cdd:pfam00483  75 ITYALQPEGK----GTAPAVALAADFLG-DEKSDVLVLGGDHIYRMDLEQAVKFHIEKAADATVTFGIVPVEPPTGYGVV 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  164 EVDDEGRMVGFEEKPKNPKAIpgdpewALVSMGNYIFETETLcEELREDAALENSSHDFGKDIIPKMFPQGGVYVYDFst 243
Cdd:pfam00483 150 EFDDNGRVIRFVEKPKLPKAS------NYASMGIYIFNSGVL-DFLAKYLEELKRGEDEITDILPKALEDGKLAYAFI-- 220

                         250       260
                  ....*....|....*....|....*....
gi 520910452  244 nkikgeKESTYWRDVGTIESYWAAHMDLL 272
Cdd:pfam00483 221 ------FKGYAWLDVGTWDSLWEANLFLL 243
glgD TIGR02092
glucose-1-phosphate adenylyltransferase, GlgD subunit; This family is GlgD, an apparent ...
 8-403 9.88e-51

glucose-1-phosphate adenylyltransferase, GlgD subunit; This family is GlgD, an apparent regulatory protein that appears in an alpha2/beta2 heterotetramer with GlgC (glucose-1-phosphate adenylyltransferase, TIGR02091) in a subset of bacteria that use GlgC for glycogen biosynthesis. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 273966 [Multi-domain]  Cd Length: 369  Bit Score: 174.49  E-value: 9.88e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452    8 ILAGGEGSRLM-PLTESRTKPAVPFGGSYRLIDFALNNFVNADLMRIYVLTQFKS-QSLYLHMKKG--WNVSSIRDR-FI 82
Cdd:TIGR02092   6 IINLTESSKNLsPLTKVRPLASLPFGGRYRLIDFPLSNMVNAGIRNVFIFFKNKErQSLFDHLGSGreWDLHRKRDGlFV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452   83 dcIPAQMRDgkRWYEGTADAIYQNLRFVEISEADQVCIFGSDHIYKMDIRQMLDYHRRKEARLTVSALRM-PLSQASQFG 161
Cdd:TIGR02092  86 --FPYNDRD--DLSEGGKRYFSQNLEFLKRSTSEYTVVLNSHMVCNIDLKAVLKYHEETGKDITVVYKKVkPADASEYDT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  162 VIEVDDEGRMvgfeekpKNPKAIPGDPEWALVSMGNYIFETETLCEELREdaALENSSHDFGKDIIPKMFPQGGVYVYDF 241
Cdd:TIGR02092 162 ILRFDESGKV-------KSIGQNLNPEEEENISLDIYIVSTDLLIELLYE--CIQRGKLTSLEELIRENLKELNINAYEY 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  242 stnkiKGekestYWRDVGTIESYWAAHMDLLEKEPPFSL-YNRSWPLHTYYPPLPPATFIdvgdKKVTITDSLVSGGSYI 320
Cdd:TIGR02092 233 -----TG-----YLANINSVKSYYKANMDLLDPQNFQSLfYSSQGPIYTKVKDEPPTYYA----ENSKVENSLVANGCII 298

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  321 QGvKIYKSILGFRSNIAAGSLISESVILGDVKIGAGCTIKRAIIDKNVEIAPGT-IIGedleldrqrfhvSDEGIVVIAK 399
Cdd:TIGR02092 299 EG-KVENSILSRGVHVGKDALIKNCIIMQRTVIGEGAHLENVIIDKDVVIEPNVkIAG------------TSEQPLVISK 365


                  ....
gi 520910452  400 GTKV 403
Cdd:TIGR02092 366 GTVV 369
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 7-277 1.76e-40

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: 143.75  E-value: 1.76e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452   7 MILAGGEGSRLMPLTESRTKPAVPFGGsyR-LIDFALNNFVNADLMRIYVLTQFKSQSLYLHMKKG--WNVSsirdrfID 83
Cdd:COG1208    3 VILAGGLGTRLRPLTDTRPKPLLPVGG--KpLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGsrFGVR------IT 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  84 CIpaqmRDGKRWyeGTADAIYQNLRFVeisEADQVCIFGSDHIYKMDIRQMLDYHRRKEARLTVSALRMPlsQASQFGVI 163
Cdd:COG1208   75 YV----DEGEPL--GTGGALKRALPLL---GDEPFLVLNGDILTDLDLAALLAFHREKGADATLALVPVP--DPSRYGVV 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 164 EVDDEGRMVGFEEKPKNPKAipgdpewALVSMGNYIFETETLcEELREDAALensshDFGkDIIPKMFPQGGVYVYdfst 243
Cdd:COG1208  144 ELDGDGRVTRFVEKPEEPPS-------NLINAGIYVLEPEIF-DYIPEGEPF-----DLE-DLLPRLIAEGRVYGY---- 205

                        250       260       270
                 ....*....|....*....|....*....|....
gi 520910452 244 nKIKGekestYWRDVGTIESYWAAHMDLLEKEPP 277
Cdd:COG1208  206 -VHDG-----YWLDIGTPEDLLEANALLLSGKAP 233
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 6-259 2.75e-39

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: 140.02  E-value: 2.75e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452   6 GMILAGGEGSRLMPLTESRTKPAVPFGGsYRLIDFALNNFVNADLMRIYVLTQFKSQSLYLHMKKG--WNVSsirdrfID 83
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAG-KPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGskFGVN------IE 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  84 CIpaqmRDGKRWyeGTADAIYQNLRFveISEADQVCIFGsDHIYKMDIRQMLDYHRRKEARLTVSALRMPlsQASQFGVI 163
Cdd:cd04181   74 YV----VQEEPL--GTAGAVRNAEDF--LGDDDFLVVNG-DVLTDLDLSELLRFHREKGADATIAVKEVE--DPSRYGVV 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 164 EVDDEGRMVGFEEKPKnpkaipgDPEWALVSMGNYIFETETLcEELREDaalENSSHDFGKDIIPKMFPQGGVYVYDFst 243
Cdd:cd04181  143 ELDDDGRVTRFVEKPT-------LPESNLANAGIYIFEPEIL-DYIPEI---LPRGEDELTDAIPLLIEEGKVYGYPV-- 209

                        250
                 ....*....|....*.
gi 520910452 244 nkikgekeSTYWRDVG 259
Cdd:cd04181  210 --------DGYWLDIG 217
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 308-403 2.82e-37

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: 130.66  E-value: 2.82e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 308 TITDSLVSGGSYIQGVKIYKSILGFRSNIAAGSLISESVILGDVKIGAGCTIKRAIIDKNVEIAPGTIIGEDLELDRQRF 387
Cdd:cd04651    9 EVKNSLVSEGCIISGGTVENSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIIDKNVVIPDGVVIGGDPEEDRARF 88

                         90
                 ....*....|....*.
gi 520910452 388 HVSDEGIVVIAKGTKV 403
Cdd:cd04651   89 YVTEDGIVVVGKGMVI 104
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 7-268 2.14e-20

WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is involved in the biosynthesis, export or translocation of capsule. It is a subfamily of nucleotidyl transferases that transfer nucleotides onto phosphosugars.


Pssm-ID: 133065 [Multi-domain]  Cd Length: 223  Bit Score: 88.76  E-value: 2.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452   7 MILAGGEGSRLMPLTESRTKPAVPFGGsYRLIDFALNNFVNADLMRIYVLTQFKSQslylhmkkgwnvsSIRDRFIDCIP 86
Cdd:cd06915    2 VILAGGLGTRLRSVVKDLPKPLAPVAG-RPFLEYLLEYLARQGISRIVLSVGYLAE-------------QIEEYFGDGYR 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  87 AQMRdgkRWYE------GTADAIYQNLRFVeisEADQVCIFGSDHIYKMDIRQMLDYHRRKEARLTVSALRMPlsQASQF 160
Cdd:cd06915   68 GGIR---IYYViepeplGTGGAIKNALPKL---PEDQFLVLNGDTYFDVDLLALLAALRASGADATMALRRVP--DASRY 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 161 GVIEVDDEGRMVGFEEKPKNPKAipgdpewALVSMGNYIFETETLCEELREDAALENsshdfgkDIIPKMFPQGGVYVYd 240
Cdd:cd06915  140 GNVTVDGDGRVIAFVEKGPGAAP-------GLINGGVYLLRKEILAEIPADAFSLEA-------DVLPALVKRGRLYGF- 204

                        250       260
                 ....*....|....*....|....*...
gi 520910452 241 fstnkikgeKESTYWRDVGTIESYWAAH 268
Cdd:cd06915  205 ---------EVDGYFIDIGIPEDYARAQ 223
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 4-273 1.95e-17

G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose.


Pssm-ID: 133032 [Multi-domain]  Cd Length: 236  Bit Score: 81.08  E-value: 1.95e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452   4 VLGMILAGGEGSRLMPLTESRTKPAVPFGGSyRLIDFALNNFVNADLMRIYVLtqfksqslylhmkkgwnVSSIRDRfid 83
Cdd:cd04189    1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGK-PIIQYAIEDLREAGIEDIGIV-----------------VGPTGEE--- 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  84 cIPAQMRDGKRW-----Y------EGTADAIYQNLRFVEISeaDQVCIFGsDHIYKMDIRQMLDYHRrkEARLTVSALRM 152
Cdd:cd04189   60 -IKEALGDGSRFgvritYilqeepLGLAHAVLAARDFLGDE--PFVVYLG-DNLIQEGISPLVRDFL--EEDADASILLA 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 153 PLSQASQFGVIEVDDeGRMVGFEEKPKNPkaiPGDpeWALVsmGNYIFeTETLCEELREdaaLENSSHdfGK----DIIP 228
Cdd:cd04189  134 EVEDPRRFGVAVVDD-GRIVRLVEKPKEP---PSN--LALV--GVYAF-TPAIFDAISR---LKPSWR--GEleitDAIQ 199

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 520910452 229 KMFPQGGvyvydfstnKIKGEKESTYWRDVGTIEsywaahmDLLE 273
Cdd:cd04189  200 WLIDRGR---------RVGYSIVTGWWKDTGTPE-------DLLE 228
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 7-268 2.14e-17

NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133048 [Multi-domain]  Cd Length: 220  Bit Score: 80.25  E-value: 2.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452   7 MILAGGEGSRLMPLTESRTKPAVPFGGSyRLIDFALNNFVNADLMRIYVLTQFKSqslylHMkkgwnvssIRDRFidcip 86
Cdd:cd06426    2 VIMAGGKGTRLRPLTENTPKPMLKVGGK-PILETIIDRFIAQGFRNFYISVNYLA-----EM--------IEDYF----- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  87 aqmRDGKRW-------YE----GTADAiyqnLRFVEISEADQVCIFGSDHIYKMDIRQMLDYHRRKEARLTVSA----LR 151
Cdd:cd06426   63 ---GDGSKFgvnisyvREdkplGTAGA----LSLLPEKPTDPFLVMNGDILTNLNYEHLLDFHKENNADATVCVreyeVQ 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 152 MPlsqasqFGVIEVDDeGRMVGFEEKPKNPKaipgdpewaLVSMGNYIFETETLceelredaalensshdfgkDIIPKmf 231
Cdd:cd06426  136 VP------YGVVETEG-GRITSIEEKPTHSF---------LVNAGIYVLEPEVL-------------------DLIPK-- 178

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 520910452 232 pqgGVYvYDFST--NKIKGEKEST-------YWRDVGTIESYWAAH 268
Cdd:cd06426  179 ---NEF-FDMPDliEKLIKEGKKVgvfpiheYWLDIGRPEDYEKAN 220
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 6-403 3.27e-17

glucose-1-phosphate thymidylylransferase, long form; The family of known and putative glucose-1-phosphate thymidyltransferase (also called dTDP-glucose synthase) shows a deep split into a short form (see TIGR01207) and a long form described by this model. The homotetrameric short form is found in numerous bacterial species that incorporate dTDP-L-rhamnose, which it helps synthesize, into the cell wall. It is subject to feedback inhibition. This form, in contrast, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced. Alternate name: dTDP-D-glucose synthase


Pssm-ID: 273500 [Multi-domain]  Cd Length: 353  Bit Score: 82.06  E-value: 3.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452    6 GMILAGGEGSRLMPLTESRTKPAVPFGGSyRLIDFALNNFVNADLMRIYVLtqfksqslylhmkkgwnvssIRDRFIDCI 85
Cdd:TIGR01208   2 ALILAAGKGTRLRPLTFTRPKQLIPVANK-PILQYAIEDLAEAGITDIGIV--------------------VGPVTGEEI 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452   86 PAQMRDGKRW-----------YEGTADAIYQNLRFVEiseADQVCIFGSDHIYKMDIRQMLDyhRRKEARLTVSALRMPL 154
Cdd:TIGR01208  61 KEIVGEGERFgakityivqgePLGLAHAVYTARDFLG---DDDFVVYLGDNLIQDGISRFVK--SFEEKDYDALILLTKV 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  155 SQASQFGVIEVDDEGRMVGFEEKPKNPkaiPGDpeWALVsmGNYIFeTETLCEELREdaaLENSSHdfGK----DIIPKM 230
Cdd:TIGR01208 136 RDPTAFGVAVLEDGKRILKLVEKPKEP---PSN--LAVV--GLYMF-RPLIFEAIKN---IKPSWR--GEleitDAIQWL 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  231 FPQGgvyvYDFSTNKIKGekestYWRDVGTIEsywaahmDLLEKeppfslyNRswplhtyypplppaTFIDVGDKKVtit 310
Cdd:TIGR01208 203 IEKG----YKVGGSKVTG-----WWKDTGKPE-------DLLDA-------NR--------------LILDEVEREV--- 242

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  311 dslvsggsyiQGVKIYKSILGfRSNIAAGSLISESVILGDVKIGAGCTIKRAIIDKNVEIAPGTIIgEDLELDRQrfhVS 390
Cdd:TIGR01208 243 ----------QGVDDESKIRG-RVVVGEGAKIVNSVIRGPAVIGEDCIIENSYIGPYTSIGEGVVI-RDAEVEHS---IV 307

                         410
                  ....*....|...
gi 520910452  391 DEGIVVIAKGTKV 403
Cdd:TIGR01208 308 LDESVIEGVQARI 320
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
6-263 7.77e-14

dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 71.27  E-value: 7.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452   6 GMILAGGEGSRLMPLTESRTKPAVPFGG---SYRLIDfalnnfvnaDLMRiyvltqfksqslylhmkkgwnvSSIRD--- 79
Cdd:COG1209    3 GIILAGGSGTRLRPLTLTVSKQLLPVYDkpmIYYPLS---------TLML----------------------AGIREili 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  80 ----RFIDCIPAQMRDGKRW-----Y------EGTADAIYQNLRFVEiseADQVCIFGSDHIYKMD-IRQMLDYHRRKEA 143
Cdd:COG1209   52 istpEDGPQFERLLGDGSQLgikisYavqpepLGLAHAFIIAEDFIG---GDPVALVLGDNIFYGDgLSELLREAAARES 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 144 RLTVSALRmpLSQASQFGVIEVDDEGRMVGFEEKPKNPKaipgdPEWALVsmGNYIFeTETLCEELREdaaLENSSHdfG 223
Cdd:COG1209  129 GATIFGYK--VEDPERYGVVEFDEDGRVVSLEEKPKEPK-----SNLAVT--GLYFY-DNDVVEIAKN---LKPSAR--G 193

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 520910452 224 K----DIIPKMFPQGGVYVYDFSTNkikgekesTYWRDVGTIES 263
Cdd:COG1209  194 EleitDANQAYLERGKLVVELLGRG--------FAWLDTGTHES 229
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 7-264 1.11e-13

N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain and a C-terminal Lefthanded-beta-Helix fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes, such as cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133047 [Multi-domain]  Cd Length: 233  Bit Score: 69.93  E-value: 1.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452   7 MILAGGEGSRLMPLTESRTKPAVPFGGSyRLIDFALNNFVNADLMRIYVLTQFKSQSLYLHMKKGWNVSSIRdrfIDCI- 85
Cdd:cd06425    4 LILVGGYGTRLRPLTLTVPKPLVEFCNK-PMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKKLGIK---ITFSi 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  86 ---PAqmrdgkrwyeGTADAIYQNLRFVEiSEADQVCIFGSDHIYKMDIRQMLDYHRRKEARLTVSALRmpLSQASQFGV 162
Cdd:cd06425   80 etePL----------GTAGPLALARDLLG-DDDEPFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTK--VEDPSKYGV 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 163 IEVD-DEGRMVGFEEKPKNPKaipGDpewaLVSMGNYIFETETLceelrEDAALENSShdFGKDIIPKMFPQGGVYVYDf 241
Cdd:cd06425  147 VVHDeNTGRIERFVEKPKVFV---GN----KINAGIYILNPSVL-----DRIPLRPTS--IEKEIFPKMASEGQLYAYE- 211

                        250       260
                 ....*....|....*....|...
gi 520910452 242 stnkIKGekestYWRDVGTIESY 264
Cdd:cd06425  212 ----LPG-----FWMDIGQPKDF 225
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 6-186 5.10e-13

G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is the short form of glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.


Pssm-ID: 133019 [Multi-domain]  Cd Length: 240  Bit Score: 68.37  E-value: 5.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452   6 GMILAGGEGSRLMPLTESRTKPAVPFGgSYRLIDFALNNFVNADLMRIYVLTQFKSQSLYLHMkkgwnvssirdrfidci 85
Cdd:cd02538    3 GIILAGGSGTRLYPLTKVVSKQLLPVY-DKPMIYYPLSTLMLAGIREILIISTPEDLPLFKEL----------------- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  86 paqMRDGKRW-----YE------GTADAIYQNLRFVEiseADQVC-IFGSDHIYKMDIRQMLDYHRRKEARLTVsaLRMP 153
Cdd:cd02538   65 ---LGDGSDLgiritYAvqpkpgGLAQAFIIGEEFIG---DDPVClILGDNIFYGQGLSPILQRAAAQKEGATV--FGYE 136

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 520910452 154 LSQASQFGVIEVDDEGRMVGFEEKPKNPK---AIPG 186
Cdd:cd02538  137 VNDPERYGVVEFDENGRVLSIEEKPKKPKsnyAVTG 172
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 7-267 6.77e-10

NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133044 [Multi-domain]  Cd Length: 221  Bit Score: 58.74  E-value: 6.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452   7 MILAGGEGSRLMPLTESRTKPAVPFGGSyRLIDFALNNFVNADLMRIYVltqfksqslylhmkkgwNVSSIRDRFIDCIP 86
Cdd:cd06422    3 MILAAGLGTRMRPLTDTRPKPLVPVAGK-PLIDHALDRLAAAGIRRIVV-----------------NTHHLADQIEAHLG 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  87 AQmRDGKRW---YE-----GTADAIYQNLRFVeisEADQVCIFGSDHIYKMDIRQMLDYHRRKEARLTVSALRMPLSQAS 158
Cdd:cd06422   65 DS-RFGLRItisDEpdellETGGGIKKALPLL---GDEPFLVVNGDILWDGDLAPLLLLHAWRMDALLLLLPLVRNPGHN 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 159 QFGVIEVDDEGRMVGFEEKPKNPkaipgdpewaLVSMGNYIFETEtLCEELREDAAlenSSHDFGKDIIPKMFPQGGVYv 238
Cdd:cd06422  141 GVGDFSLDADGRLRRGGGGAVAP----------FTFTGIQILSPE-LFAGIPPGKF---SLNPLWDRAIAAGRLFGLVY- 205

                        250       260
                 ....*....|....*....|....*....
gi 520910452 239 ydfstnkikgekeSTYWRDVGTIESYWAA 267
Cdd:cd06422  206 -------------DGLWFDVGTPERLLAA 221
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 322-379 1.91e-09

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: 53.78  E-value: 1.91e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 520910452 322 GVKIYKSILGFRSNIAAGSLISESVILGDVKIGAGCTIKRAIIDKNVEIAPG------TIIGED 379
Cdd:cd03356   11 NAIIKNSVIGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENvrvvnlCIIGDD 74
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 7-262 3.67e-09

Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 56.47  E-value: 3.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452   7 MILAGGEGSRLMPLTESRTKPAVPFGGSyRLIDFALNNFVNADLMRIYVLTQFKSQSLYLHMKKGWNVssirdRFIdcip 86
Cdd:cd02523    2 IILAAGRGSRLRPLTEDRPKCLLEINGK-PLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPNI-----KFV---- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  87 aqmrDGKRWYE-GTADAIYQNLRFVEiseaDQVCIFGSDHIYKMDIRQMLDYHRRKEArltvsALRMPLSQASQFGVIEV 165
Cdd:cd02523   72 ----YNPDYAEtNNIYSLYLARDFLD----EDFLLLEGDVVFDPSILERLLSSPADNA-----ILVDKKTKEWEDEYVKD 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 166 -DDEGRMVGFEEKPKNPKAIPGdpewalVSMGNYIFETET---LCEELRE--DAALENSSHDfgkDIIPKMFPQGGVYVY 239
Cdd:cd02523  139 lDDAGVLLGIISKAKNLEEIQG------EYVGISKFSPEDadrLAEALEEliEAGRVNLYYE---DALQRLISEEGVKVK 209

                        250       260
                 ....*....|....*....|...
gi 520910452 240 DFSTNKikgekestyWRDVGTIE 262
Cdd:cd02523  210 DISDGF---------WYEIDDLE 223
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 7-183 1.13e-08

G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; Alpha-D-Glucose-1-phosphate Cytidylyltransferase catalyzes the production of CDP-D-Glucose from alpha-D-Glucose-1-phosphate and MgCTP as substrate. CDP-D-Glucose is the precursor for synthesizing four of the five naturally occurring 3,6-dideoxy sugars-abequose (3,6-dideoxy-D-Xylo-hexose), ascarylose (3,6-dideoxy-L-arabino-hexose), paratose (3,6-dideoxy-D-ribohexose), and tyvelose (3,6-dideoxy-D-arabino-hexose. Deoxysugars are ubiquitous in nature where they function in a variety of biological processes, including cell adhesion, immune response, determination of ABO blood groups, fertilization, antibiotic function, and microbial pathogenicity.


Pssm-ID: 133015 [Multi-domain]  Cd Length: 253  Bit Score: 55.66  E-value: 1.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452   7 MILAGGEGSRLMPLTESRTKPAVPFGG------------SYRLIDFAL----------NNFVNADLMRIYVLTQFKSQSL 64
Cdd:cd02524    2 VILAGGLGTRLSEETELKPKPMVEIGGrpilwhimkiysHYGHNDFILclgykghvikEYFLNYFLHNSDVTIDLGTNRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  65 YLHMKK--GWNVSsirdrFIDCipaqmrdgkrwyeGTADAIYQNLRFVE--ISEADQVCIFGSDHIYKMDIRQMLDYHRR 140
Cdd:cd02524   82 ELHNSDieDWKVT-----LVDT-------------GLNTMTGGRLKRVRryLGDDETFMLTYGDGVSDVNINALIEFHRS 143

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 520910452 141 KEARLTVSALRMPlsqaSQFGVIEVDDEGRMVGFEEKPKNPKA 183
Cdd:cd02524  144 HGKLATVTAVHPP----GRFGELDLDDDGQVTSFTEKPQGDGG 182
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
6-61 5.33e-08

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 53.32  E-value: 5.33e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 520910452   6 GMILAGGEGSRLMPLTESRTKPAVPFGGSyRLIDFALNNFVNADLMRIYVLTQFKS 61
Cdd:COG1213    2 AVILAAGRGSRLGPLTDDIPKCLVEIGGK-TLLERQLEALAAAGIKDIVVVTGYKA 56
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 6-183 1.44e-07

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 52.75  E-value: 1.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452   6 GMILAGGEGSRLMPLTESRTKPAVPFGGSyRLIDFALNNFVNADLMRIYVLTQFKSQSLYLHMkkgwnvssirdrfidci 85
Cdd:PRK15480   6 GIILAGGSGTRLYPVTMAVSKQLLPIYDK-PMIYYPLSTLMLAGIRDILIISTPQDTPRFQQL----------------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  86 paqMRDGKRW-------YEGTADAIYQNLRFVE--ISEADQVCIFGSDHIYKMDIRQMLDYHRRKEARLTVSALRmpLSQ 156
Cdd:PRK15480  68 ---LGDGSQWglnlqykVQPSPDGLAQAFIIGEefIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYH--VND 142

                        170       180
                 ....*....|....*....|....*..
gi 520910452 157 ASQFGVIEVDDEGRMVGFEEKPKNPKA 183
Cdd:PRK15480 143 PERYGVVEFDQNGTAISLEEKPLQPKS 169
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 313-377 5.86e-07

eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 46.80  E-value: 5.86e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 520910452 313 LVSGGSYI-QGVKIYKSILGFRSNIAAGSLISESVILGDVKIGAGCTIKRAI------IDKNVEIAPGTIIG 377
Cdd:cd05787    1 VIGRGTSIgEGTTIKNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIvadgavIGKGCTIPPGSLIS 72
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 287-379 1.95e-06

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 49.25  E-value: 1.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 287 LHTYYPPLPPATFID---VGDKKVTITDSLVSG-GSYI-QGVKIyksilGFRSNIAAGSLISESVILG-DVKIGAGCTI- 359
Cdd:COG1044   86 LQLFYPPPAPAPGIHpsaVIDPSAKIGEGVSIGpFAVIgAGVVI-----GDGVVIGPGVVIGDGVVIGdDCVLHPNVTIy 160

                         90       100
                 ....*....|....*....|
gi 520910452 360 KRAIIDKNVEIAPGTIIGED 379
Cdd:COG1044  161 ERCVIGDRVIIHSGAVIGAD 180
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 341-383 4.36e-06

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 48.48  E-value: 4.36e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 520910452 341 LISESVILGD-VKIGAGCTIKRAIIDKNVEIAPGTIIgEDLELD 383
Cdd:PRK09451 279 IIEGNVTLGNrVKIGAGCVLKNCVIGDDCEISPYSVV-EDANLG 321
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 332-404 9.07e-06

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 47.32  E-value: 9.07e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 520910452 332 FRSNIAAGSLISESVILG-DVKIGAGCTI-KRAIIDKNVEIAPGTIIGEDLEL-DRQRFHVSdegiVVIAKGTKVG 404
Cdd:COG1044   95 PAPGIHPSAVIDPSAKIGeGVSIGPFAVIgAGVVIGDGVVIGPGVVIGDGVVIgDDCVLHPN----VTIYERCVIG 166
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 329-404 1.80e-05

eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 42.57  E-value: 1.80e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 520910452 329 ILGFRSNIAAGSLISESVILGDVKIGAGCTIKRAIIDKNVEIAPGTIIGEDLeldrqrfhVSDEgiVVIAKGTKVG 404
Cdd:cd05787    1 VIGRGTSIGEGTTIKNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSI--------VADG--AVIGKGCTIP 66
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 8-147 3.47e-05

The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 44.57  E-value: 3.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452   8 ILAGGEGSRLMPLTESRTKPAVPFGGsYRLIDFALNNFVNADLMRIYVLTQFKSQ-SLYLHMKKGWNVSSIRDRFIDCIP 86
Cdd:cd04198    5 ILAGGGGSRLYPLTDNIPKALLPVAN-KPMIWYPLDWLEKAGFEDVIVVVPEEEQaEISTYLRSFPLNLKQKLDEVTIVL 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520910452  87 AQmrdgkrwYEGTADAiyqnLRFVEISEADQVCIFGSDHIYKMDIRQMLDYHRRKEARLTV 147
Cdd:cd04198   84 DE-------DMGTADS----LRHIRKKIKKDFLVLSCDLITDLPLIELVDLHRSHDASLTV 133
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
334-403 3.84e-05

acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 44.70  E-value: 3.84e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 520910452 334 SNIAAGSLISESVILG-DVKIGAGCtikraIIDKNVEIAPGTIIGEdleldrqrfHVSDEGIVVIAKGTKV 403
Cdd:PRK05289   3 AKIHPTAIVEPGAKIGeNVEIGPFC-----VIGPNVVIGDGTVIGS---------HVVIDGHTTIGKNNRI 59
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 334-404 1.21e-04

Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane/envelope biogenesis]; Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 43.47  E-value: 1.21e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 520910452 334 SNIAAGSLISESVILG-DVKIGAGCtikraIIDKNVEIAPGTIIGEdleldrqrfHVSDEGIVVIAKGTKVG 404
Cdd:COG1043    2 AMIHPTAIVDPGAKLGeNVEIGPFC-----VIGPDVEIGDGTVIGS---------HVVIEGPTTIGKNNRIF 59
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 287-379 1.33e-04

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 43.59  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 287 LHTYYPPLPP--ATFID---VGDKKVTITDSLVSG-GSYI-QGVKIyksilGFRSNIAAGSlisesVILGDVKIGAGCTI 359
Cdd:PRK00892  88 AQLFDPPATPspAAGIHpsaVIDPSAKIGEGVSIGpNAVIgAGVVI-----GDGVVIGAGA-----VIGDGVKIGADCRL 157

                         90       100
                 ....*....|....*....|....*..
gi 520910452 360 K-------RAIIDKNVEIAPGTIIGED 379
Cdd:PRK00892 158 HanvtiyhAVRIGNRVIIHSGAVIGSD 184
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 8-182 1.53e-04

The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; N-terminal domain of eEIF-2B epsilon and gamma, subunits of eukaryotic translation initiators, is a subfamily of glycosyltranferase 2 and is predicted to have glycosyltranferase activity. eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133001 [Multi-domain]  Cd Length: 216  Bit Score: 42.63  E-value: 1.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452   8 ILAGGEGSRLMPLTESRTKPAVPFGGsYRLIDFALNNFVNADLMRIYVLTQFKSQSL--YLHMKKGWNVSSIRDRFIDCI 85
Cdd:cd02507    5 VLADGFGSRFLPLTSDIPKALLPVAN-VPLIDYTLEWLEKAGVEEVFVVCCEHSQAIieHLLKSKWSSLSSKMIVDVITS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452  86 PAQMRDgkrwyeGTADAIYQNLRFVeisEADQVCIFGsDHIYKMDIRQMLDyHRRKEARLTVSALRM------PLSQASQ 159
Cdd:cd02507   84 DLCESA------GDALRLRDIRGLI---RSDFLLLSC-DLVSNIPLSELLE-ERRKKDKNAIATLTVllasppVSTEQSK 152

                        170       180       190
                 ....*....|....*....|....*....|
gi 520910452 160 FG----VIEVDD---EGRMVGFEEKPKNPK 182
Cdd:cd02507  153 KTeeedVIAVDSktqRLLLLHYEEDLDEDL 182
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 305-372 5.43e-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: 38.38  E-value: 5.43e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 520910452 305 KKVTITDSLVSGGSYiqgvkiyksilgfrsnIAAGSLISESVILGDVKIGAGCTIK-RAIIDKNVEIAP 372
Cdd:cd03356   27 DGVTITNSILMDNVT----------------IGANSVIVDSIIGDNAVIGENVRVVnLCIIGDDVVVED 79
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 322-379 6.81e-04

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 40.47  E-value: 6.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 322 GVKIY-KSILGFRSNIAAGSLISE-------------------SVILGD-VKIGAGCTIKRA-----------IIDKNVE 369
Cdd:cd03352   49 NVTIYeGCIIGDRVIIHSGAVIGSdgfgfapdgggwvkipqlgGVIIGDdVEIGANTTIDRGalgdtvigdgtKIDNLVQ 128

                         90
                 ....*....|
gi 520910452 370 IAPGTIIGED 379
Cdd:cd03352  129 IAHNVRIGEN 138
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 329-379 7.40e-04

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 40.47  E-value: 7.40e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 520910452 329 ILGFRSNIAAGSLISESVILGD-VKIGAGCTI-------KRAIIDKNVEIAPGTIIGED 379
Cdd:cd03352    3 KIGENVSIGPNAVIGEGVVIGDgVVIGPGVVIgdgvvigDDCVIHPNVTIYEGCIIGDR 61
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 329-379 1.31e-03

N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix (LbH) acetyltransferase domain: GlmU is also known as UDP-N-acetylglucosamine pyrophosphorylase. It is a bifunctional bacterial enzyme that catalyzes two consecutive steps in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), an important precursor in bacterial cell wall formation. The two enzymatic activities, uridyltransferase and acetyltransferase, are carried out by two independent domains. The C-terminal LbH domain possesses the acetyltransferase activity. It catalyzes the CoA-dependent acetylation of GlcN-1-phosphate to GlcNAc-1-phosphate. The LbH domain contains 10 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X. The acetyltransferase active site is located at the interface between two subunits of the active LbH trimer.


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 39.71  E-value: 1.31e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 520910452 329 ILGFRSNIAAGSLISESVILGDVKIGAGCTIKR------AIIDKNVEIAP------GTIIGED 379
Cdd:cd03353   29 ILEGKTVIGEDCVIGPNCVIKDSTIGDGVVIKAssviegAVIGNGATVGPfahlrpGTVLGEG 91
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 6-147 1.76e-03

MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 38.71  E-value: 1.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452    6 GMILAGGEGSRLmplteSRTKPAVPFGGSyRLIDFALNNFVNAdLMRIYVLTQFKSQSLYLhmkKGWNVSSIRDRFidci 85
Cdd:pfam12804   1 AVILAGGRSSRM-----GGDKALLPLGGK-PLLERVLERLRPA-GDEVVVVANDEEVLAAL---AGLGVPVVPDPD---- 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 520910452   86 paqmrdgkrWYEGTADAIYQNLRfvEISEADQVCIFGSDHIY--KMDIRQMLDYHRRKEARLTV 147
Cdd:pfam12804  67 ---------PGQGPLAGLLAALR--AAPGADAVLVLACDMPFltPELLRRLLAAAEESGADIVV 119
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 115-239 1.97e-03

N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose pyrophosphorylase; N-terminal domain of the M1P-guanylyltransferase A-isoform like proteins: The proteins of this family are likely to be a isoform of GDP-mannose pyrophosphorylase. Their sequences are highly conserved with mannose-1-phosphate guanyltransferase, but generally about 40-60 bases longer. GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes including cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133050 [Multi-domain]  Cd Length: 257  Bit Score: 39.54  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 115 ADQVCIFgsdhiykmDIRQMLDYHRRKEARLTVSALRMPLSQASQFG-VIEVDDEGRMVGFEEKPKNPKAipgdpewALV 193
Cdd:cd06428  111 ADVCCDF--------PLQELLEFHKKHGASGTILGTEASREQASNYGcIVEDPSTGEVLHYVEKPETFVS-------DLI 175

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 194 SMGNYIFETETL------CEELREDAALENSSHDFG--------KDIIPKMFPQGGVYVY 239
Cdd:cd06428  176 NCGVYLFSPEIFdtikkaFQSRQQEAQLGDDNNREGraevirleQDVLTPLAGSGKLYVY 235
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 345-379 2.20e-03

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 38.93  E-value: 2.20e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 520910452 345 SVILG-DVKIGAGCTI-KRAIIDKNVEIAPGTIIGED 379
Cdd:cd03352    1 SAKIGeNVSIGPNAVIgEGVVIGDGVVIGPGVVIGDG 37
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 336-376 2.31e-03

N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix (LbH) acetyltransferase domain: GlmU is also known as UDP-N-acetylglucosamine pyrophosphorylase. It is a bifunctional bacterial enzyme that catalyzes two consecutive steps in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), an important precursor in bacterial cell wall formation. The two enzymatic activities, uridyltransferase and acetyltransferase, are carried out by two independent domains. The C-terminal LbH domain possesses the acetyltransferase activity. It catalyzes the CoA-dependent acetylation of GlcN-1-phosphate to GlcNAc-1-phosphate. The LbH domain contains 10 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X. The acetyltransferase active site is located at the interface between two subunits of the active LbH trimer.


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 38.94  E-value: 2.31e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 520910452 336 IAAGSLISESVILG-DVKIGAGCTIKRAIIDKNVEIAPGTII 376
Cdd:cd03353   24 IDPGVILEGKTVIGeDCVIGPNCVIKDSTIGDGVVIKASSVI 65
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 295-404 4.37e-03

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 39.04  E-value: 4.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 520910452 295 PPATFIDVGdkkVTI-TDSLVSGGSYIQGvkiyKSILGFRSNIAAGSLISESvilgdvKIGAGCTIK-----RAIIDKNV 368
Cdd:PRK14354 257 PESTYIDAD---VEIgSDTVIEPGVVIKG----NTVIGEDCVIGPGSRIVDS------TIGDGVTITnsvieESKVGDNV 323

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 520910452 369 EIA------PGTIIGEDLeldrqrfHVSDegIV-----VIAKGTKVG 404
Cdd:PRK14354 324 TVGpfahlrPGSVIGEEV-------KIGN--FVeikksTIGEGTKVS 361
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 335-404 5.04e-03

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: 35.68  E-value: 5.04e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 520910452 335 NIAAGSLISESVILGDVKIGAGCTIKRAIIDKNVEIAPG-----TIIGEDLELDRqrfHVSDEGIVVIAKGTKVG 404
Cdd:cd03356    7 VIGENAIIKNSVIGDNVRIGDGVTITNSILMDNVTIGANsvivdSIIGDNAVIGE---NVRVVNLCIIGDDVVVE 78
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 325-370 5.35e-03

eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B gamma subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH domain with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 35.63  E-value: 5.35e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 520910452 325 IYKSILGFRSNIAAGSLISESVILGDVKIGAGCTIKRAIIDKNVEI 370
Cdd:cd04652   14 IKRSVIGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVI 59
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 335-378 6.15e-03

Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p27 is part of the pointed-end subcomplex in dynactin that also includes p25, p26, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain the imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100052 [Multi-domain]  Cd Length: 164  Bit Score: 37.30  E-value: 6.15e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 520910452 335 NIAAGSLIS-ESVILGDVKIGAGCTIK-RAIIDKNveiAPGTIIGE 378
Cdd:cd04646    1 KIAPGAVVCqESEIRGDVTIGPGTVVHpRATIIAE---AGPIIIGE 43
 
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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