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Conserved domains on  [gi|1051440020|gb|AOA71562|]
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mannose-1-phosphate guanylyltransferase [Stenotrophomonas rhizophila]

Protein Classification

NDP-sugar synthase( domain architecture ID 11440233)

NDP-sugar synthase such as mannose-1-phosphate guanyltransferase and UTP--glucose-1-phosphate uridylyltransferase, which catalyzes the formation of UDP-glucose from UTP and glucose 1-phosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-233 2.23e-90

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: 265.86  E-value: 2.23e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   2 KAIIFSAGKGERMRPLTLTTPKPLLVAGGKPLIVWHLERLAAAGFSEVVINTSWLGDQFEPALGNGDRWGLRLHFIDEGA 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020  82 vPLETGGGILNALPLLGDAPFLVINGDVWTDVDVATL---PRQPKGDAHLVLVDNPMQHPRGDFILRADGTVND-----E 153
Cdd:COG1208    81 -PLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALlafHREKGADATLALVPVPDPSRYGVVELDGDGRVTRfvekpE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020 154 GDAPRLTYAGVGVYRPSILDGWRKvigategssanPPQFGLAPLMRHAMANGRVTGQHHRGKWTDVGTPERLADLDATLR 233
Cdd:COG1208   160 EPPSNLINAGIYVLEPEIFDYIPE-----------GEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLL 228
 
Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-233 2.23e-90

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: 265.86  E-value: 2.23e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   2 KAIIFSAGKGERMRPLTLTTPKPLLVAGGKPLIVWHLERLAAAGFSEVVINTSWLGDQFEPALGNGDRWGLRLHFIDEGA 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020  82 vPLETGGGILNALPLLGDAPFLVINGDVWTDVDVATL---PRQPKGDAHLVLVDNPMQHPRGDFILRADGTVND-----E 153
Cdd:COG1208    81 -PLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALlafHREKGADATLALVPVPDPSRYGVVELDGDGRVTRfvekpE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020 154 GDAPRLTYAGVGVYRPSILDGWRKvigategssanPPQFGLAPLMRHAMANGRVTGQHHRGKWTDVGTPERLADLDATLR 233
Cdd:COG1208   160 EPPSNLINAGIYVLEPEIFDYIPE-----------GEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLL 228
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-228 9.91e-85

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: 250.95  E-value: 9.91e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   2 KAIIFSAGKGERMRPLTLTTPKPLLVAGGKPLIVWHLERLAAAGFSEVVINTSWLGDQFEPALGNgDRWGLRLHFIDEGA 81
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGD-SRFGLRITISDEPD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020  82 VPLETGGGILNALPLLGDAPFLVINGDVWTDVDVATLP-----RQPKGDAHLVLVDNPMQHPRGDFILRADGTV--NDEG 154
Cdd:cd06422    80 ELLETGGGIKKALPLLGDEPFLVVNGDILWDGDLAPLLllhawRMDALLLLLPLVRNPGHNGVGDFSLDADGRLrrGGGG 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1051440020 155 DAPRLTYAGVGVYRPSILDGwrkvigategssANPPQFGLAPLMRHAMANGRVTGQHHRGKWTDVGTPERLADL 228
Cdd:cd06422   160 AVAPFTFTGIQILSPELFAG------------IPPGKFSLNPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLAA 221
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-222 2.11e-29

UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.


Pssm-ID: 274908 [Multi-domain]  Cd Length: 393  Bit Score: 113.07  E-value: 2.11e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   1 MKAIIFSAGKGERMRPLTLTTPKPLLVAGGKPLIVWHLERLAAAGFSEVVINTSWLGDQFEPALGNGDRWGLRLHFIDEG 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIEYVVQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020  81 AvPLETGGGILNALPLLGDaPFLVINGDVWTDVDvaTLPRQPKGDAHLVL---VDNPmqhprGDF-ILRADG-----TVN 151
Cdd:TIGR03992  81 E-QLGTADALGSAKEYVDD-EFLVLNGDVLLDSD--LLERLIRAEAPAIAvveVDDP-----SDYgVVETDGgrvtgIVE 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1051440020 152 DEGDAP-RLTYAGVGVYRPSILDgwrkVIGATEGSSANppQFGLAPLMRHAMANGRVTGQHHRGKWTDVGTP 222
Cdd:TIGR03992 152 KPENPPsNLINAGIYLFSPEIFE----LLEKTKLSPRG--EYELTDALQLLIDEGKVKAVELDGFWLDVGRP 217
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-232 1.53e-19

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: 83.84  E-value: 1.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   2 KAIIFSAGKGERMRPLTLTTPKPL-LVAGGKPLIVWHLERLAAAGFSE-VVINTSWLGDQFEPALGNGDRWGLRLHFIDE 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLvPVGGKYPLIDYPLSRLANAGIREiIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020  80 GaVPLETGGGILNALPLLGD--APFLVINGDVWTDVDVATLPRQ--PKGDAHLVLVDNPMQHPRGDFilradGTV--NDE 153
Cdd:pfam00483  81 P-EGKGTAPAVALAADFLGDekSDVLVLGGDHIYRMDLEQAVKFhiEKAADATVTFGIVPVEPPTGY-----GVVefDDN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020 154 GDAPRL----------TYAGVGVY--RPSILDGWRKVI-----GATEGSSANPPqfglaplmrhAMANGRVTGQH-HRGK 215
Cdd:pfam00483 155 GRVIRFvekpklpkasNYASMGIYifNSGVLDFLAKYLeelkrGEDEITDILPK----------ALEDGKLAYAFiFKGY 224

                         250
                  ....*....|....*...
gi 1051440020 216 -WTDVGTPERLadLDATL 232
Cdd:pfam00483 225 aWLDVGTWDSL--WEANL 240
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-76 1.24e-08

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 54.29  E-value: 1.24e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1051440020   2 KAIIFSAGKGERMRPLTLTTPKPLLVAGGKPLIVWHLERLAAAGFSEV-VINTSWLGDQFEPALGNGDRWGLRLHF 76
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDIlIISTPQDTPRFQQLLGDGSQWGLNLQY 80
 
Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-233 2.23e-90

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: 265.86  E-value: 2.23e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   2 KAIIFSAGKGERMRPLTLTTPKPLLVAGGKPLIVWHLERLAAAGFSEVVINTSWLGDQFEPALGNGDRWGLRLHFIDEGA 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020  82 vPLETGGGILNALPLLGDAPFLVINGDVWTDVDVATL---PRQPKGDAHLVLVDNPMQHPRGDFILRADGTVND-----E 153
Cdd:COG1208    81 -PLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALlafHREKGADATLALVPVPDPSRYGVVELDGDGRVTRfvekpE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020 154 GDAPRLTYAGVGVYRPSILDGWRKvigategssanPPQFGLAPLMRHAMANGRVTGQHHRGKWTDVGTPERLADLDATLR 233
Cdd:COG1208   160 EPPSNLINAGIYVLEPEIFDYIPE-----------GEPFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLL 228
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-228 9.91e-85

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: 250.95  E-value: 9.91e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   2 KAIIFSAGKGERMRPLTLTTPKPLLVAGGKPLIVWHLERLAAAGFSEVVINTSWLGDQFEPALGNgDRWGLRLHFIDEGA 81
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGD-SRFGLRITISDEPD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020  82 VPLETGGGILNALPLLGDAPFLVINGDVWTDVDVATLP-----RQPKGDAHLVLVDNPMQHPRGDFILRADGTV--NDEG 154
Cdd:cd06422    80 ELLETGGGIKKALPLLGDEPFLVVNGDILWDGDLAPLLllhawRMDALLLLLPLVRNPGHNGVGDFSLDADGRLrrGGGG 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1051440020 155 DAPRLTYAGVGVYRPSILDGwrkvigategssANPPQFGLAPLMRHAMANGRVTGQHHRGKWTDVGTPERLADL 228
Cdd:cd06422   160 AVAPFTFTGIQILSPELFAG------------IPPGKFSLNPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLAA 221
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-220 4.08e-48

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: 157.74  E-value: 4.08e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   3 AIIFSAGKGERMRPLTLTTPKPLLVAGGKPLIVWHLERLAAAGFSEVVINTSWLGDQFEPALGNGDRWGLRLHFIDEGaV 82
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFGVNIEYVVQE-E 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020  83 PLETGGGILNALPLLGDAPFLVINGDVWTDVDVATLPRQPK-GDAHLVLVDNPMQHPR--GDFILRADGTVND--E-GDA 156
Cdd:cd04181    80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTDLDLSELLRFHReKGADATIAVKEVEDPSryGVVELDDDGRVTRfvEkPTL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1051440020 157 PRLTYAGVGVY--RPSILDGWRKVI--GATEGSSANPpqfglaplmrHAMANGRVTGQHHRGKWTDVG 220
Cdd:cd04181   160 PESNLANAGIYifEPEILDYIPEILprGEDELTDAIP----------LLIEEGKVYGYPVDGYWLDIG 217
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 3-229 2.82e-41

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: 140.38  E-value: 2.82e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   3 AIIFSAGKGERMRPLTLTTPKPLLVAGGKPLIVWHLERLAAAGFSEVVINTSWLGDQFEPALGNGDRWGLRLHFIDEgAV 82
Cdd:cd06915     1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRGGIRIYYVIE-PE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020  83 PLETGGGILNALPLLGDAPFLVINGDVWTDVDVATLPR---QPKGDAHLVLVDNPMQHPRGDFILRADGTVN-----DEG 154
Cdd:cd06915    80 PLGTGGAIKNALPKLPEDQFLVLNGDTYFDVDLLALLAalrASGADATMALRRVPDASRYGNVTVDGDGRVIafvekGPG 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1051440020 155 DAPRLTYAGVGVYRPSILDGWrkvigategssANPPQFGLAPLMRHAMANGRVTGQHHRGKWTDVGTPERLADLD 229
Cdd:cd06915   160 AAPGLINGGVYLLRKEILAEI-----------PADAFSLEADVLPALVKRGRLYGFEVDGYFIDIGIPEDYARAQ 223
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 1-230 4.03e-37

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: 130.00  E-value: 4.03e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   1 MKAIIFSAGKGERMRPLTLTTPKPLLVAGGKPLIVWHLERLAAAGFSEVVINTSWLGDQFEPALGNGDRWGLRLHFIDEG 80
Cdd:cd04189     1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRFGVRITYILQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020  81 AvPLETGGGILNALPLLGDAPFLVINGDVWTDVDVATLPR---QPKGDAHLVL--VDNPMQH----PRGDFILRadgtVN 151
Cdd:cd04189    81 E-PLGLAHAVLAARDFLGDEPFVVYLGDNLIQEGISPLVRdflEEDADASILLaeVEDPRRFgvavVDDGRIVR----LV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020 152 DEGDAPRLTYAGVGVY--RPSILD-------GWRKVIGATEGssanppqfglapLMRHAMANGRVTGQHHRGKWTDVGTP 222
Cdd:cd04189   156 EKPKEPPSNLALVGVYafTPAIFDaisrlkpSWRGELEITDA------------IQWLIDRGRRVGYSIVTGWWKDTGTP 223


                  ....*...
gi 1051440020 223 ERLadLDA 230
Cdd:cd04189   224 EDL--LEA 229
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 3-223 5.72e-33

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: 118.77  E-value: 5.72e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   3 AIIFSAGKGERMRPLTLTTPKPLLVAGGKPLIVWHLERLAAAGFSEVVINTSWLGDQFEPALGNGDRWGLRLHFIDEGaV 82
Cdd:cd06426     1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDGSKFGVNISYVRED-K 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020  83 PLETGGGiLNALPLLGDAPFLVINGDVWTDVDVATL---PRQPKGDAHLVLVDNPMQHPRGdfILRADGT-VNDEGDAPR 158
Cdd:cd06426    80 PLGTAGA-LSLLPEKPTDPFLVMNGDILTNLNYEHLldfHKENNADATVCVREYEVQVPYG--VVETEGGrITSIEEKPT 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1051440020 159 LTY---AGVGVYRPSILDgwrkviGATEGSSANPPQfglapLMRHAMANG-RVTGQHHRGKWTDVGTPE 223
Cdd:cd06426   157 HSFlvnAGIYVLEPEVLD------LIPKNEFFDMPD-----LIEKLIKEGkKVGVFPIHEYWLDIGRPE 214
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-222 2.11e-29

UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.


Pssm-ID: 274908 [Multi-domain]  Cd Length: 393  Bit Score: 113.07  E-value: 2.11e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   1 MKAIIFSAGKGERMRPLTLTTPKPLLVAGGKPLIVWHLERLAAAGFSEVVINTSWLGDQFEPALGNGDRWGLRLHFIDEG 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIEYVVQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020  81 AvPLETGGGILNALPLLGDaPFLVINGDVWTDVDvaTLPRQPKGDAHLVL---VDNPmqhprGDF-ILRADG-----TVN 151
Cdd:TIGR03992  81 E-QLGTADALGSAKEYVDD-EFLVLNGDVLLDSD--LLERLIRAEAPAIAvveVDDP-----SDYgVVETDGgrvtgIVE 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1051440020 152 DEGDAP-RLTYAGVGVYRPSILDgwrkVIGATEGSSANppQFGLAPLMRHAMANGRVTGQHHRGKWTDVGTP 222
Cdd:TIGR03992 152 KPENPPsNLINAGIYLFSPEIFE----LLEKTKLSPRG--EYELTDALQLLIDEGKVKAVELDGFWLDVGRP 217
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-108 9.72e-26

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 101.71  E-value: 9.72e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   1 MKAIIFSAGKGERMRPLTLTTPKPLLVAGGKPLIVWHLERLAAAGFSEV-VINTSWLGDQFEPALGNGDRWGLRLHFIDE 79
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREIlIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100
                  ....*....|....*....|....*....
gi 1051440020  80 GAvPLETGGGILNALPLLGDAPFLVINGD 108
Cdd:COG1209    81 PE-PLGLAHAFIIAEDFIGGDPVALVLGD 108
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-226 1.00e-23

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 94.92  E-value: 1.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   2 KAIIFSAGKGERMRPLTLTTPKPLLVAGGKPLIVWHLERLAAAGFSEVVINTSWLGDQFEPALgngDRWGLRLHFI--DE 79
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEAL---ARPGPDVTFVynPD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020  80 GAVpLETGGGILNALPLLGDaPFLVINGDVWTDVDV-ATLPRQPKGDAhlVLVDNPMQHPRGD---FILRADGTVNDEG- 154
Cdd:COG1213    78 YDE-TNNIYSLWLAREALDE-DFLLLNGDVVFDPAIlKRLLASDGDIV--LLVDRKWEKPLDEevkVRVDEDGRIVEIGk 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020 155 DAPRLTYAG--VGVYR--PSILDGWRKVIGATEGSSAnpPQFGLAPLMRHAMANG------RVTGqhhrGKWTDVGTPER 224
Cdd:COG1213   154 KLPPEEADGeyIGIFKfsAEGAAALREALEALIDEGG--PNLYYEDALQELIDEGgpvkavDIGG----LPWVEIDTPED 227


                  ..
gi 1051440020 225 LA 226
Cdd:COG1213   228 LE 229
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-112 1.38e-20

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: 86.50  E-value: 1.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   1 MKAIIFSAGKGERMRPLTLTTPKPLLVAGGKPLIVWHLERLAAAGFSEVVINTSWLGDQFEPALGN-GDRWGLRLHFIDE 79
Cdd:cd06425     1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEyEKKLGIKITFSIE 80

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1051440020  80 gAVPLETGGGILNALPLLG--DAPFLVINGDVWTD 112
Cdd:cd06425    81 -TEPLGTAGPLALARDLLGddDEPFFVLNSDVICD 114
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 3-132 7.20e-20

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: 84.59  E-value: 7.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   3 AIIFSAGKGERMRPLTLTTPKPLLVAGGKPLIVWHLERLAAAGFSEVVINTSWLGDQFEPALGNgdrwGLRLHFIdEGAV 82
Cdd:cd02523     1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKK----YPNIKFV-YNPD 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1051440020  83 PLETGGGI--LNALPLLGDaPFLVINGDVWTDVDVA-TLPRQPKGDAhlVLVD 132
Cdd:cd02523    76 YAETNNIYslYLARDFLDE-DFLLLEGDVVFDPSILeRLLSSPADNA--ILVD 125
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-232 1.53e-19

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: 83.84  E-value: 1.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   2 KAIIFSAGKGERMRPLTLTTPKPL-LVAGGKPLIVWHLERLAAAGFSE-VVINTSWLGDQFEPALGNGDRWGLRLHFIDE 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLvPVGGKYPLIDYPLSRLANAGIREiIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020  80 GaVPLETGGGILNALPLLGD--APFLVINGDVWTDVDVATLPRQ--PKGDAHLVLVDNPMQHPRGDFilradGTV--NDE 153
Cdd:pfam00483  81 P-EGKGTAPAVALAADFLGDekSDVLVLGGDHIYRMDLEQAVKFhiEKAADATVTFGIVPVEPPTGY-----GVVefDDN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020 154 GDAPRL----------TYAGVGVY--RPSILDGWRKVI-----GATEGSSANPPqfglaplmrhAMANGRVTGQH-HRGK 215
Cdd:pfam00483 155 GRVIRFvekpklpkasNYASMGIYifNSGVLDFLAKYLeelkrGEDEITDILPK----------ALEDGKLAYAFiFKGY 224

                         250
                  ....*....|....*...
gi 1051440020 216 -WTDVGTPERLadLDATL 232
Cdd:pfam00483 225 aWLDVGTWDSL--WEANL 240
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-108 6.51e-16

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: 74.15  E-value: 6.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   1 MKAIIFSAGKGERMRPLTLTTPKPLLVAGGKPLIVWHLERLAAAGFSEV-VINTSWLGDQFEPALGNGDRWGLRLHFIDE 79
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREIlIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1051440020  80 gavplETGGGILNALPL----LGDAPFLVINGD 108
Cdd:cd02538    81 -----PKPGGLAQAFIIgeefIGDDPVCLILGD 108
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 1-114 2.96e-13

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: 66.51  E-value: 2.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   1 MKAIIFSAGKGERMRPLTLTTPKPLLVAGGKPLIVWHLERLAAAGFSEVVINTSWLGDQ----FEPALGNGDRWGLRLHF 76
Cdd:cd02507     1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAiiehLLKSKWSSLSSKMIVDV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1051440020  77 ID-EGAVPLETGGGILNALPLL-GDapFLVINGDVWTDVD 114
Cdd:cd02507    81 ITsDLCESAGDALRLRDIRGLIrSD--FLLLSCDLVSNIP 118
LicC COG4750
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid ...
 1-61 5.51e-13

CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 443784 [Multi-domain]  Cd Length: 228  Bit Score: 65.62  E-value: 5.51e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1051440020   1 MKAIIFSAGKGERMRPLTLTTPKPLLVAGGKPLIVWHLERLAAAGFSEVVINTSWLGDQFE 61
Cdd:COG4750     1 MNAIILAAGLGSRFAPITYETPKGLLKVNGEPLIERQIRQLHEAGITDITVVVGYLKEQFE 61
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-109 9.90e-11

Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose Pyrophosphorylase (UGPase) catalyzes a reversible production of UDP-Glucose and pyrophosphate (PPi) from glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids , glycoproteins , and proteoglycans. UGPase is found in both prokaryotes and eukaryotes, although prokaryotic and eukaryotic forms of UGPase catalyze the same reaction, they share low sequence similarity.


Pssm-ID: 133021 [Multi-domain]  Cd Length: 267  Bit Score: 59.85  E-value: 9.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   1 MKAIIFSAGKGERMRPLTLTTPKPLLVAGGKPLIVWHLERLAAAGFSEVVINTS----WLGDQFEPAL-------GNGDR 69
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGrgkrAIEDHFDRSYeleetleKKGKT 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1051440020  70 WGLRL----------HFIDEGaVPLETGGGILNALPLLGDAPFLVINGDV 109
Cdd:cd02541    81 DLLEEvriisdlaniHYVRQK-EPLGLGHAVLCAKPFIGDEPFAVLLGDD 129
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 1-54 3.62e-10

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: 57.67  E-value: 3.62e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1051440020   1 MKAIIFSAGKGERMRPLTLTTPKPLLVAGGKPLIVWHLERLAAAGFSEVVINTS 54
Cdd:cd04198     1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVP 54
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 3-109 1.60e-09

N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively.


Pssm-ID: 133020 [Multi-domain]  Cd Length: 229  Bit Score: 55.98  E-value: 1.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   3 AIIFSAGKGERMRPltlTTPKPLLVAGGKPLIVWHLERLAAAGFSEVVINTSWLGDQFEPALGNGDrwglrLHFIdEGAV 82
Cdd:cd02540     1 AVILAAGKGTRMKS---DLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALANPN-----VEFV-LQEE 71

                          90       100
                  ....*....|....*....|....*....
gi 1051440020  83 PLETGGGILNALPLLGD--APFLVINGDV 109
Cdd:cd02540    72 QLGTGHAVKQALPALKDfeGDVLVLYGDV 100
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 1-109 2.05e-09

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 56.96  E-value: 2.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   1 MKAIIFSAGKGERMRPltlTTPKPLLVAGGKPLIVWHLERLAAAGFSEVVINTSWLGDQFEPALGngdrwGLRLHFIDEg 80
Cdd:COG1207     3 LAVVILAAGKGTRMKS---KLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALA-----DLDVEFVLQ- 73

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1051440020  81 AVPLETGGGILNALPLLG--DAPFLVINGDV 109
Cdd:COG1207    74 EEQLGTGHAVQQALPALPgdDGTVLVLYGDV 104
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 3-118 3.42e-09

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: 55.34  E-value: 3.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   3 AIIFSAG--KGERMRPLTLTTPKPLLVAGGKPLIVWHLERLAA-AGFSEVVINTSWLGDQFEPALGNGDR-WGLRLHFID 78
Cdd:cd06428     1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKvPDLKEVLLIGFYPESVFSDFISDAQQeFNVPIRYLQ 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1051440020  79 EGAvPLETGGGILNALP-LLGDAP--FLVINGDVWTDVDVATL 118
Cdd:cd06428    81 EYK-PLGTAGGLYHFRDqILAGNPsaFFVLNADVCCDFPLQEL 122
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-76 1.24e-08

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 54.29  E-value: 1.24e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1051440020   2 KAIIFSAGKGERMRPLTLTTPKPLLVAGGKPLIVWHLERLAAAGFSEV-VINTSWLGDQFEPALGNGDRWGLRLHF 76
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDIlIISTPQDTPRFQQLLGDGSQWGLNLQY 80
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 3-118 4.92e-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: 52.19  E-value: 4.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   3 AIIFSAGKGERMRPLTLTTPKPLLVAGGKPlIVWHLERL-AAAGFSEVVI--------------NTSWLGDQFEPALGNG 67
Cdd:cd02524     1 VVILAGGLGTRLSEETELKPKPMVEIGGRP-ILWHIMKIySHYGHNDFILclgykghvikeyflNYFLHNSDVTIDLGTN 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1051440020  68 DrwgLRLH----------FIDEGavpLE--TGGGILNALPLLGDA-PFLVINGDVWTDVDVATL 118
Cdd:cd02524    80 R---IELHnsdiedwkvtLVDTG---LNtmTGGRLKRVRRYLGDDeTFMLTYGDGVSDVNINAL 137
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 3-109 1.93e-07

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: 49.12  E-value: 1.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   3 AIIFSAGKGERMRpltltTPKPLLVAGGKPLIVWHLERLAAAgFSEVVINTSWlgDQFEPALGngdrwGLRLHFIDEGAV 82
Cdd:pfam12804   1 AVILAGGRSSRMG-----GDKALLPLGGKPLLERVLERLRPA-GDEVVVVAND--EEVLAALA-----GLGVPVVPDPDP 67

                          90       100
                  ....*....|....*....|....*...
gi 1051440020  83 PLETGGGILNALPLLGDAP-FLVINGDV 109
Cdd:pfam12804  68 GQGPLAGLLAALRAAPGADaVLVLACDM 95
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 1-108 1.45e-06

MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 47.19  E-value: 1.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   1 MKAIIFSAGKGERMrpltlTTPKPLLVAGGKPLIVWHLERLAAAgFSEVVINTSwlgdqfePALGNGDRWGLRLhFIDE- 79
Cdd:cd02503     1 ITGVILAGGKSRRM-----GGDKALLELGGKPLLEHVLERLKPL-VDEVVISAN-------RDQERYALLGVPV-IPDEp 66

                          90       100       110
                  ....*....|....*....|....*....|
gi 1051440020  80 -GAVPLetgGGILNALPLLGDAPFLVINGD 108
Cdd:cd02503    67 pGKGPL---AGILAALRAAPADWVLVLACD 93
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-112 3.61e-06

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 46.81  E-value: 3.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   1 MKAIIFSAGKGERMRPLTLTTPKPLLVAGGKPLIVWHLERLAAAGFSEVVINTSwlgdQFEPALGNGDRWGLRLHFIDEG 80
Cdd:PRK10122    4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTH----ASKNAVENHFDTSYELESLLEQ 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1051440020  81 AV-------------------------PLETGGGILNALPLLGDAPFLVINGDVWTD 112
Cdd:PRK10122   80 RVkrqllaevqsicppgvtimnvrqgqPLGLGHSILCARPAIGDNPFVVVLPDVVID 136
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 3-51 4.65e-06

CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 45.98  E-value: 4.65e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1051440020   3 AIIFSAGKGERMRpltLTTPKPLLVAGGKPLIVWHLERLAAAG-FSEVVI 51
Cdd:cd02516     3 AIILAAGSGSRMG---ADIPKQFLELGGKPVLEHTLEAFLAHPaIDEIVV 49
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-103 1.45e-05

Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 44.03  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   1 MKAIIFSAGKGERMRpltltTPKPLLVAGGKPLIVWHLERLAAAgFSEVVINTSWlgDQFEPALGngdrwglrLHFIDE- 79
Cdd:COG0746     5 ITGVILAGGRSRRMG-----QDKALLPLGGRPLLERVLERLRPQ-VDEVVIVANR--PERYAALG--------VPVVPDd 68

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1051440020  80 --GAVPLetgGGILNALPLL---------GDAPFL 103
Cdd:COG0746    69 ppGAGPL---AGILAALEAApaewvlvlaCDMPFL 100
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-51 1.65e-05

CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 44.00  E-value: 1.65e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1051440020   3 AIIFSAGKGERMRpltltTPKPLLVAGGKPLIVWHLERLAAAGFSEVVI 51
Cdd:COG2068     6 AIILAAGASSRMG-----RPKLLLPLGGKPLLERAVEAALAAGLDPVVV 49
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-69 1.79e-05

GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 44.09  E-value: 1.79e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1051440020   3 AIIFSAGKGERMRpltltTPKPLLVAGGKPLIVWHLERLAAAGFSEVVINTSWLGDQFEPALGNGDR 69
Cdd:cd04182     3 AIILAAGRSSRMG-----GNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPV 64
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
3-51 2.09e-05

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 43.97  E-value: 2.09e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1051440020   3 AIIFSAGKGERMRPltlTTPKPLLVAGGKPLIVWHLERLAAAG-FSEVVI 51
Cdd:PRK00155    6 AIIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIV 52
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 11-71 9.56e-05

The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of epsilon 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 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: 133040 [Multi-domain]  Cd Length: 217  Bit Score: 42.21  E-value: 9.56e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1051440020  11 GERMRPLTLTTPKPLLVAGGKPLIVWHLERLAAAGFSEVVINTSWLGDQFEPALGNGDRWG 71
Cdd:cd04197    11 NRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKSKWSK 71
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 9-109 1.16e-04

GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 41.41  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   9 GKGERMRPltltTPKPLLVAGGKPLIVWHLERLAAAGFSEVVINTSwlgdQFEPALGNgdrwglrlHFIDEGAVPLETGG 88
Cdd:COG2266     4 GKGTRLGG----GEKPLLEICGKPMIDRVIDALEESCIDKIYVAVS----PNTPKTRE--------YLKERGVEVIETPG 67

                          90       100
                  ....*....|....*....|....*.
gi 1051440020  89 G-----ILNALPLLGDaPFLVINGDV 109
Cdd:COG2266    68 EgyvedLNEALESISG-PVLVVPADL 92
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-53 1.30e-04

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 42.20  E-value: 1.30e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1051440020   2 KAIIFSAGKGERMRPLTLTTPKPLLVAGGKPLIVWHLERLAAAGFSEVVINT 53
Cdd:PRK13389   10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVT 61
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 4-51 1.34e-04

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440824  Cd Length: 224  Bit Score: 41.65  E-value: 1.34e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1051440020   4 IIFSAGKGERMRpltLTTPKPLLVAGGKPLIVWHLERLAAAG-FSEVVI 51
Cdd:COG1211     1 IIPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVV 46
PRK05450 PRK05450
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 23-53 2.21e-04

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 235473  Cd Length: 245  Bit Score: 41.26  E-value: 2.21e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1051440020  23 KPLLVAGGKPLIVWHLERLAAAGFSEVVINT 53
Cdd:PRK05450   19 KPLADIGGKPMIVRVYERASKAGADRVVVAT 49
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-109 2.26e-04

UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 41.17  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   2 KAIIFSAGKGERMRPLTLTTPKPLLVAGGKPLIVWHLERLAAAGFSEVVINTSW----LGDQFEPAL---------GNGD 68
Cdd:COG1210     5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRgkraIEDHFDRSYeleatleakGKEE 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1051440020  69 RW--------GLRLHFIDEGAvPLETGGGILNALPLLGDAPFLVINGDV 109
Cdd:COG1210    85 LLeevrsispLANIHYVRQKE-PLGLGHAVLCARPFVGDEPFAVLLGDD 132
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 1-108 2.44e-04

bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 41.50  E-value: 2.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   1 MKAIIFSAGKGERMRPltlTTPKPLLVAGGKPLIVWHLERLAAAGFSEVVINTSWLGDQFEPAL-GNGDRWGLRlhfide 79
Cdd:PRK14358    8 LDVVILAAGQGTRMKS---ALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALqGSGVAFARQ------ 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1051440020  80 gAVPLETGGGILNALPLL--GDAPFLVINGD 108
Cdd:PRK14358   79 -EQQLGTGDAFLSGASALteGDADILVLYGD 108
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 3-51 6.64e-04

bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase protein; Provisional


Pssm-ID: 236492 [Multi-domain]  Cd Length: 378  Bit Score: 40.22  E-value: 6.64e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1051440020   3 AIIFSAGKGERmrpLTLTTPKPLLVAGGKPLIVWHLERLAAAG-FSEVVI 51
Cdd:PRK09382    8 LVIVAAGRSTR---FSAEVKKQWLRIGGKPLWLHVLENLSSAPaFKEIVV 54
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-150 2.21e-03

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 38.47  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   1 MKAIIFSAGKGERMRPltlTTPKPLLVAGGKPLIVWHLERLAAAGFSEVVINTSWLGDQFEPALGNGD-RWGLRlhfide 79
Cdd:PRK09451    6 MSVVILAAGKGTRMYS---DLPKVLHTLAGKPMVQHVIDAANELGAQHVHLVYGHGGDLLKQTLADEPlNWVLQ------ 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1051440020  80 gAVPLETGGGILNALPLLGD-APFLVINGDVwTDVDVATLPR----QPKGDAHL--VLVDNPMQHPRgdfILRADGTV 150
Cdd:PRK09451   77 -AEQLGTGHAMQQAAPFFADdEDILMLYGDV-PLISVETLQRlrdaKPQGGIGLltVKLDNPTGYGR---ITRENGKV 149
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 4-50 2.55e-03

GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133026 [Multi-domain]  Cd Length: 231  Bit Score: 38.00  E-value: 2.55e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1051440020   4 IIFSAGKGERMRPLTLTTPKPLLVAGGKPLIVWHLERLAAAGFSEVV 50
Cdd:cd04183     2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFI 48
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-51 3.05e-03

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 38.30  E-value: 3.05e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1051440020   3 AIIFSAGKGERMRPltlTTPKPLLVAGGKPLIVWHLERLAAAGFSEVVI 51
Cdd:PRK14353    8 AIILAAGEGTRMKS---SLPKVLHPVAGRPMLAHVLAAAASLGPSRVAV 53
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-109 4.91e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 37.42  E-value: 4.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   3 AIIFSAGKGERMRPLTLTTPKPLlvaGGKPLIVWHLERLAAAGFSEVVINTswlGDQFEpalgngdrwGLRLHFIDEGAV 82
Cdd:PRK14355    6 AIILAAGKGTRMKSDLVKVMHPL---AGRPMVSWPVAAAREAGAGRIVLVV---GHQAE---------KVREHFAGDGDV 70

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1051440020  83 -------PLETGGGILNALPLL--GDAPFLVINGDV 109
Cdd:PRK14355   71 sfalqeeQLGTGHAVACAAPALdgFSGTVLILCGDV 106
KdsB COG1212
CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; ...
 23-53 5.83e-03

CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; CMP-2-keto-3-deoxyoctulosonic acid synthetase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440825  Cd Length: 242  Bit Score: 36.96  E-value: 5.83e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1051440020  23 KPLLVAGGKPLIVWHLER-LAAAGFSEVVINT 53
Cdd:COG1212    19 KPLADIAGKPMIQRVYERaLASKGADRVVVAT 50
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-109 6.13e-03

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 37.21  E-value: 6.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1051440020   1 MKAI-IFSAGKGERMRPltlTTPKPLLVAGGKPLIVWHLERLAAAGFSEVVINTSWLGDQFEPALGNGDrwglRLHFIdE 79
Cdd:PRK14360    1 MLAVaILAAGKGTRMKS---SLPKVLHPLGGKSLVERVLDSCEELKPDRRLVIVGHQAEEVEQSLAHLP----GLEFV-E 72

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1051440020  80 GAVPLETGGGILNALPLL----GDapFLVINGDV 109
Cdd:PRK14360   73 QQPQLGTGHAVQQLLPVLkgfeGD--LLVLNGDV 104
 
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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