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Conserved domains on  [gi|2495647026|ref|WP_279904555|]
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MULTISPECIES: N-acetylmuramate alpha-1-phosphate uridylyltransferase MurU [unclassified Pseudomonas]

Protein Classification

nucleotidyltransferase family protein( domain architecture ID 11440233)

nucleotidyltransferase family protein such as Pseudomonas aeruginosa N-acetylmuramate alpha-1-phosphate uridylyltransferase MurU that catalyzes the formation of UDP-N-acetylmuramate (UDP-MurNAc), a crucial precursor of the bacterial peptidoglycan cell wall, from UTP and MurNAc-alpha-1P

EC:  2.7.7.-
Gene Ontology:  GO:0016779|GO:0009252
PubMed:  9445404
SCOP:  3000077

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 ...
 2-221 2.76e-95

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: 277.80  E-value: 2.76e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   2 KAMILAAGKGERLRPLTLHTPKPLVRAAGTPLIEFHVRALAAAGFTELVINHAWLGQQIEDYLGDGGRFGLRIAYSAEGE 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026  82 PLETGGGIFKALPLLGDEPFLVVNGDIWTDCDFATLR---RPLDGLAHLVLVDNPAHHQSGDFLL-RDGRVTDAV----A 153
Cdd:COG1208    81 PLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALLafhREKGADATLALVPVPDPSRYGVVELdGDGRVTRFVekpeE 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2495647026 154 GEPSLTYSGMAVLHPRLFAGCQPG-AFKLAPLLRAAMADGQVSGERFAGRWIDVGTHERLADVERLLAA 221
Cdd:COG1208   161 PPSNLINAGIYVLEPEIFDYIPEGePFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLS 229
 
Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-221 2.76e-95

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: 277.80  E-value: 2.76e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   2 KAMILAAGKGERLRPLTLHTPKPLVRAAGTPLIEFHVRALAAAGFTELVINHAWLGQQIEDYLGDGGRFGLRIAYSAEGE 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026  82 PLETGGGIFKALPLLGDEPFLVVNGDIWTDCDFATLR---RPLDGLAHLVLVDNPAHHQSGDFLL-RDGRVTDAV----A 153
Cdd:COG1208    81 PLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALLafhREKGADATLALVPVPDPSRYGVVELdGDGRVTRFVekpeE 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2495647026 154 GEPSLTYSGMAVLHPRLFAGCQPG-AFKLAPLLRAAMADGQVSGERFAGRWIDVGTHERLADVERLLAA 221
Cdd:COG1208   161 PPSNLINAGIYVLEPEIFDYIPEGePFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLS 229
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-214 5.80e-87

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: 256.34  E-value: 5.80e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   2 KAMILAAGKGERLRPLTLHTPKPLVRAAGTPLIEFHVRALAAAGFTELVINHAWLGQQIEDYLGDgGRFGLRIAYSAE-G 80
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGD-SRFGLRITISDEpD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026  81 EPLETGGGIFKALPLLGDEPFLVVNGDIWTDCDFATLRRPL-----DGLAHLVLVDNPAHHQSGDF-LLRDGRVTDAVAG 154
Cdd:cd06422    80 ELLETGGGIKKALPLLGDEPFLVVNGDILWDGDLAPLLLLHawrmdALLLLLPLVRNPGHNGVGDFsLDADGRLRRGGGG 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2495647026 155 EP-SLTYSGMAVLHPRLFAGCQPGAFKLAPLLRAAMADGQVSGERFAGRWIDVGTHERLAD 214
Cdd:cd06422   160 AVaPFTFTGIQILSPELFAGIPPGKFSLNPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLA 220
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-207 2.82e-40

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: 141.58  E-value: 2.82e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   1 MKAMILAAGKGERLRPLTLHTPKPLVRAAGTPLIEFHVRALAAAGFTELVINHAWLGQQIEDYLGDGGRFGLRIAYSAEG 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIEYVVQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026  81 EPLETGGGIFKALPLLgDEPFLVVNGDIWTDCDfaTLRRPLDGLAHLVL---VDNPAhhQSGDFLLRDGRVTDAV---AG 154
Cdd:TIGR03992  81 EQLGTADALGSAKEYV-DDEFLVLNGDVLLDSD--LLERLIRAEAPAIAvveVDDPS--DYGVVETDGGRVTGIVekpEN 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026 155 EPS-LTYSGMAVLHPRLF---AGCQP---GAFKLAPLLRAAMADGQVSGERFAGRWIDVG 207
Cdd:TIGR03992 156 PPSnLINAGIYLFSPEIFellEKTKLsprGEYELTDALQLLIDEGKVKAVELDGFWLDVG 215
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-220 8.14e-24

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: 95.01  E-value: 8.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   2 KAMILAAGKGERLRPLTLHTPKPLVRAAGT-PLIEFHVRALAAAGFTE-LVINHAWLGQQIEDYLGDGGRFGLRIAYSAE 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREiIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026  80 GEPLETGGGIFKALPLLGDE--PFLVVNGDIWTDCDF-ATLRRPLD-GLAHLVLVDNPAHHQSGDFLL----RDGRVTDA 151
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEksDVLVLGGDHIYRMDLeQAVKFHIEkAADATVTFGIVPVEPPTGYGVvefdDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026 152 V---AGEPSLTY---------SGMAVLHPRLFAGCQPGAFKLAPLLRAAMADGQVSGERF--AGRWIDVGTHERLADVER 217
Cdd:pfam00483 161 VekpKLPKASNYasmgiyifnSGVLDFLAKYLEELKRGEDEITDILPKALEDGKLAYAFIfkGYAWLDVGTWDSLWEANL 240


                  ...
gi 2495647026 218 LLA 220
Cdd:pfam00483 241 FLL 243
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-111 6.32e-08

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 51.81  E-value: 6.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   1 MKAMILAAGKGERLRPLTLHTPKPLVRAAGTPLIEFHVRALAAAGFTELVI----------NH--------AWLGQQIED 62
Cdd:PRK10122    4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLvthasknaveNHfdtsyeleSLLEQRVKR 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2495647026  63 YLGDGGRF----GLRIAYSAEGEPLETGGGIFKALPLLGDEPFLVVNGDIWTD 111
Cdd:PRK10122   84 QLLAEVQSicppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVID 136
 
Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-221 2.76e-95

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: 277.80  E-value: 2.76e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   2 KAMILAAGKGERLRPLTLHTPKPLVRAAGTPLIEFHVRALAAAGFTELVINHAWLGQQIEDYLGDGGRFGLRIAYSAEGE 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026  82 PLETGGGIFKALPLLGDEPFLVVNGDIWTDCDFATLR---RPLDGLAHLVLVDNPAHHQSGDFLL-RDGRVTDAV----A 153
Cdd:COG1208    81 PLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALLafhREKGADATLALVPVPDPSRYGVVELdGDGRVTRFVekpeE 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2495647026 154 GEPSLTYSGMAVLHPRLFAGCQPG-AFKLAPLLRAAMADGQVSGERFAGRWIDVGTHERLADVERLLAA 221
Cdd:COG1208   161 PPSNLINAGIYVLEPEIFDYIPEGePFDLEDLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLS 229
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-214 5.80e-87

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: 256.34  E-value: 5.80e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   2 KAMILAAGKGERLRPLTLHTPKPLVRAAGTPLIEFHVRALAAAGFTELVINHAWLGQQIEDYLGDgGRFGLRIAYSAE-G 80
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGD-SRFGLRITISDEpD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026  81 EPLETGGGIFKALPLLGDEPFLVVNGDIWTDCDFATLRRPL-----DGLAHLVLVDNPAHHQSGDF-LLRDGRVTDAVAG 154
Cdd:cd06422    80 ELLETGGGIKKALPLLGDEPFLVVNGDILWDGDLAPLLLLHawrmdALLLLLPLVRNPGHNGVGDFsLDADGRLRRGGGG 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2495647026 155 EP-SLTYSGMAVLHPRLFAGCQPGAFKLAPLLRAAMADGQVSGERFAGRWIDVGTHERLAD 214
Cdd:cd06422   160 AVaPFTFTGIQILSPELFAGIPPGKFSLNPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLA 220
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-207 1.17e-53

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: 171.22  E-value: 1.17e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   3 AMILAAGKGERLRPLTLHTPKPLVRAAGTPLIEFHVRALAAAGFTELVINHAWLGQQIEDYLGDGGRFGLRIAYSAEGEP 82
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFGVNIEYVVQEEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026  83 LETGGGIFKALPLLGDEPFLVVNGDIWTDCDFA---TLRRPLDGLAHLVL--VDNPahhqsGDF----LLRDGRVTDAV- 152
Cdd:cd04181    81 LGTAGAVRNAEDFLGDDDFLVVNGDVLTDLDLSellRFHREKGADATIAVkeVEDP-----SRYgvveLDDDGRVTRFVe 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2495647026 153 ---AGEPSLTYSGMAVLHPRLFAGCQPGAFK----LAPLLRAAMADGQVSGERFAGRWIDVG 207
Cdd:cd04181   156 kptLPESNLANAGIYIFEPEILDYIPEILPRgedeLTDAIPLLIEEGKVYGYPVDGYWLDIG 217
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 3-213 1.04e-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: 141.15  E-value: 1.04e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   3 AMILAAGKGERLRPLTLHTPKPLVRAAGTPLIEFHVRALAAAGFTELVINHAWLGQQIEDYLGDGGRFGLRIAYSAEGEP 82
Cdd:cd06915     1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRGGIRIYYVIEPEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026  83 LETGGGIFKALPLLGDEPFLVVNGDIWTDCDFATLRRPL---DGLAHLVLVDNPAHHQSGDFLLR-DGRVTDAVA----G 154
Cdd:cd06915    81 LGTGGAIKNALPKLPEDQFLVLNGDTYFDVDLLALLAALrasGADATMALRRVPDASRYGNVTVDgDGRVIAFVEkgpgA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026 155 EPSLTYSGMAVLHPRLFAG-CQPGAFKLAPLLRAAMADGQVSGERFAGRWIDVGTHERLA 213
Cdd:cd06915   161 APGLINGGVYLLRKEILAEiPADAFSLEADVLPALVKRGRLYGFEVDGYFIDIGIPEDYA 220
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-207 2.82e-40

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: 141.58  E-value: 2.82e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   1 MKAMILAAGKGERLRPLTLHTPKPLVRAAGTPLIEFHVRALAAAGFTELVINHAWLGQQIEDYLGDGGRFGLRIAYSAEG 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIEYVVQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026  81 EPLETGGGIFKALPLLgDEPFLVVNGDIWTDCDfaTLRRPLDGLAHLVL---VDNPAhhQSGDFLLRDGRVTDAV---AG 154
Cdd:TIGR03992  81 EQLGTADALGSAKEYV-DDEFLVLNGDVLLDSD--LLERLIRAEAPAIAvveVDDPS--DYGVVETDGGRVTGIVekpEN 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026 155 EPS-LTYSGMAVLHPRLF---AGCQP---GAFKLAPLLRAAMADGQVSGERFAGRWIDVG 207
Cdd:TIGR03992 156 PPSnLINAGIYLFSPEIFellEKTKLsprGEYELTDALQLLIDEGKVKAVELDGFWLDVG 215
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 1-219 4.85e-39

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: 134.62  E-value: 4.85e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   1 MKAMILAAGKGERLRPLTLHTPKPLVRAAGTPLIEFHVRALAAAGFTELVINHAWLGQQIEDYLGDGGRFGLRIAYSAEG 80
Cdd:cd04189     1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRFGVRITYILQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026  81 EPLETGGGIFKALPLLGDEPFLVVNGDIWTDCDFATLRRPL---DGLAHLVL--VDNPahHQSGDFLLRDGRVTDAV--- 152
Cdd:cd04189    81 EPLGLAHAVLAARDFLGDEPFVVYLGDNLIQEGISPLVRDFleeDADASILLaeVEDP--RRFGVAVVDDGRIVRLVekp 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2495647026 153 AGEPS-LTYSGMAVLHPRLF---AGCQP---GAFKLAPLLRAAMADG-QVSGERFAGRWIDVGTHERLADVERLL 219
Cdd:cd04189   159 KEPPSnLALVGVYAFTPAIFdaiSRLKPswrGELEITDAIQWLIDRGrRVGYSIVTGWWKDTGTPEDLLEANRLL 233
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 3-210 1.32e-35

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: 125.32  E-value: 1.32e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   3 AMILAAGKGERLRPLTLHTPKPLVRAAGTPLIEFHVRALAAAGFTELVINHAWLGQQIEDYLGDGGRFGLRIAYSAEGEP 82
Cdd:cd06426     1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDGSKFGVNISYVREDKP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026  83 LETGGGIfKALPLLGDEPFLVVNGDIWTDCDF-ATLRRPLDGLAHLVLVDNPAHHQS--GDFLLRDGRVTDAVAgEPSLT 159
Cdd:cd06426    81 LGTAGAL-SLLPEKPTDPFLVMNGDILTNLNYeHLLDFHKENNADATVCVREYEVQVpyGVVETEGGRITSIEE-KPTHS 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2495647026 160 Y---SGMAVLHPRLFAGCQPGAFKLAP-LLRAAMADGQVSGeRFA--GRWIDVGTHE 210
Cdd:cd06426   159 FlvnAGIYVLEPEVLDLIPKNEFFDMPdLIEKLIKEGKKVG-VFPihEYWLDIGRPE 214
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-117 8.42e-30

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: 110.38  E-value: 8.42e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   1 MKAMILAAGKGERLRPLTLHTPKPLVRAAGTPLIEFHVRALAAAGFTELVINHAWLGQQIEDYLGD-GGRFGLRIAYSAE 79
Cdd:cd06425     1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEyEKKLGIKITFSIE 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2495647026  80 GEPLETGGGIFKALPLLG--DEPFLVVNGDIWTDCDFATL 117
Cdd:cd06425    81 TEPLGTAGPLALARDLLGddDEPFFVLNSDVICDFPLAEL 120
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 2-223 9.88e-29

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: 110.57  E-value: 9.88e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   2 KAMILAAGKGERLRPLTLHTPKPLVRAAGTPLIEFHVRALAAAGFTEL-VINHAWLGQQIEDYLGDGGRFGLRIAYSAEG 80
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIgIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026  81 EPLETGGGIFKALPLLGDEPFLVVNGD------------IWTDCDFAtlrrpldglAHLVLVDNPAHHQSGDFLLRDGRV 148
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDnliqdgisrfvkSFEEKDYD---------ALILLTKVRDPTAFGVAVLEDGKR 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026 149 TDAVAGEPSLTYSGMAVLHPRLFAGCQPGAFK-LAPLLRAAM--ADG---------QVSGERFAGRWIDVGTHERLADVE 216
Cdd:TIGR01208 152 ILKLVEKPKEPPSNLAVVGLYMFRPLIFEAIKnIKPSWRGELeiTDAiqwliekgyKVGGSKVTGWWKDTGKPEDLLDAN 231


                  ....*..
gi 2495647026 217 RLLAAEA 223
Cdd:TIGR01208 232 RLILDEV 238
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-107 1.06e-25

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 100.93  E-value: 1.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   1 MKAMILAAGKGERLRPLTLHTPKPLVRAAGTPLIEFHVRALAAAGFTE-LVINHAWLGQQIEDYLGDGGRFGLRIAYSAE 79
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREiLIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100
                  ....*....|....*....|....*...
gi 2495647026  80 GEPLETGGGIFKALPLLGDEPFLVVNGD 107
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGD 108
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-220 8.14e-24

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: 95.01  E-value: 8.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   2 KAMILAAGKGERLRPLTLHTPKPLVRAAGT-PLIEFHVRALAAAGFTE-LVINHAWLGQQIEDYLGDGGRFGLRIAYSAE 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREiIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026  80 GEPLETGGGIFKALPLLGDE--PFLVVNGDIWTDCDF-ATLRRPLD-GLAHLVLVDNPAHHQSGDFLL----RDGRVTDA 151
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEksDVLVLGGDHIYRMDLeQAVKFHIEkAADATVTFGIVPVEPPTGYGVvefdDNGRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026 152 V---AGEPSLTY---------SGMAVLHPRLFAGCQPGAFKLAPLLRAAMADGQVSGERF--AGRWIDVGTHERLADVER 217
Cdd:pfam00483 161 VekpKLPKASNYasmgiyifnSGVLDFLAKYLEELKRGEDEITDILPKALEDGKLAYAFIfkGYAWLDVGTWDSLWEANL 240


                  ...
gi 2495647026 218 LLA 220
Cdd:pfam00483 241 FLL 243
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-108 3.98e-22

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 90.30  E-value: 3.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   2 KAMILAAGKGERLRPLTLHTPKPLVRAAGTPLIEFHVRALAAAGFTELVINHAWLGQQIEDYLGDGGrFGLRIAYSAEGE 81
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALARPG-PDVTFVYNPDYD 79

                          90       100
                  ....*....|....*....|....*..
gi 2495647026  82 PLETGGGIFKALPLLgDEPFLVVNGDI 108
Cdd:COG1213    80 ETNNIYSLWLAREAL-DEDFLLLNGDV 105
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 3-114 3.03e-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: 85.36  E-value: 3.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   3 AMILAAGKGERLRPLTLHTPKPLVRAAGTPLIEFHVRALAAAGFTELVINHAWLGQQIEDYLGDggRFGLRIAYSAegEP 82
Cdd:cd02523     1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKK--YPNIKFVYNP--DY 76

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2495647026  83 LETGGGI--FKALPLLgDEPFLVVNGDIWTDCDF 114
Cdd:cd02523    77 AETNNIYslYLARDFL-DEDFLLLEGDVVFDPSI 109
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 3-114 9.38e-16

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: 73.83  E-value: 9.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   3 AMILAAG--KGERLRPLTLHTPKPLVRAAGTPLIEFHVRALAA-AGFTELVINHAWLGQQIEDYLGDGGR-FGLRIAYSA 78
Cdd:cd06428     1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKvPDLKEVLLIGFYPESVFSDFISDAQQeFNVPIRYLQ 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2495647026  79 EGEPLETGGGI--FKALPLLGD-EPFLVVNGDIWtdCDF 114
Cdd:cd06428    81 EYKPLGTAGGLyhFRDQILAGNpSAFFVLNADVC--CDF 117
LicC COG4750
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid ...
 1-51 2.30e-13

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


Pssm-ID: 443784 [Multi-domain]  Cd Length: 228  Bit Score: 66.78  E-value: 2.30e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2495647026   1 MKAMILAAGKGERLRPLTLHTPKPLVRAAGTPLIEFHVRALAAAGFTELVI 51
Cdd:COG4750     1 MNAIILAAGLGSRFAPITYETPKGLLKVNGEPLIERQIRQLHEAGITDITV 51
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-107 7.35e-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: 65.29  E-value: 7.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   1 MKAMILAAGKGERLRPLTLHTPKPLVRAAGTPLIEFHVRALAAAGFTE-LVINHawlGQQIEDY---LGDGGRFGLRIAY 76
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREiLIIST---PEDLPLFkelLGDGSDLGIRITY 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2495647026  77 SAEGEPletgGGIFKALPL----LGDEPFLVVNGD 107
Cdd:cd02538    78 AVQPKP----GGLAQAFIIgeefIGDDPVCLILGD 108
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-210 4.14e-10

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: 57.93  E-value: 4.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   1 MKAMILAAGKGERLRPLTLHTPK---PLVraaGTPLIEFHVRALAAAGFTELVI-----NHAwlgqqIEDY--------- 63
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKemlPIV---DKPVIQYIVEEAVAAGIEDIIIvtgrgKRA-----IEDHfdrsyelee 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026  64 -LGDGGRFGL-----------RIAYSAEGEPLETGGGIFKALPLLGDEPFLVVNGDIWTDCDFATLRRPLD-----GLAH 126
Cdd:cd02541    73 tLEKKGKTDLleevriisdlaNIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKEPCLKQLIEayektGASV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026 127 LVLVDNPAHHQS-------GDFLLRDGRVTDAV-----AGEPSLTYS-GMAVLHPRLF---AGCQPGA---FKLAPLLRA 187
Cdd:cd02541   153 IAVEEVPPEDVSkygivkgEKIDGDVFKVKGLVekpkpEEAPSNLAIvGRYVLTPDIFdilENTKPGKggeIQLTDAIAK 232

                         250       260
                  ....*....|....*....|...
gi 2495647026 188 AMADGQVSGERFAGRWIDVGTHE 210
Cdd:cd02541   233 LLEEEPVYAYVFEGKRYDCGNKL 255
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 1-107 1.03e-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: 57.34  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   1 MKAMILAAGKGERLRPltlHTPKPLVRAAGTPLIEfHV-RALAAAGFTEL--VINHAwlGQQIEDYLGDggrFGLRIAYS 77
Cdd:COG1207     3 LAVVILAAGKGTRMKS---KLPKVLHPLAGKPMLE-HVlDAARALGPDRIvvVVGHG--AEQVRAALAD---LDVEFVLQ 73

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2495647026  78 AegEPLETGGGIFKALPLLG--DEPFLVVNGD 107
Cdd:COG1207    74 E--EQLGTGHAVQQALPALPgdDGTVLVLYGD 103
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 1-115 3.83e-09

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: 54.57  E-value: 3.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   1 MKAMILAAGKGERLRPLTLHTPKPLVRAAGTPLIEFHVRALAAAGFTELVI---NHAwlgQQIEDYLGDGGRFGLR---- 73
Cdd:cd02507     1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVvccEHS---QAIIEHLLKSKWSSLSskmi 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2495647026  74 --IAYSAEGEPLETGGGIFKALPLLgDEPFLVVNGDIWTDCDFA 115
Cdd:cd02507    78 vdVITSDLCESAGDALRLRDIRGLI-RSDFLLLSCDLVSNIPLS 120
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 3-108 5.81e-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: 54.44  E-value: 5.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   3 AMILAAGKGERLRPltlHTPKPLVRAAGTPLIEFHVRALAAAGFTE--LVINHAwlGQQIEDYLGDggrFGLRIAYSAeg 80
Cdd:cd02540     1 AVILAAGKGTRMKS---DLPKVLHPLAGKPMLEHVLDAARALGPDRivVVVGHG--AEQVKKALAN---PNVEFVLQE-- 70

                          90       100       110
                  ....*....|....*....|....*....|
gi 2495647026  81 EPLETGGGIFKALPLLGD--EPFLVVNGDI 108
Cdd:cd02540    71 EQLGTGHAVKQALPALKDfeGDVLVLYGDV 100
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 1-159 5.18e-08

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: 51.51  E-value: 5.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   1 MKAMILAAGKGERLRPLTLHTPKPLVRAAGTPLIEFHVRALAAAGFTE-LVINHAWLGQQIEDYLGDGGRFGLRIAYSAE 79
Cdd:cd04198     1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDvIVVVPEEEQAEISTYLRSFPLNLKQKLDEVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026  80 gEPLETGGGIFKALPLLGDE---PFLVVNgdiwtdCDFATlrrplDGLAHLVLVDNPAHHQSGDFLLRDGRVTDAVAGEP 156
Cdd:cd04198    81 -IVLDEDMGTADSLRHIRKKikkDFLVLS------CDLIT-----DLPLIELVDLHRSHDASLTVLLYPPPVSSEQKGGK 148


                  ...
gi 2495647026 157 SLT 159
Cdd:cd04198   149 GKS 151
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-111 6.32e-08

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 51.81  E-value: 6.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   1 MKAMILAAGKGERLRPLTLHTPKPLVRAAGTPLIEFHVRALAAAGFTELVI----------NH--------AWLGQQIED 62
Cdd:PRK10122    4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLvthasknaveNHfdtsyeleSLLEQRVKR 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2495647026  63 YLGDGGRF----GLRIAYSAEGEPLETGGGIFKALPLLGDEPFLVVNGDIWTD 111
Cdd:PRK10122   84 QLLAEVQSicppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVID 136
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-220 1.31e-07

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 50.83  E-value: 1.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   2 KAMILAAGKGERLRPLTLHTPKPLVRAAGTPLIEFHVRALAAAGFTE-LVINHAWLGQQIEDYLGDGGRFGLRIAYSAEG 80
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDiLIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026  81 EPLETGGGIFKALPLLG-DEPFLVVNGDIWTDCDF-----ATLRRPLDGLAHLVLVDNPAHHQSGDFllrDGRVTDAVAG 154
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGgDDCALVLGDNIFYGHDLpklmeAAVNKESGATVFAYHVNDPERYGVVEF---DQNGTAISLE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026 155 EPSLT------------YSGMAVLHPRLFAGCQPGAFKLAPLLRAAMADGQVS----GERFAgrWIDVGTHERLADVERL 218
Cdd:PRK15480  162 EKPLQpksnyavtglyfYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSvammGRGYA--WLDTGTHQSLIEASNF 239


                  ..
gi 2495647026 219 LA 220
Cdd:PRK15480  240 IA 241
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-64 2.70e-06

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: 46.45  E-value: 2.70e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2495647026   3 AMILAAGKGERLRPLTLHTPKPLVRAAGTPLIEFHVRALAAAGFTELVINHAWLGQQIEDYL 64
Cdd:cd04197     3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYI 64
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-107 3.44e-06

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 47.13  E-value: 3.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   3 AMILAAGKGERLRPltlHTPKPLVRAAGTPLIEFHVRALAAAGFTEL--VINHAwlGQQIEDYLGDggrfglRIAYSAEG 80
Cdd:PRK14354    5 AIILAAGKGTRMKS---KLPKVLHKVCGKPMVEHVVDSVKKAGIDKIvtVVGHG--AEEVKEVLGD------RSEFALQE 73

                          90       100
                  ....*....|....*....|....*....
gi 2495647026  81 EPLETGGGIFKALPLLGDEP--FLVVNGD 107
Cdd:PRK14354   74 EQLGTGHAVMQAEEFLADKEgtTLVICGD 102
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-107 2.41e-05

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 44.25  E-value: 2.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   2 KAMILAAGKGERLRPLTLHTPK---PLVRaagTPLIEFHVRALAAAGFTELVI-----NHAwlgqqIEDY---------- 63
Cdd:COG1210     5 KAVIPVAGLGTRFLPATKAIPKemlPIVD---KPLIQYVVEEAVAAGIEEIIFvtgrgKRA-----IEDHfdrsyeleat 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2495647026  64 LGDGGRFGL-----------RIAYSAEGEPLETGGGIFKALPLLGDEPFLVVNGD 107
Cdd:COG1210    77 LEAKGKEELleevrsisplaNIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGD 131
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-51 6.73e-05

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 42.07  E-value: 6.73e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2495647026   3 AMILAAGKGERLrpltlHTPKPLVRAAGTPLIEFHVRALAAAGFTELVI 51
Cdd:COG2068     6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVV 49
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-152 9.62e-05

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 42.71  E-value: 9.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   1 MKAMILAAGKGERLRPltlHTPKPLVRAAGTPLIEfHV----RALAAAGfTELVINHAwlGQQIEDYLGDGgrfglRIAY 76
Cdd:PRK09451    6 MSVVILAAGKGTRMYS---DLPKVLHTLAGKPMVQ-HVidaaNELGAQH-VHLVYGHG--GDLLKQTLADE-----PLNW 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026  77 SAEGEPLETGGGIFKALPLLGD-EPFLVVNGD---IWTDcdfaTLRR-----PLDGLAHL-VLVDNPAHHqsGDFLLRDG 146
Cdd:PRK09451   74 VLQAEQLGTGHAMQQAAPFFADdEDILMLYGDvplISVE----TLQRlrdakPQGGIGLLtVKLDNPTGY--GRITRENG 147


                  ....*.
gi 2495647026 147 RVTDAV 152
Cdd:PRK09451  148 KVVGIV 153
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-111 1.05e-04

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 42.20  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   2 KAMILAAGKGERLRPLTLHTPKPLVRAAGTPLIEFHVRALAAAGFTELVI----------NH--------AWLGQQIEDY 63
Cdd:PRK13389   10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLvthssknsieNHfdtsfeleAMLEKRVKRQ 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2495647026  64 LGDGGRF----GLRIAYSAEGEPLETGGGIFKALPLLGDEPFLVVNGDIWTD 111
Cdd:PRK13389   90 LLDEVQSicppHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILD 141
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-172 1.75e-04

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 41.77  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   3 AMILAAGKGERLRPltlHTPKPLVRAAGTPLIEFHVRALAAAGFTELVI---NHAwlgQQIEDYLgdgGRFGLRIAYSAE 79
Cdd:PRK14353    8 AIILAAGEGTRMKS---SLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVvvgPGA---EAVAAAA---AKIAPDAEIFVQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026  80 GEPLETGGGIFKALPLL--GDEPFLVVNGD--IWTDCDFATLRRPLDGLAHLVLV----DNPAhhQSGDFLLRDGRVT-- 149
Cdd:PRK14353   79 KERLGTAHAVLAAREALagGYGDVLVLYGDtpLITAETLARLRERLADGADVVVLgfraADPT--GYGRLIVKGGRLVai 156

                         170       180       190
                  ....*....|....*....|....*....|
gi 2495647026 150 ----DAVAGEPSLTY--SG-MAVLHPRLFA 172
Cdd:PRK14353  157 veekDASDEERAITLcnSGvMAADGADALA 186
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 3-24 2.12e-04

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 41.60  E-value: 2.12e-04
                          10        20
                  ....*....|....*....|..
gi 2495647026   3 AMILAAGKGERLRPLTLHTPKP 24
Cdd:COG0448     4 AIILAGGRGSRLGPLTKDRAKP 25
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 3-117 2.35e-04

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: 41.02  E-value: 2.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   3 AMILAAGKGERLRPLTLHTPKPLVRAAGTPLIeFHV-RALAAAGFTELVINHAWLGQQIEDYLGD-------------GG 68
Cdd:cd02524     1 VVILAGGLGTRLSEETELKPKPMVEIGGRPIL-WHImKIYSHYGHNDFILCLGYKGHVIKEYFLNyflhnsdvtidlgTN 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2495647026  69 RFGL--------RIAYSAEGEPLETGGGIFKALPLLGD-EPFLVVNGDIWTDCDFATL 117
Cdd:cd02524    80 RIELhnsdiedwKVTLVDTGLNTMTGGRLKRVRRYLGDdETFMLTYGDGVSDVNINAL 137
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 3-51 4.38e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 40.58  E-value: 4.38e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2495647026   3 AMILAAGKGERLRPLTLHTPKPLVRAAGT-PLIEFHVRALAAAGFTELVI 51
Cdd:PRK00844    8 AIVLAGGEGKRLMPLTADRAKPAVPFGGSyRLIDFVLSNLVNSGYLRIYV 57
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 3-26 6.22e-04

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: 39.45  E-value: 6.22e-04
                          10        20
                  ....*....|....*....|....
gi 2495647026   3 AMILAAGKGERLRPLTLHTPKPLV 26
Cdd:cd02508     1 AIILAGGEGTRLSPLTKKRAKPAV 24
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-107 7.30e-04

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 40.09  E-value: 7.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   3 AMILAAGKGERlrpltLHTPKPLVRAA--GTPLIEFHVRALAAAgFTE---LVINHAwlGQQIEDYLGD-GGRFGLriay 76
Cdd:PRK14356    8 ALILAAGKGTR-----MHSDKPKVLQTllGEPMLRFVYRALRPL-FGDnvwTVVGHR--ADMVRAAFPDeDARFVL---- 75

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2495647026  77 saEGEPLETGGGIFKALPLL---GDEPFLVVNGD 107
Cdd:PRK14356   76 --QEQQLGTGHALQCAWPSLtaaGLDRVLVVNGD 107
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 1-26 1.08e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 39.47  E-value: 1.08e-03
                          10        20
                  ....*....|....*....|....*.
gi 2495647026   1 MKAMILAAGKGERLRPLTLHTPKPLV 26
Cdd:PRK05293    4 MLAMILAGGQGTRLGKLTKNIAKPAV 29
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 3-108 1.15e-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: 38.33  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   3 AMILAAGKGERLRpltlhTPKPLVRAAGTPLIEFHVRALAAAgFTELVINHAWlgQQIEDYLGDGGRFGLRIAYSAEGep 82
Cdd:pfam12804   1 AVILAGGRSSRMG-----GDKALLPLGGKPLLERVLERLRPA-GDEVVVVAND--EEVLAALAGLGVPVVPDPDPGQG-- 70

                          90       100
                  ....*....|....*....|....*..
gi 2495647026  83 leTGGGIFKALPLLGD-EPFLVVNGDI 108
Cdd:pfam12804  71 --PLAGLLAALRAAPGaDAVLVLACDM 95
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 3-26 2.09e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 38.67  E-value: 2.09e-03
                          10        20
                  ....*....|....*....|....
gi 2495647026   3 AMILAAGKGERLRPLTLHTPKPLV 26
Cdd:PRK00725   18 ALILAGGRGSRLKELTDKRAKPAV 41
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-102 3.42e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 37.80  E-value: 3.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   3 AMILAAGKGERLRPLTLHTPKPLvraAGTPLIEFHVRALAAAGFTELVINHAWLGQQIEDYLGDGGrfglRIAYSAEGEP 82
Cdd:PRK14355    6 AIILAAGKGTRMKSDLVKVMHPL---AGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDG----DVSFALQEEQ 78

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2495647026  83 LETGGGIFKALP-----------LLGDEPFL 102
Cdd:PRK14355   79 LGTGHAVACAAPaldgfsgtvliLCGDVPLL 109
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-51 3.98e-03

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: 36.77  E-value: 3.98e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2495647026   3 AMILAAGKGERLrpltlHTPKPLVRAAGTPLIEFHVRALAAAGFTELVI 51
Cdd:cd04182     3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIV 46
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 1-107 5.35e-03

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 37.27  E-value: 5.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   1 MKAMILAAGKGERLRPLTlhtPKPLVRAAGTPLIEFHVRALAAAGFTELVINHAWLGQQIEDYLGDGGrfglrIAYSAEG 80
Cdd:PRK14358    8 LDVVILAAGQGTRMKSAL---PKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQGSG-----VAFARQE 79

                          90       100
                  ....*....|....*....|....*....
gi 2495647026  81 EPLETGGGIFKALPLL--GDEPFLVVNGD 107
Cdd:PRK14358   80 QQLGTGDAFLSGASALteGDADILVLYGD 108
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 6-108 5.72e-03

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: 36.40  E-value: 5.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   6 LAAGKGERLRPltlhTPKPLVRAAGTPLIEFHVRALAAAGFTELVI----NHawlgQQIEDYLGDGgrfGLRIaysaege 81
Cdd:COG2266     1 MAGGKGTRLGG----GEKPLLEICGKPMIDRVIDALEESCIDKIYVavspNT----PKTREYLKER---GVEV------- 62

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2495647026  82 pLETGGG-----IFKALPLLgDEPFLVVNGDI 108
Cdd:COG2266    63 -IETPGEgyvedLNEALESI-SGPVLVVPADL 92
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-107 9.59e-03

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: 35.94  E-value: 9.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2495647026   1 MKAMILAAGKGERLrpltlHTPKPLVRAAGTPLIEFHVRALAAAgFTELVIN------HAWLG-QQIEDYLGDGGrfglr 73
Cdd:COG0746     5 ITGVILAGGRSRRM-----GQDKALLPLGGRPLLERVLERLRPQ-VDEVVIVanrperYAALGvPVVPDDPPGAG----- 73

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2495647026  74 iaysaegePLetgGGIFKALPLLGDEPFLVVNGD 107
Cdd:COG0746    74 --------PL---AGILAALEAAPAEWVLVLACD 96
 
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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