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Conserved domains on  [gi|1740188850|ref|WP_149079947|]
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MULTISPECIES: sugar phosphate nucleotidyltransferase [Natrialba]

Protein Classification

NDP-sugar synthase; nucleotidyltransferase family protein( domain architecture ID 11440243)

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; nucleotidyltransferase family protein similar to Pseudomonas putida N-acetylmuramic acid alpha-1-phosphate (MurNAc-alpha1-P) uridylyltransferase MurU, which catalyzes the synthesis of uridine diphosphate (UDP)-MurNAc, a crucial precursor of the bacterial peptidoglycan cell wall

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 ...
 2-244 1.50e-54

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: 178.04  E-value: 1.50e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850   2 KAIVLAGGYATRLWPITRHRPKMFLPIGDATVIDRIFTELEADDrISEVFVSTNRRfADHFREHL-SGSRY--------- 71
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAG-ITEIVINVGYL-AEQIEEYFgDGSRFgvrityvde 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850  72 EKPtltveettaetekLGVVGALAQLVEREGiDEDTVVIAGDNLLSFDVSEFVDAFRSAASPM-IATYDvgsVDRASSYG 150
Cdd:COG1208    79 GEP-------------LGTGGALKRALPLLG-DEPFLVLNGDILTDLDLAALLAFHREKGADAtLALVP---VPDPSRYG 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 151 VVDV-ADGEVVDFAEKPTNPTSSLVSIACYGFPAETLPslstYLEEGNNPDEPGWFvQWLLERESIRAFPFEEAWFDIGT 229
Cdd:COG1208   142 VVELdGDGRVTRFVEKPEEPPSNLINAGIYVLEPEIFD----YIPEGEPFDLEDLL-PRLIAEGRVYGYVHDGYWLDIGT 216

                         250
                  ....*....|....*
gi 1740188850 230 PECYLDAVAWHLQGE 244
Cdd:COG1208   217 PEDLLEANALLLSGK 231
LbetaH super family cl00160
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 249-322 9.10e-07

Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.


The actual alignment was detected with superfamily member cd04651:

Pssm-ID: 469633 [Multi-domain]  Cd Length: 104  Bit Score: 46.69  E-value: 9.10e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1740188850 249 ESATVERTTLGENVHVMAGAEVTDshlsrSVIFPDATI-QDCEVRSSIIDRktaldglefnGALVGAHTRIVNGE 322
Cdd:cd04651    22 SGGTVENSVLFRGVRVGSGSVVED-----SVIMPNVGIgRNAVIRRAIIDK----------NVVIPDGVVIGGDP 81
 
Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-244 1.50e-54

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: 178.04  E-value: 1.50e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850   2 KAIVLAGGYATRLWPITRHRPKMFLPIGDATVIDRIFTELEADDrISEVFVSTNRRfADHFREHL-SGSRY--------- 71
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAG-ITEIVINVGYL-AEQIEEYFgDGSRFgvrityvde 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850  72 EKPtltveettaetekLGVVGALAQLVEREGiDEDTVVIAGDNLLSFDVSEFVDAFRSAASPM-IATYDvgsVDRASSYG 150
Cdd:COG1208    79 GEP-------------LGTGGALKRALPLLG-DEPFLVLNGDILTDLDLAALLAFHREKGADAtLALVP---VPDPSRYG 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 151 VVDV-ADGEVVDFAEKPTNPTSSLVSIACYGFPAETLPslstYLEEGNNPDEPGWFvQWLLERESIRAFPFEEAWFDIGT 229
Cdd:COG1208   142 VVELdGDGRVTRFVEKPEEPPSNLINAGIYVLEPEIFD----YIPEGEPFDLEDLL-PRLIAEGRVYGYVHDGYWLDIGT 216

                         250
                  ....*....|....*
gi 1740188850 230 PECYLDAVAWHLQGE 244
Cdd:COG1208   217 PEDLLEANALLLSGK 231
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-228 3.90e-50

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: 165.83  E-value: 3.90e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850   3 AIVLAGGYATRLWPITRHRPKMFLPIGDATVIDRIFTELEADDrISEVFVSTNRRFADHFREHLSGSRY---------EK 73
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAG-IDEIILVVGYLGEQIEEYFGDGSKFgvnieyvvqEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850  74 PtltveettaetekLGVVGALAQlVEREGIDEDTVVIAGDNLLSFDVSEFVDAFRSaaSPMIATYDVGSVDRASSYGVVD 153
Cdd:cd04181    80 P-------------LGTAGAVRN-AEDFLGDDDFLVVNGDVLTDLDLSELLRFHRE--KGADATIAVKEVEDPSRYGVVE 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1740188850 154 V-ADGEVVDFAEKPTNPTSSLVSIACYGFPAETLPSLSTYLEEGnnPDEPGWFVQWLLERESIRAFPFEEAWFDIG 228
Cdd:cd04181   144 LdDDGRVTRFVEKPTLPESNLANAGIYIFEPEILDYIPEILPRG--EDELTDAIPLLIEEGKVYGYPVDGYWLDIG 217
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-236 1.44e-32

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: 120.82  E-value: 1.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850   2 KAIVLAGGYATRLWPITRHRPKMFLPIGDA-TVIDRIFTELeADDRISEVFVSTNRRFADHFREHLsgsRYEKPTLTVEE 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRL-ANAGIREIIVILTQEHRFMLNELL---GDGSKFGVQIT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850  81 TTAETEKLGVVGALAQ---LVEREgiDEDTVVIAGDNLLSFDVSEFVDAFRSAASPMIATYDVGSVDRASSYGVVDV-AD 156
Cdd:pfam00483  77 YALQPEGKGTAPAVALaadFLGDE--KSDVLVLGGDHIYRMDLEQAVKFHIEKAADATVTFGIVPVEPPTGYGVVEFdDN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 157 GEVVDFAEKPTNPT-SSLVSIACYGFPAETLPSLSTYLEEGNN-PDEPGWFVQWLLERESIR-AFPFE-EAWFDIGTPEC 232
Cdd:pfam00483 155 GRVIRFVEKPKLPKaSNYASMGIYIFNSGVLDFLAKYLEELKRgEDEITDILPKALEDGKLAyAFIFKgYAWLDVGTWDS 234


                  ....
gi 1740188850 233 YLDA 236
Cdd:pfam00483 235 LWEA 238
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-270 5.09e-31

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: 120.39  E-value: 5.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850   1 MKAIVLAGGYATRLWPITRHRPKMFLPIGDATVIDRIFTELEaDDRISEVFVSTNRRfADHFREHLS-GSRYEKPTLTVE 79
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALR-DAGIDDFVFVVGYG-KEKVREYFGdGSRGGVPIEYVV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850  80 ETTaeteKLGVVGALAQLveREGIDEDTVVIAGDNLLSfdvSEFVDAFRSAASPMIATYDVgsvDRASSYGVVDVADGEV 159
Cdd:TIGR03992  79 QEE----QLGTADALGSA--KEYVDDEFLVLNGDVLLD---SDLLERLIRAEAPAIAVVEV---DDPSDYGVVETDGGRV 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 160 VDFAEKPTNPTSSLVSIACYGFPAETLPSLstyleEGNNPDEPGWF-----VQWLLERESIRAFPFEEAWFDIGTPECYL 234
Cdd:TIGR03992 147 TGIVEKPENPPSNLINAGIYLFSPEIFELL-----EKTKLSPRGEYeltdaLQLLIDEGKVKAVELDGFWLDVGRPWDLL 221

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1740188850 235 DAVAWHLQGETRVAESATVERTTLGENVHVMAGAEV 270
Cdd:TIGR03992 222 DANEALLDNLEPRIEGTVEENVTIKGPVVIGEGAVI 257
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 101-322 9.35e-16

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 77.22  E-value: 9.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 101 EGIDEDTVVI-AGDNLLSFDVSEFVDAFRS-AASPMIATYDVgSVDRASSYGVVDV-ADGEVVDFAEKPTNPTSSLVSIA 177
Cdd:PRK05293  113 DQYDPEYVLIlSGDHIYKMDYDKMLDYHKEkEADVTIAVIEV-PWEEASRFGIMNTdENMRIVEFEEKPKNPKSNLASMG 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 178 CYGFpaeTLPSLSTYLEEG-NNPDEPGWFVQ-----WLLERESIRAFPFEEAWFDIGTPECYLDA--------------- 236
Cdd:PRK05293  192 IYIF---NWKRLKEYLIEDeKNPNSSHDFGKnviplYLEEGEKLYAYPFKGYWKDVGTIESLWEAnmellrpenplnlfd 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 237 VAW------------HLQGETRVAES---------ATVERTTLGENVHVMAGAEVTDshlsrSVIFPDATI-QDCEVRSS 294
Cdd:PRK05293  269 RNWriysvnpnlppqYIAENAKVKNSlvvegcvvyGTVEHSVLFQGVQVGEGSVVKD-----SVIMPGAKIgENVVIERA 343

                         250       260
                  ....*....|....*....|....*...
gi 1740188850 295 IIDrktaldglefNGALVGAHTRIVNGE 322
Cdd:PRK05293  344 IIG----------ENAVIGDGVIIGGGK 361
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 249-322 9.10e-07

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


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 46.69  E-value: 9.10e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1740188850 249 ESATVERTTLGENVHVMAGAEVTDshlsrSVIFPDATI-QDCEVRSSIIDRktaldglefnGALVGAHTRIVNGE 322
Cdd:cd04651    22 SGGTVENSVLFRGVRVGSGSVVED-----SVIMPNVGIgRNAVIRRAIIDK----------NVVIPDGVVIGGDP 81
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 240-286 8.60e-04

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 40.69  E-value: 8.60e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1740188850 240 HLQGETRVAESATV-ERTTLgENVHVMAGAEVTDSHLSRSVIFPDATI 286
Cdd:PRK14352  285 QLLGRTTIGEDAVVgPDTTL-TDVTVGEGASVVRTHGSESEIGAGATV 331
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 240-286 7.66e-03

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: 37.70  E-value: 7.66e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1740188850 240 HLQGETRVAESATVERTTLGENVHVMAGAEVTDSHLSRSVIFPDATI 286
Cdd:COG1207   280 ILEGKTVIGEGVVIGPNCTLKDSTIGDGVVIKYSVIEDAVVGAGATV 326
 
Name Accession Description Interval E-value
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-244 1.50e-54

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: 178.04  E-value: 1.50e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850   2 KAIVLAGGYATRLWPITRHRPKMFLPIGDATVIDRIFTELEADDrISEVFVSTNRRfADHFREHL-SGSRY--------- 71
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAG-ITEIVINVGYL-AEQIEEYFgDGSRFgvrityvde 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850  72 EKPtltveettaetekLGVVGALAQLVEREGiDEDTVVIAGDNLLSFDVSEFVDAFRSAASPM-IATYDvgsVDRASSYG 150
Cdd:COG1208    79 GEP-------------LGTGGALKRALPLLG-DEPFLVLNGDILTDLDLAALLAFHREKGADAtLALVP---VPDPSRYG 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 151 VVDV-ADGEVVDFAEKPTNPTSSLVSIACYGFPAETLPslstYLEEGNNPDEPGWFvQWLLERESIRAFPFEEAWFDIGT 229
Cdd:COG1208   142 VVELdGDGRVTRFVEKPEEPPSNLINAGIYVLEPEIFD----YIPEGEPFDLEDLL-PRLIAEGRVYGYVHDGYWLDIGT 216

                         250
                  ....*....|....*
gi 1740188850 230 PECYLDAVAWHLQGE 244
Cdd:COG1208   217 PEDLLEANALLLSGK 231
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-228 3.90e-50

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: 165.83  E-value: 3.90e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850   3 AIVLAGGYATRLWPITRHRPKMFLPIGDATVIDRIFTELEADDrISEVFVSTNRRFADHFREHLSGSRY---------EK 73
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAG-IDEIILVVGYLGEQIEEYFGDGSKFgvnieyvvqEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850  74 PtltveettaetekLGVVGALAQlVEREGIDEDTVVIAGDNLLSFDVSEFVDAFRSaaSPMIATYDVGSVDRASSYGVVD 153
Cdd:cd04181    80 P-------------LGTAGAVRN-AEDFLGDDDFLVVNGDVLTDLDLSELLRFHRE--KGADATIAVKEVEDPSRYGVVE 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1740188850 154 V-ADGEVVDFAEKPTNPTSSLVSIACYGFPAETLPSLSTYLEEGnnPDEPGWFVQWLLERESIRAFPFEEAWFDIG 228
Cdd:cd04181   144 LdDDGRVTRFVEKPTLPESNLANAGIYIFEPEILDYIPEILPRG--EDELTDAIPLLIEEGKVYGYPVDGYWLDIG 217
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-236 1.44e-32

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: 120.82  E-value: 1.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850   2 KAIVLAGGYATRLWPITRHRPKMFLPIGDA-TVIDRIFTELeADDRISEVFVSTNRRFADHFREHLsgsRYEKPTLTVEE 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRL-ANAGIREIIVILTQEHRFMLNELL---GDGSKFGVQIT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850  81 TTAETEKLGVVGALAQ---LVEREgiDEDTVVIAGDNLLSFDVSEFVDAFRSAASPMIATYDVGSVDRASSYGVVDV-AD 156
Cdd:pfam00483  77 YALQPEGKGTAPAVALaadFLGDE--KSDVLVLGGDHIYRMDLEQAVKFHIEKAADATVTFGIVPVEPPTGYGVVEFdDN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 157 GEVVDFAEKPTNPT-SSLVSIACYGFPAETLPSLSTYLEEGNN-PDEPGWFVQWLLERESIR-AFPFE-EAWFDIGTPEC 232
Cdd:pfam00483 155 GRVIRFVEKPKLPKaSNYASMGIYIFNSGVLDFLAKYLEELKRgEDEITDILPKALEDGKLAyAFIFKgYAWLDVGTWDS 234


                  ....
gi 1740188850 233 YLDA 236
Cdd:pfam00483 235 LWEA 238
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-270 5.09e-31

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: 120.39  E-value: 5.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850   1 MKAIVLAGGYATRLWPITRHRPKMFLPIGDATVIDRIFTELEaDDRISEVFVSTNRRfADHFREHLS-GSRYEKPTLTVE 79
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALR-DAGIDDFVFVVGYG-KEKVREYFGdGSRGGVPIEYVV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850  80 ETTaeteKLGVVGALAQLveREGIDEDTVVIAGDNLLSfdvSEFVDAFRSAASPMIATYDVgsvDRASSYGVVDVADGEV 159
Cdd:TIGR03992  79 QEE----QLGTADALGSA--KEYVDDEFLVLNGDVLLD---SDLLERLIRAEAPAIAVVEV---DDPSDYGVVETDGGRV 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 160 VDFAEKPTNPTSSLVSIACYGFPAETLPSLstyleEGNNPDEPGWF-----VQWLLERESIRAFPFEEAWFDIGTPECYL 234
Cdd:TIGR03992 147 TGIVEKPENPPSNLINAGIYLFSPEIFELL-----EKTKLSPRGEYeltdaLQLLIDEGKVKAVELDGFWLDVGRPWDLL 221

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1740188850 235 DAVAWHLQGETRVAESATVERTTLGENVHVMAGAEV 270
Cdd:TIGR03992 222 DANEALLDNLEPRIEGTVEENVTIKGPVVIGEGAVI 257
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 1-241 7.25e-30

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: 113.43  E-value: 7.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850   1 MKAIVLAGGYATRLWPITRHRPKMFLPIGDATVIDRIFTELeADDRISEVFVSTNrRFADHFREHL-SGSRY-------- 71
Cdd:cd04189     1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDL-REAGIEDIGIVVG-PTGEEIKEALgDGSRFgvrityil 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850  72 -EKPtltveettaetekLGVvgALAQLVEREGI-DEDTVVIAGDNLLSFDVSEFVDAFRSAASPmiATYDVGSVDRASSY 149
Cdd:cd04189    79 qEEP-------------LGL--AHAVLAARDFLgDEPFVVYLGDNLIQEGISPLVRDFLEEDAD--ASILLAEVEDPRRF 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 150 GVVDVADGEVVDFAEKPTNPTSSLVSIACYGFPAETLPSLSTYleegnnpdEPGW--------FVQWLLER-ESIRAFPF 220
Cdd:cd04189   142 GVAVVDDGRIVRLVEKPKEPPSNLALVGVYAFTPAIFDAISRL--------KPSWrgeleitdAIQWLIDRgRRVGYSIV 213

                         250       260
                  ....*....|....*....|.
gi 1740188850 221 EEAWFDIGTPECYLDAVAWHL 241
Cdd:cd04189   214 TGWWKDTGTPEDLLEANRLLL 234
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-236 1.04e-26

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 106.33  E-value: 1.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850   1 MKAIVLAGGYATRLWPITRHRPKMFLPIGDATVIDRIFTEL-EADdrISEV-FVSTNrRFADHFREHL-SGSRY------ 71
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLmLAG--IREIlIISTP-EDGPQFERLLgDGSQLgikisy 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850  72 ---EKPtltveettaetekLGvvgaLAQ--LVEREGIDEDTVVIA-GDNLlsFDVSEFVDAFRSAASP----MIATYdvg 141
Cdd:COG1209    78 avqPEP-------------LG----LAHafIIAEDFIGGDPVALVlGDNI--FYGDGLSELLREAAAResgaTIFGY--- 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 142 SVDRASSYGVVDV-ADGEVVDFAEKPTNPTSSLVSIACYGFP------AETL-PS----------LSTYLEEGNNpdepg 203
Cdd:COG1209   136 KVEDPERYGVVEFdEDGRVVSLEEKPKEPKSNLAVTGLYFYDndvveiAKNLkPSargeleitdaNQAYLERGKL----- 210

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1740188850 204 wFVQWLLEresirafpfEEAWFDIGTPECYLDA 236
Cdd:COG1209   211 -VVELLGR---------GFAWLDTGTHESLLEA 233
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 3-233 9.15e-25

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: 99.55  E-value: 9.15e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850   3 AIVLAGGYATRLWPITRHRPKMFLPIGDATVIDRIFTELEADDrISEVFVSTNRRfADHFREHLsGSRYEKPTLTVEETT 82
Cdd:cd06915     1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQG-ISRIVLSVGYL-AEQIEEYF-GDGYRGGIRIYYVIE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850  83 AETekLGVVGALaQLVEREGIDEDTVVIAGDNLLSFDVSEFVDAFRSAASPM-IATYDVGSVDRassYGVVDV-ADGEVV 160
Cdd:cd06915    78 PEP--LGTGGAI-KNALPKLPEDQFLVLNGDTYFDVDLLALLAALRASGADAtMALRRVPDASR---YGNVTVdGDGRVI 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1740188850 161 DFAEKPTNPTSSLVSIACYGFPA---ETLPSLSTYLEEGnnpdepgwFVQWLLERESIRAFPFEEAWFDIGTPECY 233
Cdd:cd06915   152 AFVEKGPGAAPGLINGGVYLLRKeilAEIPADAFSLEAD--------VLPALVKRGRLYGFEVDGYFIDIGIPEDY 219
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 3-322 4.53e-23

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 97.84  E-value: 4.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850   3 AIVLAGGYATRLWPITRHRPKMFLPIG------DATV-------IDRIFteleaddriseVFV-----STNrrfaDHFRE 64
Cdd:COG0448     4 AIILAGGRGSRLGPLTKDRAKPAVPFGgkyriiDFPLsncvnsgIRRVG-----------VLTqykshSLN----DHIGS 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850  65 ----HLSGSR--------YEKPTLTVEEttaetekLGVVGALAQ---LVEREgiDEDTVVI-AGDNLLSFDVSEFVDAFR 128
Cdd:COG0448    69 gkpwDLDRKRggvfilppYQQREGEDWY-------QGTADAVYQnldFIERS--DPDYVLIlSGDHIYKMDYRQMLDFHI 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 129 -SAASPMIATYDVgSVDRASSYGVVDV-ADGEVVDFAEKPTNPTSSLVSIACYGFPAETLPSLSTYLEEGNNPDEPGWFV 206
Cdd:COG0448   140 eSGADITVACIEV-PREEASRFGVMEVdEDGRITEFEEKPKDPKSALASMGIYVFNKDVLIELLEEDAPNSSHDFGKDII 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 207 QWLLERESIRAFPFEEAWFDIGTPECYLDAvawH---LQGE-------------TR-------------------VAE-- 249
Cdd:COG0448   219 PRLLDRGKVYAYEFDGYWRDVGTIDSYYEA---NmdlLDPEpefnlydpewpiyTKqkdlppakfvrggkvknslVSNgc 295

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1740188850 250 --SATVERTTLGENVHVMAGAEVTDshlsrSVIFPDATI-QDCEVRSSIIDRktaldglefnGALVGAHTRIVNGE 322
Cdd:COG0448   296 iiSGTVENSVLFRGVRVESGAVVEN-----SVIMPGVVIgEGAVIENAIIDK----------NVVIPPGVVIGEDP 356
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 3-236 3.30e-20

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: 87.18  E-value: 3.30e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850   3 AIVLAGGYATRLWPITRHRPKMFLPIGDATVIDRIFTELeADDRISEVFVSTNRRfADHFREHLS-GSRY---------E 72
Cdd:cd06426     1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRF-IAQGFRNFYISVNYL-AEMIEDYFGdGSKFgvnisyvreD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850  73 KPtltveettaetekLGVVGALAQLveREGIDEDTVVIAGDNLLSFDVSEFVDAFR---SAASPMIATYDVgsvdrASSY 149
Cdd:cd06426    79 KP-------------LGTAGALSLL--PEKPTDPFLVMNGDILTNLNYEHLLDFHKennADATVCVREYEV-----QVPY 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 150 GVVDVADGEVVDFAEKPTNptSSLVSIACYGFPaetlPSLSTYLEEGNNPDEPGWFVQWLLERESIRAFPFEEAWFDIGT 229
Cdd:cd06426   139 GVVETEGGRITSIEEKPTH--SFLVNAGIYVLE----PEVLDLIPKNEFFDMPDLIEKLIKEGKKVGVFPIHEYWLDIGR 212


                  ....*..
gi 1740188850 230 PECYLDA 236
Cdd:cd06426   213 PEDYEKA 219
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-236 2.46e-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: 76.84  E-value: 2.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850   1 MKAIVLAGGYATRLWPITRHRPKMFLPIGDATVIDR-IFTELEADdrISEVFVSTNRRFADHFREHL-SGS------RY- 71
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYpLSTLMLAG--IREILIISTPEDLPLFKELLgDGSdlgiriTYa 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850  72 --EKPtltveettaeteklgvvGALAQ--LVEREGIDEDTV-VIAGDNLlsFDVSEFVDAFRSAAS----PMIATYDVGS 142
Cdd:cd02538    79 vqPKP-----------------GGLAQafIIGEEFIGDDPVcLILGDNI--FYGQGLSPILQRAAAqkegATVFGYEVND 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 143 VDRassYGVVDV-ADGEVVDFAEKPTNPTSSLVSIACYGFP------AETL-PS----------LSTYLEEGNnpdepgw 204
Cdd:cd02538   140 PER---YGVVEFdENGRVLSIEEKPKKPKSNYAVTGLYFYDndvfeiAKQLkPSargeleitdvNNEYLEKGK------- 209

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1740188850 205 fvqwlLERESI-RAFpfeeAWFDIGTPECYLDA 236
Cdd:cd02538   210 -----LSVELLgRGF----AWLDTGTHESLLEA 233
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 101-322 9.35e-16

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 77.22  E-value: 9.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 101 EGIDEDTVVI-AGDNLLSFDVSEFVDAFRS-AASPMIATYDVgSVDRASSYGVVDV-ADGEVVDFAEKPTNPTSSLVSIA 177
Cdd:PRK05293  113 DQYDPEYVLIlSGDHIYKMDYDKMLDYHKEkEADVTIAVIEV-PWEEASRFGIMNTdENMRIVEFEEKPKNPKSNLASMG 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 178 CYGFpaeTLPSLSTYLEEG-NNPDEPGWFVQ-----WLLERESIRAFPFEEAWFDIGTPECYLDA--------------- 236
Cdd:PRK05293  192 IYIF---NWKRLKEYLIEDeKNPNSSHDFGKnviplYLEEGEKLYAYPFKGYWKDVGTIESLWEAnmellrpenplnlfd 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 237 VAW------------HLQGETRVAES---------ATVERTTLGENVHVMAGAEVTDshlsrSVIFPDATI-QDCEVRSS 294
Cdd:PRK05293  269 RNWriysvnpnlppqYIAENAKVKNSlvvegcvvyGTVEHSVLFQGVQVGEGSVVKD-----SVIMPGAKIgENVVIERA 343

                         250       260
                  ....*....|....*....|....*...
gi 1740188850 295 IIDrktaldglefNGALVGAHTRIVNGE 322
Cdd:PRK05293  344 IIG----------ENAVIGDGVIIGGGK 361
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-237 5.75e-14

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: 70.64  E-value: 5.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850   1 MKAIVLAGGYATRLWPITRHRPKMFLPIGDATVIDRIFTELeADDRISEVFVSTNRR---FADHFREH--LSGSRYEKPT 75
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEA-VAAGIEDIIIVTGRGkraIEDHFDRSyeLEETLEKKGK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850  76 LTVEETTAETEKLGVV------GAL----AQLVEREGI-DEDTVVIAGDNLLSFDVS---EFVDAFRSAASPMIAtydVG 141
Cdd:cd02541    80 TDLLEEVRIISDLANIhyvrqkEPLglghAVLCAKPFIgDEPFAVLLGDDLIDSKEPclkQLIEAYEKTGASVIA---VE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 142 SVDRA--SSYGVVDVADGE-----VVDFAEKP--TNPTSSLVSIACYGFPAETLPslstYLEEgNNPDEPGWF-----VQ 207
Cdd:cd02541   157 EVPPEdvSKYGIVKGEKIDgdvfkVKGLVEKPkpEEAPSNLAIVGRYVLTPDIFD----ILEN-TKPGKGGEIqltdaIA 231

                         250       260       270
                  ....*....|....*....|....*....|
gi 1740188850 208 WLLERESIRAFPFEEAWFDIGTPECYLDAV 237
Cdd:cd02541   232 KLLEEEPVYAYVFEGKRYDCGNKLGYLKAT 261
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-241 3.08e-13

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


Pssm-ID: 133047 [Multi-domain]  Cd Length: 233  Bit Score: 68.01  E-value: 3.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850   1 MKAIVLAGGYATRLWPITRHRPKMFLPIGDATVidrIFTELEA------DDRI------SEVFVSTNRRFADHFREHLSG 68
Cdd:cd06425     1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPM---IEHQIEAlakagvKEIIlavnyrPEDMVPFLKEYEKKLGIKITF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850  69 SRYEKPtltveettaetekLGVVGALAqLVER--EGIDEDTVVIAGDNLLSFDVSEFVDAFRSAASPmiATYDVGSVDRA 146
Cdd:cd06425    78 SIETEP-------------LGTAGPLA-LARDllGDDDEPFFVLNSDVICDFPLAELLDFHKKHGAE--GTILVTKVEDP 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 147 SSYGVV--DVADGEVVDFAEKPTNPTSSLVSIACYGFPaetlPSLSTYLEEGNNPDEPGWFVQwLLERESIRAFPFEEAW 224
Cdd:cd06425   142 SKYGVVvhDENTGRIERFVEKPKVFVGNKINAGIYILN----PSVLDRIPLRPTSIEKEIFPK-MASEGQLYAYELPGFW 216

                         250
                  ....*....|....*..
gi 1740188850 225 FDIGTPECYLDAVAWHL 241
Cdd:cd06425   217 MDIGQPKDFLKGMSLYL 233
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 3-298 1.07e-12

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 68.33  E-value: 1.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850   3 AIVLAGGYATRLWPITRHRPKMFLPIGDAT-VID------------RI--FTELEADDRISEVfvstnRRFADHFREHL- 66
Cdd:PRK00725   18 ALILAGGRGSRLKELTDKRAKPAVYFGGKFrIIDfalsncinsgirRIgvLTQYKAHSLIRHI-----QRGWSFFREELg 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850  67 -------------SGSRYEkptltveettaeteklGVVGALAQ---LVEREgiDEDTVVI-AGDNLLSFDVSEFV-DAFR 128
Cdd:PRK00725   93 efvdllpaqqrvdEENWYR----------------GTADAVYQnldIIRRY--DPKYVVIlAGDHIYKMDYSRMLaDHVE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 129 SAASPMIATYDVgSVDRASSYGVVDV-ADGEVVDFAEKPTNP-------TSSLVSIACYGFPAETLpsLSTYLEEGNNPD 200
Cdd:PRK00725  155 SGADCTVACLEV-PREEASAFGVMAVdENDRITAFVEKPANPpampgdpDKSLASMGIYVFNADYL--YELLEEDAEDPN 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 201 EPGWF----VQWLLERESIRAFPFEEA-----------WFDIGTPECY----LDAVA--------------WHLQGETRV 247
Cdd:PRK00725  232 SSHDFgkdiIPKIVEEGKVYAHPFSDScvrsdpeeepyWRDVGTLDAYwqanLDLASvtpeldlydrnwpiWTYQEQLPP 311

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1740188850 248 A------------------------ESATVERTTLGENVHVMAGAEVTDshlsrSVIFPDATI-QDCEVRSSIIDR 298
Cdd:PRK00725  312 AkfvfdrsgrrgmainslvsggciiSGAVVRRSVLFSRVRVNSFSNVED-----SVLLPDVNVgRSCRLRRCVIDR 382
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-236 1.75e-11

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: 62.59  E-value: 1.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850   2 KAIVLAGGYATRLWPITRHRPKMFLPIGDATVIDRIFTELeADDRISEVFVSTNrRFADHFREHLSGSRY--------EK 73
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRL-AAAGIRRIVVNTH-HLADQIEAHLGDSRFglritisdEP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850  74 PTLtveettaetekLGVVGALAQlVEREGIDEDTVVIAGDNLLSFDVSEFVDAFRSAASPMIATYDVGSVDRASSYGVVD 153
Cdd:cd06422    79 DEL-----------LETGGGIKK-ALPLLGDEPFLVVNGDILWDGDLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFS 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 154 VADGEVVDFAEKPTNPTSSLVSIACY------GFPAETLpSLSTYLEEgnnpdepgwfvqwLLERESIRAFPFEEAWFDI 227
Cdd:cd06422   147 LDADGRLRRGGGGAVAPFTFTGIQILspelfaGIPPGKF-SLNPLWDR-------------AIAAGRLFGLVYDGLWFDV 212


                  ....*....
gi 1740188850 228 GTPECYLDA 236
Cdd:cd06422   213 GTPERLLAA 221
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 1-66 9.32e-10

GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes.


Pssm-ID: 133003 [Multi-domain]  Cd Length: 274  Bit Score: 58.36  E-value: 9.32e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1740188850   1 MKAIVLAGGYATRLWPITR-HRPKMFLPI-GDATVIDRIFTELEADDRISEVFVSTNRRFADHFREHL 66
Cdd:cd02509     1 IYPVILAGGSGTRLWPLSReSYPKQFLKLfGDKSLLQQTLDRLKGLVPPDRILVVTNEEYRFLVREQL 68
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 3-298 1.86e-09

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 58.30  E-value: 1.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850   3 AIVLAGGYATRLWPITRHRPKMFLPIGDA-TVIDRIFTELeADDRISEVFV-------STNR---------RFADHF--- 62
Cdd:PRK00844    8 AIVLAGGEGKRLMPLTADRAKPAVPFGGSyRLIDFVLSNL-VNSGYLRIYVltqykshSLDRhisqtwrlsGLLGNYitp 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850  63 -----RehlSGSRYekptltveettaeteKLGVVGALAQ---LVEREgiDEDTVVIAG-DNLLSFDVSEFVDAFR-SAAS 132
Cdd:PRK00844   87 vpaqqR---LGKRW---------------YLGSADAIYQslnLIEDE--DPDYVVVFGaDHVYRMDPRQMVDFHIeSGAG 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 133 PMIATYDVgSVDRASSYGVVDV-ADGEVVDFAEKPTNPTS-------SLVSIACYGFPAETLpsLSTYLEEGNNPDEP-- 202
Cdd:PRK00844  147 VTVAAIRV-PREEASAFGVIEVdPDGRIRGFLEKPADPPGlpddpdeALASMGNYVFTTDAL--VDALRRDAADEDSShd 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 203 --GWFVQWLLERESIRAFPFEEA------------WFDIGTPECYLDA----VA-----------WHL------------ 241
Cdd:PRK00844  224 mgGDIIPRLVERGRAYVYDFSTNevpgaterdrgyWRDVGTIDAYYDAhmdlLSvhpvfnlynreWPIytsspnlppakf 303

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1740188850 242 ----QGETRVAES----------ATVERTTLGENVHVMAGAEVTDshlsrSVIFPDATI-QDCEVRSSIIDR 298
Cdd:PRK00844  304 vdggGRVGSAQDSlvsagsiisgATVRNSVLSPNVVVESGAEVED-----SVLMDGVRIgRGAVVRRAILDK 370
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-66 4.14e-09

Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 57.00  E-value: 4.14e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1740188850   1 MKAIVLAGGYATRLWPITR-HRPKMFLPI-GDATVIDRIFTELEADDRISEVFVSTNRRFADHFREHL 66
Cdd:COG0836     3 IYPVILAGGSGTRLWPLSReSYPKQFLPLlGEKSLLQQTVERLAGLVPPENILVVTNEEHRFLVAEQL 70
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 3-166 5.93e-09

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 56.79  E-value: 5.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850   3 AIVLAGGYATRLWPITRHRPKMFLPIGDA-TVIDRIFTELEADDrISEVFV-------STNR------------RFADHF 62
Cdd:PLN02241    6 AIILGGGAGTRLFPLTKRRAKPAVPIGGNyRLIDIPMSNCINSG-INKIYVltqfnsaSLNRhlsraynfgnggNFGDGF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850  63 REHLSGsrYEKPTLTVEEttaetekLGVVGALAQ---LVE--REGIDEDTVVIAGDNLLSFDVSEFVDAFR-SAASPMIA 136
Cdd:PLN02241   85 VEVLAA--TQTPGEKGWF-------QGTADAVRQflwLFEdaKNKNVEEVLILSGDHLYRMDYMDFVQKHReSGADITIA 155

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1740188850 137 TYDVGSvDRASSYGVVDVAD-GEVVDFAEKP 166
Cdd:PLN02241  156 CLPVDE-SRASDFGLMKIDDtGRIIEFSEKP 185
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 1-236 3.33e-08

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 54.51  E-value: 3.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850   1 MK---AIVLAGGYATRLWPITRHRPKMFLPIG------DATV-------IDRIF--TELEAddrisevfVSTNR------ 56
Cdd:PRK02862    1 MKrvlAIILGGGAGTRLYPLTKLRAKPAVPLAgkyrliDIPIsncinsgINKIYvlTQFNS--------ASLNRhisqty 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850  57 ---RFADHFREHL-------SGSRYEkptltveettaeteklGVVGALAQ---LVEREGIDEdtVVI-AGDNLLSFDVSE 122
Cdd:PRK02862   73 nfdGFSGGFVEVLaaqqtpeNPSWFQ----------------GTADAVRKylwHFQEWDVDE--YLIlSGDQLYRMDYRL 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 123 FVDAFRSA-ASPMIATYDVGSvDRASSYGVVDV-ADGEVVDFAEKPTN--------PTSS-------------LVSIACY 179
Cdd:PRK02862  135 FVQHHRETgADITLAVLPVDE-KDASGFGLMKTdDDGRITEFSEKPKGdelkamavDTSRlglspeeakgkpyLASMGIY 213

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 180 GFPAETLPSLstyLEegNNPDE--------PgwfvqwllerESIR-----AFPFEEAWFDIGTPECYLDA 236
Cdd:PRK02862  214 VFSRDVLFDL---LN--KNPEYtdfgkeiiP----------EAIRdykvqSYLFDGYWEDIGTIEAFYEA 268
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-66 3.98e-08

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 53.32  E-value: 3.98e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1740188850   2 KAIVLAGGYATRLWPITRHRPKMFLPIGDATVIDRIFTELEADDrISEVFVSTNRRfADHFREHL 66
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAG-IKDIVVVTGYK-AELIEEAL 63
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 1-137 6.00e-08

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: 52.26  E-value: 6.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850   1 MKAIVLAGGYATRLWPITRHRPKMFLPIGDATVIDRIFTELEADDrISEVFVSTNRRFADHfREHLSGSRYEKPTLTVEE 80
Cdd:cd02507     1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAG-VEEVFVVCCEHSQAI-IEHLLKSKWSSLSSKMIV 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1740188850  81 TTAETEKLGVVG-ALAQLVEREGIDEDTVVIAGDNLLSFDVSEFVDAFRSAASPMIAT 137
Cdd:cd02507    79 DVITSDLCESAGdALRLRDIRGLIRSDFLLLSCDLVSNIPLSELLEERRKKDKNAIAT 136
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 1-129 1.40e-07

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: 51.12  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850   1 MKAIVLAGGYATRLWPITRHRPKMFLPIGDATVIDRIFTELEADDrISEVFVSTNRRFADHFREHLSGSRYEKPTLTVEE 80
Cdd:cd04198     1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAG-FEDVIVVVPEEEQAEISTYLRSFPLNLKQKLDEV 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1740188850  81 TTAETEKLGVVGALaQLVEREgIDEDTVVIAGDNLLSFDVSEFVDAFRS 129
Cdd:cd04198    80 TIVLDEDMGTADSL-RHIRKK-IKKDFLVLSCDLITDLPLIELVDLHRS 126
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 249-322 9.10e-07

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


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 46.69  E-value: 9.10e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1740188850 249 ESATVERTTLGENVHVMAGAEVTDshlsrSVIFPDATI-QDCEVRSSIIDRktaldglefnGALVGAHTRIVNGE 322
Cdd:cd04651    22 SGGTVENSVLFRGVRVGSGSVVED-----SVIMPNVGIgRNAVIRRAIIDK----------NVVIPDGVVIGGDP 81
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-231 1.59e-06

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: 47.88  E-value: 1.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850   1 MKAIVLAGGYATRLWpitrhRPKMFLPIGDATVIDRIFTELEADdrISEVFVSTNRRfadhfrehlsgSRYEkptltvee 80
Cdd:COG0746     5 ITGVILAGGRSRRMG-----QDKALLPLGGRPLLERVLERLRPQ--VDEVVIVANRP-----------ERYA-------- 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850  81 ttaeTEKLGVV-------GALAqlvereGI--------DEDTVVIAGD--NLLSFDVSEFVDAFRSAASPMIATYDvgsv 143
Cdd:COG0746    59 ----ALGVPVVpddppgaGPLA------GIlaaleaapAEWVLVLACDmpFLPPDLVRRLLEALEEGADAVVPRSG---- 124

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 144 drassygvvdvadgevvDFAEkPTnptsslvsIACYgfPAETLPSLSTYLEEGNNPdepgwfVQWLLERESIRAFPFEE- 222
Cdd:COG0746   125 -----------------GRLE-PL--------FALY--RRSLLPALEAALAEGERS------LRALLERLDVVYVPFEDl 170

                         250
                  ....*....|.
gi 1740188850 223 --AWFDIGTPE 231
Cdd:COG0746   171 ddAFFNVNTPE 181
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-176 1.70e-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: 47.99  E-value: 1.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850   3 AIVLAGGYATRLWPITRHRPKMFLPIGDATVIDRIFTELEADDrISEVFVSTnRRFADHFREHLSGSRYEKPTLTVEETT 82
Cdd:cd04197     3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNG-VEEVFVFC-CSHSDQIKEYIEKSKWSKPKSSLMIVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850  83 AETEKLGV-VG-ALAQLVEREGIDEDTVVIAGDNLLSFDVSEFVDAFR-------SAASPMIATyDVGSVDRASSYG--- 150
Cdd:cd04197    81 IIMSEDCRsLGdALRDLDAKGLIRGDFILVSGDVVSNIDLKEILEEHKerrkkdkNAIMTMVLK-EASPPHRTRRTGeef 159

                         170       180
                  ....*....|....*....|....*...
gi 1740188850 151 --VVDVADGEVVDFAEKPTNPTSSLVSI 176
Cdd:cd04197   160 viAVDPKTSRLLHYEELPGSKYRSITDL 187
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 3-231 3.70e-06

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: 47.23  E-value: 3.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850   3 AIVLAGGYATRLWPITRHRPKMFLPIGDATVIDRIFTELEADDrISEVFVSTNRRfADHFREHLSG---------SRYEK 73
Cdd:cd02523     1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAG-IDDIVIVTGYK-KEQIEELLKKypnikfvynPDYAE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850  74 PtltveettaeteklGVVGALAQLveREGIDEDTVVIAGDNLlsFDVSEFVDAFRSAASPMIATYDVGS--VDRASSYGV 151
Cdd:cd02523    79 T--------------NNIYSLYLA--RDFLDEDFLLLEGDVV--FDPSILERLLSSPADNAILVDKKTKewEDEYVKDLD 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 152 VDVADGEVVDFAEKPTNPTSSLVSIA--CYGFPAETLPSLSTYLEEGNNPDEpgW--FVQWLLERESIRAFPFEE-AWFD 226
Cdd:cd02523   141 DAGVLLGIISKAKNLEEIQGEYVGISkfSPEDADRLAEALEELIEAGRVNLY--YedALQRLISEEGVKVKDISDgFWYE 218


                  ....*
gi 1740188850 227 IGTPE 231
Cdd:cd02523   219 IDDLE 223
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 4-74 1.04e-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: 42.81  E-value: 1.04e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1740188850   4 IVLAGGYATRLwpiTRHRPKMFLPIGDATVIDRIFTELEADDRISEVFVSTNRRFADHFREHLSGSRYEKP 74
Cdd:COG1211     1 IIPAAGSGSRM---GAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVVPPDDIEYFEELLAKYGIDKP 68
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 1-66 1.06e-04

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: 42.18  E-value: 1.06e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1740188850   1 MKAIVLAGGYATRLwpitrHRPKMFLPIGDATVIDRIFTELEAddRISEVFVSTNRRFADHFREHL 66
Cdd:cd02503     1 ITGVILAGGKSRRM-----GGDKALLELGGKPLLEHVLERLKP--LVDEVVISANRDQERYALLGV 59
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 3-57 1.41e-04

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: 41.41  E-value: 1.41e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1740188850   3 AIVLAGGYATRLwpitrHRPKMFLPIGDATVIDRIFTELEAddRISEVFVSTNRR 57
Cdd:pfam12804   1 AVILAGGRSSRM-----GGDKALLPLGGKPLLERVLERLRP--AGDEVVVVANDE 48
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-236 1.50e-04

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 42.74  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850   2 KAIVLAGGYATRLWPITRHRPKMFLPIGDATVIDRIFTELEADDrISEVFVSTNRRFADHFREHL-SGSRYEKPTLTVEE 80
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAG-IRDILIISTPQDTPRFQQLLgDGSQWGLNLQYKVQ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850  81 TTAETEklgvvgALAQLVEREGI-DEDTVVIAGDNLL-SFDVSEFVD-AFRSAASPMIATYDVGSVDRassYGVVDV-AD 156
Cdd:PRK15480   84 PSPDGL------AQAFIIGEEFIgGDDCALVLGDNIFyGHDLPKLMEaAVNKESGATVFAYHVNDPER---YGVVEFdQN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 157 GEVVDFAEKPTNPTSSLVSIACYGFPAETLPSLSTYLEEGNNPDEPGWFVQWLLE--RESIRAFPFEEAWFDIGTPECYL 234
Cdd:PRK15480  155 GTAISLEEKPLQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEqgRLSVAMMGRGYAWLDTGTHQSLI 234


                  ..
gi 1740188850 235 DA 236
Cdd:PRK15480  235 EA 236
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 3-67 4.76e-04

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: 40.58  E-value: 4.76e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1740188850   3 AIVLAGGYATRLwpiTRHRPKMFLPIGDATVIDRIFTELEADDRISEVFVSTNRRFADHFREHLS 67
Cdd:cd02516     3 AIILAAGSGSRM---GADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKELAK 64
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 240-286 8.60e-04

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 40.69  E-value: 8.60e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1740188850 240 HLQGETRVAESATV-ERTTLgENVHVMAGAEVTDSHLSRSVIFPDATI 286
Cdd:PRK14352  285 QLLGRTTIGEDAVVgPDTTL-TDVTVGEGASVVRTHGSESEIGAGATV 331
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 100-184 2.31e-03

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


Pssm-ID: 133050 [Multi-domain]  Cd Length: 257  Bit Score: 38.77  E-value: 2.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 100 REGIDEDTVVIAGDNLLSFDVSEFVDAFRSAASPM-IATYDVgSVDRASSYG--VVDVADGEVVDFAEKPTNPTSSLVSI 176
Cdd:cd06428    99 LAGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGtILGTEA-SREQASNYGciVEDPSTGEVLHYVEKPETFVSDLINC 177


                  ....*...
gi 1740188850 177 ACYGFPAE 184
Cdd:cd06428   178 GVYLFSPE 185
cpsB PRK15460
mannose-1-phosphate guanyltransferase; Provisional
 4-171 3.13e-03

mannose-1-phosphate guanyltransferase; Provisional


Pssm-ID: 185357 [Multi-domain]  Cd Length: 478  Bit Score: 39.19  E-value: 3.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850   4 IVLAGGYATRLWPITR-HRPKMFLPI-GDATVIDRIFTELEADDRISEVFVSTNR-RF--ADHFRE--HLSGSRYEKPTL 76
Cdd:PRK15460    9 VVMAGGSGSRLWPLSRvLYPKQFLCLkGDLTMLQTTICRLNGVECESPVVICNEQhRFivAEQLRQlnKLTENIILEPAG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850  77 TVEETTAeteklgVVGALAQLVEREGIDEDTVVIAGDNLLSfDVSEFVDAFRS----AASPMIATYDV---------GSV 143
Cdd:PRK15460   89 RNTAPAI------ALAALAAKRHSPESDPLMLVLAADHVIA-DEDAFRAAVRNampyAEAGKLVTFGIvpdlpetgyGYI 161

                         170       180
                  ....*....|....*....|....*....
gi 1740188850 144 DRAS-SYGVVDVADGEVVDFAEKPTNPTS 171
Cdd:PRK15460  162 RRGEvSAGEQDTVAFEVAQFVEKPNLETA 190
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 3-29 5.32e-03

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: 37.52  E-value: 5.32e-03
                          10        20
                  ....*....|....*....|....*..
gi 1740188850   3 AIVLAGGYATRLWPITRHRPKMFLPIG 29
Cdd:cd02508     1 AIILAGGEGTRLSPLTKKRAKPAVPFG 27
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 243-321 7.35e-03

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


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 34.91  E-value: 7.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1740188850 243 GETRVAESATVERTTLGENVHVMAGAEVTDshlsrSVIFPDATIQD-CEVRSSIIdrktaldgleFNGALVGAHTRIVNG 321
Cdd:cd03356     4 ESTVIGENAIIKNSVIGDNVRIGDGVTITN-----SILMDNVTIGAnSVIVDSII----------GDNAVIGENVRVVNL 68
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 240-286 7.66e-03

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: 37.70  E-value: 7.66e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1740188850 240 HLQGETRVAESATVERTTLGENVHVMAGAEVTDSHLSRSVIFPDATI 286
Cdd:COG1207   280 ILEGKTVIGEGVVIGPNCTLKDSTIGDGVVIKYSVIEDAVVGAGATV 326
 
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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