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Conserved domains on  [gi|334882323|emb|CCB83320|]
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UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase [Lactiplantibacillus pentosus MP-10]

Protein Classification

UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase( domain architecture ID 11431234)

UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase catalyzes the last step in the intracellular phase of peptidoglycan biosynthesis

CATH:  3.40.50.2000
CAZY:  GT28
EC:  2.4.1.227
Gene Ontology:  GO:0051991|GO:0008360|GO:0050511|GO:0051301|GO:0071555|GO:0030259|GO:0009252|GO:0005975|GO:0005886
PubMed:  12455415|11699883|12691742|16263268|16037492
SCOP:  4000825

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MurG COG0707
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ...
 1-364 6.23e-167

UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase is part of the Pathway/BioSystem: Mureine biosynthesis


:

Pssm-ID: 440471 [Multi-domain]  Cd Length: 363  Bit Score: 470.38  E-value: 6.23e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323   1 MRLMISGGGTGGHIYPALALIDALKAHDpeAQVQFVGTHRGLESRIVPERGIDFKTIKIQGFKRSLSLQNVKTVYLFLKS 80
Cdd:COG0707    3 KRILIAGGGTGGHIFPALALAEELRERG--AEVLFIGTKRGLEARLVPAAGYPLHTIPVGGLRRKGSLKNLKAPFRLLKA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323  81 VVTARKYIKAFKPDVVVGTGGYVSGAVVFAASQMHIPTVIHEQNSVVGVTNKFLSRFVDKIAISFESARSQFPEQKVVMT 160
Cdd:COG0707   81 LLQARKILKRFKPDVVVGFGGYVSGPVGLAARLLGIPLVIHEQNAVPGLANRLLARFADRVALAFPETKKYFPKKKAVVT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 161 GNPRAQQVANIKKTGALAQFELDPEIPTALIFGGSRGAARINAAAVEALPELDKRDYQTLFVTGQVHYDKIKDGLsATAL 240
Cdd:COG0707  161 GNPVRKEILELDRPEARAKLGLDPDKPTLLVFGGSQGARALNEAVPAALAALLEARLQVVHQTGKGDYEEVRAAY-AAAI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 241 APNVKIVPYIKNMPAILPEVAVILGRAGATSIAEITALGIPSILVPSPYVTNDHQTKNAQSLVNAGAAELIKESDLTGAT 320
Cdd:COG0707  240 RPNAEVFPFIDDMADAYAAADLVISRAGASTVAELAALGKPAILVPLPHAADDHQTKNARALVEAGAAVLIPQSELTPEK 319

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 334882323 321 LVAALDRLLQSSTHREAMAANAKKLGMPDAADQLLHVLESVVKS 364
Cdd:COG0707  320 LAEALEELLEDPERLAKMAEAARALARPDAAERIADLILELAKG 363
 
Name Accession Description Interval E-value
MurG COG0707
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ...
 1-364 6.23e-167

UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440471 [Multi-domain]  Cd Length: 363  Bit Score: 470.38  E-value: 6.23e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323   1 MRLMISGGGTGGHIYPALALIDALKAHDpeAQVQFVGTHRGLESRIVPERGIDFKTIKIQGFKRSLSLQNVKTVYLFLKS 80
Cdd:COG0707    3 KRILIAGGGTGGHIFPALALAEELRERG--AEVLFIGTKRGLEARLVPAAGYPLHTIPVGGLRRKGSLKNLKAPFRLLKA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323  81 VVTARKYIKAFKPDVVVGTGGYVSGAVVFAASQMHIPTVIHEQNSVVGVTNKFLSRFVDKIAISFESARSQFPEQKVVMT 160
Cdd:COG0707   81 LLQARKILKRFKPDVVVGFGGYVSGPVGLAARLLGIPLVIHEQNAVPGLANRLLARFADRVALAFPETKKYFPKKKAVVT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 161 GNPRAQQVANIKKTGALAQFELDPEIPTALIFGGSRGAARINAAAVEALPELDKRDYQTLFVTGQVHYDKIKDGLsATAL 240
Cdd:COG0707  161 GNPVRKEILELDRPEARAKLGLDPDKPTLLVFGGSQGARALNEAVPAALAALLEARLQVVHQTGKGDYEEVRAAY-AAAI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 241 APNVKIVPYIKNMPAILPEVAVILGRAGATSIAEITALGIPSILVPSPYVTNDHQTKNAQSLVNAGAAELIKESDLTGAT 320
Cdd:COG0707  240 RPNAEVFPFIDDMADAYAAADLVISRAGASTVAELAALGKPAILVPLPHAADDHQTKNARALVEAGAAVLIPQSELTPEK 319

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 334882323 321 LVAALDRLLQSSTHREAMAANAKKLGMPDAADQLLHVLESVVKS 364
Cdd:COG0707  320 LAEALEELLEDPERLAKMAEAARALARPDAAERIADLILELAKG 363
murG PRK00726
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
 1-364 2.65e-162

undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional


Pssm-ID: 234825 [Multi-domain]  Cd Length: 357  Bit Score: 458.44  E-value: 2.65e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323   1 MRLMISGGGTGGHIYPALALIDALKAHDpeAQVQFVGTHRGLESRIVPERGIDFKTIKIQGFKRSLSLQNVKTVYLFLKS 80
Cdd:PRK00726   2 KKILLAGGGTGGHVFPALALAEELKKRG--WEVLYLGTARGMEARLVPKAGIEFHFIPSGGLRRKGSLANLKAPFKLLKG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323  81 VVTARKYIKAFKPDVVVGTGGYVSGAVVFAASQMHIPTVIHEQNSVVGVTNKFLSRFVDKIAISFESARSQFPEQKVVMT 160
Cdd:PRK00726  80 VLQARKILKRFKPDVVVGFGGYVSGPGGLAARLLGIPLVIHEQNAVPGLANKLLARFAKKVATAFPGAFPEFFKPKAVVT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 161 GNPRAQQVANIKKTGalAQFELDPEIPTALIFGGSRGAARINAAAVEALPELDKrDYQTLFVTGQVHYDKIKDGLsatAL 240
Cdd:PRK00726 160 GNPVREEILALAAPP--ARLAGREGKPTLLVVGGSQGARVLNEAVPEALALLPE-ALQVIHQTGKGDLEEVRAAY---AA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 241 APNVKIVPYIKNMPAILPEVAVILGRAGATSIAEITALGIPSILVPSPYVTNDHQTKNAQSLVNAGAAELIKESDLTGAT 320
Cdd:PRK00726 234 GINAEVVPFIDDMAAAYAAADLVICRAGASTVAELAAAGLPAILVPLPHAADDHQTANARALVDAGAALLIPQSDLTPEK 313

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 334882323 321 LVAALDRLLQSSTHREAMAANAKKLGMPDAADQLLHVLESVVKS 364
Cdd:PRK00726 314 LAEKLLELLSDPERLEAMAEAARALGKPDAAERLADLIEELARK 357
GT28_MurG cd03785
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ...
 2-355 1.28e-151

undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains, each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340818 [Multi-domain]  Cd Length: 350  Bit Score: 430.87  E-value: 1.28e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323   2 RLMISGGGTGGHIYPALALIDALKAHdpEAQVQFVGTHRGLESRIVPERGIDFKTIKIQGFKRSLSLQNVKTVYLFLKSV 81
Cdd:cd03785    1 KILIAGGGTGGHIFPALALAEELRKR--GAEILFIGTKRGLEAKLVPEAGIPFHTIPISGLRRKGSLKNLKAPFKLLKGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323  82 VTARKYIKAFKPDVVVGTGGYVSGAVVFAASQMHIPTVIHEQNSVVGVTNKFLSRFVDKIAISFESARSQFPEQKVVMTG 161
Cdd:cd03785   79 RQARKILRKFKPDVVIGFGGYVSGPVVLAARLLGIPLIIHEQNAVPGLANRLLSRFADKVAVSFPETKKYFPAAKVVVTG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 162 NPRAQQVANIKKtgALAQFELDPEIPTALIFGGSRGAARINAAAVEALPELDKRDYQTLFVTGQVHYDKIKDGLSatALA 241
Cdd:cd03785  159 NPVREEILNLRK--ELKRFGLPPDKPTLLVFGGSQGARAINRAVPKALPKLLERGIQVIHQTGKGDYDEVKKLYE--DLG 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 242 PNVKIVPYIKNMPAILPEVAVILGRAGATSIAEITALGIPSILVPSPYVTNDHQTKNAQSLVNAGAAELIKESDLTGATL 321
Cdd:cd03785  235 INVKVFPFIDDMAAAYAAADLVISRAGASTIAELTAAGKPAILIPYPYAADDHQEANARALEKAGAAIVIDQEELTPEVL 314

                        330       340       350
                 ....*....|....*....|....*....|....
gi 334882323 322 VAALDRLLQSSTHREAMAANAKKLGMPDAADQLL 355
Cdd:cd03785  315 AEAILDLLNDPERLKKMAEAAKKLAKPDAAERIA 348
murG TIGR01133
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT ...
 1-354 2.04e-115

undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT The final step of peptidoglycan subunit assembly in Escherichia coli occurs in the cytoplasm. RA Bupp K, van Heijenoort J. RL J Bacteriol 1993 Mar;175(6):1841-3 [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273460 [Multi-domain]  Cd Length: 348  Bit Score: 338.88  E-value: 2.04e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323    1 MRLMISGGGTGGHIYPALALIDALKAHDPEaqVQFVGTHRGLESRIVPERGIDFKTIKIQGFKRSLSLQNVKTVYLFLKS 80
Cdd:TIGR01133   1 KKIALAAGGTGGHIFPALAVAEELIKRGVE--VLWLGTKRGLEKRLVPKAGIEFYFIPVGGLRRKGSKKLLKTPLKLLKA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323   81 VVTARKYIKAFKPDVVVGTGGYVSGAVVFAASQMHIPTVIHEQNSVVGVTNKFLSRFVDKIAISFESARSQFpeqKVVMT 160
Cdd:TIGR01133  79 VFKARRILKKFKPDVVVGFGGYVSGPAGLAAKLLGIPLIHHEQNAVPGLTNKLLSRFAKKVLVSFPGAKDHF---EAVLV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323  161 GNPRAQQVANIKKtgALAQFELDPEIPTALIFGGSRGAARINAAAVEALPELDKRDYQTLFVTGQVHYDKIKDGLSATAL 240
Cdd:TIGR01133 156 GNPVRKEIRSLPV--PRERFGRREGKPTILVLGGSQGAKILNELVPKALAKLQEKGIQIVHQGGKGDLEKVKNVYQELGQ 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323  241 ApnvKIVPYI-KNMPAILPEVAVILGRAGATSIAEITALGIPSILVPSPYVtNDHQTKNAQSLVNAGAAELIKESDLTGA 319
Cdd:TIGR01133 234 E---KIVTFIdENMAAAYAAADLVISRAGASTVAELAAAGVPAILIPYPYA-ADDQYYNAKFLEDLGAGLVIRQKELLPE 309

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 334882323  320 TLVAALDRLLQSSTHREAMAANAKKLGMPDAADQL 354
Cdd:TIGR01133 310 KLLEALLKLLLDPANLENMAEAARKLAKPDAAKRI 344
Glyco_transf_28 pfam03033
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes ...
 3-143 2.21e-48

Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). This N-terminal domain contains the acceptor binding site and likely membrane association site. This family also contains a large number of proteins that probably have quite distinct activities.


Pssm-ID: 427107 [Multi-domain]  Cd Length: 139  Bit Score: 160.15  E-value: 2.21e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323    3 LMISGGGTGGHIYPALALIDALKAHDPEaqVQFVGTHRGLESRIVPERGIDFKTIKIQGFKRSLSLQNVKTVYLFLKSVV 82
Cdd:pfam03033   1 IVLAGGGTGGHVFPALALAKELKKRGHE--VRVLGTKRGFEEFLVEKAGIEFEPIPGGGLRRKFSPKNLKEPFKLLKGIV 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334882323   83 TARKYIKAFKPDVVVGTGGYVSGAVVFAASQMHIPTVIHEQNSVVGVTNKFLSRFVDKIAI 143
Cdd:pfam03033  79 KAFRILKEFKPDAVIGFGGYVSLPAVIAAPLAGIPIIIHEQNGIPGLTNKTLPRTATKVAP 139
 
Name Accession Description Interval E-value
MurG COG0707
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ...
 1-364 6.23e-167

UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440471 [Multi-domain]  Cd Length: 363  Bit Score: 470.38  E-value: 6.23e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323   1 MRLMISGGGTGGHIYPALALIDALKAHDpeAQVQFVGTHRGLESRIVPERGIDFKTIKIQGFKRSLSLQNVKTVYLFLKS 80
Cdd:COG0707    3 KRILIAGGGTGGHIFPALALAEELRERG--AEVLFIGTKRGLEARLVPAAGYPLHTIPVGGLRRKGSLKNLKAPFRLLKA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323  81 VVTARKYIKAFKPDVVVGTGGYVSGAVVFAASQMHIPTVIHEQNSVVGVTNKFLSRFVDKIAISFESARSQFPEQKVVMT 160
Cdd:COG0707   81 LLQARKILKRFKPDVVVGFGGYVSGPVGLAARLLGIPLVIHEQNAVPGLANRLLARFADRVALAFPETKKYFPKKKAVVT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 161 GNPRAQQVANIKKTGALAQFELDPEIPTALIFGGSRGAARINAAAVEALPELDKRDYQTLFVTGQVHYDKIKDGLsATAL 240
Cdd:COG0707  161 GNPVRKEILELDRPEARAKLGLDPDKPTLLVFGGSQGARALNEAVPAALAALLEARLQVVHQTGKGDYEEVRAAY-AAAI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 241 APNVKIVPYIKNMPAILPEVAVILGRAGATSIAEITALGIPSILVPSPYVTNDHQTKNAQSLVNAGAAELIKESDLTGAT 320
Cdd:COG0707  240 RPNAEVFPFIDDMADAYAAADLVISRAGASTVAELAALGKPAILVPLPHAADDHQTKNARALVEAGAAVLIPQSELTPEK 319

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 334882323 321 LVAALDRLLQSSTHREAMAANAKKLGMPDAADQLLHVLESVVKS 364
Cdd:COG0707  320 LAEALEELLEDPERLAKMAEAARALARPDAAERIADLILELAKG 363
murG PRK00726
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
 1-364 2.65e-162

undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional


Pssm-ID: 234825 [Multi-domain]  Cd Length: 357  Bit Score: 458.44  E-value: 2.65e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323   1 MRLMISGGGTGGHIYPALALIDALKAHDpeAQVQFVGTHRGLESRIVPERGIDFKTIKIQGFKRSLSLQNVKTVYLFLKS 80
Cdd:PRK00726   2 KKILLAGGGTGGHVFPALALAEELKKRG--WEVLYLGTARGMEARLVPKAGIEFHFIPSGGLRRKGSLANLKAPFKLLKG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323  81 VVTARKYIKAFKPDVVVGTGGYVSGAVVFAASQMHIPTVIHEQNSVVGVTNKFLSRFVDKIAISFESARSQFPEQKVVMT 160
Cdd:PRK00726  80 VLQARKILKRFKPDVVVGFGGYVSGPGGLAARLLGIPLVIHEQNAVPGLANKLLARFAKKVATAFPGAFPEFFKPKAVVT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 161 GNPRAQQVANIKKTGalAQFELDPEIPTALIFGGSRGAARINAAAVEALPELDKrDYQTLFVTGQVHYDKIKDGLsatAL 240
Cdd:PRK00726 160 GNPVREEILALAAPP--ARLAGREGKPTLLVVGGSQGARVLNEAVPEALALLPE-ALQVIHQTGKGDLEEVRAAY---AA 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 241 APNVKIVPYIKNMPAILPEVAVILGRAGATSIAEITALGIPSILVPSPYVTNDHQTKNAQSLVNAGAAELIKESDLTGAT 320
Cdd:PRK00726 234 GINAEVVPFIDDMAAAYAAADLVICRAGASTVAELAAAGLPAILVPLPHAADDHQTANARALVDAGAALLIPQSDLTPEK 313

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 334882323 321 LVAALDRLLQSSTHREAMAANAKKLGMPDAADQLLHVLESVVKS 364
Cdd:PRK00726 314 LAEKLLELLSDPERLEAMAEAARALGKPDAAERLADLIEELARK 357
GT28_MurG cd03785
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4. ...
 2-355 1.28e-151

undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; MurG (EC 2.4.1.227) is an N-acetylglucosaminyltransferase, the last enzyme involved in the intracellular phase of peptidoglycan biosynthesis. It transfers N-acetyl-D-glucosamine (GlcNAc) from UDP-GlcNAc to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM). The resulting disaccharide is then transported across the cell membrane, where it is polymerized into NAG-NAM cell-wall repeat structure. MurG belongs to the GT-B structural superfamily of glycoslytransferases, which have characteristic N- and C-terminal domains, each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340818 [Multi-domain]  Cd Length: 350  Bit Score: 430.87  E-value: 1.28e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323   2 RLMISGGGTGGHIYPALALIDALKAHdpEAQVQFVGTHRGLESRIVPERGIDFKTIKIQGFKRSLSLQNVKTVYLFLKSV 81
Cdd:cd03785    1 KILIAGGGTGGHIFPALALAEELRKR--GAEILFIGTKRGLEAKLVPEAGIPFHTIPISGLRRKGSLKNLKAPFKLLKGL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323  82 VTARKYIKAFKPDVVVGTGGYVSGAVVFAASQMHIPTVIHEQNSVVGVTNKFLSRFVDKIAISFESARSQFPEQKVVMTG 161
Cdd:cd03785   79 RQARKILRKFKPDVVIGFGGYVSGPVVLAARLLGIPLIIHEQNAVPGLANRLLSRFADKVAVSFPETKKYFPAAKVVVTG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 162 NPRAQQVANIKKtgALAQFELDPEIPTALIFGGSRGAARINAAAVEALPELDKRDYQTLFVTGQVHYDKIKDGLSatALA 241
Cdd:cd03785  159 NPVREEILNLRK--ELKRFGLPPDKPTLLVFGGSQGARAINRAVPKALPKLLERGIQVIHQTGKGDYDEVKKLYE--DLG 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 242 PNVKIVPYIKNMPAILPEVAVILGRAGATSIAEITALGIPSILVPSPYVTNDHQTKNAQSLVNAGAAELIKESDLTGATL 321
Cdd:cd03785  235 INVKVFPFIDDMAAAYAAADLVISRAGASTIAELTAAGKPAILIPYPYAADDHQEANARALEKAGAAIVIDQEELTPEVL 314

                        330       340       350
                 ....*....|....*....|....*....|....
gi 334882323 322 VAALDRLLQSSTHREAMAANAKKLGMPDAADQLL 355
Cdd:cd03785  315 AEAILDLLNDPERLKKMAEAAKKLAKPDAAERIA 348
murG TIGR01133
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT ...
 1-354 2.04e-115

undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; RM 8449890 RT The final step of peptidoglycan subunit assembly in Escherichia coli occurs in the cytoplasm. RA Bupp K, van Heijenoort J. RL J Bacteriol 1993 Mar;175(6):1841-3 [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]


Pssm-ID: 273460 [Multi-domain]  Cd Length: 348  Bit Score: 338.88  E-value: 2.04e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323    1 MRLMISGGGTGGHIYPALALIDALKAHDPEaqVQFVGTHRGLESRIVPERGIDFKTIKIQGFKRSLSLQNVKTVYLFLKS 80
Cdd:TIGR01133   1 KKIALAAGGTGGHIFPALAVAEELIKRGVE--VLWLGTKRGLEKRLVPKAGIEFYFIPVGGLRRKGSKKLLKTPLKLLKA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323   81 VVTARKYIKAFKPDVVVGTGGYVSGAVVFAASQMHIPTVIHEQNSVVGVTNKFLSRFVDKIAISFESARSQFpeqKVVMT 160
Cdd:TIGR01133  79 VFKARRILKKFKPDVVVGFGGYVSGPAGLAAKLLGIPLIHHEQNAVPGLTNKLLSRFAKKVLVSFPGAKDHF---EAVLV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323  161 GNPRAQQVANIKKtgALAQFELDPEIPTALIFGGSRGAARINAAAVEALPELDKRDYQTLFVTGQVHYDKIKDGLSATAL 240
Cdd:TIGR01133 156 GNPVRKEIRSLPV--PRERFGRREGKPTILVLGGSQGAKILNELVPKALAKLQEKGIQIVHQGGKGDLEKVKNVYQELGQ 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323  241 ApnvKIVPYI-KNMPAILPEVAVILGRAGATSIAEITALGIPSILVPSPYVtNDHQTKNAQSLVNAGAAELIKESDLTGA 319
Cdd:TIGR01133 234 E---KIVTFIdENMAAAYAAADLVISRAGASTVAELAAAGVPAILIPYPYA-ADDQYYNAKFLEDLGAGLVIRQKELLPE 309

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 334882323  320 TLVAALDRLLQSSTHREAMAANAKKLGMPDAADQL 354
Cdd:TIGR01133 310 KLLEALLKLLLDPANLENMAEAARKLAKPDAAKRI 344
PRK12446 PRK12446
undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed
 2-361 1.67e-51

undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase; Reviewed


Pssm-ID: 171505 [Multi-domain]  Cd Length: 352  Bit Score: 175.05  E-value: 1.67e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323   2 RLMISGGGTGGHIYPALALIDALKAHDpeAQVQFVGTHRGLESRIVPERGIDFKTIKIQGFKRSLSLQNVKTVYLFLKSV 81
Cdd:PRK12446   3 KIVFTGGGSAGHVTPNLAIIPYLKEDN--WDISYIGSHQGIEKTIIEKENIPYYSISSGKLRRYFDLKNIKDPFLVMKGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323  82 VTARKYIKAFKPDVVVGTGGYVSGAVVFAASQMHIPTVIHEQNSVVGVTNKFLSRFVDKIAISFESARSQFPEQKVVMTG 161
Cdd:PRK12446  81 MDAYVRIRKLKPDVIFSKGGFVSVPVVIGGWLNRVPVLLHESDMTPGLANKIALRFASKIFVTFEEAAKHLPKEKVIYTG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 162 NPRAQQV--ANIKKTGALAQFELDPeiPTALIFGGSRGAARINAAAVEALPELdKRDYQTLFVTGQVHYDKIKDGLSAta 239
Cdd:PRK12446 161 SPVREEVlkGNREKGLAFLGFSRKK--PVITIMGGSLGAKKINETVREALPEL-LLKYQIVHLCGKGNLDDSLQNKEG-- 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 240 lapnVKIVPYI-KNMPAILPEVAVILGRAGATSIAEITALGIPSILVP-SPYVTNDHQTKNAQSLVNAGAAELIKESDLT 317
Cdd:PRK12446 236 ----YRQFEYVhGELPDILAITDFVISRAGSNAIFEFLTLQKPMLLIPlSKFASRGDQILNAESFERQGYASVLYEEDVT 311

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 334882323 318 GATLVAALDRLlqsSTHREAMAANAKKLGMPDAADQLLHVLESV 361
Cdd:PRK12446 312 VNSLIKHVEEL---SHNNEKYKTALKKYNGKEAIQTIIDHISEA 352
Glyco_transf_28 pfam03033
Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes ...
 3-143 2.21e-48

Glycosyltransferase family 28 N-terminal domain; The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). This N-terminal domain contains the acceptor binding site and likely membrane association site. This family also contains a large number of proteins that probably have quite distinct activities.


Pssm-ID: 427107 [Multi-domain]  Cd Length: 139  Bit Score: 160.15  E-value: 2.21e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323    3 LMISGGGTGGHIYPALALIDALKAHDPEaqVQFVGTHRGLESRIVPERGIDFKTIKIQGFKRSLSLQNVKTVYLFLKSVV 82
Cdd:pfam03033   1 IVLAGGGTGGHVFPALALAKELKKRGHE--VRVLGTKRGFEEFLVEKAGIEFEPIPGGGLRRKFSPKNLKEPFKLLKGIV 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334882323   83 TARKYIKAFKPDVVVGTGGYVSGAVVFAASQMHIPTVIHEQNSVVGVTNKFLSRFVDKIAI 143
Cdd:pfam03033  79 KAFRILKEFKPDAVIGFGGYVSLPAVIAAPLAGIPIIIHEQNGIPGLTNKTLPRTATKVAP 139
Glyco_tran_28_C pfam04101
Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes ...
 188-354 1.13e-43

Glycosyltransferase family 28 C-terminal domain; The glycosyltransferase family 28 includes monogalactosyldiacylglycerol synthase (EC 2.4.1.46) and UDP-N-acetylglucosamine transferase (EC 2.4.1.-). Structural analysis suggests the C-terminal domain contains the UDP-GlcNAc binding site.


Pssm-ID: 427711 [Multi-domain]  Cd Length: 166  Bit Score: 148.63  E-value: 1.13e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323  188 TALIFGGSRGAARINAAAVEALPEL-DKRDYQTLFVTGQVHYDKIKDGLSAtaLAPNVKIVPYIKNMPAILPEVAVILGR 266
Cdd:pfam04101   1 TILVTGGSQGARALNELVLSVLPLLeLKGELQVLHQTGKGDLEEVKIDYAE--LGINYEVFPFIDNMAEYIKAADLVISR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323  267 AGATSIAEITALGIPSILVPSPYVTNDHQTKNAQSLVNAGAAELIKESDLTGATLVAALDRLLQSSTHREAMAANAKKLG 346
Cdd:pfam04101  79 AGAGTIAELLALGKPAILVPNPSAARGHQDNNAKELVKAGAALVILQKELTPEKLIEALLKLLLNPLRLAEMAKASKASG 158


                  ....*...
gi 334882323  347 MPDAADQL 354
Cdd:pfam04101 159 FKDAAKRL 166
GT28_Beta-DGS-like cd17507
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ...
 3-356 3.91e-21

beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol synthase (processive diacylglycerol beta-glucosyltransferase EC 2.4.1.315) is involved in the biosynthesis of both the bilayer- and non-bilayer-forming membrane glucolipids. This family of glycosyltransferases also contains plant major galactolipid synthase (chloroplastic monogalactosyldiacylglycerol synthase 1 EC 2.4.1.46). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340861 [Multi-domain]  Cd Length: 364  Bit Score: 93.15  E-value: 3.91e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323   3 LMISGGGTGGHIYPALALIDALKAHDPEAQVQ----FVGTHRGLESRIVPERGIDFKTIKI-----QGFKRSLSLQNVKT 73
Cdd:cd17507    2 LILTASTGGGHIQAAQALKEAFREKFDNYEVIiedlLKYSNPVVNKILKRGEKLYKKAPTLyklfyNLTSDRLNSISNKA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323  74 VYLFLKSVvtaRKYIKAFKPDVVVGTGGYVSGAV-VFAASQMH-IP--TVI-----HEQnsvvgvtnkFLSRFVDKIAIS 144
Cdd:cd17507   82 ARLGLKKL---KELLREEQPDVIISTFPLMSALVeLFKRKGLLpIPvyTVItdyvlHST---------WIHPEVDRYFVA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 145 FESARSQF-----PEQKVVMTGNP-RAQQVANIKKTGALAQFELDPEIPTALIFGGSRGAARInAAAVEALPELDkRDYQ 218
Cdd:cd17507  150 SEEVKRELvergvTPSQIKVTGIPvRPSFAEVRDKDEARNELNLSPDKPTVLLMGGGGGMGPV-KETVEALLDSL-RAGQ 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 219 TLFVTGQVH--YDKIkdgLSATALAPNVKIVPYIKNMPAILPEVAVILGRAGATSIAEITALGIPSILV-PSPyvtnDHQ 295
Cdd:cd17507  228 VLVVCGKNKklYEKL---SGLEEDYINVRVLGYVDDMNELMAASDLVITKPGGLTISEALARGLPVIIYdPIP----GQE 300

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 334882323 296 TKNAQSLVNAGAAELIKeSDLTGATLVAaldrLLQSSTHREAMAANAKKLGMPDAADQLLH 356
Cdd:cd17507  301 EENADFLENNGAGIIAR-DPEELLEIVA----RLIDPPSLLRMMSEAAKELKPPAAAKVIA 356
YjiC COG1819
UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];
2-345 2.14e-20

UDP:flavonoid glycosyltransferase YjiC, YdhE family [Carbohydrate transport and metabolism];


Pssm-ID: 441424 [Multi-domain]  Cd Length: 268  Bit Score: 89.53  E-value: 2.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323   2 RLMISGGGTGGHIYPALALIDALKA--HDpeaqVQFVGTHRGLEsrIVPERGIDFKtikiqgfkrslslqnvktvylflk 79
Cdd:COG1819    1 RILFVTLGGRGHVNPLLALARALRArgHE----VTFATGPDFAD--LVEAAGLEFV------------------------ 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323  80 svvtarkyikAFKPDVVVGTGGYVSGAVvfAASQMHIPTVIHeqnsvvgvtnkfLSRfvdkiaiSFESARSQFPEqKVVM 159
Cdd:COG1819   51 ----------DWRPDLVVSDPLALAAAL--AAEALGIPVVSL------------TPP-------ELEYPRPPDPA-NVRF 98

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 160 TGNPRAqqvaniKKTGALAQFEL-DPEIPTALI-FGGS-RGAARINAAAVEALPELDkrdYQTLFVTGQVHYDKIKDgls 236
Cdd:COG1819   99 VGPLLP------DGPAELPPWLEeDAGRPLVYVtLGTSaNDRADLLRAVLEALADLG---VRVVVTTGGLDPAELGP--- 166

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 237 ataLAPNVKIVPYIkNMPAILPEVAVILGRAGATSIAEITALGIPSILVPspyVTNDhQTKNAQSLVNAGAAELIKESDL 316
Cdd:COG1819  167 ---LPDNVRVVDYV-PQDALLPRADAVVHHGGAGTTAEALRAGVPQVVVP---FGGD-QPLNAARVERLGAGLALPPRRL 238

                        330       340
                 ....*....|....*....|....*....
gi 334882323 317 TGATLVAALDRLLQSSTHREAMAANAKKL 345
Cdd:COG1819  239 TAEALRAALRRLLADPSYRERAARLAAEI 267
PLN02605 PLN02605
monogalactosyldiacylglycerol synthase
 128-351 1.24e-09

monogalactosyldiacylglycerol synthase


Pssm-ID: 215325 [Multi-domain]  Cd Length: 382  Bit Score: 59.21  E-value: 1.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 128 GVTNKFL-SRFVDKIAIsfesaRSQFPEQKVVMTGNP-RAQQVANIKKTGALA-QFELDPEIPTALIFGGSRGAARINAA 204
Cdd:PLN02605 150 GVTRCFCpSEEVAKRAL-----KRGLEPSQIRVYGLPiRPSFARAVRPKDELRrELGMDEDLPAVLLMGGGEGMGPLEET 224

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 205 AvEAL------PELDKRDYQTLFVTGQvhYDKIKDGLSATALAPNVKIVPYIKNMPAILPEVAVILGRAGATSIAEITAL 278
Cdd:PLN02605 225 A-RALgdslydKNLGKPIGQVVVICGR--NKKLQSKLESRDWKIPVKVRGFVTNMEEWMGACDCIITKAGPGTIAEALIR 301

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 279 GIPSIL---VPS------PYVtndhqtknaqslVNAGAAELIKESDLTGATLVaalDRLLQSSTHREAMAANAKKLGMPD 349
Cdd:PLN02605 302 GLPIILngyIPGqeegnvPYV------------VDNGFGAFSESPKEIARIVA---EWFGDKSDELEAMSENALKLARPE 366


                 ..
gi 334882323 350 AA 351
Cdd:PLN02605 367 AV 368
PRK13609 PRK13609
diacylglycerol glucosyltransferase; Provisional
 151-358 2.68e-08

diacylglycerol glucosyltransferase; Provisional


Pssm-ID: 237445 [Multi-domain]  Cd Length: 380  Bit Score: 55.12  E-value: 2.68e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 151 QFPEQKVVMTGNP-RAQQVANIKKTGALAQFELDPEIPTALIFGGSRGAARINAAAVEALpeLDKRDYQTLFVTGQvhYD 229
Cdd:PRK13609 166 GVPPEQVVETGIPiRSSFELKINPDIIYNKYQLCPNKKILLIMAGAHGVLGNVKELCQSL--MSVPDLQVVVVCGK--NE 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 230 KIKDGLSAT-ALAPN-VKIVPYIKNMPAILPEVAVILGRAGATSIAEITALGIPSILV-PSPyvtnDHQTKNAQSLVNAG 306
Cdd:PRK13609 242 ALKQSLEDLqETNPDaLKVFGYVENIDELFRVTSCMITKPGGITLSEAAALGVPVILYkPVP----GQEKENAMYFERKG 317

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 334882323 307 AAELIKESDltgaTLVAALDRLLQSSTHREAMAANAKKLGMPDAADQLLHVL 358
Cdd:PRK13609 318 AAVVIRDDE----EVFAKTEALLQDDMKLLQMKEAMKSLYLPEPADHIVDDI 365
GT1_Gtf-like cd03784
UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of ...
 1-358 1.21e-07

UDP-glycosyltransferases and similar proteins; This family includes the Gtfs, a group of homologous glycosyltransferases involved in the final stages of the biosynthesis of antibiotics vancomycin and related chloroeremomycin. Gtfs transfer sugar moieties from an activated NDP-sugar donor to the oxidatively cross-linked heptapeptide core of vancomycin group antibiotics. The core structure is important for the bioactivity of the antibiotics.


Pssm-ID: 340817 [Multi-domain]  Cd Length: 404  Bit Score: 52.94  E-value: 1.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323   1 MRLMISGGGTGGHIYPALALIDALKAHDpeAQVQFVGTHRGLESRI-------------VPERGIDFKTIKIQGFKRSLS 67
Cdd:cd03784    1 MRILFVPFPGQGHVNPMLPLAKALAARG--HEVTVATPPFNFADLVeaagltfvpvgddPDELELDSETNLGPDSLLELL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323  68 LQNVKTVYLFLKSVVtaRKYIKAFKPDVVVGTGGYVSGAVVfaASQMHIPTVIH-------EQNSVVGVTNKFLSRFVDK 140
Cdd:cd03784   79 RRLLKAADELLDDLL--AALRSSWKPDLVIADPFAYAGPLV--AEELGIPSVRLftgpatlLSAYLHPFGVLNLLLSSLL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 141 IAISFES-ARSQFPEQKVVMTGNPRAQQVANIKKTGALAQF-----ELDPEIPTALIFGGSRGAARINAAAVEALPE--L 212
Cdd:cd03784  155 EPELFLDpLLEVLDRLRERLGLPPFSLVLLLLRLVPPLYVIgptfpSLPPDRPRLPSVLGGLRIVPKNGPLPDELWEwlD 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 213 DKRDYQTLFVT-GQVHYDKIKD--GLSATALA----------------------PNVKIVPYIkNMPAIL--PEVAVILG 265
Cdd:cd03784  235 KQPPRSVVYVSfGSMVRDLPEEllELIAEALAslgqrflwvvgpdplgglerlpDNVLVVKWV-PQDELLahPAVGAFVT 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 266 RAGATSIAEITALGIPSILVPspyVTNDhQTKNAQSLVNAGAAELIKESDLTGATLVAALDRLLQSSTHREAMAANAKKL 345
Cdd:cd03784  314 HGGWNSTLEALYAGVPMVVVP---LFAD-QPNNAARVEELGAGVELDKDELTAEELAKAVREVLEDESYRRAAELLAELR 389

                        410
                 ....*....|....*
gi 334882323 346 GM--PDAADQLLHVL 358
Cdd:cd03784  390 EEdgAPSAADVVERL 404
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 8-265 2.15e-04

Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.


Pssm-ID: 340846 [Multi-domain]  Cd Length: 345  Bit Score: 42.73  E-value: 2.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323   8 GGTGGHIYpalALIDALKAHDPEAQVQFVGThrglesRIVPERGIDfkTIKIQGFKRSLSLqnvktvylFLKSVVTARKY 87
Cdd:cd03819   11 GGAETYIL---DLARALAERGHRVLVVTAGG------PLLPRLRQI--GIGLPGLKVPLLR--------ALLGNVRLARL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323  88 IKAFKPDVV-VGTGGYV-SGAVvfAASQMHIPTVIHEQNSVVGVTN-----KFLSRFVDK-IAISfESARSQ------FP 153
Cdd:cd03819   72 IRRERIDLIhAHSRAPAwLGWL--ASRLTGVPLVTTVHGSYLATYHpkdfaLAVRARGDRvIAVS-ELVRDHliealgVD 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 154 EQKV------VMTGNPRAQQVAnikktGALAQFELDPEIPTALIFGgsrgaaRINA-----AAVEALPELDKRDYQTLFV 222
Cdd:cd03819  149 PERIrvipngVDTDRFPPEAEA-----EERAQLGLPEGKPVVGYVG------RLSPekgwlLLVDAAAELKDEPDFRLLV 217

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 334882323 223 TGQVH-YDKIKDGLSATALAPNVKIVPYIKNMPAILPEVAVILG 265
Cdd:cd03819  218 AGDGPeRDEIRRLVERLGLRDRVTFTGFREDVPAALAASDVVVL 261
PRK13608 PRK13608
diacylglycerol glucosyltransferase; Provisional
 92-360 9.01e-04

diacylglycerol glucosyltransferase; Provisional


Pssm-ID: 184179 [Multi-domain]  Cd Length: 391  Bit Score: 40.93  E-value: 9.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323  92 KPDVVVGTGGYVSGAVVFAASQMHIP--TVIHE----QNSVVGVTNKFlsrFVDKIAISFESARSQFPEQKVVMTGNPRA 165
Cdd:PRK13608 104 KPDLILLTFPTPVMSVLTEQFNINIPvaTVMTDyrlhKNWITPYSTRY---YVATKETKQDFIDVGIDPSTVKVTGIPID 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 166 QQV-ANIKKTGALAQFELDPEIPTALI----FGGSRGAARINAAAVEALPEldkrdYQTLFVTGQvhYDKIKDGLSATAL 240
Cdd:PRK13608 181 NKFeTPIDQKQWLIDNNLDPDKQTILMsagaFGVSKGFDTMITDILAKSAN-----AQVVMICGK--SKELKRSLTAKFK 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 241 A-PNVKIVPYIKNMPAILPEVAVILGRAGATSIAEITALGIPSI-LVPSPyvtnDHQTKNAQSLVNAGAAELikeSDLTG 318
Cdd:PRK13608 254 SnENVLILGYTKHMNEWMASSQLMITKPGGITISEGLARCIPMIfLNPAP----GQELENALYFEEKGFGKI---ADTPE 326

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 334882323 319 ATLVAALDrLLQSSTHREAMAANAKKLGMPDAA----DQLLHVLES 360
Cdd:PRK13608 327 EAIKIVAS-LTNGNEQLTNMISTMEQDKIKYATqticRDLLDLIGH 371
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 8-345 5.16e-03

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.


Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 38.67  E-value: 5.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323   8 GGTGGHIYpalALIDALKAhdpeaqvqfvgthRGLESRIVPERGIDFKTIKIQGFKRSLSLQNVKTVYLFLKSVVTARKY 87
Cdd:cd03801   14 GGAERHVR---ELARALAA-------------RGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLRELRPL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323  88 IKAFKPDVVVGTGGYVSGAVVFAASQMHIPTVIHEQNSVVGVTNKFL---SRFVDKIAISFESAR-----SQFPEQKVVM 159
Cdd:cd03801   78 LRLRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLaaeRRLLARAEALLRRADaviavSEALRDELRA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 160 TGNPRAQQVA--------NIKKTGALAQFELDPEIPTALIFGGSRGAARINAAaVEALPELDKRDYQ-TLFVTGQvhYDK 230
Cdd:cd03801  158 LGGIPPEKIVvipngvdlERFSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLL-LEALAKLLRRGPDvRLVIVGG--DGP 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 231 IKDGLSATA--LAPNVKIVPYI--KNMPAILPEVAVILgragATSIAE---ITAL-----GIPSILVPSPYVTndhqtkn 298
Cdd:cd03801  235 LRAELEELElgLGDRVRFLGFVpdEELPALYAAADVFV----LPSRYEgfgLVVLeamaaGLPVVATDVGGLP------- 303

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 334882323 299 aqSLVNAGAAELIKESDLTGAtLVAALDRLLQSSTHREAMAANAKKL 345
Cdd:cd03801  304 --EVVEDGEGGLVVPPDDVEA-LADALLRLLADPELRARLGRAARER 347
PRK05749 PRK05749
3-deoxy-D-manno-octulosonic-acid transferase; Reviewed
 277-360 5.23e-03

3-deoxy-D-manno-octulosonic-acid transferase; Reviewed


Pssm-ID: 235589 [Multi-domain]  Cd Length: 425  Bit Score: 38.67  E-value: 5.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334882323 277 ALGIPSILvpSPYVTNdhQTKNAQSLVNAGAAELIKESDltgaTLVAALDRLLQSSTHREAMAANAKKL--GMPDAADQL 354
Cdd:PRK05749 342 AFGVPVIS--GPHTFN--FKEIFERLLQAGAAIQVEDAE----DLAKAVTYLLTDPDARQAYGEAGVAFlkQNQGALQRT 413


                 ....*.
gi 334882323 355 LHVLES 360
Cdd:PRK05749 414 LQLLEP 419
 
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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