NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2501001744|gb|WGV36161|]
View 

serine O-acetyltransferase [synthetic construct]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PLN02357 PLN02357
serine acetyltransferase
 17-391 0e+00

serine acetyltransferase


:

Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 665.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744  17 LRSSSPHINHHSFLLPSFVsskfKHHTLSPPPSPPppppMAACIDTCRTGKPQISPrdssKHHDDESGFRYMNYFRYPDR 96
Cdd:PLN02357    1 LRSSSPHISLHSFLLPPFS----CTSTFSLPKSRP----MAACIDTCRTGTSQLSP----KHHDDDSHFYYIKNFCRPSF 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744  97 SSFNGTQTKTLHTRPLLEDLDrdaEVDDVWAKIREEAKSDIAKEPIVSAYYHASIVSQRSLEAALANTLSVKLSNLNLPS 176
Cdd:PLN02357   69 SPFSGNHTKTIHTRPVEDDLD---RDDDVWLKIQEEAKSDVEQEPILSSYYYASILSHRSLESALANHLSVKLSNLNLPS 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 177 NTLFDLFSGVLQGNPDIVESVKLDLLAVKERDPACISYVHCFLHFKGFLACQAHRIAHELWTQDRKILALLIQNRVSEAF 256
Cdd:PLN02357  146 NTLFDLFIGVLEESPEIIESVKQDLRAVKERDPACISYVHCFLNFKGFLACQAHRIAHKLWTQGRKILALLIQNRVSEAF 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 257 AVDFHPGAKIGTGILLDHATAIVIGETAVVGNNVSILHNVTLGGTGKQCGDRHPKIGDGVLIGAGTCILGNITIGEGAKI 336
Cdd:PLN02357  226 AVDIHPGAKIGQGILLDHATGVVIGETAVVGNNVSILHNVTLGGTGKQSGDRHPKIGDGVLIGAGTCILGNITIGEGAKI 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2501001744 337 GAGSVVLKDVPPRTTAVGNPARLLGGKDNPKTHDKIPGLTMDQTSHISEWSDYVI 391
Cdd:PLN02357  306 GAGSVVLKDVPPRTTAVGNPARLIGGKENPIKHDKIPSLTMDQTSHISEWSDYVI 360
 
Name Accession Description Interval E-value
PLN02357 PLN02357
serine acetyltransferase
 17-391 0e+00

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 665.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744  17 LRSSSPHINHHSFLLPSFVsskfKHHTLSPPPSPPppppMAACIDTCRTGKPQISPrdssKHHDDESGFRYMNYFRYPDR 96
Cdd:PLN02357    1 LRSSSPHISLHSFLLPPFS----CTSTFSLPKSRP----MAACIDTCRTGTSQLSP----KHHDDDSHFYYIKNFCRPSF 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744  97 SSFNGTQTKTLHTRPLLEDLDrdaEVDDVWAKIREEAKSDIAKEPIVSAYYHASIVSQRSLEAALANTLSVKLSNLNLPS 176
Cdd:PLN02357   69 SPFSGNHTKTIHTRPVEDDLD---RDDDVWLKIQEEAKSDVEQEPILSSYYYASILSHRSLESALANHLSVKLSNLNLPS 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 177 NTLFDLFSGVLQGNPDIVESVKLDLLAVKERDPACISYVHCFLHFKGFLACQAHRIAHELWTQDRKILALLIQNRVSEAF 256
Cdd:PLN02357  146 NTLFDLFIGVLEESPEIIESVKQDLRAVKERDPACISYVHCFLNFKGFLACQAHRIAHKLWTQGRKILALLIQNRVSEAF 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 257 AVDFHPGAKIGTGILLDHATAIVIGETAVVGNNVSILHNVTLGGTGKQCGDRHPKIGDGVLIGAGTCILGNITIGEGAKI 336
Cdd:PLN02357  226 AVDIHPGAKIGQGILLDHATGVVIGETAVVGNNVSILHNVTLGGTGKQSGDRHPKIGDGVLIGAGTCILGNITIGEGAKI 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2501001744 337 GAGSVVLKDVPPRTTAVGNPARLLGGKDNPKTHDKIPGLTMDQTSHISEWSDYVI 391
Cdd:PLN02357  306 GAGSVVLKDVPPRTTAVGNPARLIGGKENPIKHDKIPSLTMDQTSHISEWSDYVI 360
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 193-366 2.57e-93

Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440667 [Multi-domain]  Cd Length: 174  Bit Score: 276.96  E-value: 2.57e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 193 IVESVKLDLLAVKERDPACISYVHCFLHFKGFLACQAHRIAHELWTQDRKILALLIQNRVSEAFAVDFHPGAKIGTGILL 272
Cdd:COG1045     1 MLKALREDIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHPGATIGRGFFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 273 DHATAIVIGETAVVGNNVSILHNVTLGGTGKQCGDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTA 352
Cdd:COG1045    81 DHGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTV 160

                         170
                  ....*....|....
gi 2501001744 353 VGNPARLLGGKDNP 366
Cdd:COG1045   161 VGVPARIVKRKGSK 174
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 197-358 1.57e-83

serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 251.83  E-value: 1.57e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 197 VKLDLLAVKERDPACISYVHCFLHFKGFLACQAHRIAHELWTQDRKILALLIQNRVSEAFAVDFHPGAKIGTGILLDHAT 276
Cdd:TIGR01172   1 IREDIRAVRERDPAARSYLEVLLYYPGFHALWAYRFAHFLWKRGFKFLARLLSNFIRVLTGVDIHPGARIGRGVFIDHGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 277 AIVIGETAVVGNNVSILHNVTLGGTGKQCGDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNP 356
Cdd:TIGR01172  81 GVVIGETAVIGDDVTIYHGVTLGGTGKEKGKRHPTIGEGVMIGAGAKVLGNIEVGENAKIGANSVVLKDVPPGATVVGVP 160


                  ..
gi 2501001744 357 AR 358
Cdd:TIGR01172 161 AR 162
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 256-356 2.90e-53

Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetylserine, as the first step of a two-step biosynthetic pathway in bacteria and plants leading to the formation of L-cysteine. This reaction represents a key metabolic point of regulation for the cysteine biosynthetic pathway due to its feedback inhibition by cysteine. The enzyme is a 175 kDa homohexamer, composed of a dimer of homotrimers. Each subunit contains an N-terminal alpha helical region and a C-terminal left-handed beta-helix (LbH) subdomain with 5 turns, each containing a hexapeptide repeat motif characteristic of the acyltransferase superfamily of enzymes. The trimer interface mainly involves the C-terminal LbH subdomain while the dimer (of trimers) interface is mediated by the N-terminal alpha helical subdomain.


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 171.85  E-value: 2.90e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 256 FAVDFHPGAKIGTGILLDHATAIVIGETAVVGNNVSILHNVTLGGTGKQCGDRHPKIGDGVLIGAGTCILGNITIGEGAK 335
Cdd:cd03354     1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                          90       100
                  ....*....|....*....|.
gi 2501001744 336 IGAGSVVLKDVPPRTTAVGNP 356
Cdd:cd03354    81 IGANAVVTKDVPANSTVVGVP 101
SATase_N pfam06426
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 125-228 1.30e-49

Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a sequence that is conserved in plants and bacteria.


Pssm-ID: 461909 [Multi-domain]  Cd Length: 104  Bit Score: 162.63  E-value: 1.30e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 125 VWAKIREEAKSDIAKEPIVSAYYHASIVSQRSLEAALANTLSVKLSNLNLPSNTLFDLFSGVLQGNPDIVESVKLDLLAV 204
Cdd:pfam06426   1 VWARLRAEAEEAAEREPLLASFLYATILSHDSLESALAFRLANKLANSTLPATLLRELFEDALEADPEIVEAARADLQAV 80

                          90       100
                  ....*....|....*....|....
gi 2501001744 205 KERDPACISYVHCFLHFKGFLACQ 228
Cdd:pfam06426  81 YERDPACDRYLTPLLYFKGFHALQ 104
SATase_N smart00971
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 125-229 2.89e-47

Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a sequence that is conserved in plants.and bacteria.


Pssm-ID: 198039 [Multi-domain]  Cd Length: 105  Bit Score: 156.55  E-value: 2.89e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744  125 VWAKIREEAKSDIAKEPIVSAYYHASIVSQRSLEAALANTLSVKLSNLNLPSNTLFDLFSGVLQGNPDIVESVKLDLLAV 204
Cdd:smart00971   1 VWQRIRAEAREAAEREPILASFLYATILNHDSLEAALAYRLANKLGNADMSADLLRELFEDAYAADPEIVEAAAADIQAV 80

                           90       100
                   ....*....|....*....|....*
gi 2501001744  205 KERDPACISYVHCFLHFKGFLACQA 229
Cdd:smart00971  81 YDRDPACDRYLTPLLYFKGFHALQA 105
 
Name Accession Description Interval E-value
PLN02357 PLN02357
serine acetyltransferase
 17-391 0e+00

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 665.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744  17 LRSSSPHINHHSFLLPSFVsskfKHHTLSPPPSPPppppMAACIDTCRTGKPQISPrdssKHHDDESGFRYMNYFRYPDR 96
Cdd:PLN02357    1 LRSSSPHISLHSFLLPPFS----CTSTFSLPKSRP----MAACIDTCRTGTSQLSP----KHHDDDSHFYYIKNFCRPSF 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744  97 SSFNGTQTKTLHTRPLLEDLDrdaEVDDVWAKIREEAKSDIAKEPIVSAYYHASIVSQRSLEAALANTLSVKLSNLNLPS 176
Cdd:PLN02357   69 SPFSGNHTKTIHTRPVEDDLD---RDDDVWLKIQEEAKSDVEQEPILSSYYYASILSHRSLESALANHLSVKLSNLNLPS 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 177 NTLFDLFSGVLQGNPDIVESVKLDLLAVKERDPACISYVHCFLHFKGFLACQAHRIAHELWTQDRKILALLIQNRVSEAF 256
Cdd:PLN02357  146 NTLFDLFIGVLEESPEIIESVKQDLRAVKERDPACISYVHCFLNFKGFLACQAHRIAHKLWTQGRKILALLIQNRVSEAF 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 257 AVDFHPGAKIGTGILLDHATAIVIGETAVVGNNVSILHNVTLGGTGKQCGDRHPKIGDGVLIGAGTCILGNITIGEGAKI 336
Cdd:PLN02357  226 AVDIHPGAKIGQGILLDHATGVVIGETAVVGNNVSILHNVTLGGTGKQSGDRHPKIGDGVLIGAGTCILGNITIGEGAKI 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2501001744 337 GAGSVVLKDVPPRTTAVGNPARLLGGKDNPKTHDKIPGLTMDQTSHISEWSDYVI 391
Cdd:PLN02357  306 GAGSVVLKDVPPRTTAVGNPARLIGGKENPIKHDKIPSLTMDQTSHISEWSDYVI 360
PLN02694 PLN02694
serine O-acetyltransferase
 91-391 1.11e-137

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 394.78  E-value: 1.11e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744  91 FRYPDRSSFNGTQTKtlhtrplledldrDAEVDDVWAKIREEAKSDIAKEPIVSAYYHASIVSQRSLEAALANTLSVKLS 170
Cdd:PLN02694    7 LRHPSPPKTNSATTA-------------DEEAAWLWTQIKAEARRDAESEPALASYLYSTILSHSSLERSLSFHLGNKLC 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 171 NLNLPSNTLFDLFSGVLQGNPDIVESVKLDLLAVKERDPACISYVHCFLHFKGFLACQAHRIAHELWTQDRKILALLIQN 250
Cdd:PLN02694   74 SSTLLSTLLYDLFLNTFSSDPSLRAATVADLRAARVRDPACVSFSHCLLNYKGFLACQAHRVAHKLWTQSRRPLALALHS 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 251 RVSEAFAVDFHPGAKIGTGILLDHATAIVIGETAVVGNNVSILHNVTLGGTGKQCGDRHPKIGDGVLIGAGTCILGNITI 330
Cdd:PLN02694  154 RISDVFAVDIHPAAKIGKGILFDHATGVVIGETAVIGNNVSILHHVTLGGTGKACGDRHPKIGDGVLIGAGATILGNVKI 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2501001744 331 GEGAKIGAGSVVLKDVPPRTTAVGNPARLLGGKDNPKTHDKIPGLTMDQTSHISEWSDYVI 391
Cdd:PLN02694  234 GEGAKIGAGSVVLIDVPPRTTAVGNPARLVGGKEKPAKHEECPGESMDHTSFISEWSDYII 294
cysE PRK11132
serine acetyltransferase; Provisional
 118-379 3.23e-114

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 333.97  E-value: 3.23e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 118 RDAEVDDVWAKIREEAKSDIAKEPIVSAYYHASIVSQRSLEAALANTLSVKLSNLNLPSNTLFDLFSGVLQGNPDIVESV 197
Cdd:PRK11132    2 SCEELEIVWNNIKAEARALADCEPMLASFYHATLLKHENLGSALSYMLANKLASPIMPAIAIREVVEEAYAADPEMIASA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 198 KLDLLAVKERDPACISYVHCFLHFKGFLACQAHRIAHELWTQDRKILALLIQNRVSEAFAVDFHPGAKIGTGILLDHATA 277
Cdd:PRK11132   82 ACDIQAVRTRDPAVDKYSTPLLYLKGFHALQAYRIGHWLWNQGRRALAIYLQNQISVAFQVDIHPAAKIGRGIMLDHATG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 278 IVIGETAVVGNNVSILHNVTLGGTGKQCGDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPA 357
Cdd:PRK11132  162 IVIGETAVIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPA 241

                         250       260
                  ....*....|....*....|..
gi 2501001744 358 RLLGgkdNPKThDKiPGLTMDQ 379
Cdd:PRK11132  242 RIVG---KPES-DK-PSMDMDQ 258
PLN02739 PLN02739
serine acetyltransferase
 68-378 2.09e-108

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 322.37  E-value: 2.09e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744  68 PQISPRDSSKHHDDESG--FRYMNYFRYPDRSSFNGTqtktlhTRPLLEDLDrDAEVDDVWAKIREEAKSDIAKEPIVSA 145
Cdd:PLN02739   21 PMIVSRNFSARDDGETGdeFPFERGFPVYARGTLNPV------ADPVLLDFT-NSRYDPIWDSIREEAKLEAEEEPVLSS 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 146 YYHASIVSQRSLEAALANTLSVKLSNLNLPSNTLFDLFSGVLQGNPDIVESVKLDLLAVKERDPACISYVHCFLHFKGFL 225
Cdd:PLN02739   94 FLYASILSHDCLEQALSFVLANRLQNPTLLATQLMDIFCNVMVHDRGIQSSIRLDVQAFKDRDPACLSYSSAILHLKGYL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 226 ACQAHRIAHELWTQDRKILALLIQNRVSEAFAVDFHPGAKIGTGILLDHATAIVIGETAVVGNNVSILHNVTLGGTGKQC 305
Cdd:PLN02739  174 ALQAYRVAHKLWKQGRKLLALALQSRVSEVFGIDIHPAARIGKGILLDHGTGVVIGETAVIGDRVSILHGVTLGGTGKET 253

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2501001744 306 GDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLLGGKDnpkthDKIPGLTMD 378
Cdd:PLN02739  254 GDRHPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFVD-----EQDPSLTME 321
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 193-366 2.57e-93

Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440667 [Multi-domain]  Cd Length: 174  Bit Score: 276.96  E-value: 2.57e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 193 IVESVKLDLLAVKERDPACISYVHCFLHFKGFLACQAHRIAHELWTQDRKILALLIQNRVSEAFAVDFHPGAKIGTGILL 272
Cdd:COG1045     1 MLKALREDIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHPGATIGRGFFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 273 DHATAIVIGETAVVGNNVSILHNVTLGGTGKQCGDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTA 352
Cdd:COG1045    81 DHGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTV 160

                         170
                  ....*....|....
gi 2501001744 353 VGNPARLLGGKDNP 366
Cdd:COG1045   161 VGVPARIVKRKGSK 174
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 197-358 1.57e-83

serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 251.83  E-value: 1.57e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 197 VKLDLLAVKERDPACISYVHCFLHFKGFLACQAHRIAHELWTQDRKILALLIQNRVSEAFAVDFHPGAKIGTGILLDHAT 276
Cdd:TIGR01172   1 IREDIRAVRERDPAARSYLEVLLYYPGFHALWAYRFAHFLWKRGFKFLARLLSNFIRVLTGVDIHPGARIGRGVFIDHGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 277 AIVIGETAVVGNNVSILHNVTLGGTGKQCGDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNP 356
Cdd:TIGR01172  81 GVVIGETAVIGDDVTIYHGVTLGGTGKEKGKRHPTIGEGVMIGAGAKVLGNIEVGENAKIGANSVVLKDVPPGATVVGVP 160


                  ..
gi 2501001744 357 AR 358
Cdd:TIGR01172 161 AR 162
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 256-356 2.90e-53

Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetylserine, as the first step of a two-step biosynthetic pathway in bacteria and plants leading to the formation of L-cysteine. This reaction represents a key metabolic point of regulation for the cysteine biosynthetic pathway due to its feedback inhibition by cysteine. The enzyme is a 175 kDa homohexamer, composed of a dimer of homotrimers. Each subunit contains an N-terminal alpha helical region and a C-terminal left-handed beta-helix (LbH) subdomain with 5 turns, each containing a hexapeptide repeat motif characteristic of the acyltransferase superfamily of enzymes. The trimer interface mainly involves the C-terminal LbH subdomain while the dimer (of trimers) interface is mediated by the N-terminal alpha helical subdomain.


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 171.85  E-value: 2.90e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 256 FAVDFHPGAKIGTGILLDHATAIVIGETAVVGNNVSILHNVTLGGTGKQCGDRHPKIGDGVLIGAGTCILGNITIGEGAK 335
Cdd:cd03354     1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                          90       100
                  ....*....|....*....|.
gi 2501001744 336 IGAGSVVLKDVPPRTTAVGNP 356
Cdd:cd03354    81 IGANAVVTKDVPANSTVVGVP 101
SATase_N pfam06426
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 125-228 1.30e-49

Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a sequence that is conserved in plants and bacteria.


Pssm-ID: 461909 [Multi-domain]  Cd Length: 104  Bit Score: 162.63  E-value: 1.30e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 125 VWAKIREEAKSDIAKEPIVSAYYHASIVSQRSLEAALANTLSVKLSNLNLPSNTLFDLFSGVLQGNPDIVESVKLDLLAV 204
Cdd:pfam06426   1 VWARLRAEAEEAAEREPLLASFLYATILSHDSLESALAFRLANKLANSTLPATLLRELFEDALEADPEIVEAARADLQAV 80

                          90       100
                  ....*....|....*....|....
gi 2501001744 205 KERDPACISYVHCFLHFKGFLACQ 228
Cdd:pfam06426  81 YERDPACDRYLTPLLYFKGFHALQ 104
SATase_N smart00971
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 125-229 2.89e-47

Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a sequence that is conserved in plants.and bacteria.


Pssm-ID: 198039 [Multi-domain]  Cd Length: 105  Bit Score: 156.55  E-value: 2.89e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744  125 VWAKIREEAKSDIAKEPIVSAYYHASIVSQRSLEAALANTLSVKLSNLNLPSNTLFDLFSGVLQGNPDIVESVKLDLLAV 204
Cdd:smart00971   1 VWQRIRAEAREAAEREPILASFLYATILNHDSLEAALAYRLANKLGNADMSADLLRELFEDAYAADPEIVEAAAADIQAV 80

                           90       100
                   ....*....|....*....|....*
gi 2501001744  205 KERDPACISYVHCFLHFKGFLACQA 229
Cdd:smart00971  81 YDRDPACDRYLTPLLYFKGFHALQA 105
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
254-361 1.33e-25

Acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 100.72  E-value: 1.33e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 254 EAFAVDFHPGAKIGTGILLDHATAIVIGETAVVGNNVSILHNVTLggtgkqCGDRHP--------------KIGDGVLIG 319
Cdd:COG0110    18 GPGVRIYGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTI------LTGNHPiddpatfplrtgpvTIGDDVWIG 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2501001744 320 AGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLLG 361
Cdd:COG0110    92 AGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIR 133
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 266-360 3.74e-23

Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 92.90  E-value: 3.74e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 266 IGTGILLDHATAIVIGETAVVGNNVSIL---HNVTLGGTGKQCGDRHP--KIGDGVLIGAGTCILGNITIGEGAKIGAGS 340
Cdd:cd04647    10 IGPGCVISAGGGITIGDNVLIGPNVTIYdhnHDIDDPERPIEQGVTSApiVIGDDVWIGANVVILPGVTIGDGAVVGAGS 89

                          90       100
                  ....*....|....*....|
gi 2501001744 341 VVLKDVPPRTTAVGNPARLL 360
Cdd:cd04647    90 VVTKDVPPNSIVAGNPAKVI 109
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 262-357 7.21e-23

sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff.


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 94.87  E-value: 7.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 262 PGAKIGTGILLDhaTAIVIGETAVVGNNVSILHNVTLGGtgkqcgdrHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSV 341
Cdd:TIGR03570 116 PDVRIGDNVIIN--TGAIVEHDCVIGDFVHIAPGVTLSG--------GVVIGEGVFIGAGATIIQGVTIGAGAIVGAGAV 185

                          90
                  ....*....|....*.
gi 2501001744 342 VLKDVPPRTTAVGNPA 357
Cdd:TIGR03570 186 VTKDIPDGGVVVGVPA 201
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 270-360 4.91e-22

Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively at the C6 position of the nonreducing end glucosyl moiety. GAT specifically acetylates galactopyranosides. Furthermore, MAT shows higher affinity toward artificial substrates containing an alkyl or hydrophobic chain as well as a glucosyl unit. Active MAT and GAT are homotrimers, with each subunit consisting of an N-terminal alpha-helical region and a C-terminal left-handed parallel alpha-helix (LbH) subdomain with 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100047 [Multi-domain]  Cd Length: 169  Bit Score: 91.71  E-value: 4.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 270 ILLDHAtAIVIGETAVVGNNVSIL---H--NVTLGGTGKQCGdrHP-KIGDGVLIGAGTCILGNITIGEGAKIGAGSVVL 343
Cdd:cd03357    76 TILDVA-PVTIGDNVLIGPNVQIYtagHplDPEERNRGLEYA--KPiTIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVT 152

                          90
                  ....*....|....*..
gi 2501001744 344 KDVPPRTTAVGNPARLL 360
Cdd:cd03357   153 KDIPANVVAAGNPARVI 169
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 265-361 6.79e-22

WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of Xanthomonas campestris WcxM and proteins with similarity to the WcxM N-terminal domain. WcxM is thought to be bifunctional, catalyzing both the isomerization and transacetylation reactions of keto-hexoses. It contains an N-terminal LbH domain responsible for the transacetylation function and a C-terminal isomerase domain. The LbH domain contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), typical of enzymes with acyltransferase activity.


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 89.87  E-value: 6.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 265 KIGTGILLDHATaiVIGETAVVGNNVSILHNVTLGG---TGKQC---GDRHP-------------KIGDGVLIGAGTCIL 325
Cdd:cd03358     6 IIGTNVFIENDV--KIGDNVKIQSNVSIYEGVTIEDdvfIGPNVvftNDLYPrskiyrkwelkgtTVKRGASIGANATIL 83

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2501001744 326 GNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLLG 361
Cdd:cd03358    84 PGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 262-356 2.42e-21

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 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. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 90.62  E-value: 2.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 262 PGAKIGTGILLDhaTAIVIGETAVVGNNVSILHNVTLGGtgkqcgdrHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSV 341
Cdd:cd03360   113 PDARIGDNVIIN--TGAVIGHDCVIGDFVHIAPGVVLSG--------GVTIGEGAFIGAGATIIQGVTIGAGAIIGAGAV 182

                          90
                  ....*....|....*
gi 2501001744 342 VLKDVPPRTTAVGNP 356
Cdd:cd03360   183 VTKDVPDGSVVVGNP 197
PRK10191 PRK10191
putative acyl transferase; Provisional
 229-359 3.85e-18

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 80.32  E-value: 3.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 229 AHRIAH------------ELWTQDRKILALLIQNRVseaFAVDFHPGAKIGTGILLDHATAIVIGETAVVGNNVSILHNV 296
Cdd:PRK10191    4 AYRVAHfcsvwrkknvlnNLWAAPLLVLYRIITECF---FGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGV 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2501001744 297 TLGGTGKQ---CgdrhPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARL 359
Cdd:PRK10191   81 TIGNRGADnmaC----PHIGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKARV 142
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 278-372 1.38e-16

Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of a large number of microbial enzymes that catalyze the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. Members of this class of enzymes include Enterococcus faecium streptogramin A acetyltransferase and Pseudomonas aeruginosa chloramphenicol acetyltransferase. They contain repeated copies of a six-residue hexapeptide repeat sequence motif (X-[STAV]-X-[LIV]-[GAED]-X) and adopt a left-handed parallel beta helix (LbH) structure. The active enzyme is a trimer with CoA and substrate binding sites at the interface of two separate LbH subunits. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients.


Pssm-ID: 100040 [Multi-domain]  Cd Length: 145  Bit Score: 76.04  E-value: 1.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 278 IVIGETAVVGNNVSILHNVTLGGTGKQCGDR---HP-----------------------KIGDGVLIGAGTCILGNITIG 331
Cdd:cd03349    16 DVGGDKLSIGKFCSIAPGVKIGLGGNHPTDWvstYPfyifggeweddakfddwpskgdvIIGNDVWIGHGATILPGVTIG 95

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2501001744 332 EGAKIGAGSVVLKDVPPRTTAVGNPARLLGGKDNPKTHDKI 372
Cdd:cd03349    96 DGAVIAAGAVVTKDVPPYAIVGGNPAKVIRYRFDEETIERL 136
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 264-343 1.60e-16

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.


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 73.82  E-value: 1.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 264 AKIGTGILLDHATaiVIGETAVVGNNVSILHNVTLGGTGKQCGDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVL 343
Cdd:cd00208     1 VFIGEGVKIHPKA--VIRGPVVIGDNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 274-360 4.42e-15

Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 72.37  E-value: 4.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 274 HATAiviGETAVVGNNVSILHNVTLGGtgkqCgdrhpKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVL--KDVPPRTT 351
Cdd:COG0663    65 HVDP---GYPLTIGDDVTIGHGAILHG----C-----TIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTegKVVPPGSL 132


                  ....*....
gi 2501001744 352 AVGNPARLL 360
Cdd:COG0663   133 VVGSPAKVV 141
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 274-360 5.45e-14

Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 68.98  E-value: 5.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 274 HATAiviGETAVVGNNVSILHNVTLGGtgkqCgdrhpKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVL--KDVPPRTT 351
Cdd:cd04645    54 HVDP---GYPTIIGDNVTVGHGAVLHG----C-----TIGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPpgKVIPPGSL 121


                  ....*....
gi 2501001744 352 AVGNPARLL 360
Cdd:cd04645   122 VAGSPAKVV 130
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 181-346 5.52e-14

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 72.36  E-value: 5.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 181 DLFSGVLQGNPDI-VESV-KLDllavkERDPACISYVHCFLHFKGFLACQAhR--IAHELWTQDRKILALLIQNRVSEAF 256
Cdd:COG1044     9 ELLGGELVGDGDLeITGVaPLE-----EAGPGDLSFLANPKYAKQLATTKA-SavIVPPDFAAALPGLALIVVDNPYLAF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 257 AV---DFHPGAKIGTGIlldHATAiVIGETAVVGNNVSILHNVTLGgtgkqcgdRHPKIGDGVLIGAGTCILGNITIGEG 333
Cdd:COG1044    83 AKllqLFYPPPAPAPGI---HPSA-VIDPSAKIGEGVSIGPFAVIG--------AGVVIGDGVVIGPGVVIGDGVVIGDD 150

                         170
                  ....*....|...
gi 2501001744 334 AKIGAGSVVLKDV 346
Cdd:COG1044   151 CVLHPNVTIYERC 163
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 285-361 8.54e-14

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 70.82  E-value: 8.54e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2501001744 285 VVGNNVSILHNVTLGGtgkqcgdrHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLLG 361
Cdd:COG1043   124 VVGNNVILANNATLAG--------HVEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDVPPYVLAAGNPARLRG 192
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
285-361 1.52e-13

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 70.13  E-value: 1.52e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2501001744 285 VVGNNVSILHNVTLGGtgkqcgdrHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLLG 361
Cdd:PRK05289  125 VVGNHVILANNATLAG--------HVEVGDYAIIGGLTAVHQFVRIGAHAMVGGMSGVSQDVPPYVLAEGNPARLRG 193
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 285-361 2.15e-13

UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this family catalyze the transfer of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to UDP-GlcNAc. It is the first enzyme in the lipid A biosynthetic pathway and is also referred to as LpxA. Lipid A is essential for the growth of Escherichia coli and related bacteria. It is also essential for maintaining the integrity of the outer membrane. UDP-GlcNAc acyltransferase is a homotrimer of left-handed parallel beta helix (LbH) subunits. Each subunit contains an N-terminal LbH region with 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal alpha-helical region.


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 69.38  E-value: 2.15e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2501001744 285 VVGNNVSILHNVTLGGtgkqcgdrHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLLG 361
Cdd:cd03351   122 VIGNNVILANNATLAG--------HVEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARLRG 190
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 266-360 2.39e-13

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 68.49  E-value: 2.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 266 IGTGILLDHATAIVIGETAVVGNNVSILHNVTLGGTGkqcgdrHP----------------KIGDGVLIGAGTCILGNIT 329
Cdd:PRK09527   78 IGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTG------HPvhhelrkngemysfpiTIGNNVWIGSHVVINPGVT 151

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2501001744 330 IGEGAKIGAGSVVLKDVPPRTTAVGNPARLL 360
Cdd:PRK09527  152 IGDNSVIGAGSVVTKDIPPNVVAAGVPCRVI 182
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 266-360 1.65e-12

wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar proteins. WcaF is part of the gene cluster responsible for the biosynthesis of the extracellular polysaccharide colanic acid. The wcaF protein is predicted to contain a left-handed parallel beta-helix (LbH) domain encoded by imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Many are trimeric in their active forms.


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 63.39  E-value: 1.65e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 266 IGTGILLDHATAIVIGETAVVGNNVSIL---HNVTLggtgkqcgDRHP------KIGDGVLIGAGTCILGNITIGEGAKI 336
Cdd:cd05825    12 IGEGVWIYNLAPVTIGSDACISQGAYLCtgsHDYRS--------PAFPlitapiVIGDGAWVAAEAFVGPGVTIGEGAVV 83

                          90       100
                  ....*....|....*....|....
gi 2501001744 337 GAGSVVLKDVPPRTTAVGNPARLL 360
Cdd:cd05825    84 GARSVVVRDLPAWTVYAGNPAVPV 107
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 280-361 3.24e-12

acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes LpxA, an enzyme for the biosynthesis of lipid A, a component oflipopolysaccharide (LPS) in the outer membrane outer leaflet of most Gram-negative bacteria. Some differences are found between lipid A of different species, but this protein represents the first step (from UDP-N-acetyl-D-glucosamine) and appears to be conserved in function. Proteins from this family contain many copies of the bacterial transferase hexapeptide repeat (pfam00132). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 66.13  E-value: 3.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 280 IGETAVVGNNVSILHNVTLGGtgkqcgdrHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARL 359
Cdd:TIGR01852 116 IAHDCVVGNHVILANNATLAG--------HVEVGDYAIIGGLVAVHQFVRIGRYAMIGGLSAVSKDVPPYCLAEGNRARL 187


                  ..
gi 2501001744 360 LG 361
Cdd:TIGR01852 188 RG 189
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 279-358 3.31e-12

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 65.12  E-value: 3.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 279 VIGETAVVGNNVSILHNVTLGgtgkqcgdRH------------PKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDV 346
Cdd:cd03352   116 VIGDGTKIDNLVQIAHNVRIG--------ENcliaaqvgiagsTTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIV 187

                          90
                  ....*....|..
gi 2501001744 347 PPRTTAVGNPAR 358
Cdd:cd03352   188 PPGEYVSGTPAQ 199
PRK10502 PRK10502
putative acyl transferase; Provisional
 263-358 3.63e-12

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 64.59  E-value: 3.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 263 GAKIGTGILLDHATAI------VIGETAVVGNNVSI--LHNVTLGgtgKQC----------GDRHPK------------I 312
Cdd:PRK10502   51 GAKIGKGVVIRPSVRItypwklTIGDYAWIGDDVWLynLGEITIG---AHCvisqksylctGSHDYSdphfdlntapivI 127

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2501001744 313 GDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPAR 358
Cdd:PRK10502  128 GEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAV 173
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 251-346 1.07e-11

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 65.55  E-value: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 251 RVSEAFAVDFHPGAKigTGIlldHATAiVIGETAVVGNNVSILHNVTLGgtgkqcgdRHPKIGDGVLIGAGTCILGNITI 330
Cdd:PRK00892   86 RLAQLFDPPATPSPA--AGI---HPSA-VIDPSAKIGEGVSIGPNAVIG--------AGVVIGDGVVIGAGAVIGDGVKI 151

                          90
                  ....*....|....*.
gi 2501001744 331 GEGAKIGAGSVVLKDV 346
Cdd:PRK00892  152 GADCRLHANVTIYHAV 167
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 279-358 1.32e-11

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 65.04  E-value: 1.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 279 VIGETAVVGNNVSILHNVTLGgtgkqcgdRH------------PKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDV 346
Cdd:COG1044   224 VIGDGTKIDNLVQIAHNVRIG--------EHtaiaaqvgiagsTKIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSI 295

                          90
                  ....*....|..
gi 2501001744 347 PPRTTAVGNPAR 358
Cdd:COG1044   296 PEGGVYSGSPAQ 307
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 311-354 4.30e-10

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 58.59  E-value: 4.30e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2501001744 311 KIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVG 354
Cdd:cd03353   146 VIGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGALAIA 189
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 279-358 4.45e-09

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 57.46  E-value: 4.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 279 VIGETAVVGNNVSILHNVTLGgtgkqcgdRH------------PKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDV 346
Cdd:PRK00892  227 VIGEGVKIDNLVQIAHNVVIG--------RHtaiaaqvgiagsTKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSI 298

                          90
                  ....*....|...
gi 2501001744 347 PPRTTAVGN-PAR 358
Cdd:PRK00892  299 PEPGEYSSGiPAQ 311
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 264-354 6.30e-09

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 57.47  E-value: 6.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 264 AKIGTGILLDHATaiVIGEtAVVGNNVSI-LHNVTLGGTGKQcgdRHPK-IGDGVLIGAGTCILGNITIGEGAKIGAGSV 341
Cdd:PRK14357  342 STIGENTKAQHLT--YLGD-ATVGKNVNIgAGTITCNYDGKK---KNPTfIEDGAFIGSNSSLVAPVRIGKGALIGAGSV 415

                          90
                  ....*....|...
gi 2501001744 342 VLKDVPPRTTAVG 354
Cdd:PRK14357  416 ITEDVPPYSLALG 428
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 263-357 1.97e-08

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP succinyltransferase): THDP N-succinyltransferase catalyzes the conversion of tetrahydrodipicolinate and succinyl-CoA to N-succinyltetrahydrodipicolinate and CoA. It is the committed step in the succinylase pathway by which bacteria synthesize L-lysine and meso-diaminopimelate, a component of peptidoglycan. The enzyme is homotrimeric and each subunit contains an N-terminal region with alpha helices and hairpin loops, as well as a C-terminal region with a left-handed parallel alpha-helix (LbH) structural motif encoded by hexapeptide repeat motifs.


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 52.77  E-value: 1.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 263 GAKIGTGILLD-HATaivIGETAVVGNNVSILHNVTLGGTGKQCGDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSV 341
Cdd:cd03350    31 GAYVDEGTMVDsWAT---VGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVV 107

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2501001744 342 V---------------LKDVPPRTTAV-GNPA 357
Cdd:cd03350   108 LtqstpiydretgeiyYGRVPPGSVVVaGSLP 139
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 311-360 2.32e-08

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 53.73  E-value: 2.32e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2501001744 311 KIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLL 360
Cdd:PRK09677  132 VIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKII 181
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 284-354 2.33e-08

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: 55.42  E-value: 2.33e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2501001744 284 AVVGNNVSIlhnvtlG-GT------GKqcgDRHP-KIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVG 354
Cdd:COG1207   370 AEIGEGVNI------GaGTitcnydGV---NKHRtVIGDGAFIGSNTNLVAPVTIGDGATIGAGSTITKDVPAGALAIA 439
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 312-354 4.75e-08

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 54.73  E-value: 4.75e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2501001744 312 IGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVG 354
Cdd:PRK14356  401 IGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSLAIA 443
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 264-358 4.92e-08

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 54.56  E-value: 4.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 264 AKIGTGILLDHATAI---VIGETAVVGNNvSILhnVTLGGTGKqcgdRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGS 340
Cdd:PRK14352  358 ATIGRGTKVPHLTYVgdaDIGEHSNIGAS-SVF--VNYDGVNK----HRTTIGSHVRTGSDTMFVAPVTVGDGAYTGAGT 430

                          90
                  ....*....|....*....
gi 2501001744 341 VVLKDVPPRTTAV-GNPAR 358
Cdd:PRK14352  431 VIREDVPPGALAVsEGPQR 449
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 312-360 7.13e-08

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 52.12  E-value: 7.13e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2501001744 312 IGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLL 360
Cdd:PRK10092  132 IGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARII 180
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 254-336 1.37e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 52.83  E-value: 1.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 254 EAFAVdFHPGAKIGTGILLdHATAiVIGETAVVGN------NVSILHNVTLG-------GT--GkQCG-------DRHPK 311
Cdd:PRK00892  122 GPNAV-IGAGVVIGDGVVI-GAGA-VIGDGVKIGAdcrlhaNVTIYHAVRIGnrviihsGAviG-SDGfgfandrGGWVK 197

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2501001744 312 --------IGDGVLIGAGTCI----LGNITIGEGAKI 336
Cdd:PRK00892  198 ipqlgrviIGDDVEIGANTTIdrgaLDDTVIGEGVKI 234
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 286-360 2.46e-07

Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in iron acquisition. It binds iron when it is complexed with pyochelin. It adopts the left-handed parallel beta-helix (LbH) structure, and contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Acyltransferase activity has not been observed in this group.


Pssm-ID: 100055 [Multi-domain]  Cd Length: 154  Bit Score: 49.88  E-value: 2.46e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2501001744 286 VGNNVSILHNVTLGGTgkqcgdrhpKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVL--KDVPPRTTAVGNPARLL 360
Cdd:cd04650    64 IGDYVTIGHNAVVHGA---------KVGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTpgKEIPDYSLVLGVPAKVV 131
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 264-342 3.28e-07

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 50.48  E-value: 3.28e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2501001744 264 AKIGTGILLDHATaiVIGETAVVGNNVSILHNVTlggtgkqcgdrhpkIGDGVLIGAGTCILGNITIGEGAKIGAGSVV 342
Cdd:cd03352     2 AKIGENVSIGPNA--VIGEGVVIGDGVVIGPGVV--------------IGDGVVIGDDCVIHPNVTIYEGCIIGDRVII 64
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 263-357 4.18e-07

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 52.06  E-value: 4.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 263 GAKIGTGILLDHATaivIGETAVVgnnvSILHNVTLG-GTGKQCG---DR-----HPKIGDGVLIGAGTCILGNITIGEG 333
Cdd:TIGR02353 597 GVKIGRGVYIDGTD---LTERDLV----TIGDDSTLNeGSVIQTHlfeDRvmksdTVTIGDGATLGPGAIVLYGVVMGEG 669

                          90       100
                  ....*....|....*....|....*.
gi 2501001744 334 AKIGAGSVVLK--DVPPRTTAVGNPA 357
Cdd:TIGR02353 670 SVLGPDSLVMKgeEVPAHTRWRGNPA 695
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 263-354 5.04e-07

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 51.37  E-value: 5.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 263 GAKIGTGILLDHATaiVIGEtAVVGNNVsilhNVTLG-------GTGKQcgdrHPKIGDGVLIGAGTCILGNITIGEGAK 335
Cdd:PRK14354  351 KSTIGEGTKVSHLT--YIGD-AEVGENV----NIGCGtitvnydGKNKF----KTIIGDNAFIGCNSNLVAPVTVGDNAY 419

                          90
                  ....*....|....*....
gi 2501001744 336 IGAGSVVLKDVPPRTTAVG 354
Cdd:PRK14354  420 IAAGSTITKDVPEDALAIA 438
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 312-354 5.88e-07

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 51.02  E-value: 5.88e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2501001744 312 IGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVG 354
Cdd:PRK14353  383 IGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALG 425
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 271-359 9.85e-07

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 48.96  E-value: 9.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 271 LLDHATaIVIGETAVVGNNVSILHNVTLGGtgkqcgdrHPKIGDGVLIGAGtCILGNITIGEGAKIGAGSVVLKDVPPRT 350
Cdd:cd03353     4 LIDPET-TYIDGDVEIGVDVVIDPGVILEG--------KTVIGEDCVIGPN-CVIKDSTIGDGVVIKASSVIEGAVIGNG 73


                  ....*....
gi 2501001744 351 TAVGNPARL 359
Cdd:cd03353    74 ATVGPFAHL 82
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
309-338 1.55e-06

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 44.25  E-value: 1.55e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 2501001744 309 HPKIGDGVLIGAGTCILGNITIGEGAKIGA 338
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
lipid_A_lpxD TIGR01853
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD; This model describes LpxD, an ...
 262-336 2.35e-06

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD; This model describes LpxD, an enzyme for the biosynthesis of lipid A, a component oflipopolysaccharide (LPS) in the outer membrane outer leaflet of most Gram-negative bacteria. Some differences are found between lipid A of different species. This protein represents the third step from UDP-N-acetyl-D-glucosamine. The group added at this step generally is 14:0(3-OH) (myristate) but may vary; in Aquifex it appears to be 16:0(3-OH) (palmitate). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 273834 [Multi-domain]  Cd Length: 324  Bit Score: 48.83  E-value: 2.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 262 PGAKIGTGILLDHATAI----VIGETAVVGNNVSILHNVTLGGTG----KQCGDRHPKI--------GDGVLIGAGTCI- 324
Cdd:TIGR01853 132 PGVVIGDDVVIGDGSRIhpnvVIYERVQLGKNVIIHSGAVIGSDGfgyaHTANGGHVKIpqigrviiEDDVEIGANTTId 211

                          90
                  ....*....|....*
gi 2501001744 325 ---LGNITIGEGAKI 336
Cdd:TIGR01853 212 rgaFDDTIIGEGTKI 226
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 263-365 2.51e-06

Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; Tetrahydrodipicolinate N-succinyltransferase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 441774 [Multi-domain]  Cd Length: 268  Bit Score: 48.57  E-value: 2.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 263 GAKIGTGILLD-HATaivIGETAVVGNNVSILHNVTLGGT----GKQcgdrhP-KIGDGVLIGAGTCILGNITIGEGAKI 336
Cdd:COG2171   126 GAYVDEGTMVDtWAT---VGSCAQIGKNVHLSGGAGIGGVleplQAA-----PvIIEDNCFIGARSGVVEGVIVGEGAVL 197

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2501001744 337 GAGsVVL----------------KDVPPRTTAVgnpARLLGGKDN 365
Cdd:COG2171   198 GAG-VYLtastkiydrvtgevyyGRVPAGSVVV---PGSLPGKDG 238
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 283-346 2.76e-06

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 47.79  E-value: 2.76e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2501001744 283 TAVVGNNVSILHNVTLGgtgkqcgdRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDV 346
Cdd:cd03352     1 SAKIGENVSIGPNAVIG--------EGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGC 56
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 263-361 3.12e-06

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 49.36  E-value: 3.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 263 GAKIGTGILLdHATAIVIGETAVVGNNVSILHNVTLGGTGKQcGDR----HPKIGDGVLIGAGTCILGNITIGEGAKIGA 338
Cdd:TIGR02353 112 GAKIGKGVDI-GSLPPVCTDLLTIGAGTIVRKEVMLLGYRAE-RGRlhtgPVTLGRDAFIGTRSTLDIDTSIGDGAQLGH 189

                          90       100
                  ....*....|....*....|....*
gi 2501001744 339 GSVVLKD--VPPRTTAVGNPARLLG 361
Cdd:TIGR02353 190 GSALQGGqsIPDGERWHGSPAQKTG 214
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 261-342 3.22e-06

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 48.09  E-value: 3.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 261 HPGAKIGTGIlldhataiVIGETAVVGNNVsilhnvtlggtgkqcgdrhpKIGDGVLIGAGTCILGNITIGEGAKIGAGS 340
Cdd:COG1043    11 DPGAKLGENV--------EIGPFCVIGPDV--------------------EIGDGTVIGSHVVIEGPTTIGKNNRIFPFA 62


                  ..
gi 2501001744 341 VV 342
Cdd:COG1043    63 SI 64
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
261-342 5.35e-06

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 47.40  E-value: 5.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 261 HPGAKIGTGIlldhataiVIGETAVVGNNVsilhnvtlggtgkqcgdrhpKIGDGVLIGAGTCILGNITIGEGAKIGAGS 340
Cdd:PRK05289   12 EPGAKIGENV--------EIGPFCVIGPNV--------------------VIGDGTVIGSHVVIDGHTTIGKNNRIFPFA 63


                  ..
gi 2501001744 341 VV 342
Cdd:PRK05289   64 SI 65
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 242-342 1.82e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 46.29  E-value: 1.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 242 KILALLIQNRVSEAFAvDFHPGAKIGTGILLDHATAI----VIGETAVVGNNVSILHNVTLGGtGKQCGDR---HP---- 310
Cdd:PRK00892   86 RLAQLFDPPATPSPAA-GIHPSAVIDPSAKIGEGVSIgpnaVIGAGVVIGDGVVIGAGAVIGD-GVKIGADcrlHAnvti 163

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2501001744 311 ----KIGDGVLIGAGTCI-------------------LGNITIGEGAKIGAGSVV 342
Cdd:PRK00892  164 yhavRIGNRVIIHSGAVIgsdgfgfandrggwvkipqLGRVIIGDDVEIGANTTI 218
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 308-354 2.19e-05

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 46.46  E-value: 2.19e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2501001744 308 RHP-KIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVG 354
Cdd:PRK14360  388 KHRtVIGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLAIA 435
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 261-342 2.24e-05

UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this family catalyze the transfer of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to UDP-GlcNAc. It is the first enzyme in the lipid A biosynthetic pathway and is also referred to as LpxA. Lipid A is essential for the growth of Escherichia coli and related bacteria. It is also essential for maintaining the integrity of the outer membrane. UDP-GlcNAc acyltransferase is a homotrimer of left-handed parallel beta helix (LbH) subunits. Each subunit contains an N-terminal LbH region with 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal alpha-helical region.


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 45.50  E-value: 2.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 261 HPGAKIGTGIlldhataiVIGETAVVGNNVsilhnvtlggtgkqcgdrhpKIGDGVLIGAGTCILGNITIGEGAKIGAGS 340
Cdd:cd03351     9 DPGAKIGENV--------EIGPFCVIGPNV--------------------EIGDGTVIGSHVVIDGPTTIGKNNRIFPFA 60


                  ..
gi 2501001744 341 VV 342
Cdd:cd03351    61 SI 62
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 271-342 3.45e-05

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: 45.79  E-value: 3.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 271 LLDHATaIVIGETAVVGNNVSILHNVTL-GGTgkqcgdrhpKIGDGVLIGAGtCILGNITIG----------EGAKIGAG 339
Cdd:COG1207   255 IIDPAT-TYIDGDVEIGRDVVIDPNVILeGKT---------VIGEGVVIGPN-CTLKDSTIGdgvvikysviEDAVVGAG 323


                  ...
gi 2501001744 340 SVV 342
Cdd:COG1207   324 ATV 326
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 261-365 7.38e-05

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 43.86  E-value: 7.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 261 HPGAKIGTGIlldhataiVIGETAVVGNNVSIlhnvtlggtgkqcgdrhpkiGDGVLIGAGTCILGNITIGEGAKIGAGS 340
Cdd:PRK12461    9 DPSAKLGSGV--------EIGPFAVIGANVEI--------------------GDGTWIGPHAVILGPTRIGKNNKIHQGA 60

                          90       100
                  ....*....|....*....|....*
gi 2501001744 341 VVlKDVPPRTTAVGNPARLLGGKDN 365
Cdd:PRK12461   61 VV-GDEPQDFTYKGEESRLEIGDRN 84
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 280-361 7.73e-05

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 43.86  E-value: 7.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 280 IGETAVVGNNVSILHNVTLGGtgkqcgdrHPKIGDGVLIGaGTCILGNIT-IGEGAKIGAGSVVLKDVPPRTTAVGNPAR 358
Cdd:PRK12461  116 VAHDCQIGNNVILVNGALLAG--------HVTVGDRAIIS-GNCLVHQFCrIGALAMMAGGSRISKDVPPYCMMAGHPTN 186


                  ...
gi 2501001744 359 LLG 361
Cdd:PRK12461  187 VHG 189
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 284-347 7.81e-05

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.


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 40.70  E-value: 7.81e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2501001744 284 AVVGNNVSILHNVTLGGTGKQCGDRHpkIGDGVLIGAGTCILGN--ITIGEGAKIGAGSVVLKDVP 347
Cdd:cd00208     1 VFIGEGVKIHPKAVIRGPVVIGDNVN--IGPGAVIGAATGPNEKnpTIIGDNVEIGANAVIHGGVK 64
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 264-346 8.95e-05

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 44.25  E-value: 8.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 264 AKIGTGILLDHATaiVIGEtAVVGNNVSIlhnvtlgGTGK-QCG-DRHPK----IGDGVLIGAGTCILGNITIGEGAKIG 337
Cdd:PRK09451  353 ARLGKGSKAGHLT--YLGD-AEIGDNVNI-------GAGTiTCNyDGANKfktiIGDDVFVGSDTQLVAPVTVGKGATIG 422


                  ....*....
gi 2501001744 338 AGSVVLKDV 346
Cdd:PRK09451  423 AGTTVTRDV 431
PLN02296 PLN02296
carbonate dehydratase
 284-360 9.78e-05

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 43.58  E-value: 9.78e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2501001744 284 AVVGNNVSILHNVTLGGtgkqCgdrhpKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKD--VPPRTTAVGNPARLL 360
Cdd:PLN02296  120 TIIGDNVTIGHSAVLHG----C-----TVEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNtrIPSGEVWAGNPAKFL 189
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 280-360 1.68e-04

paaY-like: This group is composed by uncharacterized proteins with similarity to the protein product of the E. coli paaY gene, which is part of the paa gene cluster responsible for phenylacetic acid degradation. Proteins in this group are expected to adopt the left-handed parallel beta-helix (LbH) structure. They contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Similarity to gamma carbonic anhydrase and Ferripyochelin Binding Protein (FBP) may suggest metal binding capacity.


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 41.58  E-value: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 280 IGETAVVGNNVSILHNVTLGGTgkqcgdrhpKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLK--DVPPRTTAVGNPA 357
Cdd:cd04745    58 PGQDTVLEENGHIGHGAILHGC---------TIGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAgtVIPPRSLIAGSPA 128


                  ...
gi 2501001744 358 RLL 360
Cdd:cd04745   129 KVI 131
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 312-353 1.93e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 43.19  E-value: 1.93e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2501001744 312 IGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAV 353
Cdd:PRK14355  400 IEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPPDSLAI 441
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 263-343 3.74e-04

2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 41.72  E-value: 3.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 263 GAKIGTGILLD-HATaivIGETAVVGNNVSILHNVTLGGTGKQCGDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGsV 341
Cdd:PRK11830  132 GAYVDEGTMVDtWAT---VGSCAQIGKNVHLSGGVGIGGVLEPLQANPVIIEDNCFIGARSEVVEGVIVEEGSVLGMG-V 207


                  ..
gi 2501001744 342 VL 343
Cdd:PRK11830  208 FL 209
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
311-344 3.96e-04

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 37.42  E-value: 3.96e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2501001744 311 KIGDGVLIGAGTCIlgNITIGEGAKIGAGSVVLK 344
Cdd:pfam14602   2 IIGDNCLIGANSGI--GVSLGDNCVVGAGVVITA 33
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 225-372 1.91e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 40.11  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 225 LACQAHRIAHE---LWTQDRKILA---LLIQNRVSEAFAVDfhpgakiGTGILLDHATAIVIGetAVVGNNVSILHNVTL 298
Cdd:PRK14355  213 LRCLAFPVADPdeiMGVNDRAQLAeaaRVLRRRINRELMLA-------GVTLIDPETTYIDRG--VVIGRDTTIYPGVCI 283

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2501001744 299 GGTgkqcgdrhPKIGDGVLIGAGTCILGnITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLLGGKDnPKTHDKI 372
Cdd:PRK14355  284 SGD--------TRIGEGCTIEQGVVIKG-CRIGDDVTVKAGSVLEDSVVGDDVAIGPMAHLRPGTE-LSAHVKI 347
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 311-346 2.04e-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: 40.01  E-value: 2.04e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2501001744 311 KIGDGVLIGAGTCILGNITIGEGAKIGAGSvVLKDV 346
Cdd:COG1207   268 EIGRDVVIDPNVILEGKTVIGEGVVIGPNC-TLKDS 302
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 262-342 2.76e-03

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


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 36.40  E-value: 2.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 262 PGAKIGTGILLDHAtaiVIGETAVVGNNVSIlhnvtlggtgkqcgdRHPKIGDGVLIGAGT----CILGN-ITIGEGAKI 336
Cdd:cd05787     4 RGTSIGEGTTIKNS---VIGRNCKIGKNVVI---------------DNSYIWDDVTIEDGCtihhSIVADgAVIGKGCTI 65


                  ....*.
gi 2501001744 337 GAGSVV 342
Cdd:cd05787    66 PPGSLI 71
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 279-351 3.34e-03

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


Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 36.02  E-value: 3.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 279 VIGETAVVGNNVSILHNVTlggtGKQCgdrhpKIG-----------DGVLIGAGtCILGNITIGEGAKIGAGSvVLKD-- 345
Cdd:cd04652     1 LVGENTQVGEKTSIKRSVI----GANC-----KIGkrvkitncvimDNVTIEDG-CTLENCIIGNGAVIGEKC-KLKDcl 69

                          90
                  ....*....|..
gi 2501001744 346 ------VPPRTT 351
Cdd:cd04652    70 vgsgyrVEAGTE 81
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 262-337 4.91e-03

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 38.76  E-value: 4.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2501001744 262 PGAKIGTGILLdhataivigETAVVGNNVSILHNVTlggtgkqcgdRHPKIGDGVLIGAGTCILGNITIGEGAKIG 337
Cdd:PRK14360  285 SGCRIGPGSLI---------ENSQIGENVTVLYSVV----------SDSQIGDGVKIGPYAHLRPEAQIGSNCRIG 341
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 287-383 5.08e-03

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 38.85  E-value: 5.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 287 GNNVSILHNVTLGGtgkqcgdrHPKIGDGVLIGAGtCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLLggkdnp 366
Cdd:PRK09451  269 GRDVEIDTNVIIEG--------NVTLGNRVKIGAG-CVLKNCVIGDDCEISPYSVVEDANLGAACTIGPFARLR------ 333

                          90
                  ....*....|....*..
gi 2501001744 367 kthdkiPGLTMDQTSHI 383
Cdd:PRK09451  334 ------PGAELAEGAHV 344
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 262-346 6.51e-03

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


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 35.30  E-value: 6.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 262 PGAKIGTGILLDHAtaiVIGETAVVGNNVSILHNVTLGGTgkqcgdrhpKIGDGVLIgAGTCILGNITIGEGAKIGAGSV 341
Cdd:cd03356     4 ESTVIGENAIIKNS---VIGDNVRIGDGVTITNSILMDNV---------TIGANSVI-VDSIIGDNAVIGENVRVVNLCI 70


                  ....*
gi 2501001744 342 VLKDV 346
Cdd:cd03356    71 IGDDV 75
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 278-358 6.81e-03

Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p25 is part of the pointed-end subcomplex in dynactin that also includes p26, p27, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100049 [Multi-domain]  Cd Length: 161  Bit Score: 37.19  E-value: 6.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2501001744 278 IVIGETAVVGNNVSI---LHNVTLGG---TGKQCGDRHP-------------KIGDGVLIGAGT---------------- 322
Cdd:cd03359    22 IVLNGKTIIQSDVIIrgdLATVSIGRyciLSEGCVIRPPfkkfskgvaffplHIGDYVFIGENCvvnaaqigsyvhigkn 101

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2501001744 323 CILGNIT-IGEGAKIGAGSVVLKD--VPPRTTAVGNPAR 358
Cdd:cd03359   102 CVIGRRCiIKDCVKILDGTVVPPDtvIPPYSVVSGRPAR 140
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
278-320 6.99e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.85  E-value: 6.99e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2501001744 278 IVIGETAVVGNNVSILHNVtlggtgkqcgdrhpKIGDGVLIGA 320
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGV--------------IIGDNVIIGA 30
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH