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Conserved domains on  [gi|1901122555|emb|CAD5330044|]
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unnamed protein product [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02739 PLN02739
serine acetyltransferase
 1-355 0e+00

serine acetyltransferase


:

Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 774.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555   1 MACINGENRDFSSSSSLSSLPMIVSRNFSARDDGETGDEFPFERIFPVYARGTLNPVADPVLLDFTNSSYDPIWDSIREE 80
Cdd:PLN02739    1 MACINGENCDFSCSSSLSSLPMIVSRNFSARDDGETGDEFPFERGFPVYARGTLNPVADPVLLDFTNSRYDPIWDSIREE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555  81 AKLEAEEEPVLSSFLYASILSHDCLEQALSFVLANRLQNPTLLATQLMDIFCNVMVHDRGIQSSIRLDVQAFKDRDPACL 160
Cdd:PLN02739   81 AKLEAEEEPVLSSFLYASILSHDCLEQALSFVLANRLQNPTLLATQLMDIFCNVMVHDRGIQSSIRLDVQAFKDRDPACL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 161 SYSSAILHLKGYLALQAYRVAHKLWKQGRKLLALALQSRVSEVFGIDIHPAARIGKGILLDHGTGVVIGETAVIGDRVSI 240
Cdd:PLN02739  161 SYSSAILHLKGYLALQAYRVAHKLWKQGRKLLALALQSRVSEVFGIDIHPAARIGKGILLDHGTGVVIGETAVIGDRVSI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 241 LHGVTLGGTGKETGDRHPNIGDGALLGACVTILGNIKIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFVDEQDPSMTM 320
Cdd:PLN02739  241 LHGVTLGGTGKETGDRHPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFVDEQDPSLTM 320

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1901122555 321 EHDATREFFQNVAVAYRETIPNGSSVSGSCRERRH 355
Cdd:PLN02739  321 EYDATREFFQNVAVAYRETIPNGSSVSGSCREKRH 355
 
Name Accession Description Interval E-value
PLN02739 PLN02739
serine acetyltransferase
 1-355 0e+00

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 774.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555   1 MACINGENRDFSSSSSLSSLPMIVSRNFSARDDGETGDEFPFERIFPVYARGTLNPVADPVLLDFTNSSYDPIWDSIREE 80
Cdd:PLN02739    1 MACINGENCDFSCSSSLSSLPMIVSRNFSARDDGETGDEFPFERGFPVYARGTLNPVADPVLLDFTNSRYDPIWDSIREE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555  81 AKLEAEEEPVLSSFLYASILSHDCLEQALSFVLANRLQNPTLLATQLMDIFCNVMVHDRGIQSSIRLDVQAFKDRDPACL 160
Cdd:PLN02739   81 AKLEAEEEPVLSSFLYASILSHDCLEQALSFVLANRLQNPTLLATQLMDIFCNVMVHDRGIQSSIRLDVQAFKDRDPACL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 161 SYSSAILHLKGYLALQAYRVAHKLWKQGRKLLALALQSRVSEVFGIDIHPAARIGKGILLDHGTGVVIGETAVIGDRVSI 240
Cdd:PLN02739  161 SYSSAILHLKGYLALQAYRVAHKLWKQGRKLLALALQSRVSEVFGIDIHPAARIGKGILLDHGTGVVIGETAVIGDRVSI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 241 LHGVTLGGTGKETGDRHPNIGDGALLGACVTILGNIKIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFVDEQDPSMTM 320
Cdd:PLN02739  241 LHGVTLGGTGKETGDRHPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFVDEQDPSLTM 320

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1901122555 321 EHDATREFFQNVAVAYRETIPNGSSVSGSCRERRH 355
Cdd:PLN02739  321 EYDATREFFQNVAVAYRETIPNGSSVSGSCREKRH 355
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 141-309 1.46e-91

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: 271.19  E-value: 1.46e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 141 IQSSIRLDVQAFKDRDPACLSYSSAILHLKGYLALQAYRVAHKLWKQGRKLLALALQSRVSEVFGIDIHPAARIGKGILL 220
Cdd:COG1045     1 MLKALREDIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHPGATIGRGFFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 221 DHGTGVVIGETAVIGDRVSILHGVTLGGTGKETGDRHPNIGDGALLGACVTILGNIKIGAGAMVAAGSLVLKDVPSHSMV 300
Cdd:COG1045    81 DHGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTV 160


                  ....*....
gi 1901122555 301 AGNPAKLIG 309
Cdd:COG1045   161 VGVPARIVK 169
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 145-306 9.17e-81

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


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 243.35  E-value: 9.17e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 145 IRLDVQAFKDRDPACLSYSSAILHLKGYLALQAYRVAHKLWKQGRKLLALALQSRVSEVFGIDIHPAARIGKGILLDHGT 224
Cdd:TIGR01172   1 IREDIRAVRERDPAARSYLEVLLYYPGFHALWAYRFAHFLWKRGFKFLARLLSNFIRVLTGVDIHPGARIGRGVFIDHGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 225 GVVIGETAVIGDRVSILHGVTLGGTGKETGDRHPNIGDGALLGACVTILGNIKIGAGAMVAAGSLVLKDVPSHSMVAGNP 304
Cdd:TIGR01172  81 GVVIGETAVIGDDVTIYHGVTLGGTGKEKGKRHPTIGEGVMIGAGAKVLGNIEVGENAKIGANSVVLKDVPPGATVVGVP 160


                  ..
gi 1901122555 305 AK 306
Cdd:TIGR01172 161 AR 162
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 204-304 3.78e-51

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: 165.31  E-value: 3.78e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 204 FGIDIHPAARIGKGILLDHGTGVVIGETAVIGDRVSILHGVTLGGTGKETGDRHPNIGDGALLGACVTILGNIKIGAGAM 283
Cdd:cd03354     1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                          90       100
                  ....*....|....*....|.
gi 1901122555 284 VAAGSLVLKDVPSHSMVAGNP 304
Cdd:cd03354    81 IGANAVVTKDVPANSTVVGVP 101
SATase_N pfam06426
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 73-176 1.45e-43

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: 146.07  E-value: 1.45e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555  73 IWDSIREEAKLEAEEEPVLSSFLYASILSHDCLEQALSFVLANRLQNPTLLATQLMDIFCNVMVHDRGIQSSIRLDVQAF 152
Cdd:pfam06426   1 VWARLRAEAEEAAEREPLLASFLYATILSHDSLESALAFRLANKLANSTLPATLLRELFEDALEADPEIVEAARADLQAV 80

                          90       100
                  ....*....|....*....|....
gi 1901122555 153 KDRDPACLSYSSAILHLKGYLALQ 176
Cdd:pfam06426  81 YERDPACDRYLTPLLYFKGFHALQ 104
SATase_N smart00971
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 73-177 8.54e-37

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: 128.43  E-value: 8.54e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555   73 IWDSIREEAKLEAEEEPVLSSFLYASILSHDCLEQALSFVLANRLQNPTLLATQLMDIFCNVMVHDRGIQSSIRLDVQAF 152
Cdd:smart00971   1 VWQRIRAEAREAAEREPILASFLYATILNHDSLEAALAYRLANKLGNADMSADLLRELFEDAYAADPEIVEAAAADIQAV 80

                           90       100
                   ....*....|....*....|....*
gi 1901122555  153 KDRDPACLSYSSAILHLKGYLALQA 177
Cdd:smart00971  81 YDRDPACDRYLTPLLYFKGFHALQA 105
 
Name Accession Description Interval E-value
PLN02739 PLN02739
serine acetyltransferase
 1-355 0e+00

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 774.59  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555   1 MACINGENRDFSSSSSLSSLPMIVSRNFSARDDGETGDEFPFERIFPVYARGTLNPVADPVLLDFTNSSYDPIWDSIREE 80
Cdd:PLN02739    1 MACINGENCDFSCSSSLSSLPMIVSRNFSARDDGETGDEFPFERGFPVYARGTLNPVADPVLLDFTNSRYDPIWDSIREE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555  81 AKLEAEEEPVLSSFLYASILSHDCLEQALSFVLANRLQNPTLLATQLMDIFCNVMVHDRGIQSSIRLDVQAFKDRDPACL 160
Cdd:PLN02739   81 AKLEAEEEPVLSSFLYASILSHDCLEQALSFVLANRLQNPTLLATQLMDIFCNVMVHDRGIQSSIRLDVQAFKDRDPACL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 161 SYSSAILHLKGYLALQAYRVAHKLWKQGRKLLALALQSRVSEVFGIDIHPAARIGKGILLDHGTGVVIGETAVIGDRVSI 240
Cdd:PLN02739  161 SYSSAILHLKGYLALQAYRVAHKLWKQGRKLLALALQSRVSEVFGIDIHPAARIGKGILLDHGTGVVIGETAVIGDRVSI 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 241 LHGVTLGGTGKETGDRHPNIGDGALLGACVTILGNIKIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFVDEQDPSMTM 320
Cdd:PLN02739  241 LHGVTLGGTGKETGDRHPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFVDEQDPSLTM 320

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1901122555 321 EHDATREFFQNVAVAYRETIPNGSSVSGSCRERRH 355
Cdd:PLN02739  321 EYDATREFFQNVAVAYRETIPNGSSVSGSCREKRH 355
PLN02694 PLN02694
serine O-acetyltransferase
 52-322 1.26e-109

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 321.98  E-value: 1.26e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555  52 GTLNPVADPVLLDFTNSSYDP--IWDSIREEAKLEAEEEPVLSSFLYASILSHDCLEQALSFVLANRLQNPTLLATQLMD 129
Cdd:PLN02694    5 GELRHPSPPKTNSATTADEEAawLWTQIKAEARRDAESEPALASYLYSTILSHSSLERSLSFHLGNKLCSSTLLSTLLYD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 130 IFCNVMVHDRGIQSSIRLDVQAFKDRDPACLSYSSAILHLKGYLALQAYRVAHKLWKQGRKLLALALQSRVSEVFGIDIH 209
Cdd:PLN02694   85 LFLNTFSSDPSLRAATVADLRAARVRDPACVSFSHCLLNYKGFLACQAHRVAHKLWTQSRRPLALALHSRISDVFAVDIH 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 210 PAARIGKGILLDHGTGVVIGETAVIGDRVSILHGVTLGGTGKETGDRHPNIGDGALLGACVTILGNIKIGAGAMVAAGSL 289
Cdd:PLN02694  165 PAAKIGKGILFDHATGVVIGETAVIGNNVSILHHVTLGGTGKACGDRHPKIGDGVLIGAGATILGNVKIGEGAKIGAGSV 244

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1901122555 290 VLKDVPSHSMVAGNPAKLIGFVD-----EQDPSMTMEH 322
Cdd:PLN02694  245 VLIDVPPRTTAVGNPARLVGGKEkpakhEECPGESMDH 282
cysE PRK11132
serine acetyltransferase; Provisional
 73-321 9.29e-108

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 316.25  E-value: 9.29e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555  73 IWDSIREEAKLEAEEEPVLSSFLYASILSHDCLEQALSFVLANRLQNPTLLATQLMDIFCNVMVHDRGIQSSIRLDVQAF 152
Cdd:PRK11132    9 VWNNIKAEARALADCEPMLASFYHATLLKHENLGSALSYMLANKLASPIMPAIAIREVVEEAYAADPEMIASAACDIQAV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 153 KDRDPACLSYSSAILHLKGYLALQAYRVAHKLWKQGRKLLALALQSRVSEVFGIDIHPAARIGKGILLDHGTGVVIGETA 232
Cdd:PRK11132   89 RTRDPAVDKYSTPLLYLKGFHALQAYRIGHWLWNQGRRALAIYLQNQISVAFQVDIHPAAKIGRGIMLDHATGIVIGETA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 233 VIGDRVSILHGVTLGGTGKETGDRHPNIGDGALLGACVTILGNIKIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFVD 312
Cdd:PRK11132  169 VIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVGKPE 248


                  ....*....
gi 1901122555 313 EQDPSMTME 321
Cdd:PRK11132  249 SDKPSMDMD 257
PLN02357 PLN02357
serine acetyltransferase
 60-322 3.14e-107

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 318.36  E-value: 3.14e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555  60 PVLLDFtnSSYDPIWDSIREEAKLEAEEEPVLSSFLYASILSHDCLEQALSFVLANRLQNPTLLATQLMDIFCNVMVHDR 139
Cdd:PLN02357   83 PVEDDL--DRDDDVWLKIQEEAKSDVEQEPILSSYYYASILSHRSLESALANHLSVKLSNLNLPSNTLFDLFIGVLEESP 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 140 GIQSSIRLDVQAFKDRDPACLSYSSAILHLKGYLALQAYRVAHKLWKQGRKLLALALQSRVSEVFGIDIHPAARIGKGIL 219
Cdd:PLN02357  161 EIIESVKQDLRAVKERDPACISYVHCFLNFKGFLACQAHRIAHKLWTQGRKILALLIQNRVSEAFAVDIHPGAKIGQGIL 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 220 LDHGTGVVIGETAVIGDRVSILHGVTLGGTGKETGDRHPNIGDGALLGACVTILGNIKIGAGAMVAAGSLVLKDVPSHSM 299
Cdd:PLN02357  241 LDHATGVVIGETAVVGNNVSILHNVTLGGTGKQSGDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTT 320

                         250       260
                  ....*....|....*....|....*...
gi 1901122555 300 VAGNPAKLIGFVD-----EQDPSMTMEH 322
Cdd:PLN02357  321 AVGNPARLIGGKEnpikhDKIPSLTMDQ 348
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 141-309 1.46e-91

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: 271.19  E-value: 1.46e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 141 IQSSIRLDVQAFKDRDPACLSYSSAILHLKGYLALQAYRVAHKLWKQGRKLLALALQSRVSEVFGIDIHPAARIGKGILL 220
Cdd:COG1045     1 MLKALREDIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHPGATIGRGFFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 221 DHGTGVVIGETAVIGDRVSILHGVTLGGTGKETGDRHPNIGDGALLGACVTILGNIKIGAGAMVAAGSLVLKDVPSHSMV 300
Cdd:COG1045    81 DHGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTV 160


                  ....*....
gi 1901122555 301 AGNPAKLIG 309
Cdd:COG1045   161 VGVPARIVK 169
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 145-306 9.17e-81

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


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 243.35  E-value: 9.17e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 145 IRLDVQAFKDRDPACLSYSSAILHLKGYLALQAYRVAHKLWKQGRKLLALALQSRVSEVFGIDIHPAARIGKGILLDHGT 224
Cdd:TIGR01172   1 IREDIRAVRERDPAARSYLEVLLYYPGFHALWAYRFAHFLWKRGFKFLARLLSNFIRVLTGVDIHPGARIGRGVFIDHGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 225 GVVIGETAVIGDRVSILHGVTLGGTGKETGDRHPNIGDGALLGACVTILGNIKIGAGAMVAAGSLVLKDVPSHSMVAGNP 304
Cdd:TIGR01172  81 GVVIGETAVIGDDVTIYHGVTLGGTGKEKGKRHPTIGEGVMIGAGAKVLGNIEVGENAKIGANSVVLKDVPPGATVVGVP 160


                  ..
gi 1901122555 305 AK 306
Cdd:TIGR01172 161 AR 162
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 204-304 3.78e-51

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: 165.31  E-value: 3.78e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 204 FGIDIHPAARIGKGILLDHGTGVVIGETAVIGDRVSILHGVTLGGTGKETGDRHPNIGDGALLGACVTILGNIKIGAGAM 283
Cdd:cd03354     1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                          90       100
                  ....*....|....*....|.
gi 1901122555 284 VAAGSLVLKDVPSHSMVAGNP 304
Cdd:cd03354    81 IGANAVVTKDVPANSTVVGVP 101
SATase_N pfam06426
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 73-176 1.45e-43

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: 146.07  E-value: 1.45e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555  73 IWDSIREEAKLEAEEEPVLSSFLYASILSHDCLEQALSFVLANRLQNPTLLATQLMDIFCNVMVHDRGIQSSIRLDVQAF 152
Cdd:pfam06426   1 VWARLRAEAEEAAEREPLLASFLYATILSHDSLESALAFRLANKLANSTLPATLLRELFEDALEADPEIVEAARADLQAV 80

                          90       100
                  ....*....|....*....|....
gi 1901122555 153 KDRDPACLSYSSAILHLKGYLALQ 176
Cdd:pfam06426  81 YERDPACDRYLTPLLYFKGFHALQ 104
SATase_N smart00971
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 73-177 8.54e-37

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: 128.43  E-value: 8.54e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555   73 IWDSIREEAKLEAEEEPVLSSFLYASILSHDCLEQALSFVLANRLQNPTLLATQLMDIFCNVMVHDRGIQSSIRLDVQAF 152
Cdd:smart00971   1 VWQRIRAEAREAAEREPILASFLYATILNHDSLEAALAYRLANKLGNADMSADLLRELFEDAYAADPEIVEAAAADIQAV 80

                           90       100
                   ....*....|....*....|....*
gi 1901122555  153 KDRDPACLSYSSAILHLKGYLALQA 177
Cdd:smart00971  81 YDRDPACDRYLTPLLYFKGFHALQA 105
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
213-316 1.98e-25

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 99.56  E-value: 1.98e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 213 RIGKGILLDHGTGVVIGETAVIGDRVSILHGVTLGGTGKETGDRHPN--------IGDGALLGACVTILGNIKIGAGAMV 284
Cdd:COG0110    29 TIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPATFplrtgpvtIGDDVWIGAGATILPGVTIGDGAVV 108

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1901122555 285 AAGSLVLKDVPSHSMVAGNPAKLIGFVDEQDP 316
Cdd:COG0110   109 GAGSVVTKDVPPYAIVAGNPARVIRKRDEEER 140
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 205-308 5.66e-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: 92.13  E-value: 5.66e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 205 GIDIHPAARIGKGILLDHGTGVVIGETAVIGDRVSIL---HGVTLGGTGKETGDRHP--NIGDGALLGACVTILGNIKIG 279
Cdd:cd04647     1 NISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYdhnHDIDDPERPIEQGVTSApiVIGDDVWIGANVVILPGVTIG 80

                          90       100
                  ....*....|....*....|....*....
gi 1901122555 280 AGAMVAAGSLVLKDVPSHSMVAGNPAKLI 308
Cdd:cd04647    81 DGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
PRK10191 PRK10191
putative acyl transferase; Provisional
 177-307 2.04e-22

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 91.87  E-value: 2.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 177 AYRVAH--KLWKQGRKL------LALALQSRVSE-VFGIDIHPAARIGKGILLDHGTGVVIGETAVIGDRVSILHGVTLG 247
Cdd:PRK10191    4 AYRVAHfcSVWRKKNVLnnlwaaPLLVLYRIITEcFFGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGVTIG 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 248 GTGKETgDRHPNIGDGALLGACVTILGNIKIGAGAMVAAGSLVLKDVPSHSMVAGNPAKL 307
Cdd:PRK10191   84 NRGADN-MACPHIGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKARV 142
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 205-309 2.99e-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: 90.25  E-value: 2.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 205 GIDIHPAARIGKGILLdhGTGVVIGETAVIGDRVSILHGVTLggtgkeTGDRHPN-------------IGDGALLGACVT 271
Cdd:cd03358    10 NVFIENDVKIGDNVKI--QSNVSIYEGVTIEDDVFIGPNVVF------TNDLYPRskiyrkwelkgttVKRGASIGANAT 81

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1901122555 272 ILGNIKIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIG 309
Cdd:cd03358    82 ILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 144-305 7.33e-21

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: 89.09  E-value: 7.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 144 SIRLDVQAFKDRDPACLSYSSAILHLKGYL-ALQAYRVAHKLW------KQGRKLLALALQSRvSEVFGIDIHPAARIGK 216
Cdd:TIGR03570  20 RSGWEVVGFLDDNPALQGTEVDGLPVLGGDeDLLRYPPDEVDLvvaigdNKLRRRLVEKLKAK-GYRFATLIHPSAIVSP 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 217 GILLDHG----------------------TGVVIGETAVIGDRVSILHGVTLGGtgketgdrHPNIGDGALLGACVTILG 274
Cdd:TIGR03570  99 SASIGEGtvimagavinpdvrigdnviinTGAIVEHDCVIGDFVHIAPGVTLSG--------GVVIGEGVFIGAGATIIQ 170

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1901122555 275 NIKIGAGAMVAAGSLVLKDVPSHSMVAGNPA 305
Cdd:TIGR03570 171 GVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 208-304 8.89e-19

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: 83.30  E-value: 8.89e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 208 IHPAARIGKGILLDhgTGVVIGETAVIGDRVSILHGVTLGGtgketgdrHPNIGDGALLGACVTILGNIKIGAGAMVAAG 287
Cdd:cd03360   111 INPDARIGDNVIIN--TGAVIGHDCVIGDFVHIAPGVVLSG--------GVTIGEGAFIGAGATIIQGVTIGAGAIIGAG 180

                          90
                  ....*....|....*..
gi 1901122555 288 SLVLKDVPSHSMVAGNP 304
Cdd:cd03360   181 AVVTKDVPDGSVVVGNP 197
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 213-322 5.35e-17

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 77.37  E-value: 5.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 213 RIGKG-ILLDhgtGVVI----GETAVIGDRVSILHGVTL-GGTgketgdrhpnIGDGALLGACVTILGNIKIGAGAMVAA 286
Cdd:COG0663    51 RIGEGsNIQD---GVVLhvdpGYPLTIGDDVTIGHGAILhGCT----------IGDNVLIGMGAIVLDGAVIGDGSIVGA 117

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1901122555 287 GSLVL--KDVPSHSMVAGNPAKLIGFVDEQDPSMTMEH 322
Cdd:COG0663   118 GALVTegKVVPPGSLVVGSPAKVVRELTEEEIAFLRES 155
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 204-308 7.87e-17

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: 77.08  E-value: 7.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 204 FGIDIHpaarIGKG-------ILLDHGtGVVIGETAVIGDRVSIL---HGV--TLGGTGKETGdrHP-NIGDGALLGACV 270
Cdd:cd03357    59 YGYNIH----IGDNfyanfncTILDVA-PVTIGDNVLIGPNVQIYtagHPLdpEERNRGLEYA--KPiTIGDNVWIGGGV 131

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1901122555 271 TILGNIKIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLI 308
Cdd:cd03357   132 IILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 226-314 9.27e-17

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: 9.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 226 VVIGETAVIGDRVSILHGVTLGGTG---------------------KETGDRHPN-----IGDGALLGACVTILGNIKIG 279
Cdd:cd03349    16 DVGGDKLSIGKFCSIAPGVKIGLGGnhptdwvstypfyifggewedDAKFDDWPSkgdviIGNDVWIGHGATILPGVTIG 95

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1901122555 280 AGAMVAAGSLVLKDVPSHSMVAGNPAKLIG--FVDEQ 314
Cdd:cd03349    96 DGAVIAAGAVVTKDVPPYAIVGGNPAKVIRyrFDEET 132
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 213-338 9.39e-17

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: 76.30  E-value: 9.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 213 RIGKG--------ILLDHGTGVVIGETAVIGDRVsILHGVTlggtgketgdrhpnIGDGALLGACVTILGNIKIGAGAMV 284
Cdd:cd04645    40 RIGERtniqdgsvLHVDPGYPTIIGDNVTVGHGA-VLHGCT--------------IGDNCLIGMGAIILDGAVIGKGSIV 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1901122555 285 AAGSLVL--KDVPSHSMVAGNPAKLIGFVDEQDpsmtmehdatREFFQNVAVAYRE 338
Cdd:cd04645   105 AAGSLVPpgKVIPPGSLVAGSPAKVVRELTDEE----------IAELRESAEHYVE 150
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 212-291 2.55e-15

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: 69.97  E-value: 2.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 212 ARIGKGILLDHGtgVVIGETAVIGDRVSILHGVTLGGTGKETGDRHPNIGDGALLGACVTILGNIKIGAGAMVAAGSLVL 291
Cdd:cd00208     1 VFIGEGVKIHPK--AVIRGPVVIGDNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 233-309 1.06e-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: 70.15  E-value: 1.06e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1901122555 233 VIGDRVSILHGVTLGGtgketgdrHPNIGDGALLGACVTILGNIKIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIG 309
Cdd:cd03351   122 VIGNNVILANNATLAG--------HVEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARLRG 190
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 233-309 1.38e-13

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: 69.66  E-value: 1.38e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1901122555 233 VIGDRVSILHGVTLGGtgketgdrHPNIGDGALLGACVTILGNIKIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIG 309
Cdd:COG1043   124 VVGNNVILANNATLAG--------HVEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDVPPYVLAAGNPARLRG 192
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
233-309 2.09e-13

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 69.36  E-value: 2.09e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1901122555 233 VIGDRVSILHGVTLGGtgketgdrHPNIGDGALLGACVTILGNIKIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIG 309
Cdd:PRK05289  125 VVGNHVILANNATLAG--------HVEVGDYAIIGGLTAVHQFVRIGAHAMVGGMSGVSQDVPPYVLAEGNPARLRG 193
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 214-308 3.25e-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: 62.24  E-value: 3.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 214 IGKGILLDHGTGVVIGETAVIGDRVSILhgvtlGGTGKETGDRHP------NIGDGALLGACVTILGNIKIGAGAMVAAG 287
Cdd:cd05825    12 IGEGVWIYNLAPVTIGSDACISQGAYLC-----TGSHDYRSPAFPlitapiVIGDGAWVAAEAFVGPGVTIGEGAVVGAR 86

                          90       100
                  ....*....|....*....|.
gi 1901122555 288 SLVLKDVPSHSMVAGNPAKLI 308
Cdd:cd05825    87 SVVVRDLPAWTVYAGNPAVPV 107
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 213-306 1.67e-11

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: 62.81  E-value: 1.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 213 RIGKGILLDHGtgVVIGETAVIGDRVSILHGVTLGGTGKetgdrhpnIGDGALLGACVTILGNIKIGAGAMVAAGSLVLK 292
Cdd:cd03352   116 VIGDGTKIDNL--VQIAHNVRIGENCLIAAQVGIAGSTT--------IGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTS 185

                          90
                  ....*....|....
gi 1901122555 293 DVPSHSMVAGNPAK 306
Cdd:cd03352   186 IVPPGEYVSGTPAQ 199
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 208-288 3.15e-10

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 60.54  E-value: 3.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 208 IHPAARIGKGILLDHGtgVVIGETAVIGDRVSILHGVTLGgtgketgdRHPNIGDGALLGACVTILGNIKIGAGAMVAAG 287
Cdd:PRK00892  109 IDPSAKIGEGVSIGPN--AVIGAGVVIGDGVVIGAGAVIG--------DGVKIGADCRLHANVTIYHAVRIGNRVIIHSG 178


                  .
gi 1901122555 288 S 288
Cdd:PRK00892  179 A 179
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 228-309 4.06e-10

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: 59.58  E-value: 4.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 228 IGETAVIGDRVSILHGVTLGGtgketgdrHPNIGDGALLGACVTILGNIKIGAGAMVAAGSLVLKDVPSHSMVAGNPAKL 307
Cdd:TIGR01852 116 IAHDCVVGNHVILANNATLAG--------HVEVGDYAIIGGLVAVHQFVRIGRYAMIGGLSAVSKDVPPYCLAEGNRARL 187


                  ..
gi 1901122555 308 IG 309
Cdd:TIGR01852 188 RG 189
PRK10502 PRK10502
putative acyl transferase; Provisional
 212-306 1.14e-09

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 56.88  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 212 ARIGKGILLDHGTGV------VIGETAVIGDRVSI--LHGVTLGG-----------TG-----KETGD---RHPNIGDGA 264
Cdd:PRK10502   52 AKIGKGVVIRPSVRItypwklTIGDYAWIGDDVWLynLGEITIGAhcvisqksylcTGshdysDPHFDlntAPIVIGEGC 131

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1901122555 265 LLGACVTILGNIKIGAGAMVAAGSLVLKDVPSHSMVAGNPAK 306
Cdd:PRK10502  132 WLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAV 173
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 213-306 1.96e-09

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: 58.11  E-value: 1.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 213 RIGKGILLD------HGtgVVIGE-TAVIGdrvsilhGVTLGGTGKetgdrhpnIGDGALLGACVTILGNIKIGAGAMVA 285
Cdd:COG1044   224 VIGDGTKIDnlvqiaHN--VRIGEhTAIAA-------QVGIAGSTK--------IGDNVVIGGQVGIAGHLTIGDGVIIG 286

                          90       100
                  ....*....|....*....|.
gi 1901122555 286 AGSLVLKDVPSHSMVAGNPAK 306
Cdd:COG1044   287 AQSGVTKSIPEGGVYSGSPAQ 307
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 192-288 6.06e-09

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: 56.56  E-value: 6.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 192 LALAlqsRVSEVF--------GID----IHPAARIGKGILLdhGTGVVIGETAVIGDRVSILHGVTLGgtgketgdrhPN 259
Cdd:COG1044    80 LAFA---KLLQLFypppapapGIHpsavIDPSAKIGEGVSI--GPFAVIGAGVVIGDGVVIGPGVVIG----------DG 144

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1901122555 260 --IGDGALLGACVTILGNIKIGAGAMVAAGS 288
Cdd:COG1044   145 vvIGDDCVLHPNVTIYERCVIGDRVIIHSGA 175
PLN02296 PLN02296
carbonate dehydratase
 232-308 7.65e-09

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 55.90  E-value: 7.65e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1901122555 232 AVIGDRVSILHGVTLGGTGKEtgdrhpnigDGALLGACVTILGNIKIGAGAMVAAGSLVLKD--VPSHSMVAGNPAKLI 308
Cdd:PLN02296  120 TIIGDNVTIGHSAVLHGCTVE---------DEAFVGMGATLLDGVVVEKHAMVAAGALVRQNtrIPSGEVWAGNPAKFL 189
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 200-315 1.35e-08

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 54.24  E-value: 1.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 200 VSEVFGIDIHpaarIGKGILLDHGTGVVIGETAVIGDRVSILHGVTLGGTG-------KETGDRHP---NIGDGALLGAC 269
Cdd:PRK09527   68 VYFSYGSNIH----IGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGhpvhhelRKNGEMYSfpiTIGNNVWIGSH 143

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1901122555 270 VTILGNIKIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFVDEQD 315
Cdd:PRK09527  144 VVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIREINDRD 189
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 260-314 1.89e-08

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 53.73  E-value: 1.89e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1901122555 260 IGDGALLGACVTILGNIKIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFVDEQ 314
Cdd:PRK09677  133 IGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKKYNHE 187
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 211-309 1.11e-07

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 52.33  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 211 AARIGKG-ILLDHgtgVVIGETAVIGDRVSILHGVTLGGtgketgdrHPNIGDGALLGACVTILGNIKIGAGAMVAAGSL 289
Cdd:PRK12461  101 VTRIGNDnLLMAY---SHVAHDCQIGNNVILVNGALLAG--------HVTVGDRAIISGNCLVHQFCRIGALAMMAGGSR 169

                          90       100
                  ....*....|....*....|
gi 1901122555 290 VLKDVPSHSMVAGNPAKLIG 309
Cdd:PRK12461  170 ISKDVPPYCMMAGHPTNVHG 189
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 212-312 1.33e-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: 50.13  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 212 ARIGKGILLdHGTGVVIGETAVIGDRVSILHGVTLGGTGKETGDRHPN---IGDGALLGACVTILGNIKIGAGAMVAAGS 288
Cdd:TIGR02353 113 AKIGKGVDI-GSLPPVCTDLLTIGAGTIVRKEVMLLGYRAERGRLHTGpvtLGRDAFIGTRSTLDIDTSIGDGAQLGHGS 191

                          90       100
                  ....*....|....*....|....*.
gi 1901122555 289 LVLKD--VPSHSMVAGNPAKLIGFVD 312
Cdd:TIGR02353 192 ALQGGqsIPDGERWHGSPAQKTGADY 217
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 214-302 1.55e-06

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 49.76  E-value: 1.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 214 IGKGILLDHGTgvVIGEtAVIGDRVSILHG-VTLGGTGKEtgdRHPN-IGDGALLGACVTILGNIKIGAGAMVAAGSLVL 291
Cdd:PRK14357  344 IGENTKAQHLT--YLGD-ATVGKNVNIGAGtITCNYDGKK---KNPTfIEDGAFIGSNSSLVAPVRIGKGALIGAGSVIT 417

                          90
                  ....*....|.
gi 1901122555 292 KDVPSHSMVAG 302
Cdd:PRK14357  418 EDVPPYSLALG 428
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 249-308 1.83e-06

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 47.89  E-value: 1.83e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 249 TGKETGdRHPNIGDGALLGACVTILGNIKIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLI 308
Cdd:PRK10092  122 SGAELG-KPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARII 180
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 260-300 3.08e-06

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: 47.03  E-value: 3.08e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1901122555 260 IGDGALLGACVTILGNIKIGAGAMVAAGSLVLKDVPSHSMV 300
Cdd:cd03353   147 IGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGALA 187
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 221-322 3.96e-06

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: 46.41  E-value: 3.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 221 DHGTGVVIGETAVIGDRvSILHGVTLGGtgketgdrHPNIGDGALLGACVTILGNIKIGAGAMVAAGslvlKDVPSHSMV 300
Cdd:cd04650    57 DHGYPTEIGDYVTIGHN-AVVHGAKVGN--------YVIVGMGAILLNGAKIGDHVIIGAGAVVTPG----KEIPDYSLV 123

                          90       100
                  ....*....|....*....|..
gi 1901122555 301 AGNPAKLIGFVDEQDPSMTMEH 322
Cdd:cd04650   124 LGVPAKVVRKLTEEEIEWIKKN 145
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 207-299 4.30e-06

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 48.29  E-value: 4.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 207 DIHPAARIG-----KGILLDHGTGV----VIGEtAVIGDRVSILHG-VTLGGTGKETgdRHPNIGDGALLGACVTILGNI 276
Cdd:PRK14354  336 VIGEEVKIGnfveiKKSTIGEGTKVshltYIGD-AEVGENVNIGCGtITVNYDGKNK--FKTIIGDNAFIGCNSNLVAPV 412

                          90       100
                  ....*....|....*....|...
gi 1901122555 277 KIGAGAMVAAGSLVLKDVPSHSM 299
Cdd:PRK14354  413 TVGDNAYIAAGSTITKDVPEDAL 435
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 213-306 9.25e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 47.06  E-value: 9.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 213 RIGKGILLDH----GTGVVIGE-TAVIGdrvsilhGVTLGGTGKetgdrhpnIGDGALLGACVTILGNIKIGAGAMVAAG 287
Cdd:PRK00892  227 VIGEGVKIDNlvqiAHNVVIGRhTAIAA-------QVGIAGSTK--------IGRYCMIGGQVGIAGHLEIGDGVTITAM 291

                          90       100
                  ....*....|....*....|
gi 1901122555 288 SLVLKDVPSH-SMVAGNPAK 306
Cdd:PRK00892  292 SGVTKSIPEPgEYSSGIPAQ 311
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 212-305 1.39e-05

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: 47.05  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 212 ARIGKGILLDhgtGVVIGETavigDRVSILHGVTLG-GTGKETG---DR-----HPNIGDGALLGACVTILGNIKIGAGA 282
Cdd:TIGR02353 598 VKIGRGVYID---GTDLTER----DLVTIGDDSTLNeGSVIQTHlfeDRvmksdTVTIGDGATLGPGAIVLYGVVMGEGS 670

                          90       100
                  ....*....|....*....|....*
gi 1901122555 283 MVAAGSLVLK--DVPSHSMVAGNPA 305
Cdd:TIGR02353 671 VLGPDSLVMKgeEVPAHTRWRGNPA 695
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 212-299 1.83e-05

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 46.26  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 212 ARIGKGILLDHGTgvVIGEtAVIGDRVSILHG-VTLGGTGKETgdRHPNIGDGALLGACVTILGNIKIGAGAMVAAGSLV 290
Cdd:PRK14356  357 AVLGKGAKANHLT--YLGD-AEIGAGANIGAGtITCNYDGVNK--HRTVIGEGAFIGSNTALVAPVTIGDGALVGAGSVI 431


                  ....*....
gi 1901122555 291 LKDVPSHSM 299
Cdd:PRK14356  432 TKDVPDGSL 440
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 211-302 2.52e-05

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 46.01  E-value: 2.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 211 AARIGKGILLDHGTgvVIGEtAVIGDRVSIlhgvtlgGTGKET------GDRHPNIGDGALLGACVTILGNIKIGAGAMV 284
Cdd:PRK14353  338 NAKLGEGAKVNHLT--YIGD-ATIGAGANI-------GAGTITcnydgfNKHRTEIGAGAFIGSNSALVAPVTIGDGAYI 407

                          90
                  ....*....|....*...
gi 1901122555 285 AAGSLVLKDVPSHSMVAG 302
Cdd:PRK14353  408 ASGSVITEDVPDDALALG 425
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 207-294 4.22e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 44.74  E-value: 4.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 207 DIHPAArigkgilldhgtgvVIGETAVIGDRVSILHGVTLGgtgketgdrhPN--IGDGALLGACVTILGNIKIGAGAMV 284
Cdd:PRK00892  102 GIHPSA--------------VIDPSAKIGEGVSIGPNAVIG----------AGvvIGDGVVIGAGAVIGDGVKIGADCRL 157

                          90
                  ....*....|
gi 1901122555 285 AAGSLVLKDV 294
Cdd:PRK00892  158 HANVTIYHAV 167
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 222-315 8.63e-05

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: 42.36  E-value: 8.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 222 HGTgvvIGETAVIGDRVSILHGVTLGGTgketgdrhpNIGDGALLGACVTILGNIKIGAGAMVAAGSLVLK--DVPSHSM 299
Cdd:cd04745    55 HGF---PGQDTVLEENGHIGHGAILHGC---------TIGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAgtVIPPRSL 122

                          90
                  ....*....|....*.
gi 1901122555 300 VAGNPAKLIGFVDEQD 315
Cdd:cd04745   123 IAGSPAKVIRELSDEE 138
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 212-295 1.05e-04

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: 41.60  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 212 ARIGKGILLDhgTGVVIGETAVIGDRVSILHGVTLGGTGKETGDRHPNIGDGALLGACVTILGNIKIGAGAMVAAGSLVL 291
Cdd:cd03350    32 AYVDEGTMVD--SWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLT 109


                  ....
gi 1901122555 292 KDVP 295
Cdd:cd03350   110 QSTP 113
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 232-300 1.58e-04

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: 43.48  E-value: 1.58e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1901122555 232 AVIGDRVSIlhgvtlG-GT------GKetgDRHP-NIGDGALLGACVTILGNIKIGAGAMVAAGSLVLKDVPSHSMV 300
Cdd:COG1207   370 AEIGEGVNI------GaGTitcnydGV---NKHRtVIGDGAFIGSNTNLVAPVTIGDGATIGAGSTITKDVPAGALA 437
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 208-281 1.72e-04

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: 42.70  E-value: 1.72e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1901122555 208 IHPAARIGKGilldhgtgVVIGETAVIGDRVSIlhgvtlggtgketgdrhpniGDGALLGACVTILGNIKIGAG 281
Cdd:COG1043    10 VDPGAKLGEN--------VEIGPFCVIGPDVEI--------------------GDGTVIGSHVVIEGPTTIGKN 55
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 212-300 4.93e-04

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 41.94  E-value: 4.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 212 ARIGKGILLDHGTgvVIGEtAVIGDRVSILHGV-TLGGTGketGDRHPN-IGDGALLGACVTILGNIKIGAGAMVAAGSL 289
Cdd:PRK09451  353 ARLGKGSKAGHLT--YLGD-AEIGDNVNIGAGTiTCNYDG---ANKFKTiIGDDVFVGSDTQLVAPVTVGKGATIGAGTT 426

                          90
                  ....*....|.
gi 1901122555 290 VLKDVPSHSMV 300
Cdd:PRK09451  427 VTRDVAENELV 437
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 207-302 5.07e-04

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 41.84  E-value: 5.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 207 DIHPAARIG-----KGILLDHGTGV----VIGEtAVIGDRVSIlhgvtlgGTGKETGD-----RHP-NIGDGALLGACVT 271
Cdd:PRK14360  333 QIGSNCRIGnfveiKKSQLGEGSKVnhlsYIGD-ATLGEQVNI-------GAGTITANydgvkKHRtVIGDRSKTGANSV 404

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1901122555 272 ILGNIKIGAGAMVAAGSLVLKDVPSHSMVAG 302
Cdd:PRK14360  405 LVAPITLGEDVTVAAGSTITKDVPDNSLAIA 435
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 226-329 6.02e-04

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: 39.89  E-value: 6.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 226 VVIGETAVIGDRvSILHGVTLGGtgketgdrHPNIGDGALLGACVTILGNIKIGAGAMVAAGSLVlkdvPSHSMVAGNPA 305
Cdd:cd03359    73 LHIGDYVFIGEN-CVVNAAQIGS--------YVHIGKNCVIGRRCIIKDCVKILDGTVVPPDTVI----PPYSVVSGRPA 139

                          90       100
                  ....*....|....*....|....*..
gi 1901122555 306 KLIGFVdeqdPSMT---MEhDATREFF 329
Cdd:cd03359   140 RFIGEL----PECTqelME-EETKEYY 161
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 212-287 6.22e-04

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: 40.87  E-value: 6.22e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1901122555 212 ARIGKGILLDhgTGVVIGETAVIGDRVSILHGVTLGGTgKETGDRHPN-IGDGALLGA-CVTILGnIKIGAGAMVAAG 287
Cdd:COG2171   127 AYVDEGTMVD--TWATVGSCAQIGKNVHLSGGAGIGGV-LEPLQAAPViIEDNCFIGArSGVVEG-VIVGEGAVLGAG 200
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 208-340 1.25e-03

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 39.41  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 208 IHPAA-RIGKGILldhGTGVVIGETAVI-GD--RVSILHGVTL-------GGTGKETgDRHPN--IGDGALLGACV---- 270
Cdd:PRK13627   19 VHPSAvLIGDVIV---GAGVYIGPLASLrGDygRLIVQAGANLqdgcimhGYCDTDT-IVGENghIGHGAILHGCVigrd 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 271 -------TILGNIKIGAGAMVAAGSLV---LKDVPSHsMVAGNPAKLIGFVDEQDpsMTMEHDATREfFQNVAVAYRETI 340
Cdd:PRK13627   95 alvgmnsVIMDGAVIGEESIVAAMSFVkagFQGEKRQ-LLMGTPARAVRSVSDDE--LHWKRLNTKE-YQDLVGRCHASL 170
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
257-286 1.50e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.78  E-value: 1.50e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1901122555 257 HPNIGDGALLGACVTILGNIKIGAGAMVAA 286
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 208-308 2.19e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 39.24  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 208 IHPAARIGKGILLdhGTGVVIGETAVIGDRVSIlhgvtlggtgketgdrhpniGDGALLGACVTILGNIKIGAGAMVAAG 287
Cdd:PRK12461    2 IHPTAVIDPSAKL--GSGVEIGPFAVIGANVEI--------------------GDGTWIGPHAVILGPTRIGKNNKIHQG 59

                          90       100
                  ....*....|....*....|.
gi 1901122555 288 SlVLKDVPSHSMVAGNPAKLI 308
Cdd:PRK12461   60 A-VVGDEPQDFTYKGEESRLE 79
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 205-299 2.69e-03

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 39.58  E-value: 2.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1901122555 205 GIDIHPAARIGKGILLDHGT---------------GVVIGETAVIGDrVSILHGVTLG-GTGKETGD---RHPN-IGDGA 264
Cdd:PRK14358  328 GSDVGPFARLRPGTVLGEGVhignfvetknarldaGVKAGHLAYLGD-VTIGAETNVGaGTIVANFDgvnKHQSkVGAGV 406

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1901122555 265 LLGACVTILGNIKIGAGAMVAAGSLVLKDVPSHSM 299
Cdd:PRK14358  407 FIGSNTTLIAPRVVGDAAFIAAGSAVHDDVPEGAM 441
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 260-299 6.78e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 38.19  E-value: 6.78e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1901122555 260 IGDGALLGACVTILGNIKIGAGAMVAAGSLVLKDVPSHSM 299
Cdd:PRK14355  400 IEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPPDSL 439
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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