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Conserved domains on  [gi|491993812|ref|WP_005710883|]
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serine O-acetyltransferase [Glaesserella parasuis]

Protein Classification

serine O-acetyltransferase( domain architecture ID 11485218)

serine O-acetyltransferase (SAT) catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetyl-L-serine

CATH:  2.160.10.10
EC:  2.3.1.30
Gene Ontology:  GO:0009001|GO:0006535
PubMed:  15500694|11747907|15581568
SCOP:  4001889

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
cysE PRK11132
serine acetyltransferase; Provisional
 1-268 0e+00

serine acetyltransferase; Provisional


:

Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 565.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812   1 MTNQPLDLIWQNIRNEAQELVNSEPMLASFFHATILKHHHLGDALSYILANKLANAIMPAIALKEIIEEAYQADPQIIAS 80
Cdd:PRK11132   1 MSCEELEIVWNNIKAEARALADCEPMLASFYHATLLKHENLGSALSYMLANKLASPIMPAIAIREVVEEAYAADPEMIAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812  81 AACDIEAVRTRDPAVDKWSTPLLYLKGYHALQSYRVTHYLWQQGRKALAIYLQNEISVAFDVDIHPAASVGCGIMLDHAT 160
Cdd:PRK11132  81 AACDIQAVRTRDPAVDKYSTPLLYLKGFHALQAYRIGHWLWNQGRRALAIYLQNQISVAFQVDIHPAAKIGRGIMLDHAT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812 161 GIVVGETAVIENDVSILQGVTLGGTGKEHGDRHPKIREGVMIGAGAKILGNIEIGRYSKIGANSVVLQAVPEYATAAGVP 240
Cdd:PRK11132 161 GIVIGETAVIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVP 240

                        250       260
                 ....*....|....*....|....*...
gi 491993812 241 ARIIGHSQQQKPAFEMNQYFDDTNKEIN 268
Cdd:PRK11132 241 ARIVGKPESDKPSMDMDQHFNGINHTFE 268
 
Name Accession Description Interval E-value
cysE PRK11132
serine acetyltransferase; Provisional
 1-268 0e+00

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 565.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812   1 MTNQPLDLIWQNIRNEAQELVNSEPMLASFFHATILKHHHLGDALSYILANKLANAIMPAIALKEIIEEAYQADPQIIAS 80
Cdd:PRK11132   1 MSCEELEIVWNNIKAEARALADCEPMLASFYHATLLKHENLGSALSYMLANKLASPIMPAIAIREVVEEAYAADPEMIAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812  81 AACDIEAVRTRDPAVDKWSTPLLYLKGYHALQSYRVTHYLWQQGRKALAIYLQNEISVAFDVDIHPAASVGCGIMLDHAT 160
Cdd:PRK11132  81 AACDIQAVRTRDPAVDKYSTPLLYLKGFHALQAYRIGHWLWNQGRRALAIYLQNQISVAFQVDIHPAAKIGRGIMLDHAT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812 161 GIVVGETAVIENDVSILQGVTLGGTGKEHGDRHPKIREGVMIGAGAKILGNIEIGRYSKIGANSVVLQAVPEYATAAGVP 240
Cdd:PRK11132 161 GIVIGETAVIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVP 240

                        250       260
                 ....*....|....*....|....*...
gi 491993812 241 ARIIGHSQQQKPAFEMNQYFDDTNKEIN 268
Cdd:PRK11132 241 ARIVGKPESDKPSMDMDQHFNGINHTFE 268
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 81-242 1.28e-94

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


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 275.33  E-value: 1.28e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812   81 AACDIEAVRTRDPAVDKWSTPLLYLKGYHALQSYRVTHYLWQQGRKALAIYLQNEISVAFDVDIHPAASVGCGIMLDHAT 160
Cdd:TIGR01172   1 IREDIRAVRERDPAARSYLEVLLYYPGFHALWAYRFAHFLWKRGFKFLARLLSNFIRVLTGVDIHPGARIGRGVFIDHGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812  161 GIVVGETAVIENDVSILQGVTLGGTGKEHGDRHPKIREGVMIGAGAKILGNIEIGRYSKIGANSVVLQAVPEYATAAGVP 240
Cdd:TIGR01172  81 GVVIGETAVIGDDVTIYHGVTLGGTGKEKGKRHPTIGEGVMIGAGAKVLGNIEVGENAKIGANSVVLKDVPPGATVVGVP 160


                  ..
gi 491993812  241 AR 242
Cdd:TIGR01172 161 AR 162
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 77-247 2.61e-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: 272.34  E-value: 2.61e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812  77 IIASAACDIEAVRTRDPAVDKWSTPLLYLKGYHALQSYRVTHYLWQQGRKALAIYLQNEISVAFDVDIHPAASVGCGIML 156
Cdd:COG1045    1 MLKALREDIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHPGATIGRGFFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812 157 DHATGIVVGETAVIENDVSILQGVTLGGTGKEHGDRHPKIREGVMIGAGAKILGNIEIGRYSKIGANSVVLQAVPEYATA 236
Cdd:COG1045   81 DHGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTV 160

                        170
                 ....*....|.
gi 491993812 237 AGVPARIIGHS 247
Cdd:COG1045  161 VGVPARIVKRK 171
SATase_N smart00971
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 9-113 1.13e-58

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: 181.97  E-value: 1.13e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812     9 IWQNIRNEAQELVNSEPMLASFFHATILKHHHLGDALSYILANKLANAIMPAIALKEIIEEAYQADPQIIASAACDIEAV 88
Cdd:smart00971   1 VWQRIRAEAREAAEREPILASFLYATILNHDSLEAALAYRLANKLGNADMSADLLRELFEDAYAADPEIVEAAAADIQAV 80

                           90       100
                   ....*....|....*....|....*
gi 491993812    89 RTRDPAVDKWSTPLLYLKGYHALQS 113
Cdd:smart00971  81 YDRDPACDRYLTPLLYFKGFHALQA 105
SATase_N pfam06426
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 9-112 2.36e-57

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: 178.42  E-value: 2.36e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812    9 IWQNIRNEAQELVNSEPMLASFFHATILKHHHLGDALSYILANKLANAIMPAIALKEIIEEAYQADPQIIASAACDIEAV 88
Cdd:pfam06426   1 VWARLRAEAEEAAEREPLLASFLYATILSHDSLESALAFRLANKLANSTLPATLLRELFEDALEADPEIVEAARADLQAV 80

                          90       100
                  ....*....|....*....|....
gi 491993812   89 RTRDPAVDKWSTPLLYLKGYHALQ 112
Cdd:pfam06426  81 YERDPACDRYLTPLLYFKGFHALQ 104
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 140-240 4.00e-50

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: 159.91  E-value: 4.00e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812 140 FDVDIHPAASVGCGIMLDHATGIVVGETAVIENDVSILQGVTLGGTGKEHGDRHPKIREGVMIGAGAKILGNIEIGRYSK 219
Cdd:cd03354    1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                         90       100
                 ....*....|....*....|.
gi 491993812 220 IGANSVVLQAVPEYATAAGVP 240
Cdd:cd03354   81 IGANAVVTKDVPANSTVVGVP 101
 
Name Accession Description Interval E-value
cysE PRK11132
serine acetyltransferase; Provisional
 1-268 0e+00

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 565.86  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812   1 MTNQPLDLIWQNIRNEAQELVNSEPMLASFFHATILKHHHLGDALSYILANKLANAIMPAIALKEIIEEAYQADPQIIAS 80
Cdd:PRK11132   1 MSCEELEIVWNNIKAEARALADCEPMLASFYHATLLKHENLGSALSYMLANKLASPIMPAIAIREVVEEAYAADPEMIAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812  81 AACDIEAVRTRDPAVDKWSTPLLYLKGYHALQSYRVTHYLWQQGRKALAIYLQNEISVAFDVDIHPAASVGCGIMLDHAT 160
Cdd:PRK11132  81 AACDIQAVRTRDPAVDKYSTPLLYLKGFHALQAYRIGHWLWNQGRRALAIYLQNQISVAFQVDIHPAAKIGRGIMLDHAT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812 161 GIVVGETAVIENDVSILQGVTLGGTGKEHGDRHPKIREGVMIGAGAKILGNIEIGRYSKIGANSVVLQAVPEYATAAGVP 240
Cdd:PRK11132 161 GIVIGETAVIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVP 240

                        250       260
                 ....*....|....*....|....*...
gi 491993812 241 ARIIGHSQQQKPAFEMNQYFDDTNKEIN 268
Cdd:PRK11132 241 ARIVGKPESDKPSMDMDQHFNGINHTFE 268
PLN02739 PLN02739
serine acetyltransferase
 2-266 6.29e-97

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 288.47  E-value: 6.29e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812   2 TNQPLDLIWQNIRNEAQELVNSEPMLASFFHATILKHHHLGDALSYILANKLANAIMPAIALKEIIEEAYQADPQIIASA 81
Cdd:PLN02739  66 TNSRYDPIWDSIREEAKLEAEEEPVLSSFLYASILSHDCLEQALSFVLANRLQNPTLLATQLMDIFCNVMVHDRGIQSSI 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812  82 ACDIEAVRTRDPAVDKWSTPLLYLKGYHALQSYRVTHYLWQQGRKALAIYLQNEISVAFDVDIHPAASVGCGIMLDHATG 161
Cdd:PLN02739 146 RLDVQAFKDRDPACLSYSSAILHLKGYLALQAYRVAHKLWKQGRKLLALALQSRVSEVFGIDIHPAARIGKGILLDHGTG 225

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812 162 IVVGETAVIENDVSILQGVTLGGTGKEHGDRHPKIREGVMIGAGAKILGNIEIGRYSKIGANSVVLQAVPEYATAAGVPA 241
Cdd:PLN02739 226 VVIGETAVIGDRVSILHGVTLGGTGKETGDRHPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPA 305

                        250       260
                 ....*....|....*....|....*
gi 491993812 242 RIIGHSQQQKPAFEMNQyfdDTNKE 266
Cdd:PLN02739 306 KLIGFVDEQDPSLTMEY---DATRE 327
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 81-242 1.28e-94

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


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 275.33  E-value: 1.28e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812   81 AACDIEAVRTRDPAVDKWSTPLLYLKGYHALQSYRVTHYLWQQGRKALAIYLQNEISVAFDVDIHPAASVGCGIMLDHAT 160
Cdd:TIGR01172   1 IREDIRAVRERDPAARSYLEVLLYYPGFHALWAYRFAHFLWKRGFKFLARLLSNFIRVLTGVDIHPGARIGRGVFIDHGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812  161 GIVVGETAVIENDVSILQGVTLGGTGKEHGDRHPKIREGVMIGAGAKILGNIEIGRYSKIGANSVVLQAVPEYATAAGVP 240
Cdd:TIGR01172  81 GVVIGETAVIGDDVTIYHGVTLGGTGKEKGKRHPTIGEGVMIGAGAKVLGNIEVGENAKIGANSVVLKDVPPGATVVGVP 160


                  ..
gi 491993812  241 AR 242
Cdd:TIGR01172 161 AR 162
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 77-247 2.61e-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: 272.34  E-value: 2.61e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812  77 IIASAACDIEAVRTRDPAVDKWSTPLLYLKGYHALQSYRVTHYLWQQGRKALAIYLQNEISVAFDVDIHPAASVGCGIML 156
Cdd:COG1045    1 MLKALREDIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHPGATIGRGFFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812 157 DHATGIVVGETAVIENDVSILQGVTLGGTGKEHGDRHPKIREGVMIGAGAKILGNIEIGRYSKIGANSVVLQAVPEYATA 236
Cdd:COG1045   81 DHGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTV 160

                        170
                 ....*....|.
gi 491993812 237 AGVPARIIGHS 247
Cdd:COG1045  161 VGVPARIVKRK 171
PLN02357 PLN02357
serine acetyltransferase
 7-258 1.05e-91

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 275.22  E-value: 1.05e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812   7 DLIWQNIRNEAQELVNSEPMLASFFHATILKHHHLGDALSYILANKLANAIMPAIALKEIIEEAYQADPQIIASAACDIE 86
Cdd:PLN02357  92 DDVWLKIQEEAKSDVEQEPILSSYYYASILSHRSLESALANHLSVKLSNLNLPSNTLFDLFIGVLEESPEIIESVKQDLR 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812  87 AVRTRDPAVDKWSTPLLYLKGYHALQSYRVTHYLWQQGRKALAIYLQNEISVAFDVDIHPAASVGCGIMLDHATGIVVGE 166
Cdd:PLN02357 172 AVKERDPACISYVHCFLNFKGFLACQAHRIAHKLWTQGRKILALLIQNRVSEAFAVDIHPGAKIGQGILLDHATGVVIGE 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812 167 TAVIENDVSILQGVTLGGTGKEHGDRHPKIREGVMIGAGAKILGNIEIGRYSKIGANSVVLQAVPEYATAAGVPARIIGH 246
Cdd:PLN02357 252 TAVVGNNVSILHNVTLGGTGKQSGDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLIGG 331

                        250
                 ....*....|....*..
gi 491993812 247 SQQQK-----PAFEMNQ 258
Cdd:PLN02357 332 KENPIkhdkiPSLTMDQ 348
PLN02694 PLN02694
serine O-acetyltransferase
 8-253 1.68e-91

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 272.29  E-value: 1.68e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812   8 LIWQNIRNEAQELVNSEPMLASFFHATILKHHHLGDALSYILANKLANAIMPAIALKEIIEEAYQADPQIIASAACDIEA 87
Cdd:PLN02694  27 WLWTQIKAEARRDAESEPALASYLYSTILSHSSLERSLSFHLGNKLCSSTLLSTLLYDLFLNTFSSDPSLRAATVADLRA 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812  88 VRTRDPAVDKWSTPLLYLKGYHALQSYRVTHYLWQQGRKALAIYLQNEISVAFDVDIHPAASVGCGIMLDHATGIVVGET 167
Cdd:PLN02694 107 ARVRDPACVSFSHCLLNYKGFLACQAHRVAHKLWTQSRRPLALALHSRISDVFAVDIHPAAKIGKGILFDHATGVVIGET 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812 168 AVIENDVSILQGVTLGGTGKEHGDRHPKIREGVMIGAGAKILGNIEIGRYSKIGANSVVLQAVPEYATAAGVPARIIGhs 247
Cdd:PLN02694 187 AVIGNNVSILHHVTLGGTGKACGDRHPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLVG-- 264


                 ....*.
gi 491993812 248 QQQKPA 253
Cdd:PLN02694 265 GKEKPA 270
SATase_N smart00971
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 9-113 1.13e-58

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: 181.97  E-value: 1.13e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812     9 IWQNIRNEAQELVNSEPMLASFFHATILKHHHLGDALSYILANKLANAIMPAIALKEIIEEAYQADPQIIASAACDIEAV 88
Cdd:smart00971   1 VWQRIRAEAREAAEREPILASFLYATILNHDSLEAALAYRLANKLGNADMSADLLRELFEDAYAADPEIVEAAAADIQAV 80

                           90       100
                   ....*....|....*....|....*
gi 491993812    89 RTRDPAVDKWSTPLLYLKGYHALQS 113
Cdd:smart00971  81 YDRDPACDRYLTPLLYFKGFHALQA 105
SATase_N pfam06426
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 9-112 2.36e-57

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: 178.42  E-value: 2.36e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812    9 IWQNIRNEAQELVNSEPMLASFFHATILKHHHLGDALSYILANKLANAIMPAIALKEIIEEAYQADPQIIASAACDIEAV 88
Cdd:pfam06426   1 VWARLRAEAEEAAEREPLLASFLYATILSHDSLESALAFRLANKLANSTLPATLLRELFEDALEADPEIVEAARADLQAV 80

                          90       100
                  ....*....|....*....|....
gi 491993812   89 RTRDPAVDKWSTPLLYLKGYHALQ 112
Cdd:pfam06426  81 YERDPACDRYLTPLLYFKGFHALQ 104
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 140-240 4.00e-50

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: 159.91  E-value: 4.00e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812 140 FDVDIHPAASVGCGIMLDHATGIVVGETAVIENDVSILQGVTLGGTGKEHGDRHPKIREGVMIGAGAKILGNIEIGRYSK 219
Cdd:cd03354    1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                         90       100
                 ....*....|....*....|.
gi 491993812 220 IGANSVVLQAVPEYATAAGVP 240
Cdd:cd03354   81 IGANAVVTKDVPANSTVVGVP 101
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
162-246 5.00e-19

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 80.69  E-value: 5.00e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812 162 IVVGETAVIENDVSILQGVTLGGTGKEHGD--------RHPKIREGVMIGAGAKILGNIEIGRYSKIGANSVVLQAVPEY 233
Cdd:COG0110   42 IDDPGGITIGDNVLIGPGVTILTGNHPIDDpatfplrtGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPY 121

                         90
                 ....*....|...
gi 491993812 234 ATAAGVPARIIGH 246
Cdd:COG0110  122 AIVAGNPARVIRK 134
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 149-245 1.68e-16

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: 73.30  E-value: 1.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812 149 SVGCGIMLDHatGIVVGETAVIENDVSILQGVTLG-----------------GTGKEHGD--RHPKIREGVMIGAGAKIL 209
Cdd:cd03358    6 IIGTNVFIEN--DVKIGDNVKIQSNVSIYEGVTIEddvfigpnvvftndlypRSKIYRKWelKGTTVKRGASIGANATIL 83

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 491993812 210 GNIEIGRYSKIGANSVVLQAVPEYATAAGVPARIIG 245
Cdd:cd03358   84 PGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 149-244 4.93e-16

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: 71.72  E-value: 4.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812 149 SVGCGIMLDHATGIVvgetavIENDVSILQGVTLGGTGKEHGDRHPK-----------IREGVMIGAGAKILGNIEIGRY 217
Cdd:cd04647    9 YIGPGCVISAGGGIT------IGDNVLIGPNVTIYDHNHDIDDPERPieqgvtsapivIGDDVWIGANVVILPGVTIGDG 82

                         90       100
                 ....*....|....*....|....*..
gi 491993812 218 SKIGANSVVLQAVPEYATAAGVPARII 244
Cdd:cd04647   83 AVVGAGSVVTKDVPPNSIVAGNPAKVI 109
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 144-241 1.15e-15

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: 73.30  E-value: 1.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812  144 IHPAASVGCGIMLDHA----TGIVVGETAVIENDVSILQGVTLGGtgkehgdrHPKIREGVMIGAGAKILGNIEIGRYSK 219
Cdd:TIGR03570 108 IMAGAVINPDVRIGDNviinTGAIVEHDCVIGDFVHIAPGVTLSG--------GVVIGEGVFIGAGATIIQGVTIGAGAI 179

                          90       100
                  ....*....|....*....|..
gi 491993812  220 IGANSVVLQAVPEYATAAGVPA 241
Cdd:TIGR03570 180 VGAGAVVTKDIPDGGVVVGVPA 201
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 144-240 4.92e-14

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: 68.67  E-value: 4.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812 144 IHPAASVGCGIML-DHA---TGIVVGETAVIENDVSILQGVTLGGtgkehgdrHPKIREGVMIGAGAKILGNIEIGRYSK 219
Cdd:cd03360  105 IMAGAVINPDARIgDNViinTGAVIGHDCVIGDFVHIAPGVVLSG--------GVTIGEGAFIGAGATIIQGVTIGAGAI 176

                         90       100
                 ....*....|....*....|.
gi 491993812 220 IGANSVVLQAVPEYATAAGVP 240
Cdd:cd03360  177 IGAGAVVTKDVPDGSVVVGNP 197
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 148-227 5.98e-14

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: 65.35  E-value: 5.98e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812 148 ASVGCGIMLDHatGIVVGETAVIENDVSILQGVTLGGTGKEHGDRHPKIREGVMIGAGAKILGNIEIGRYSKIGANSVVL 227
Cdd:cd00208    1 VFIGEGVKIHP--KAVIRGPVVIGDNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
PRK10191 PRK10191
putative acyl transferase; Provisional
 140-243 3.55e-13

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 65.30  E-value: 3.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812 140 FDVDIHPAASVGCGIMLDHATGIVVGETAVIENDVSILQGVTLGGTGKEhGDRHPKIREGVMIGAGAKILGNIEIGRYSK 219
Cdd:PRK10191  40 FGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGVTIGNRGAD-NMACPHIGNGVELGANVIILGDITIGNNVT 118

                         90       100
                 ....*....|....*....|....
gi 491993812 220 IGANSVVLQAVPEYATAAGVPARI 243
Cdd:PRK10191 119 VGAGSVVLDSVPDNALVVGEKARV 142
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 196-244 2.07e-09

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: 55.12  E-value: 2.07e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 491993812 196 IREGVMIGAGAKILGNIEIGRYSKIGANSVVLQAVPEYATAAGVPARII 244
Cdd:cd03357  121 IGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 141-244 5.47e-09

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: 53.57  E-value: 5.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812 141 DVDIHPAASVGCGIML--DHATgIVVGE----------------TAVIENDVSILQGVTLggtgkeHGDRhpkIREGVMI 202
Cdd:cd04645   17 DVTLGEGSSVWFGAVLrgDVNP-IRIGErtniqdgsvlhvdpgyPTIIGDNVTVGHGAVL------HGCT---IGDNCLI 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 491993812 203 GAGAKILGNIEIGRYSKIGANSVVLQA--VPEYATAAGVPARII 244
Cdd:cd04645   87 GMGAIILDGAVIGKGSIVAAGSLVPPGkvIPPGSLVAGSPAKVV 130
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 200-244 6.21e-09

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: 53.32  E-value: 6.21e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 491993812 200 VMIGAGAKILGNIEIGRYSKIGANSVVLQAVPEYATAAGVPARII 244
Cdd:cd03349   80 VWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVI 124
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 158-244 1.01e-08

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 53.49  E-value: 1.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812 158 HATGivvGETAVIENDVSILQGVTLggtgkeHGDRhpkIREGVMIGAGAKILGNIEIGRYSKIGANSVVLQ--AVPEYAT 235
Cdd:COG0663   65 HVDP---GYPLTIGDDVTIGHGAIL------HGCT---IGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEgkVVPPGSL 132


                 ....*....
gi 491993812 236 AAGVPARII 244
Cdd:COG0663  133 VVGSPAKVV 141
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 124-262 5.32e-07

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 48.85  E-value: 5.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812 124 GRKAlaiYLQNEISVAFDVDIHpaasVGCGIMLDHATGIVVGETAVIENDVSILQGVTLGGTG-------KEHGDRHP-- 194
Cdd:PRK09527  59 GENA---WVEPPVYFSYGSNIH----IGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGhpvhhelRKNGEMYSfp 131

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491993812 195 -KIREGVMIGAGAKILGNIEIGRYSKIGANSVVLQAVPEYATAAGVPARIIGHSQQQKPAFemnqYFDD 262
Cdd:PRK09527 132 iTIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIREINDRDKQY----YFKD 196
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 159-230 8.08e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 49.37  E-value: 8.08e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491993812 159 ATGI----VVGETAVIENDVSILQGVTLGgtgkehgdRHPKIREGVMIGAGAKILGNIEIGRYSKIGANSVVLQAV 230
Cdd:PRK00892 100 AAGIhpsaVIDPSAKIGEGVSIGPNAVIG--------AGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAV 167
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 174-244 1.61e-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: 46.79  E-value: 1.61e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491993812 174 VSILQGVTLGGTGKEHGdrhPKIREGVMIGAGAKILGNIEIGRYSKIGANSVVLQA--VPEYATAAGVPARII 244
Cdd:cd04650   62 TEIGDYVTIGHNAVVHG---AKVGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTPGkeIPDYSLVLGVPAKVV 131
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 195-244 3.29e-06

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 46.41  E-value: 3.29e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 491993812 195 KIREGVMIGAGAKILGNIEIGRYSKIGANSVVLQAVPEYATAAGVPARII 244
Cdd:PRK09677 132 VIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKII 181
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 169-245 6.66e-06

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: 46.27  E-value: 6.66e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491993812 169 VIENDVSILQGVTLGGtgkehgdrHPKIREGVMIGAGAKILGNIEIGRYSKIGANSVVLQAVPEYATAAGVPARIIG 245
Cdd:cd03351  122 VIGNNVILANNATLAG--------HVEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARLRG 190
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 169-245 7.19e-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: 46.16  E-value: 7.19e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491993812 169 VIENDVSILQGVTLGGtgkehgdrHPKIREGVMIGAGAKILGNIEIGRYSKIGANSVVLQAVPEYATAAGVPARIIG 245
Cdd:COG1043  124 VVGNNVILANNATLAG--------HVEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDVPPYVLAAGNPARLRG 192
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
169-245 8.57e-06

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 45.86  E-value: 8.57e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491993812 169 VIENDVSILQGVTLGGtgkehgdrHPKIREGVMIGAGAKILGNIEIGRYSKIGANSVVLQAVPEYATAAGVPARIIG 245
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 ...
 169-244 1.21e-05

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: 43.36  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812 169 VIENDVSILQGVTL-GGTgkeHGDRHPK---------IREGVMIGAGAKILGNIEIGRYSKIGANSVVLQAVPEYATAAG 238
Cdd:cd05825   25 TIGSDACISQGAYLcTGS---HDYRSPAfplitapivIGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAG 101


                 ....*.
gi 491993812 239 VPARII 244
Cdd:cd05825  102 NPAVPV 107
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
193-222 3.43e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 40.01  E-value: 3.43e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 491993812  193 HPKIREGVMIGAGAKILGNIEIGRYSKIGA 222
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 144-226 3.55e-05

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: 44.24  E-value: 3.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812 144 IHPAAsvgcgimldhatgiVVGETAVIENDVSILQGVTLGgtgkehgdRHPKIREGVMIGAGAKILGNIEIGRYSKIGAN 223
Cdd:COG1044   99 IHPSA--------------VIDPSAKIGEGVSIGPFAVIG--------AGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPN 156


                 ...
gi 491993812 224 SVV 226
Cdd:COG1044  157 VTI 159
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 148-242 5.53e-05

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: 41.98  E-value: 5.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812 148 ASVGCGIMLDhaTGIVVGETAVIENDVSILQGVTLGGTGKEHGDRHPKIREGVMIGAGAKILGNIEIGRYSKIGANSVVL 227
Cdd:cd03350   32 AYVDEGTMVD--SWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLT 109

                         90       100
                 ....*....|....*....|.
gi 491993812 228 QAVPEYATAAG------VPAR 242
Cdd:cd03350  110 QSTPIYDRETGeiyygrVPPG 130
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 195-242 5.88e-04

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: 40.77  E-value: 5.88e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 491993812 195 KIREGVMIGAGAKILGNIEIGRYSKIGANSVVLQAVPEYATAAGVPAR 242
Cdd:COG1044  260 KIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSGSPAQ 307
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 148-244 8.58e-04

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 40.13  E-value: 8.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812 148 ASVGCGIMLDHATGIvvGEtAVIENDVSILQG-VTLGGTGKEhgdRHPK-IREGVMIGAGAKILGNIEIGRYSKIGANSV 225
Cdd:PRK14357 342 STIGENTKAQHLTYL--GD-ATVGKNVNIGAGtITCNYDGKK---KNPTfIEDGAFIGSNSSLVAPVRIGKGALIGAGSV 415

                         90
                 ....*....|....*....
gi 491993812 226 VLQAVPEYATAAGVPARII 244
Cdd:PRK14357 416 ITEDVPPYSLALGRARQIV 434
PRK10502 PRK10502
putative acyl transferase; Provisional
 164-244 1.25e-03

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 38.78  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812 164 VGETAV--------IENDVSILQGVTLGGTGKEHGDRHPKIR-------EGVMIGAGAKILGNIEIGRYSKIGANSVVLQ 228
Cdd:PRK10502  80 IGDDVWlynlgeitIGAHCVISQKSYLCTGSHDYSDPHFDLNtapivigEGCWLAADVFVAPGVTIGSGAVVGARSSVFK 159

                         90
                 ....*....|....*.
gi 491993812 229 AVPEYATAAGVPARII 244
Cdd:PRK10502 160 SLPANTICRGNPAVPI 175
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 141-242 1.34e-03

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: 38.93  E-value: 1.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812 141 DVDIHPAASVGCGIMLDhaTgiVVGETAVIENDVSILQGVTLGgtgkEH----------GdrHPKIREGVMIGAGAKILG 210
Cdd:cd03352   98 DVEIGANTTIDRGALGD--T--VIGDGTKIDNLVQIAHNVRIG----ENcliaaqvgiaG--STTIGDNVIIGGQVGIAG 167

                         90       100       110
                 ....*....|....*....|....*....|..
gi 491993812 211 NIEIGRYSKIGANSVVLQAVPEYATAAGVPAR 242
Cdd:cd03352  168 HLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQ 199
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 144-229 1.46e-03

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: 39.23  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812 144 IHPAASVGcgimldhaTGIVVGETAVIENDVSILQGVTLGGtgkehgdrHPKIREGVMIGAGAKILGNIEIGRYSKIGAN 223
Cdd:COG1044  105 IDPSAKIG--------EGVSIGPFAVIGAGVVIGDGVVIGP--------GVVIGDGVVIGDDCVLHPNVTIYERCVIGDR 168


                 ....*.
gi 491993812 224 sVVLQA 229
Cdd:COG1044  169 -VIIHS 173
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 144-226 7.65e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 37.04  E-value: 7.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491993812 144 IHPAASVGCGIMLDHatGIVVGETAVIENDVSILQGVTLGgtgkehgdRHPKIREGVMIGAGAKILGNIEIGRYSKIGAN 223
Cdd:PRK00892 109 IDPSAKIGEGVSIGP--NAVIGAGVVIGDGVVIGAGAVIG--------DGVKIGADCRLHANVTIYHAVRIGNRVIIHSG 178


                 ...
gi 491993812 224 SVV 226
Cdd:PRK00892 179 AVI 181
 
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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