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Conserved domains on  [gi|495040456|ref|WP_007765485|]
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MULTISPECIES: serine O-acetyltransferase [Cronobacter]

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
 1-273 0e+00

serine acetyltransferase; Provisional


:

Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 627.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456   1 MPCEELDLVWKNIKAEARQLADCEPMLASFYHATLLKHENLGSALSYMLANKLASPIMPAIAIREVVEEAYRADPEMIAS 80
Cdd:PRK11132   1 MSCEELEIVWNNIKAEARALADCEPMLASFYHATLLKHENLGSALSYMLANKLASPIMPAIAIREVVEEAYAADPEMIAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456  81 AACDIQAVRTRDPAVDKYSTPLLYLKGFHALQAHRIGHWLWQQGRQALAIFLQNQVSVSFQVDIHPAATIGRGIMLDHAT 160
Cdd:PRK11132  81 AACDIQAVRTRDPAVDKYSTPLLYLKGFHALQAYRIGHWLWNQGRRALAIYLQNQISVAFQVDIHPAAKIGRGIMLDHAT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 161 GIVIGETAVVEDDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVP 240
Cdd:PRK11132 161 GIVIGETAVIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVP 240

                        250       260       270
                 ....*....|....*....|....*....|...
gi 495040456 241 ARIVGKPESDKPSMDMDQHFNGINHGFEYGDGI 273
Cdd:PRK11132 241 ARIVGKPESDKPSMDMDQHFNGINHTFEYGDGI 273
 
Name Accession Description Interval E-value
cysE PRK11132
serine acetyltransferase; Provisional
 1-273 0e+00

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 627.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456   1 MPCEELDLVWKNIKAEARQLADCEPMLASFYHATLLKHENLGSALSYMLANKLASPIMPAIAIREVVEEAYRADPEMIAS 80
Cdd:PRK11132   1 MSCEELEIVWNNIKAEARALADCEPMLASFYHATLLKHENLGSALSYMLANKLASPIMPAIAIREVVEEAYAADPEMIAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456  81 AACDIQAVRTRDPAVDKYSTPLLYLKGFHALQAHRIGHWLWQQGRQALAIFLQNQVSVSFQVDIHPAATIGRGIMLDHAT 160
Cdd:PRK11132  81 AACDIQAVRTRDPAVDKYSTPLLYLKGFHALQAYRIGHWLWNQGRRALAIYLQNQISVAFQVDIHPAAKIGRGIMLDHAT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 161 GIVIGETAVVEDDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVP 240
Cdd:PRK11132 161 GIVIGETAVIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVP 240

                        250       260       270
                 ....*....|....*....|....*....|...
gi 495040456 241 ARIVGKPESDKPSMDMDQHFNGINHGFEYGDGI 273
Cdd:PRK11132 241 ARIVGKPESDKPSMDMDQHFNGINHTFEYGDGI 273
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 77-250 1.82e-100

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: 290.83  E-value: 1.82e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456  77 MIASAACDIQAVRTRDPAVDKYSTPLLYLKGFHALQAHRIGHWLWQQGRQALAIFLQNQVSVSFQVDIHPAATIGRGIML 156
Cdd:COG1045    1 MLKALREDIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHPGATIGRGFFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 157 DHATGIVIGETAVVEDDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTA 236
Cdd:COG1045   81 DHGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTV 160

                        170
                 ....*....|....
gi 495040456 237 AGVPARIVGKPESD 250
Cdd:COG1045  161 VGVPARIVKRKGSK 174
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 81-242 7.29e-97

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


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 281.10  E-value: 7.29e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456   81 AACDIQAVRTRDPAVDKYSTPLLYLKGFHALQAHRIGHWLWQQGRQALAIFLQNQVSVSFQVDIHPAATIGRGIMLDHAT 160
Cdd:TIGR01172   1 IREDIRAVRERDPAARSYLEVLLYYPGFHALWAYRFAHFLWKRGFKFLARLLSNFIRVLTGVDIHPGARIGRGVFIDHGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456  161 GIVIGETAVVEDDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVP 240
Cdd:TIGR01172  81 GVVIGETAVIGDDVTIYHGVTLGGTGKEKGKRHPTIGEGVMIGAGAKVLGNIEVGENAKIGANSVVLKDVPPGATVVGVP 160


                  ..
gi 495040456  241 AR 242
Cdd:TIGR01172 161 AR 162
SATase_N smart00971
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 9-113 3.71e-60

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: 185.82  E-value: 3.71e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456     9 VWKNIKAEARQLADCEPMLASFYHATLLKHENLGSALSYMLANKLASPIMPAIAIREVVEEAYRADPEMIASAACDIQAV 88
Cdd:smart00971   1 VWQRIRAEAREAAEREPILASFLYATILNHDSLEAALAYRLANKLGNADMSADLLRELFEDAYAADPEIVEAAAADIQAV 80

                           90       100
                   ....*....|....*....|....*
gi 495040456    89 RTRDPAVDKYSTPLLYLKGFHALQA 113
Cdd:smart00971  81 YDRDPACDRYLTPLLYFKGFHALQA 105
SATase_N pfam06426
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 9-112 5.14e-58

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: 180.35  E-value: 5.14e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456    9 VWKNIKAEARQLADCEPMLASFYHATLLKHENLGSALSYMLANKLASPIMPAIAIREVVEEAYRADPEMIASAACDIQAV 88
Cdd:pfam06426   1 VWARLRAEAEEAAEREPLLASFLYATILSHDSLESALAFRLANKLANSTLPATLLRELFEDALEADPEIVEAARADLQAV 80

                          90       100
                  ....*....|....*....|....
gi 495040456   89 RTRDPAVDKYSTPLLYLKGFHALQ 112
Cdd:pfam06426  81 YERDPACDRYLTPLLYFKGFHALQ 104
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 140-240 1.92e-52

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: 166.08  E-value: 1.92e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 140 FQVDIHPAATIGRGIMLDHATGIVIGETAVVEDDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAK 219
Cdd:cd03354    1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                         90       100
                 ....*....|....*....|.
gi 495040456 220 IGAGSVVLQPVPPHTTAAGVP 240
Cdd:cd03354   81 IGANAVVTKDVPANSTVVGVP 101
 
Name Accession Description Interval E-value
cysE PRK11132
serine acetyltransferase; Provisional
 1-273 0e+00

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 627.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456   1 MPCEELDLVWKNIKAEARQLADCEPMLASFYHATLLKHENLGSALSYMLANKLASPIMPAIAIREVVEEAYRADPEMIAS 80
Cdd:PRK11132   1 MSCEELEIVWNNIKAEARALADCEPMLASFYHATLLKHENLGSALSYMLANKLASPIMPAIAIREVVEEAYAADPEMIAS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456  81 AACDIQAVRTRDPAVDKYSTPLLYLKGFHALQAHRIGHWLWQQGRQALAIFLQNQVSVSFQVDIHPAATIGRGIMLDHAT 160
Cdd:PRK11132  81 AACDIQAVRTRDPAVDKYSTPLLYLKGFHALQAYRIGHWLWNQGRRALAIYLQNQISVAFQVDIHPAAKIGRGIMLDHAT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 161 GIVIGETAVVEDDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVP 240
Cdd:PRK11132 161 GIVIGETAVIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVP 240

                        250       260       270
                 ....*....|....*....|....*....|...
gi 495040456 241 ARIVGKPESDKPSMDMDQHFNGINHGFEYGDGI 273
Cdd:PRK11132 241 ARIVGKPESDKPSMDMDQHFNGINHTFEYGDGI 273
PLN02694 PLN02694
serine O-acetyltransferase
 4-258 5.37e-102

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 299.25  E-value: 5.37e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456   4 EELDLVWKNIKAEARQLADCEPMLASFYHATLLKHENLGSALSYMLANKLASPIMPAIAIREVVEEAYRADPEMIASAAC 83
Cdd:PLN02694  23 EEAAWLWTQIKAEARRDAESEPALASYLYSTILSHSSLERSLSFHLGNKLCSSTLLSTLLYDLFLNTFSSDPSLRAATVA 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456  84 DIQAVRTRDPAVDKYSTPLLYLKGFHALQAHRIGHWLWQQGRQALAIFLQNQVSVSFQVDIHPAATIGRGIMLDHATGIV 163
Cdd:PLN02694 103 DLRAARVRDPACVSFSHCLLNYKGFLACQAHRVAHKLWTQSRRPLALALHSRISDVFAVDIHPAAKIGKGILFDHATGVV 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 164 IGETAVVEDDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARI 243
Cdd:PLN02694 183 IGETAVIGNNVSILHHVTLGGTGKACGDRHPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARL 262

                        250       260
                 ....*....|....*....|
gi 495040456 244 VGKPES-----DKPSMDMDQ 258
Cdd:PLN02694 263 VGGKEKpakheECPGESMDH 282
PLN02357 PLN02357
serine acetyltransferase
 4-258 1.67e-101

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 300.26  E-value: 1.67e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456   4 EELDLVWKNIKAEARQLADCEPMLASFYHATLLKHENLGSALSYMLANKLASPIMPAIAIREVVEEAYRADPEMIASAAC 83
Cdd:PLN02357  89 DRDDDVWLKIQEEAKSDVEQEPILSSYYYASILSHRSLESALANHLSVKLSNLNLPSNTLFDLFIGVLEESPEIIESVKQ 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456  84 DIQAVRTRDPAVDKYSTPLLYLKGFHALQAHRIGHWLWQQGRQALAIFLQNQVSVSFQVDIHPAATIGRGIMLDHATGIV 163
Cdd:PLN02357 169 DLRAVKERDPACISYVHCFLNFKGFLACQAHRIAHKLWTQGRKILALLIQNRVSEAFAVDIHPGAKIGQGILLDHATGVV 248

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 164 IGETAVVEDDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARI 243
Cdd:PLN02357 249 IGETAVVGNNVSILHNVTLGGTGKQSGDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARL 328

                        250       260
                 ....*....|....*....|
gi 495040456 244 VGKPES----DK-PSMDMDQ 258
Cdd:PLN02357 329 IGGKENpikhDKiPSLTMDQ 348
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 77-250 1.82e-100

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: 290.83  E-value: 1.82e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456  77 MIASAACDIQAVRTRDPAVDKYSTPLLYLKGFHALQAHRIGHWLWQQGRQALAIFLQNQVSVSFQVDIHPAATIGRGIML 156
Cdd:COG1045    1 MLKALREDIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHPGATIGRGFFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 157 DHATGIVIGETAVVEDDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTA 236
Cdd:COG1045   81 DHGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTV 160

                        170
                 ....*....|....
gi 495040456 237 AGVPARIVGKPESD 250
Cdd:COG1045  161 VGVPARIVKRKGSK 174
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 81-242 7.29e-97

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


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 281.10  E-value: 7.29e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456   81 AACDIQAVRTRDPAVDKYSTPLLYLKGFHALQAHRIGHWLWQQGRQALAIFLQNQVSVSFQVDIHPAATIGRGIMLDHAT 160
Cdd:TIGR01172   1 IREDIRAVRERDPAARSYLEVLLYYPGFHALWAYRFAHFLWKRGFKFLARLLSNFIRVLTGVDIHPGARIGRGVFIDHGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456  161 GIVIGETAVVEDDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVP 240
Cdd:TIGR01172  81 GVVIGETAVIGDDVTIYHGVTLGGTGKEKGKRHPTIGEGVMIGAGAKVLGNIEVGENAKIGANSVVLKDVPPGATVVGVP 160


                  ..
gi 495040456  241 AR 242
Cdd:TIGR01172 161 AR 162
PLN02739 PLN02739
serine acetyltransferase
 7-257 5.55e-96

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 286.16  E-value: 5.55e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456   7 DLVWKNIKAEARQLADCEPMLASFYHATLLKHENLGSALSYMLANKLASPIMPAIAIREVVEEAYRADPEMIASAACDIQ 86
Cdd:PLN02739  71 DPIWDSIREEAKLEAEEEPVLSSFLYASILSHDCLEQALSFVLANRLQNPTLLATQLMDIFCNVMVHDRGIQSSIRLDVQ 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456  87 AVRTRDPAVDKYSTPLLYLKGFHALQAHRIGHWLWQQGRQALAIFLQNQVSVSFQVDIHPAATIGRGIMLDHATGIVIGE 166
Cdd:PLN02739 151 AFKDRDPACLSYSSAILHLKGYLALQAYRVAHKLWKQGRKLLALALQSRVSEVFGIDIHPAARIGKGILLDHGTGVVIGE 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 167 TAVVEDDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVGK 246
Cdd:PLN02739 231 TAVIGDRVSILHGVTLGGTGKETGDRHPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGF 310

                        250
                 ....*....|.
gi 495040456 247 PESDKPSMDMD 257
Cdd:PLN02739 311 VDEQDPSLTME 321
SATase_N smart00971
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 9-113 3.71e-60

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: 185.82  E-value: 3.71e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456     9 VWKNIKAEARQLADCEPMLASFYHATLLKHENLGSALSYMLANKLASPIMPAIAIREVVEEAYRADPEMIASAACDIQAV 88
Cdd:smart00971   1 VWQRIRAEAREAAEREPILASFLYATILNHDSLEAALAYRLANKLGNADMSADLLRELFEDAYAADPEIVEAAAADIQAV 80

                           90       100
                   ....*....|....*....|....*
gi 495040456    89 RTRDPAVDKYSTPLLYLKGFHALQA 113
Cdd:smart00971  81 YDRDPACDRYLTPLLYFKGFHALQA 105
SATase_N pfam06426
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 9-112 5.14e-58

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: 180.35  E-value: 5.14e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456    9 VWKNIKAEARQLADCEPMLASFYHATLLKHENLGSALSYMLANKLASPIMPAIAIREVVEEAYRADPEMIASAACDIQAV 88
Cdd:pfam06426   1 VWARLRAEAEEAAEREPLLASFLYATILSHDSLESALAFRLANKLANSTLPATLLRELFEDALEADPEIVEAARADLQAV 80

                          90       100
                  ....*....|....*....|....
gi 495040456   89 RTRDPAVDKYSTPLLYLKGFHALQ 112
Cdd:pfam06426  81 YERDPACDRYLTPLLYFKGFHALQ 104
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 140-240 1.92e-52

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: 166.08  E-value: 1.92e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 140 FQVDIHPAATIGRGIMLDHATGIVIGETAVVEDDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAK 219
Cdd:cd03354    1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                         90       100
                 ....*....|....*....|.
gi 495040456 220 IGAGSVVLQPVPPHTTAAGVP 240
Cdd:cd03354   81 IGANAVVTKDVPANSTVVGVP 101
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
150-252 1.81e-21

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 87.23  E-value: 1.81e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 150 IGRGIMLDHATGIVIGetavveDDVSILQSVTLGGTG-----KTSGDRHPK---IREGVMIGAGAKILGNIEVGRGAKIG 221
Cdd:COG0110   36 IGPGVTIDDPGGITIG------DNVLIGPGVTILTGNhpiddPATFPLRTGpvtIGDDVWIGAGATILPGVTIGDGAVVG 109

                         90       100       110
                 ....*....|....*....|....*....|.
gi 495040456 222 AGSVVLQPVPPHTTAAGVPARIVGKPESDKP 252
Cdd:COG0110  110 AGSVVTKDVPPYAIVAGNPARVIRKRDEEER 140
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 142-245 4.01e-19

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: 80.62  E-value: 4.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 142 VDIHPAATIGRGIMLDhaTGIVIGETAVVEDDVSILQSVTlggtgkTSGDRHP-------------KIREGVMIGAGAKI 208
Cdd:cd03358   11 VFIENDVKIGDNVKIQ--SNVSIYEGVTIEDDVFIGPNVV------FTNDLYPrskiyrkwelkgtTVKRGASIGANATI 82

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 495040456 209 LGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVG 245
Cdd:cd03358   83 LPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 149-244 2.45e-18

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: 78.27  E-value: 2.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 149 TIGRGIMLDHATGIVIGetavveDDVSILQSVTL--GGTGKTSGDRHP---------KIREGVMIGAGAKILGNIEVGRG 217
Cdd:cd04647    9 YIGPGCVISAGGGITIG------DNVLIGPNVTIydHNHDIDDPERPIeqgvtsapiVIGDDVWIGANVVILPGVTIGDG 82

                         90       100
                 ....*....|....*....|....*..
gi 495040456 218 AKIGAGSVVLQPVPPHTTAAGVPARIV 244
Cdd:cd04647   83 AVVGAGSVVTKDVPPNSIVAGNPAKVI 109
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 144-241 4.59e-18

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: 79.84  E-value: 4.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456  144 IHPAATIGRGIMLDhaTGIVIGETAVVEDDVSILQSVTLGGtgktsgdrHPKIREGVMIGAGAKILGNIEVGRGAKIGAG 223
Cdd:TIGR03570 114 INPDVRIGDNVIIN--TGAIVEHDCVIGDFVHIAPGVTLSG--------GVVIGEGVFIGAGATIIQGVTIGAGAIVGAG 183

                          90
                  ....*....|....*...
gi 495040456  224 SVVLQPVPPHTTAAGVPA 241
Cdd:TIGR03570 184 AVVTKDIPDGGVVVGVPA 201
PRK10191 PRK10191
putative acyl transferase; Provisional
 140-243 9.06e-17

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 75.31  E-value: 9.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 140 FQVDIHPAATIGRGIMLDHATGIVIGETAVVEDDVSILQSVTLGGTGKTSgDRHPKIREGVMIGAGAKILGNIEVGRGAK 219
Cdd:PRK10191  40 FGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGVTIGNRGADN-MACPHIGNGVELGANVIILGDITIGNNVT 118

                         90       100
                 ....*....|....*....|....
gi 495040456 220 IGAGSVVLQPVPPHTTAAGVPARI 243
Cdd:PRK10191 119 VGAGSVVLDSVPDNALVVGEKARV 142
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 144-240 1.23e-16

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: 75.98  E-value: 1.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 144 IHPAATIGRGIMLDhaTGIVIGETAVVEDDVSILQSVTLGGtgktsgdrHPKIREGVMIGAGAKILGNIEVGRGAKIGAG 223
Cdd:cd03360  111 INPDARIGDNVIIN--TGAVIGHDCVIGDFVHIAPGVVLSG--------GVTIGEGAFIGAGATIIQGVTIGAGAIIGAG 180

                         90
                 ....*....|....*..
gi 495040456 224 SVVLQPVPPHTTAAGVP 240
Cdd:cd03360  181 AVVTKDVPDGSVVVGNP 197
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 148-227 1.49e-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: 1.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 148 ATIGRGIMLDHatGIVIGETAVVEDDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVL 227
Cdd:cd00208    1 VFIGEGVKIHP--KAVIRGPVVIGDNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 196-244 1.60e-11

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: 61.28  E-value: 1.60e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 495040456 196 IREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIV 244
Cdd:cd03357  121 IGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 200-246 3.80e-11

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: 59.48  E-value: 3.80e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 495040456 200 VMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVGK 246
Cdd:cd03349   80 VWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRY 126
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 124-246 4.34e-10

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 58.09  E-value: 4.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 124 GRQAlaiFLQNQVSVSFQVDIHpaatIGRGIMLDHATGIVIGETAVVEDDVSILQSVTLGGTG-------KTSGDRHP-- 194
Cdd:PRK09527  59 GENA---WVEPPVYFSYGSNIH----IGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGhpvhhelRKNGEMYSfp 131

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 495040456 195 -KIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVGK 246
Cdd:PRK09527 132 iTIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIRE 184
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 135-246 5.23e-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: 53.95  E-value: 5.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 135 QVSVSFQV----DIHPAaTIGRG--------IMLDHATGIVIGetavveDDVSILQSVTL-GGTgktsgdrhpkIREGVM 201
Cdd:cd04645   23 GSSVWFGAvlrgDVNPI-RIGERtniqdgsvLHVDPGYPTIIG------DNVTVGHGAVLhGCT----------IGDNCL 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 495040456 202 IGAGAKILGNIEVGRGAKIGAGSVVL--QPVPPHTTAAGVPARIVGK 246
Cdd:cd04645   86 IGMGAIILDGAVIGKGSIVAAGSLVPpgKVIPPGSLVAGSPAKVVRE 132
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 158-244 1.39e-07

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 50.03  E-value: 1.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 158 HATGiviGETAVVEDDVSILQSVTL-GGTgktsgdrhpkIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQ--PVPPHT 234
Cdd:COG0663   65 HVDP---GYPLTIGDDVTIGHGAILhGCT----------IGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEgkVVPPGS 131

                         90
                 ....*....|
gi 495040456 235 TAAGVPARIV 244
Cdd:COG0663  132 LVVGSPAKVV 141
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 148-244 1.62e-07

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: 48.76  E-value: 1.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 148 ATIGRGIMLDHATGIVIGETAVVEDDVSILqsvtlGGTGKTSGDRHP------KIREGVMIGAGAKILGNIEVGRGAKIG 221
Cdd:cd05825   10 SWIGEGVWIYNLAPVTIGSDACISQGAYLC-----TGSHDYRSPAFPlitapiVIGDGAWVAAEAFVGPGVTIGEGAVVG 84

                         90       100
                 ....*....|....*....|...
gi 495040456 222 AGSVVLQPVPPHTTAAGVPARIV 244
Cdd:cd05825   85 ARSVVVRDLPAWTVYAGNPAVPV 107
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 169-245 5.92e-07

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: 49.25  E-value: 5.92e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495040456 169 VVEDDVSILQSVTLGGtgktsgdrHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVG 245
Cdd:COG1043  124 VVGNNVILANNATLAG--------HVEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDVPPYVLAAGNPARLRG 192
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
169-245 6.96e-07

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 49.33  E-value: 6.96e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495040456 169 VVEDDVSILQSVTLGGtgktsgdrHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVG 245
Cdd:PRK05289 125 VVGNHVILANNATLAG--------HVEVGDYAIIGGLTAVHQFVRIGAHAMVGGMSGVSQDVPPYVLAEGNPARLRG 193
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 162-246 1.57e-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: 1.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 162 IVIGETAVVEDDVSILQS----------VTLGGTGKTSGdrhPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQ--P 229
Cdd:cd04650   40 IYIGKYSNVQENVSIHTDhgypteigdyVTIGHNAVVHG---AKVGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTPgkE 116

                         90
                 ....*....|....*..
gi 495040456 230 VPPHTTAAGVPARIVGK 246
Cdd:cd04650  117 IPDYSLVLGVPAKVVRK 133
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 169-245 2.55e-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: 47.43  E-value: 2.55e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495040456 169 VVEDDVSILQSVTLGGtgktsgdrHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVG 245
Cdd:cd03351  122 VIGNNVILANNATLAG--------HVEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARLRG 190
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 149-242 2.96e-06

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 46.63  E-value: 2.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 149 TIGRGIMLDH----ATGIVIGETAVVEDDVSILQSVTLGgtgktsgdrhpkirEGVMIGAGAKILGNIEVGRGAKIGAGS 224
Cdd:cd03352  116 VIGDGTKIDNlvqiAHNVRIGENCLIAAQVGIAGSTTIG--------------DNVIIGGQVGIAGHLTIGDGVVIGAGS 181

                         90
                 ....*....|....*...
gi 495040456 225 VVLQPVPPHTTAAGVPAR 242
Cdd:cd03352  182 GVTSIVPPGEYVSGTPAQ 199
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 195-242 6.24e-06

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: 46.55  E-value: 6.24e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 495040456 195 KIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPAR 242
Cdd:COG1044  260 KIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSGSPAQ 307
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 148-244 1.03e-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: 44.29  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 148 ATIGRGIMLDhaTGIVIGETAVVEDDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVL 227
Cdd:cd03350   32 AYVDEGTMVD--SWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLT 109

                         90       100
                 ....*....|....*....|...
gi 495040456 228 QPVPPHTTAAG------VPARIV 244
Cdd:cd03350  110 QSTPIYDRETGeiyygrVPPGSV 132
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 132-244 1.63e-05

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 45.52  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 132 LQNQVSVSFQVDIHpAATIGRGIMLDHATgiVIGEtAVVEDDVSI-LQSVTLGGTGKTsgdRHPK-IREGVMIGAGAKIL 209
Cdd:PRK14357 327 LKKSVKIGNFVEIK-KSTIGENTKAQHLT--YLGD-ATVGKNVNIgAGTITCNYDGKK---KNPTfIEDGAFIGSNSSLV 399

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 495040456 210 GNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIV 244
Cdd:PRK14357 400 APVRIGKGALIGAGSVITEDVPPYSLALGRARQIV 434
PRK10502 PRK10502
putative acyl transferase; Provisional
 150-244 2.88e-05

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 43.78  E-value: 2.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 150 IGRGIMLDHATGIVIGETAVVEDDVSIL------QSVTLGGTGKtsgdrhP-KIREGVMIGAGAKILGNIEVGRGAKIGA 222
Cdd:PRK10502  80 IGDDVWLYNLGEITIGAHCVISQKSYLCtgshdySDPHFDLNTA------PiVIGEGCWLAADVFVAPGVTIGSGAVVGA 153

                         90       100
                 ....*....|....*....|..
gi 495040456 223 GSVVLQPVPPHTTAAGVPARIV 244
Cdd:PRK10502 154 RSSVFKSLPANTICRGNPAVPI 175
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 128-226 2.99e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 44.74  E-value: 2.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 128 LAIFLQNQVSVSFQVDIHPAAtigrgimldhatgiVIGETAVVEDDVSILQSVTLGgtgktsgdRHPKIREGVMIGAGAK 207
Cdd:PRK00892  87 LAQLFDPPATPSPAAGIHPSA--------------VIDPSAKIGEGVSIGPNAVIG--------AGVVIGDGVVIGAGAV 144

                         90
                 ....*....|....*....
gi 495040456 208 ILGNIEVGRGAKIGAGSVV 226
Cdd:PRK00892 145 IGDGVKIGADCRLHANVTI 163
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
193-222 3.33e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 40.01  E-value: 3.33e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 495040456  193 HPKIREGVMIGAGAKILGNIEVGRGAKIGA 222
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 195-246 3.57e-05

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 43.71  E-value: 3.57e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 495040456 195 KIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVGK 246
Cdd:PRK09677 132 VIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKK 183
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 126-225 7.99e-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: 43.47  E-value: 7.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 126 QALAIFLQNQVsvsFQVDIHPAAtigrgimldhatgiVIGETAVVEDDVSILQSVTlggtgktsgdrhpkIREGVMIGAG 205
Cdd:COG1044   84 KLLQLFYPPPA---PAPGIHPSA--------------VIDPSAKIGEGVSIGPFAV--------------IGAGVVIGDG 132

                         90       100
                 ....*....|....*....|
gi 495040456 206 AKILGNIEVGRGAKIGAGSV 225
Cdd:COG1044  133 VVIGPGVVIGDGVVIGDDCV 152
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 150-242 1.28e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 42.82  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 150 IGRGIMLDH----ATGIVIGETAVVEDDVSILQSVTLGgtgktsgdrhpkirEGVMIGAGAKILGNIEVGRGAKIGAGSV 225
Cdd:PRK00892 228 IGEGVKIDNlvqiAHNVVIGRHTAIAAQVGIAGSTKIG--------------RYCMIGGQVGIAGHLEIGDGVTITAMSG 293

                         90
                 ....*....|....*...
gi 495040456 226 VLQPVP-PHTTAAGVPAR 242
Cdd:PRK00892 294 VTKSIPePGEYSSGIPAQ 311
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 154-246 2.73e-04

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 40.95  E-value: 2.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 154 IMLDhATGIVIGETAVVEDDVSILQSV-TLGGTGKTSGDRHPK---IREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQP 229
Cdd:PRK10092  87 VMLD-VCPIRIGDNCMLAPGVHIYTAThPLDPVARNSGAELGKpvtIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKD 165

                         90
                 ....*....|....*..
gi 495040456 230 VPPHTTAAGVPARIVGK 246
Cdd:PRK10092 166 VPDNVVVGGNPARIIKK 182
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 148-241 4.48e-04

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: 41.27  E-value: 4.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456  148 ATIGRGIMLDhatGIVIGETAVVE--DDV-----SILQSVTL-GGTGKTSGDRhpkIREGVMIGAGAKILGNIEVGRGAK 219
Cdd:TIGR02353 598 VKIGRGVYID---GTDLTERDLVTigDDStlnegSVIQTHLFeDRVMKSDTVT---IGDGATLGPGAIVLYGVVMGEGSV 671

                          90       100
                  ....*....|....*....|....
gi 495040456  220 IGAGSVVL--QPVPPHTTAAGVPA 241
Cdd:TIGR02353 672 LGPDSLVMkgEEVPAHTRWRGNPA 695
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 144-226 8.77e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 40.12  E-value: 8.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 144 IHPAATIGRGIMLDHatGIVIGETAVVEDDVSILQSVTLGgtgktsgdRHPKIREGVMIGAGAKILGNIEVGRGAKIGAG 223
Cdd:PRK00892 109 IDPSAKIGEGVSIGP--NAVIGAGVVIGDGVVIGAGAVIG--------DGVKIGADCRLHANVTIYHAVRIGNRVIIHSG 178


                 ...
gi 495040456 224 SVV 226
Cdd:PRK00892 179 AVI 181
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 195-236 9.15e-04

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: 39.33  E-value: 9.15e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 495040456 195 KIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTA 236
Cdd:cd03353  146 VIGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGALA 187
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 148-246 1.12e-03

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: 40.12  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456  148 ATIGRGIMLD----HATGIV-IGETAVVEDDVSILQSVTLGGTGKTSgdrHPKIREGVMIGAGAKILGNIEVGRGAKIGA 222
Cdd:TIGR02353 113 AKIGKGVDIGslppVCTDLLtIGAGTIVRKEVMLLGYRAERGRLHTG---PVTLGRDAFIGTRSTLDIDTSIGDGAQLGH 189

                          90       100
                  ....*....|....*....|....*.
gi 495040456  223 GSVVL--QPVPPHTTAAGVPARIVGK 246
Cdd:TIGR02353 190 GSALQggQSIPDGERWHGSPAQKTGA 215
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 162-254 4.61e-03

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


Pssm-ID: 100049 [Multi-domain]  Cd Length: 161  Bit Score: 36.81  E-value: 4.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 162 IVIGETAVVEDDVSI---LQSVTLG-----GTG-----------KTSGDRHPKIREGVMIGAG-----AKILGNIEVGRG 217
Cdd:cd03359   22 IVLNGKTIIQSDVIIrgdLATVSIGrycilSEGcvirppfkkfsKGVAFFPLHIGDYVFIGENcvvnaAQIGSYVHIGKN 101

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 495040456 218 AKIGAGSV-----------VLQP---VPPHTTAAGVPARIVGK-PESDKPSM 254
Cdd:cd03359  102 CVIGRRCIikdcvkildgtVVPPdtvIPPYSVVSGRPARFIGElPECTQELM 153
CcmA COG1664
Cytoskeletal protein CcmA, bactofilin family [Cytoskeleton];
162-241 7.49e-03

Cytoskeletal protein CcmA, bactofilin family [Cytoskeleton];


Pssm-ID: 441270 [Multi-domain]  Cd Length: 129  Bit Score: 35.65  E-value: 7.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 162 IVIGETAVVEDDVSIlQSVTLGGTGKtsGDRHpkIREGVMIGAGAKILGNIEVGR-----GAKIgAGSVVLQPVPPHTTA 236
Cdd:COG1664   49 LVIGEGGVVEGDIEA-DNVVINGTVE--GNIT--ASEKLELLSTARVEGDITAGSleieeGAVF-EGKCEMGEDEAAPAA 122


                 ....*
gi 495040456 237 AGVPA 241
Cdd:COG1664  123 SPAPA 127
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 144-226 8.78e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 36.92  E-value: 8.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495040456 144 IHPAATIGRGIMLdhATGIVIGETAVVEDDVSIlqsvtlggtgktsGDrhpkireGVMIGAGAKILGNIEVGRGAKIGAG 223
Cdd:PRK12461   2 IHPTAVIDPSAKL--GSGVEIGPFAVIGANVEI-------------GD-------GTWIGPHAVILGPTRIGKNNKIHQG 59


                 ...
gi 495040456 224 SVV 226
Cdd:PRK12461  60 AVV 62
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 202-236 9.34e-03

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 37.31  E-value: 9.34e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 495040456 202 IGAGAKILGN------IEVGRGAKIGAGSVVLQPVPPHTTA 236
Cdd:COG1207  397 IGDGAFIGSNtnlvapVTIGDGATIGAGSTITKDVPAGALA 437
 
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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