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Conserved domains on  [gi|489054208|ref|WP_002964384|]
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MULTISPECIES: serine O-acetyltransferase [Brucella]

Protein Classification

LbetaH domain-containing protein( domain architecture ID 372)

LbetaH (left-handed parallel beta-helix) domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LbetaH super family cl00160
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 14-274 4.77e-122

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.


The actual alignment was detected with superfamily member PRK11132:

Pssm-ID: 469633 [Multi-domain]  Cd Length: 273  Bit Score: 349.38  E-value: 4.77e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208  14 DQVDPIWHSIRAEAEEATRNDPVLGAFLYATILNQPSLEEAVMHRIAERLGHPDVSADILRQTFDTMLEANPEWSHVLRV 93
Cdd:PRK11132   4 EELEIVWNNIKAEARALADCEPMLASFYHATLLKHENLGSALSYMLANKLASPIMPAIAIREVVEEAYAADPEMIASAAC 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208  94 DIQAVYDRDPAYSRFMDPVLYLKGFHAIQTHRLAHWLYKQGRKDFAYYLQSRSSSIFQTDIHPAARLGSGLFLDHATGLV 173
Cdd:PRK11132  84 DIQAVRTRDPAVDKYSTPLLYLKGFHALQAYRIGHWLWNQGRRALAIYLQNQISVAFQVDIHPAAKIGRGIMLDHATGIV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208 174 VGETAVVEDNVSILHGVTLGGTGKSSGDRHPKIRQGVLIGAGAKILGNIQVGQCSKIAAGSVVLKSVPHNVTVAGVPARI 253
Cdd:PRK11132 164 IGETAVIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARI 243

                        250       260       270
                 ....*....|....*....|....*....|
gi 489054208 254 IGETGCTEPSRVMDQ---------MLGDGI 274
Cdd:PRK11132 244 VGKPESDKPSMDMDQhfnginhtfEYGDGI 273
 
Name Accession Description Interval E-value
cysE PRK11132
serine acetyltransferase; Provisional
 14-274 4.77e-122

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 349.38  E-value: 4.77e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208  14 DQVDPIWHSIRAEAEEATRNDPVLGAFLYATILNQPSLEEAVMHRIAERLGHPDVSADILRQTFDTMLEANPEWSHVLRV 93
Cdd:PRK11132   4 EELEIVWNNIKAEARALADCEPMLASFYHATLLKHENLGSALSYMLANKLASPIMPAIAIREVVEEAYAADPEMIASAAC 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208  94 DIQAVYDRDPAYSRFMDPVLYLKGFHAIQTHRLAHWLYKQGRKDFAYYLQSRSSSIFQTDIHPAARLGSGLFLDHATGLV 173
Cdd:PRK11132  84 DIQAVRTRDPAVDKYSTPLLYLKGFHALQAYRIGHWLWNQGRRALAIYLQNQISVAFQVDIHPAAKIGRGIMLDHATGIV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208 174 VGETAVVEDNVSILHGVTLGGTGKSSGDRHPKIRQGVLIGAGAKILGNIQVGQCSKIAAGSVVLKSVPHNVTVAGVPARI 253
Cdd:PRK11132 164 IGETAVIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARI 243

                        250       260       270
                 ....*....|....*....|....*....|
gi 489054208 254 IGETGCTEPSRVMDQ---------MLGDGI 274
Cdd:PRK11132 244 VGKPESDKPSMDMDQhfnginhtfEYGDGI 273
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 91-259 4.52e-99

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: 287.36  E-value: 4.52e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208  91 LRVDIQAVYDRDPAYSRFMDPVLYLKGFHAIQTHRLAHWLYKQGRKDFAYYLQSRSSSIFQTDIHPAARLGSGLFLDHAT 170
Cdd:COG1045    5 LREDIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHPGATIGRGFFIDHGT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208 171 GLVVGETAVVEDNVSILHGVTLGGTGKSSGDRHPKIRQGVLIGAGAKILGNIQVGQCSKIAAGSVVLKSVPHNVTVAGVP 250
Cdd:COG1045   85 GVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVP 164


                 ....*....
gi 489054208 251 ARIIGETGC 259
Cdd:COG1045  165 ARIVKRKGS 173
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 91-252 8.18e-87

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


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 255.68  E-value: 8.18e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208   91 LRVDIQAVYDRDPAYSRFMDPVLYLKGFHAIQTHRLAHWLYKQGRKDFAYYLQSRSSSIFQTDIHPAARLGSGLFLDHAT 170
Cdd:TIGR01172   1 IREDIRAVRERDPAARSYLEVLLYYPGFHALWAYRFAHFLWKRGFKFLARLLSNFIRVLTGVDIHPGARIGRGVFIDHGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208  171 GLVVGETAVVEDNVSILHGVTLGGTGKSSGDRHPKIRQGVLIGAGAKILGNIQVGQCSKIAAGSVVLKSVPHNVTVAGVP 250
Cdd:TIGR01172  81 GVVIGETAVIGDDVTIYHGVTLGGTGKEKGKRHPTIGEGVMIGAGAKVLGNIEVGENAKIGANSVVLKDVPPGATVVGVP 160


                  ..
gi 489054208  251 AR 252
Cdd:TIGR01172 161 AR 162
SATase_N smart00971
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 19-123 2.44e-56

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: 176.19  E-value: 2.44e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208    19 IWHSIRAEAEEATRNDPVLGAFLYATILNQPSLEEAVMHRIAERLGHPDVSADILRQTFDTMLEANPEWSHVLRVDIQAV 98
Cdd:smart00971   1 VWQRIRAEAREAAEREPILASFLYATILNHDSLEAALAYRLANKLGNADMSADLLRELFEDAYAADPEIVEAAAADIQAV 80

                           90       100
                   ....*....|....*....|....*
gi 489054208    99 YDRDPAYSRFMDPVLYLKGFHAIQT 123
Cdd:smart00971  81 YDRDPACDRYLTPLLYFKGFHALQA 105
SATase_N pfam06426
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 19-122 3.26e-51

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: 163.02  E-value: 3.26e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208   19 IWHSIRAEAEEATRNDPVLGAFLYATILNQPSLEEAVMHRIAERLGHPDVSADILRQTFDTMLEANPEWSHVLRVDIQAV 98
Cdd:pfam06426   1 VWARLRAEAEEAAEREPLLASFLYATILSHDSLESALAFRLANKLANSTLPATLLRELFEDALEADPEIVEAARADLQAV 80

                          90       100
                  ....*....|....*....|....
gi 489054208   99 YDRDPAYSRFMDPVLYLKGFHAIQ 122
Cdd:pfam06426  81 YERDPACDRYLTPLLYFKGFHALQ 104
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 150-250 1.83e-49

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: 158.37  E-value: 1.83e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208 150 FQTDIHPAARLGSGLFLDHATGLVVGETAVVEDNVSILHGVTLGGTGKSSGDRHPKIRQGVLIGAGAKILGNIQVGQCSK 229
Cdd:cd03354    1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                         90       100
                 ....*....|....*....|.
gi 489054208 230 IAAGSVVLKSVPHNVTVAGVP 250
Cdd:cd03354   81 IGANAVVTKDVPANSTVVGVP 101
 
Name Accession Description Interval E-value
cysE PRK11132
serine acetyltransferase; Provisional
 14-274 4.77e-122

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 349.38  E-value: 4.77e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208  14 DQVDPIWHSIRAEAEEATRNDPVLGAFLYATILNQPSLEEAVMHRIAERLGHPDVSADILRQTFDTMLEANPEWSHVLRV 93
Cdd:PRK11132   4 EELEIVWNNIKAEARALADCEPMLASFYHATLLKHENLGSALSYMLANKLASPIMPAIAIREVVEEAYAADPEMIASAAC 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208  94 DIQAVYDRDPAYSRFMDPVLYLKGFHAIQTHRLAHWLYKQGRKDFAYYLQSRSSSIFQTDIHPAARLGSGLFLDHATGLV 173
Cdd:PRK11132  84 DIQAVRTRDPAVDKYSTPLLYLKGFHALQAYRIGHWLWNQGRRALAIYLQNQISVAFQVDIHPAAKIGRGIMLDHATGIV 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208 174 VGETAVVEDNVSILHGVTLGGTGKSSGDRHPKIRQGVLIGAGAKILGNIQVGQCSKIAAGSVVLKSVPHNVTVAGVPARI 253
Cdd:PRK11132 164 IGETAVIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARI 243

                        250       260       270
                 ....*....|....*....|....*....|
gi 489054208 254 IGETGCTEPSRVMDQ---------MLGDGI 274
Cdd:PRK11132 244 VGKPESDKPSMDMDQhfnginhtfEYGDGI 273
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 91-259 4.52e-99

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: 287.36  E-value: 4.52e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208  91 LRVDIQAVYDRDPAYSRFMDPVLYLKGFHAIQTHRLAHWLYKQGRKDFAYYLQSRSSSIFQTDIHPAARLGSGLFLDHAT 170
Cdd:COG1045    5 LREDIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHPGATIGRGFFIDHGT 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208 171 GLVVGETAVVEDNVSILHGVTLGGTGKSSGDRHPKIRQGVLIGAGAKILGNIQVGQCSKIAAGSVVLKSVPHNVTVAGVP 250
Cdd:COG1045   85 GVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVP 164


                 ....*....
gi 489054208 251 ARIIGETGC 259
Cdd:COG1045  165 ARIVKRKGS 173
PLN02739 PLN02739
serine acetyltransferase
 17-267 2.93e-93

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 279.23  E-value: 2.93e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208  17 DPIWHSIRAEAEEATRNDPVLGAFLYATILNQPSLEEAVMHRIAERLGHPDVSADILRQTFDTMLEANPEWSHVLRVDIQ 96
Cdd:PLN02739  71 DPIWDSIREEAKLEAEEEPVLSSFLYASILSHDCLEQALSFVLANRLQNPTLLATQLMDIFCNVMVHDRGIQSSIRLDVQ 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208  97 AVYDRDPAYSRFMDPVLYLKGFHAIQTHRLAHWLYKQGRKDFAYYLQSRSSSIFQTDIHPAARLGSGLFLDHATGLVVGE 176
Cdd:PLN02739 151 AFKDRDPACLSYSSAILHLKGYLALQAYRVAHKLWKQGRKLLALALQSRVSEVFGIDIHPAARIGKGILLDHGTGVVIGE 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208 177 TAVVEDNVSILHGVTLGGTGKSSGDRHPKIRQGVLIGAGAKILGNIQVGQCSKIAAGSVVLKSVPHNVTVAGVPARIIGE 256
Cdd:PLN02739 231 TAVIGDRVSILHGVTLGGTGKETGDRHPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGF 310

                        250
                 ....*....|.
gi 489054208 257 TGCTEPSRVMD 267
Cdd:PLN02739 311 VDEQDPSLTME 321
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 91-252 8.18e-87

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


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 255.68  E-value: 8.18e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208   91 LRVDIQAVYDRDPAYSRFMDPVLYLKGFHAIQTHRLAHWLYKQGRKDFAYYLQSRSSSIFQTDIHPAARLGSGLFLDHAT 170
Cdd:TIGR01172   1 IREDIRAVRERDPAARSYLEVLLYYPGFHALWAYRFAHFLWKRGFKFLARLLSNFIRVLTGVDIHPGARIGRGVFIDHGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208  171 GLVVGETAVVEDNVSILHGVTLGGTGKSSGDRHPKIRQGVLIGAGAKILGNIQVGQCSKIAAGSVVLKSVPHNVTVAGVP 250
Cdd:TIGR01172  81 GVVIGETAVIGDDVTIYHGVTLGGTGKEKGKRHPTIGEGVMIGAGAKVLGNIEVGENAKIGANSVVLKDVPPGATVVGVP 160


                  ..
gi 489054208  251 AR 252
Cdd:TIGR01172 161 AR 162
PLN02357 PLN02357
serine acetyltransferase
 13-255 2.48e-86

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 261.74  E-value: 2.48e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208  13 LDQVDPIWHSIRAEAEEATRNDPVLGAFLYATILNQPSLEEAVMHRIAERLGHPDVSADILRQTFDTMLEANPEWSHVLR 92
Cdd:PLN02357  88 LDRDDDVWLKIQEEAKSDVEQEPILSSYYYASILSHRSLESALANHLSVKLSNLNLPSNTLFDLFIGVLEESPEIIESVK 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208  93 VDIQAVYDRDPAYSRFMDPVLYLKGFHAIQTHRLAHWLYKQGRKDFAYYLQSRSSSIFQTDIHPAARLGSGLFLDHATGL 172
Cdd:PLN02357 168 QDLRAVKERDPACISYVHCFLNFKGFLACQAHRIAHKLWTQGRKILALLIQNRVSEAFAVDIHPGAKIGQGILLDHATGV 247

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208 173 VVGETAVVEDNVSILHGVTLGGTGKSSGDRHPKIRQGVLIGAGAKILGNIQVGQCSKIAAGSVVLKSVPHNVTVAGVPAR 252
Cdd:PLN02357 248 VIGETAVVGNNVSILHNVTLGGTGKQSGDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPAR 327


                 ...
gi 489054208 253 IIG 255
Cdd:PLN02357 328 LIG 330
PLN02694 PLN02694
serine O-acetyltransferase
 19-264 4.81e-83

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 251.10  E-value: 4.81e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208  19 IWHSIRAEAEEATRNDPVLGAFLYATILNQPSLEEAVMHRIAERLGHPDVSADILRQTFDTMLEANPEWSHVLRVDIQAV 98
Cdd:PLN02694  28 LWTQIKAEARRDAESEPALASYLYSTILSHSSLERSLSFHLGNKLCSSTLLSTLLYDLFLNTFSSDPSLRAATVADLRAA 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208  99 YDRDPAYSRFMDPVLYLKGFHAIQTHRLAHWLYKQGRKDFAYYLQSRSSSIFQTDIHPAARLGSGLFLDHATGLVVGETA 178
Cdd:PLN02694 108 RVRDPACVSFSHCLLNYKGFLACQAHRVAHKLWTQSRRPLALALHSRISDVFAVDIHPAAKIGKGILFDHATGVVIGETA 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208 179 VVEDNVSILHGVTLGGTGKSSGDRHPKIRQGVLIGAGAKILGNIQVGQCSKIAAGSVVLKSVPHNVTVAGVPARIIGetG 258
Cdd:PLN02694 188 VIGNNVSILHHVTLGGTGKACGDRHPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLVG--G 265


                 ....*.
gi 489054208 259 CTEPSR 264
Cdd:PLN02694 266 KEKPAK 271
SATase_N smart00971
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 19-123 2.44e-56

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: 176.19  E-value: 2.44e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208    19 IWHSIRAEAEEATRNDPVLGAFLYATILNQPSLEEAVMHRIAERLGHPDVSADILRQTFDTMLEANPEWSHVLRVDIQAV 98
Cdd:smart00971   1 VWQRIRAEAREAAEREPILASFLYATILNHDSLEAALAYRLANKLGNADMSADLLRELFEDAYAADPEIVEAAAADIQAV 80

                           90       100
                   ....*....|....*....|....*
gi 489054208    99 YDRDPAYSRFMDPVLYLKGFHAIQT 123
Cdd:smart00971  81 YDRDPACDRYLTPLLYFKGFHALQA 105
SATase_N pfam06426
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 19-122 3.26e-51

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: 163.02  E-value: 3.26e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208   19 IWHSIRAEAEEATRNDPVLGAFLYATILNQPSLEEAVMHRIAERLGHPDVSADILRQTFDTMLEANPEWSHVLRVDIQAV 98
Cdd:pfam06426   1 VWARLRAEAEEAAEREPLLASFLYATILSHDSLESALAFRLANKLANSTLPATLLRELFEDALEADPEIVEAARADLQAV 80

                          90       100
                  ....*....|....*....|....
gi 489054208   99 YDRDPAYSRFMDPVLYLKGFHAIQ 122
Cdd:pfam06426  81 YERDPACDRYLTPLLYFKGFHALQ 104
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 150-250 1.83e-49

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: 158.37  E-value: 1.83e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208 150 FQTDIHPAARLGSGLFLDHATGLVVGETAVVEDNVSILHGVTLGGTGKSSGDRHPKIRQGVLIGAGAKILGNIQVGQCSK 229
Cdd:cd03354    1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                         90       100
                 ....*....|....*....|.
gi 489054208 230 IAAGSVVLKSVPHNVTVAGVP 250
Cdd:cd03354   81 IGANAVVTKDVPANSTVVGVP 101
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 133-251 1.97e-17

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: 78.30  E-value: 1.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208  133 QGRKDFAYYLQSRSSSiFQTDIHPAAR------LGSGLFL-------------DHA---TGLVVGETAVVEDNVSILHGV 190
Cdd:TIGR03570  70 KLRRRLVEKLKAKGYR-FATLIHPSAIvspsasIGEGTVImagavinpdvrigDNViinTGAIVEHDCVIGDFVHIAPGV 148

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489054208  191 TLGGtgkssgdrHPKIRQGVLIGAGAKILGNIQVGQCSKIAAGSVVLKSVPHNVTVAGVPA 251
Cdd:TIGR03570 149 TLSG--------GVVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
159-256 4.58e-17

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 75.68  E-value: 4.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208 159 RLGSGLFLDHATGLVVGETAVVEDNVSILHGVTLGGTGKSSGD--------RHPKIRQGVLIGAGAKILGNIQVGQCSKI 230
Cdd:COG0110   29 TIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDpatfplrtGPVTIGDDVWIGAGATILPGVTIGDGAVV 108

                         90       100
                 ....*....|....*....|....*.
gi 489054208 231 AAGSVVLKSVPHNVTVAGVPARIIGE 256
Cdd:COG0110  109 GAGSVVTKDVPPYAIVAGNPARVIRK 134
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 174-255 1.24e-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: 74.07  E-value: 1.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208 174 VGETAVVEDNVSILHGVTL------GGTGKSSGD-RHPKIRQGVLIGAGAKILGNIQVGQCSKIAAGSVVLKSVPHNVTV 246
Cdd:cd03358   31 IYEGVTIEDDVFIGPNVVFtndlypRSKIYRKWElKGTTVKRGASIGANATILPGVTIGEYALVGAGAVVTKDVPPYALV 110


                 ....*....
gi 489054208 247 AGVPARIIG 255
Cdd:cd03358  111 VGNPARIIG 119
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 159-254 1.35e-15

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: 70.95  E-value: 1.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208 159 RLGSGLFLDHATGLVVGetavveDNVSILHGVTLGGTGKSSGDRHPKIRQG-----------VLIGAGAKILGNIQVGQC 227
Cdd:cd04647    9 YIGPGCVISAGGGITIG------DNVLIGPNVTIYDHNHDIDDPERPIEQGvtsapivigddVWIGANVVILPGVTIGDG 82

                         90       100
                 ....*....|....*....|....*..
gi 489054208 228 SKIAAGSVVLKSVPHNVTVAGVPARII 254
Cdd:cd04647   83 AVVGAGSVVTKDVPPNSIVAGNPAKVI 109
PRK10191 PRK10191
putative acyl transferase; Provisional
 149-253 3.07e-15

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 71.07  E-value: 3.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208 149 IFQTDIHPAARLGSGLFLDHATGLVVGETAVVEDNVSILHGVTLGGTGKSSgDRHPKIRQGVLIGAGAKILGNIQVGQCS 228
Cdd:PRK10191  39 FFGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGVTIGNRGADN-MACPHIGNGVELGANVIILGDITIGNNV 117

                         90       100
                 ....*....|....*....|....*
gi 489054208 229 KIAAGSVVLKSVPHNVTVAGVPARI 253
Cdd:PRK10191 118 TVGAGSVVLDSVPDNALVVGEKARV 142
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 154-250 2.82e-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: 69.44  E-value: 2.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208 154 IHPAARLGSGLFLDhaTGLVVGETAVVEDNVSILHGVTLGGtgkssgdrHPKIRQGVLIGAGAKILGNIQVGQCSKIAAG 233
Cdd:cd03360  111 INPDARIGDNVIIN--TGAVIGHDCVIGDFVHIAPGVVLSG--------GVTIGEGAFIGAGATIIQGVTIGAGAIIGAG 180

                         90
                 ....*....|....*..
gi 489054208 234 SVVLKSVPHNVTVAGVP 250
Cdd:cd03360  181 AVVTKDVPDGSVVVGNP 197
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 158-237 1.90e-12

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: 61.50  E-value: 1.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208 158 ARLGSGLFLDHATglVVGETAVVEDNVSILHGVTLGGTGKSSGDRHPKIRQGVLIGAGAKILGNIQVGQCSKIAAGSVVL 237
Cdd:cd00208    1 VFIGEGVKIHPKA--VIRGPVVIGDNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 206-254 5.27e-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: 59.74  E-value: 5.27e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 489054208 206 IRQGVLIGAGAKILGNIQVGQCSKIAAGSVVLKSVPHNVTVAGVPARII 254
Cdd:cd03357  121 IGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 168-256 1.66e-09

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 55.80  E-value: 1.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208 168 HATGlvvGETAVVEDNVSILHGVTL-GGTgkssgdrhpkIRQGVLIGAGAKILGNIQVGQCSKIAAGSVVL--KSVPHNV 244
Cdd:COG0663   65 HVDP---GYPLTIGDDVTIGHGAILhGCT----------IGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTegKVVPPGS 131

                         90
                 ....*....|..
gi 489054208 245 TVAGVPARIIGE 256
Cdd:COG0663  132 LVVGSPAKVVRE 143
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 179-256 1.07e-08

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: 52.80  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208 179 VVEDNVSILHGVTL-GGTgkssgdrhpkIRQGVLIGAGAKILGNIQVGQCSKIAAGSVVL--KSVPHNVTVAGVPARIIG 255
Cdd:cd04645   62 IIGDNVTVGHGAVLhGCT----------IGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPpgKVIPPGSLVAGSPAKVVR 131


                 .
gi 489054208 256 E 256
Cdd:cd04645  132 E 132
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 160-256 4.30e-08

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 52.31  E-value: 4.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208 160 LGSGLFLDHATGLVVGETAVVEDNVSILHGVTLGGTG-------KSSGDRHP---KIRQGVLIGAGAKILGNIQVGQCSK 229
Cdd:PRK09527  78 IGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGhpvhhelRKNGEMYSfpiTIGNNVWIGSHVVINPGVTIGDNSV 157

                         90       100
                 ....*....|....*....|....*..
gi 489054208 230 IAAGSVVLKSVPHNVTVAGVPARIIGE 256
Cdd:PRK09527 158 IGAGSVVTKDIPPNVVAAGVPCRVIRE 184
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 210-254 5.57e-07

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: 47.92  E-value: 5.57e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 489054208 210 VLIGAGAKILGNIQVGQCSKIAAGSVVLKSVPHNVTVAGVPARII 254
Cdd:cd03349   80 VWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVI 124
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 182-254 3.64e-06

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 46.34  E-value: 3.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208 182 DNVSILHGV-------TLGGTGKSSGDRHPK---IRQGVLIGAGAKILGNIQVGQCSKIAAGSVVLKSVPHNVTVAGVPA 251
Cdd:PRK10092  98 DNCMLAPGVhiytathPLDPVARNSGAELGKpvtIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPA 177


                 ...
gi 489054208 252 RII 254
Cdd:PRK10092 178 RII 180
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 205-254 9.80e-06

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 45.25  E-value: 9.80e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 489054208 205 KIRQGVLIGAGAKILGNIQVGQCSKIAAGSVVLKSVPHNVTVAGVPARII 254
Cdd:PRK09677 132 VIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKII 181
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 174-254 1.39e-05

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: 44.10  E-value: 1.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208 174 VGETAVVEDNVSIL--HG--------VTLGGTGKSSGdrhPKIRQGVLIGAGAKILGNIQVGQCSKIAAGSVVL--KSVP 241
Cdd:cd04650   42 IGKYSNVQENVSIHtdHGypteigdyVTIGHNAVVHG---AKVGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTpgKEIP 118

                         90
                 ....*....|...
gi 489054208 242 HNVTVAGVPARII 254
Cdd:cd04650  119 DYSLVLGVPAKVV 131
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 125-236 2.01e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 45.13  E-value: 2.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208 125 RLAHWLYKQGRKDFAyylqsrsssifqTDIHPAArlgsglfldhatglVVGETAVVEDNVSILHGVTLGgtgkssgdRHP 204
Cdd:PRK00892  86 RLAQLFDPPATPSPA------------AGIHPSA--------------VIDPSAKIGEGVSIGPNAVIG--------AGV 131

                         90       100       110
                 ....*....|....*....|....*....|..
gi 489054208 205 KIRQGVLIGAGAKILGNIQVGQCSKIAAGSVV 236
Cdd:PRK00892 132 VIGDGVVIGAGAVIGDGVKIGADCRLHANVTI 163
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 205-252 6.72e-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: 6.72e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 489054208 205 KIRQGVLIGAGAKILGNIQVGQCSKIAAGSVVLKSVPHNVTVAGVPAR 252
Cdd:COG1044  260 KIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSGSPAQ 307
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 182-256 1.14e-04

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: 42.01  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208 182 DN-VSILHGVTLG---------GTGKSSgdrhpKIRQGVLIGAGAKILGNIQVGQCSKIAAGSVVLKSVPHNVTVAGVPA 251
Cdd:cd03352  124 DNlVQIAHNVRIGencliaaqvGIAGST-----TIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPA 198


                 ....*
gi 489054208 252 RIIGE 256
Cdd:cd03352  199 QPHRE 203
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 158-241 3.29e-04

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


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 40.06  E-value: 3.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208 158 ARLGSGLFLDhaTGLVVGETAVVEDNVSILHGVTLGGTGKSSGDRHPKIRQGVLIGAGAKILGNIQVGQCSKIAAGSVVL 237
Cdd:cd03350   32 AYVDEGTMVD--SWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLT 109


                 ....
gi 489054208 238 KSVP 241
Cdd:cd03350  110 QSTP 113
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 206-254 3.51e-04

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: 39.13  E-value: 3.51e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 489054208 206 IRQGVLIGAGAKILGNIQVGQCSKIAAGSVVLKSVPHNVTVAGVPARII 254
Cdd:cd05825   59 IGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 182-252 4.45e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 40.89  E-value: 4.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208 182 DN-VSILHGVTLG-------GTGKSSGdrhPKIRQGVLIGAGAKILGNIQVGQCSKIAAGSVVLKSVP-HNVTVAGVPAR 252
Cdd:PRK00892 235 DNlVQIAHNVVIGrhtaiaaQVGIAGS---TKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPePGEYSSGIPAQ 311
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 175-256 8.90e-04

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


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 38.89  E-value: 8.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208 175 GETAVVEDNVSILHGVTLGGTgkssgdrhpKIRQGVLIGAGAKILGNIQVGQCSKIAAGSVVlKS---VPHNVTVAGVPA 251
Cdd:cd04745   59 GQDTVLEENGHIGHGAILHGC---------TIGRNALVGMNAVVMDGAVIGEESIVGAMAFV-KAgtvIPPRSLIAGSPA 128


                 ....*
gi 489054208 252 RIIGE 256
Cdd:cd04745  129 KVIRE 133
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 179-255 1.57e-03

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: 38.95  E-value: 1.57e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489054208 179 VVEDNVSILHGVTLGGtgkssgdrHPKIRQGVLIGAGAKILGNIQVGQCSKIAAGSVVLKSVPHNVTVAGVPARIIG 255
Cdd:cd03351  122 VIGNNVILANNATLAG--------HVEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARLRG 190
PRK10502 PRK10502
putative acyl transferase; Provisional
 206-268 2.13e-03

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 38.01  E-value: 2.13e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489054208 206 IRQGVLIGAGAKILGNIQVGQCSKIAAGSVVLKSVPHNVTVAGVPARIIGEtgctepsRVMDQ 268
Cdd:PRK10502 127 IGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIRP-------RVETE 182
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 150-236 2.13e-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: 38.85  E-value: 2.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489054208 150 FQTDIHPAArlgsglfldhatglVVGETAVVEDNVSILHGVTLGgtgkssgdRHPKIRQGVLIGAGAKILGNIQVGQCSK 229
Cdd:COG1044   95 PAPGIHPSA--------------VIDPSAKIGEGVSIGPFAVIG--------AGVVIGDGVVIGPGVVIGDGVVIGDDCV 152


                 ....*..
gi 489054208 230 IAAGSVV 236
Cdd:COG1044  153 LHPNVTI 159
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 179-255 2.74e-03

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: 38.46  E-value: 2.74e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489054208 179 VVEDNVSILHGVTLGGtgkssgdrHPKIRQGVLIGAGAKILGNIQVGQCSKIAAGSVVLKSVPHNVTVAGVPARIIG 255
Cdd:COG1043  124 VVGNNVILANNATLAG--------HVEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDVPPYVLAAGNPARLRG 192
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
179-255 6.16e-03

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 37.39  E-value: 6.16e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489054208 179 VVEDNVSILHGVTLGGtgkssgdrHPKIRQGVLIGAGAKILGNIQVGQCSKIAAGSVVLKSVPHNVTVAGVPARIIG 255
Cdd:PRK05289 125 VVGNHVILANNATLAG--------HVEVGDYAIIGGLTAVHQFVRIGAHAMVGGMSGVSQDVPPYVLAEGNPARLRG 193
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
203-232 7.10e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.46  E-value: 7.10e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 489054208  203 HPKIRQGVLIGAGAKILGNIQVGQCSKIAA 232
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 210-262 7.94e-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: 36.04  E-value: 7.94e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 489054208 210 VLIGAGAkILGN-IQVGQCSKIAAGSVVLKS--VPHNVTVAGVPARIIGETG-CTEP 262
Cdd:cd03359   96 VHIGKNC-VIGRrCIIKDCVKILDGTVVPPDtvIPPYSVVSGRPARFIGELPeCTQE 151
 
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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