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Conserved domains on  [gi|577245503|gb|EUE62396|]
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serine acetyltransferase [Staphylococcus aureus M0680]

Protein Classification

serine O-acetyltransferase( domain architecture ID 11437200)

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 COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 14-187 6.07e-106

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: 302.77  E-value: 6.07e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  14 LLKRMRDDIKMVFEQDPAARSTLEVITTYAGLHAVWSHLIAHKLYNQKKYVAARAISQISRFFTGIEIHPGAKIGKRLFI 93
Cdd:COG1045    1 MLKALREDIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHPGATIGRGFFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  94 DHGMGVVIGETCTIGDNVTIYQGVTLGGTGKERGKRHPDIGDNVLIAAGAKVLGNIKINSNVNIGANSVVLQSVPSYSTV 173
Cdd:COG1045   81 DHGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTV 160

                        170
                 ....*....|....
gi 577245503 174 VGIPGHIVKQDGVR 187
Cdd:COG1045  161 VGVPARIVKRKGSK 174
 
Name Accession Description Interval E-value
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 14-187 6.07e-106

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: 302.77  E-value: 6.07e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  14 LLKRMRDDIKMVFEQDPAARSTLEVITTYAGLHAVWSHLIAHKLYNQKKYVAARAISQISRFFTGIEIHPGAKIGKRLFI 93
Cdd:COG1045    1 MLKALREDIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHPGATIGRGFFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  94 DHGMGVVIGETCTIGDNVTIYQGVTLGGTGKERGKRHPDIGDNVLIAAGAKVLGNIKINSNVNIGANSVVLQSVPSYSTV 173
Cdd:COG1045   81 DHGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTV 160

                        170
                 ....*....|....
gi 577245503 174 VGIPGHIVKQDGVR 187
Cdd:COG1045  161 VGVPARIVKRKGSK 174
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 18-178 1.98e-94

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


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 273.02  E-value: 1.98e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503   18 MRDDIKMVFEQDPAARSTLEVITTYAGLHAVWSHLIAHKLYNQKKYVAARAISQISRFFTGIEIHPGAKIGKRLFIDHGM 97
Cdd:TIGR01172   1 IREDIRAVRERDPAARSYLEVLLYYPGFHALWAYRFAHFLWKRGFKFLARLLSNFIRVLTGVDIHPGARIGRGVFIDHGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503   98 GVVIGETCTIGDNVTIYQGVTLGGTGKERGKRHPDIGDNVLIAAGAKVLGNIKINSNVNIGANSVVLQSVPSYSTVVGIP 177
Cdd:TIGR01172  81 GVVIGETAVIGDDVTIYHGVTLGGTGKEKGKRHPTIGEGVMIGAGAKVLGNIEVGENAKIGANSVVLKDVPPGATVVGVP 160


                  .
gi 577245503  178 G 178
Cdd:TIGR01172 161 A 161
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 77-177 3.73e-55

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


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 171.47  E-value: 3.73e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  77 TGIEIHPGAKIGKRLFIDHGMGVVIGETCTIGDNVTIYQGVTLGGTGKERGKRHPDIGDNVLIAAGAKVLGNIKINSNVN 156
Cdd:cd03354    1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                         90       100
                 ....*....|....*....|.
gi 577245503 157 IGANSVVLQSVPSYSTVVGIP 177
Cdd:cd03354   81 IGANAVVTKDVPANSTVVGVP 101
cysE PRK11132
serine acetyltransferase; Provisional
 21-184 5.20e-54

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 174.11  E-value: 5.20e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  21 DIKMVFEQDPAARSTLEVITTYAGLHAVWSHLIAHKLYNQKKYvaARAI---SQISRFFtGIEIHPGAKIGKRLFIDHGM 97
Cdd:PRK11132  84 DIQAVRTRDPAVDKYSTPLLYLKGFHALQAYRIGHWLWNQGRR--ALAIylqNQISVAF-QVDIHPAAKIGRGIMLDHAT 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  98 GVVIGETCTIGDNVTIYQGVTLGGTGKERGKRHPDIGDNVLIAAGAKVLGNIKINSNVNIGANSVVLQSVPSYSTVVGIP 177
Cdd:PRK11132 161 GIVIGETAVIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVP 240


                 ....*..
gi 577245503 178 GHIVKQD 184
Cdd:PRK11132 241 ARIVGKP 247
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
133-159 2.60e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 34.23  E-value: 2.60e-03
                          10        20
                  ....*....|....*....|....*..
gi 577245503  133 IGDNVLIAAGAKVLGNIKINSNVNIGA 159
Cdd:pfam00132   4 IGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 14-187 6.07e-106

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: 302.77  E-value: 6.07e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  14 LLKRMRDDIKMVFEQDPAARSTLEVITTYAGLHAVWSHLIAHKLYNQKKYVAARAISQISRFFTGIEIHPGAKIGKRLFI 93
Cdd:COG1045    1 MLKALREDIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHPGATIGRGFFI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  94 DHGMGVVIGETCTIGDNVTIYQGVTLGGTGKERGKRHPDIGDNVLIAAGAKVLGNIKINSNVNIGANSVVLQSVPSYSTV 173
Cdd:COG1045   81 DHGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTV 160

                        170
                 ....*....|....
gi 577245503 174 VGIPGHIVKQDGVR 187
Cdd:COG1045  161 VGVPARIVKRKGSK 174
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 18-178 1.98e-94

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


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 273.02  E-value: 1.98e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503   18 MRDDIKMVFEQDPAARSTLEVITTYAGLHAVWSHLIAHKLYNQKKYVAARAISQISRFFTGIEIHPGAKIGKRLFIDHGM 97
Cdd:TIGR01172   1 IREDIRAVRERDPAARSYLEVLLYYPGFHALWAYRFAHFLWKRGFKFLARLLSNFIRVLTGVDIHPGARIGRGVFIDHGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503   98 GVVIGETCTIGDNVTIYQGVTLGGTGKERGKRHPDIGDNVLIAAGAKVLGNIKINSNVNIGANSVVLQSVPSYSTVVGIP 177
Cdd:TIGR01172  81 GVVIGETAVIGDDVTIYHGVTLGGTGKEKGKRHPTIGEGVMIGAGAKVLGNIEVGENAKIGANSVVLKDVPPGATVVGVP 160


                  .
gi 577245503  178 G 178
Cdd:TIGR01172 161 A 161
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 77-177 3.73e-55

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


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 171.47  E-value: 3.73e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  77 TGIEIHPGAKIGKRLFIDHGMGVVIGETCTIGDNVTIYQGVTLGGTGKERGKRHPDIGDNVLIAAGAKVLGNIKINSNVN 156
Cdd:cd03354    1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                         90       100
                 ....*....|....*....|.
gi 577245503 157 IGANSVVLQSVPSYSTVVGIP 177
Cdd:cd03354   81 IGANAVVTKDVPANSTVVGVP 101
cysE PRK11132
serine acetyltransferase; Provisional
 21-184 5.20e-54

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 174.11  E-value: 5.20e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  21 DIKMVFEQDPAARSTLEVITTYAGLHAVWSHLIAHKLYNQKKYvaARAI---SQISRFFtGIEIHPGAKIGKRLFIDHGM 97
Cdd:PRK11132  84 DIQAVRTRDPAVDKYSTPLLYLKGFHALQAYRIGHWLWNQGRR--ALAIylqNQISVAF-QVDIHPAAKIGRGIMLDHAT 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  98 GVVIGETCTIGDNVTIYQGVTLGGTGKERGKRHPDIGDNVLIAAGAKVLGNIKINSNVNIGANSVVLQSVPSYSTVVGIP 177
Cdd:PRK11132 161 GIVIGETAVIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVP 240


                 ....*..
gi 577245503 178 GHIVKQD 184
Cdd:PRK11132 241 ARIVGKP 247
PLN02357 PLN02357
serine acetyltransferase
 3-181 2.04e-51

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 170.06  E-value: 2.04e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503   3 LRSSIIEEEMILLKRMRDDIKMVFEQDPAARSTLEVITTYAGLHAVWSHLIAHKLYNQKKYVAARAI-SQISRFFtGIEI 81
Cdd:PLN02357 151 LFIGVLEESPEIIESVKQDLRAVKERDPACISYVHCFLNFKGFLACQAHRIAHKLWTQGRKILALLIqNRVSEAF-AVDI 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  82 HPGAKIGKRLFIDHGMGVVIGETCTIGDNVTIYQGVTLGGTGKERGKRHPDIGDNVLIAAGAKVLGNIKINSNVNIGANS 161
Cdd:PLN02357 230 HPGAKIGQGILLDHATGVVIGETAVVGNNVSILHNVTLGGTGKQSGDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGS 309

                        170       180
                 ....*....|....*....|
gi 577245503 162 VVLQSVPSYSTVVGIPGHIV 181
Cdd:PLN02357 310 VVLKDVPPRTTAVGNPARLI 329
PLN02739 PLN02739
serine acetyltransferase
 18-182 3.16e-51

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 169.45  E-value: 3.16e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  18 MRDDIKMVFEQDPAARSTLEVITTYAGLHAVWSHLIAHKLYNQKKYVAARAI-SQISRFFtGIEIHPGAKIGKRLFIDHG 96
Cdd:PLN02739 145 IRLDVQAFKDRDPACLSYSSAILHLKGYLALQAYRVAHKLWKQGRKLLALALqSRVSEVF-GIDIHPAARIGKGILLDHG 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  97 MGVVIGETCTIGDNVTIYQGVTLGGTGKERGKRHPDIGDNVLIAAGAKVLGNIKINSNVNIGANSVVLQSVPSYSTVVGI 176
Cdd:PLN02739 224 TGVVIGETAVIGDRVSILHGVTLGGTGKETGDRHPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGN 303


                 ....*.
gi 577245503 177 PGHIVK 182
Cdd:PLN02739 304 PAKLIG 309
PLN02694 PLN02694
serine O-acetyltransferase
 21-181 6.62e-51

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 167.13  E-value: 6.62e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  21 DIKMVFEQDPAARSTLEVITTYAGLHAVWSHLIAHKLYNQKKYVAARAI-SQISRFFtGIEIHPGAKIGKRLFIDHGMGV 99
Cdd:PLN02694 103 DLRAARVRDPACVSFSHCLLNYKGFLACQAHRVAHKLWTQSRRPLALALhSRISDVF-AVDIHPAAKIGKGILFDHATGV 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503 100 VIGETCTIGDNVTIYQGVTLGGTGKERGKRHPDIGDNVLIAAGAKVLGNIKINSNVNIGANSVVLQSVPSYSTVVGIPGH 179
Cdd:PLN02694 182 VIGETAVIGNNVSILHHVTLGGTGKACGDRHPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPAR 261


                 ..
gi 577245503 180 IV 181
Cdd:PLN02694 262 LV 263
PRK10191 PRK10191
putative acyl transferase; Provisional
 72-175 4.93e-20

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 82.63  E-value: 4.93e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  72 ISRFFTGIEIHPGAKIGKRLFIDHGMGVVIGETCTIGDNVTIYQGVTLGGTGKErGKRHPDIGDNVLIAAGAKVLGNIKI 151
Cdd:PRK10191  35 ITECFFGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGVTIGNRGAD-NMACPHIGNGVELGANVIILGDITI 113

                         90       100
                 ....*....|....*....|....
gi 577245503 152 NSNVNIGANSVVLQSVPSYSTVVG 175
Cdd:PRK10191 114 GNNVTVGAGSVVLDSVPDNALVVG 137
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
61-183 2.92e-19

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 80.30  E-value: 2.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  61 KKYVAARAISQISRFFTGIEIHPG-AKIGKRLFIDHGMGVVIGETCTIGDNVTIYQGVTLGGTG--------KERGKRHP 131
Cdd:COG0110    3 LLLLFGARIGDGVVIGPGVRIYGGnITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNhpiddpatFPLRTGPV 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 577245503 132 DIGDNVLIAAGAKVLGNIKINSNVNIGANSVVLQSVPSYSTVVGIPGHIVKQ 183
Cdd:COG0110   83 TIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRK 134
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 81-177 3.35e-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: 76.38  E-value: 3.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503   81 IHPGAKIGKRLFIDHGmgVVIGETCTIGDNVTIYQGVTLGGTGKergkrhpdIGDNVLIAAGAKVLGNIKINSNVNIGAN 160
Cdd:TIGR03570 114 INPDVRIGDNVIINTG--AIVEHDCVIGDFVHIAPGVTLSGGVV--------IGEGVFIGAGATIIQGVTIGAGAIVGAG 183

                          90
                  ....*....|....*..
gi 577245503  161 SVVLQSVPSYSTVVGIP 177
Cdd:TIGR03570 184 AVVTKDIPDGGVVVGVP 200
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 81-177 1.65e-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: 74.44  E-value: 1.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  81 IHPGAKIGKRLFIDHGmgVVIGETCTIGDNVTIYQGVTLGGTGKergkrhpdIGDNVLIAAGAKVLGNIKINSNVNIGAN 160
Cdd:cd03360  111 INPDARIGDNVIINTG--AVIGHDCVIGDFVHIAPGVVLSGGVT--------IGEGAFIGAGATIIQGVTIGAGAIIGAG 180

                         90
                 ....*....|....*..
gi 577245503 161 SVVLQSVPSYSTVVGIP 177
Cdd:cd03360  181 AVVTKDVPDGSVVVGNP 197
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 78-181 1.51e-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: 69.79  E-value: 1.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  78 GIEIHPGAKIGKRLFIDHGMGVVIGETCTIGDNVTIY---QGVTLGGTGKERGKRHPD--IGDNVLIAAGAKVLGNIKIN 152
Cdd:cd04647    1 NISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYdhnHDIDDPERPIEQGVTSAPivIGDDVWIGANVVILPGVTIG 80

                         90       100
                 ....*....|....*....|....*....
gi 577245503 153 SNVNIGANSVVLQSVPSYSTVVGIPGHIV 181
Cdd:cd04647   81 DGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 86-181 2.04e-14

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: 68.22  E-value: 2.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  86 KIGKRLFIDHGM------GVVIGETCTIGDNVTIYQG-----VTLGGTGKERGKrhP-DIGDNVLIAAGAKVLGNIKINS 153
Cdd:cd03357   64 HIGDNFYANFNCtildvaPVTIGDNVLIGPNVQIYTAghpldPEERNRGLEYAK--PiTIGDNVWIGGGVIILPGVTIGD 141

                         90       100
                 ....*....|....*....|....*...
gi 577245503 154 NVNIGANSVVLQSVPSYSTVVGIPGHIV 181
Cdd:cd03357  142 NSVIGAGSVVTKDIPANVVAAGNPARVI 169
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 85-164 8.47e-14

Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 64.19  E-value: 8.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  85 AKIGKRLFIDHGmgVVIGETCTIGDNVTIYQGVTLGGTGKERGKRHPDIGDNVLIAAGAKVLGNIKINSNVNIGANSVVL 164
Cdd:cd00208    1 VFIGEGVKIHPK--AVIRGPVVIGDNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 86-182 2.24e-12

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: 61.75  E-value: 2.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  86 KIGKRLFIDHGmgVVIGETCTIGDNVTIYQGVTLG-----------------GTGKERGK--RHPDIGDNVLIAAGAKVL 146
Cdd:cd03358    6 IIGTNVFIEND--VKIGDNVKIQSNVSIYEGVTIEddvfigpnvvftndlypRSKIYRKWelKGTTVKRGASIGANATIL 83

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 577245503 147 GNIKINSNVNIGANSVVLQSVPSYSTVVGIPGHIVK 182
Cdd:cd03358   84 PGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 65-163 3.10e-11

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 61.57  E-value: 3.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  65 AARAISQISRFFTGIE----IHPGAKIGKRLFIDHGmgVVIGETCTIGDNVTIYQGVTLGgtgkergkrhPD--IGDNVL 138
Cdd:COG1044   85 LLQLFYPPPAPAPGIHpsavIDPSAKIGEGVSIGPF--AVIGAGVVIGDGVVIGPGVVIG----------DGvvIGDDCV 152

                         90       100
                 ....*....|....*....|....*
gi 577245503 139 IAAGAKVLGNIKINSNVNIGANSVV 163
Cdd:COG1044  153 LHPNVTIYERCVIGDRVIIHSGAVI 177
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 98-183 1.50e-10

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 57.73  E-value: 1.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  98 GVVI----GETCTIGDNVTIYQGVTL-GGTgkergkrhpdIGDNVLIAAGAKVLGNIKINSNVNIGANSVVLQ--SVPSY 170
Cdd:COG0663   61 GVVLhvdpGYPLTIGDDVTIGHGAILhGCT----------IGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEgkVVPPG 130

                         90
                 ....*....|...
gi 577245503 171 STVVGIPGHIVKQ 183
Cdd:COG0663  131 SLVVGSPAKVVRE 143
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 79-183 6.05e-10

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: 55.88  E-value: 6.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  79 IEIHPGAKIGKR--LFIDHGMGVVIGETCTIGDNVTIYqgvtlGGTgkergkrhpdIGDNVLIAAGAKVLGNIKINSNVN 156
Cdd:cd04645   39 IRIGERTNIQDGsvLHVDPGYPTIIGDNVTVGHGAVLH-----GCT----------IGDNCLIGMGAIILDGAVIGKGSI 103

                         90       100
                 ....*....|....*....|....*....
gi 577245503 157 IGANSVVL--QSVPSYSTVVGIPGHIVKQ 183
Cdd:cd04645  104 VAAGSLVPpgKVIPPGSLVAGSPAKVVRE 132
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 79-183 1.49e-09

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


Pssm-ID: 100040 [Multi-domain]  Cd Length: 145  Bit Score: 54.47  E-value: 1.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  79 IEIHPGAKIGKRLFIDHGMGVVIGETCTIGDNVTI---------------YQGVTLGGTGKERGKRHPD-----IGDNVL 138
Cdd:cd03349    2 ISVGDYSYGSGPDCDVGGDKLSIGKFCSIAPGVKIglggnhptdwvstypFYIFGGEWEDDAKFDDWPSkgdviIGNDVW 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 577245503 139 IAAGAKVLGNIKINSNVNIGANSVVLQSVPSYSTVVGIPGHIVKQ 183
Cdd:cd03349   82 IGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRY 126
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 94-183 2.85e-09

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: 54.11  E-value: 2.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  94 DHGMGVVIGETCTIGDNVTIYqgvtlggtgkerGKRhpdIGDNVLIAAGAKVLGNIKINSNVNIGANSVVLQS--VPSYS 171
Cdd:cd04650   57 DHGYPTEIGDYVTIGHNAVVH------------GAK---VGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTPGkeIPDYS 121

                         90
                 ....*....|..
gi 577245503 172 TVVGIPGHIVKQ 183
Cdd:cd04650  122 LVLGVPAKVVRK 133
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 81-211 3.37e-09

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 55.79  E-value: 3.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  81 IHPGAKIGKRLFIDHGmgVVIGETCTIGDNVTIYQGVTLGGTG-----KERGKRHP------------------------ 131
Cdd:COG1044  141 IGDGVVIGDDCVLHPN--VTIYERCVIGDRVIIHSGAVIGADGfgfapDEDGGWVKipqlgrvvigddveiganttidrg 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503 132 -------------D----------------------------IGDNVLIAAGAKVLGNIKINSNVNIGANSVVLQSVPSY 170
Cdd:COG1044  219 algdtvigdgtkiDnlvqiahnvrigehtaiaaqvgiagstkIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEG 298

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 577245503 171 STVVGIPGHIVKqDGVRVGKTFdhRHLPDpIYEQIKHLERQ 211
Cdd:COG1044  299 GVYSGSPAQPHR-EWLRNAAAL--RRLPE-LAKRLKELEKK 335
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 78-163 3.47e-09

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: 54.72  E-value: 3.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  78 GIEIHPGAKIGKRLFIdhGMGVVIGETCTIGDNVTIYQGVTlggtgkergkrhpdIGDNVLIAAGAKV------------ 145
Cdd:cd03352   19 GVVIGDGVVIGPGVVI--GDGVVIGDDCVIHPNVTIYEGCI--------------IGDRVIIHSGAVIgsdgfgfapdgg 82

                         90       100
                 ....*....|....*....|....*
gi 577245503 146 -------LGNIKINSNVNIGANSVV 163
Cdd:cd03352   83 gwvkipqLGGVIIGDDVEIGANTTI 107
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 81-163 4.73e-09

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 55.41  E-value: 4.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  81 IHPGAKIGKRLFIdhGMGVVIGETCTIGD------NVTIYQGVTlggtgkergkrhpdIGDNVLIAAGA----------- 143
Cdd:COG1044  123 IGAGVVIGDGVVI--GPGVVIGDGVVIGDdcvlhpNVTIYERCV--------------IGDRVIIHSGAvigadgfgfap 186

                         90       100
                 ....*....|....*....|....*....
gi 577245503 144 -------KV--LGNIKINSNVNIGANSVV 163
Cdd:COG1044  187 dedggwvKIpqLGRVVIGDDVEIGANTTI 215
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 75-183 6.90e-09

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 53.85  E-value: 6.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  75 FFTGIEIHpgakIGKRLFIDHGMGVVIGETCTIGDNVTIYQGVTLGGTG-------KERGKRHP---DIGDNVLIAAGAK 144
Cdd:PRK09527  70 FSYGSNIH----IGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGhpvhhelRKNGEMYSfpiTIGNNVWIGSHVV 145

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 577245503 145 VLGNIKINSNVNIGANSVVLQSVPSYSTVVGIPGHIVKQ 183
Cdd:PRK09527 146 INPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIRE 184
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 81-163 7.17e-09

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 54.76  E-value: 7.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  81 IHPGAKIGKrlfidhgmGVVIGETCTIGDNVTIYQGVTlggtgkergkrhpdIGDNVLIAAGAKV--------------- 145
Cdd:PRK00892 139 IGAGAVIGD--------GVKIGADCRLHANVTIYHAVR--------------IGNRVIIHSGAVIgsdgfgfandrggwv 196

                         90       100
                 ....*....|....*....|..
gi 577245503 146 ----LGNIKINSNVNIGANSVV 163
Cdd:PRK00892 197 kipqLGRVIIGDDVEIGANTTI 218
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 85-163 1.80e-08

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: 52.80  E-value: 1.80e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577245503  85 AKIGKRLFIDHGmgVVIGETCTIGDNVTIYQGVTLGgtgkergkRHPDIGDNVLIAAGAKVLGNIKINSNVNIGANSVV 163
Cdd:cd03352    2 AKIGENVSIGPN--AVIGEGVVIGDGVVIGPGVVIG--------DGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 80-167 2.49e-08

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 53.22  E-value: 2.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  80 EIHPGAKIGKrlfidhgmGVVIGETCTIGDNVTIYQGVTlggtgkergkrhpdIGDNVLIAAGAKVLGNIKINSNVNIGA 159
Cdd:PRK00892 102 GIHPSAVIDP--------SAKIGEGVSIGPNAVIGAGVV--------------IGDGVVIGAGAVIGDGVKIGADCRLHA 159


                 ....*...
gi 577245503 160 NSVVLQSV 167
Cdd:PRK00892 160 NVTIYHAV 167
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 63-179 8.36e-08

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


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 49.69  E-value: 8.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  63 YVAARAIsqisrFFTGIEIHPGAKIGKRLFIDhgMGVVIGETCTIGDNVTIYQGVTLGGTGKERGKRHPDIGDNVLIAAG 142
Cdd:cd03350   15 FIGPGAV-----LMMPSYVNIGAYVDEGTMVD--SWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIEDDVFIGAN 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 577245503 143 AKVLGNIKINSNVNIGANSVVLQS---------------VPSYSTVVgiPGH 179
Cdd:cd03350   88 CEVVEGVIVGKGAVLAAGVVLTQStpiydretgeiyygrVPPGSVVV--AGS 137
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 73-188 2.44e-07

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 50.52  E-value: 2.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503   73 SRFFTGIEIHP------GAKIGKRLFIdHGMGVVIGETCTIGDNVTIYQGVTLGGTGKERGKRHP---DIGDNVLIAAGA 143
Cdd:TIGR02353  95 TVLLSGSPLYSlylralGAKIGKGVDI-GSLPPVCTDLLTIGAGTIVRKEVMLLGYRAERGRLHTgpvTLGRDAFIGTRS 173

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 577245503  144 KVLGNIKINSNVNIGANSVVL--QSVPSYSTVVGIPGHIVKQDGVRV 188
Cdd:TIGR02353 174 TLDIDTSIGDGAQLGHGSALQggQSIPDGERWHGSPAQKTGADYRKV 220
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 99-214 5.25e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 49.37  E-value: 5.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  99 VVIGETCTIGDNVTIYQGVTLGGTGKergkrhpdIGDNVLIAAGAKVLGNIKINSNVNIGANSVVLQSVPSYSTVV-GIP 177
Cdd:PRK00892 238 VQIAHNVVIGRHTAIAAQVGIAGSTK--------IGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEPGEYSsGIP 309

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 577245503 178 GHIVKQ---DGVRVgktfdhRHLPDpIYEQIKHLERQLEK 214
Cdd:PRK00892 310 AQPNKEwlrTAARL------RRLDE-LRKRLKALEKKVEQ 342
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 99-177 5.37e-07

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 48.56  E-value: 5.37e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577245503  99 VVIGETCTIGDNVTIYQGVTLGGTGKergkrhpdIGDNVLIAAGAKVLGNIKINSNVNIGANSVVLQSVPSYSTVVGIP 177
Cdd:cd03352  127 VQIAHNVRIGENCLIAAQVGIAGSTT--------IGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTP 197
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 101-181 6.10e-07

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: 48.58  E-value: 6.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503 101 IGETCTIGDNVTIYQGVTLGGtgkergkrHPDIGDNVLIAAGAKVLGNIKINSNVNIGANSVVLQSVPSYSTVVGIPGHI 180
Cdd:cd03351  117 VAHDCVIGNNVILANNATLAG--------HVEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARL 188


                 .
gi 577245503 181 V 181
Cdd:cd03351  189 R 189
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 106-181 6.93e-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: 46.44  E-value: 6.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503 106 TIGDNVTIYQGVTL-GGTGKERGKRHP------DIGDNVLIAAGAKVLGNIKINSNVNIGANSVVLQSVPSYSTVVGIPG 178
Cdd:cd05825   25 TIGSDACISQGAYLcTGSHDYRSPAFPlitapiVIGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPA 104


                 ...
gi 577245503 179 HIV 181
Cdd:cd05825  105 VPV 107
PRK10502 PRK10502
putative acyl transferase; Provisional
 84-183 9.63e-07

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 47.25  E-value: 9.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  84 GAKIGKRLFI---------------DH---GMGVVIG--ETCTIGDNVTIYQGVTLGgTGKERGKRhPD---------IG 134
Cdd:PRK10502  51 GAKIGKGVVIrpsvritypwkltigDYawiGDDVWLYnlGEITIGAHCVISQKSYLC-TGSHDYSD-PHfdlntapivIG 128

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 577245503 135 DNVLIAAGAKVLGNIKINSNVNIGANSVVLQSVPSYSTVVGIPGHIVKQ 183
Cdd:PRK10502 129 EGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIRP 177
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 105-181 2.26e-06

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 46.94  E-value: 2.26e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 577245503 105 CTIGDNVTIYQGVTLGGtgkergkrHPDIGDNVLIAAGAKVLGNIKINSNVNIGANSVVLQSVPSYSTVVGIPGHIV 181
Cdd:COG1043  123 CVVGNNVILANNATLAG--------HVEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDVPPYVLAAGNPARLR 191
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 99-183 2.59e-06

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 46.34  E-value: 2.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  99 VVIGETCTIGDNVTIYQGV-----TLGGTGKERGKrhP-DIGDNVLIAAGAKVLGNIKINSNVNIGANSVVLQSVPSYST 172
Cdd:PRK10092  94 IRIGDNCMLAPGVHIYTAThpldpVARNSGAELGK--PvTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVV 171

                         90
                 ....*....|.
gi 577245503 173 VVGIPGHIVKQ 183
Cdd:PRK10092 172 VGGNPARIIKK 182
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 103-182 4.04e-06

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 45.64  E-value: 4.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503 103 ETCTIGDNVTIYQGVTLG----GTGKE-----RGKRHPD----------IGDNVLIAAGAKVLGNIKINSNVNIGANSVV 163
Cdd:PRK09677  84 ESITIGRDTLIASKVFITdhnhGSFKHsddfsSPNLPPDmrtlessavvIGQRVWIGENVTILPGVSIGNGCIVGANSVV 163

                         90
                 ....*....|....*....
gi 577245503 164 LQSVPSYSTVVGIPGHIVK 182
Cdd:PRK09677 164 TKSIPENTVIAGNPAKIIK 182
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 81-159 2.14e-05

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


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 41.46  E-value: 2.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  81 IHPGAKIGKRLFIDHgmgVVIGETCTIGDNVTIYQGVTLGGT--GKERGKRHPDIGDNVLIAAGAKVLGNIKINSNVNIG 158
Cdd:cd03356    2 IGESTVIGENAIIKN---SVIGDNVRIGDGVTITNSILMDNVtiGANSVIVDSIIGDNAVIGENVRVVNLCIIGDDVVVE 78


                 .
gi 577245503 159 A 159
Cdd:cd03356   79 D 79
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 81-175 8.91e-05

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


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 39.87  E-value: 8.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  81 IHPGAKIGKRLFIDHGmgvVIGETCTIGDNVTIYQGVtlggtgkergkrhpdIGDNVLIAAGAKVLGNIkINSNVNIGAN 160
Cdd:cd05787    2 IGRGTSIGEGTTIKNS---VIGRNCKIGKNVVIDNSY---------------IWDDVTIEDGCTIHHSI-VADGAVIGKG 62

                         90
                 ....*....|....*.
gi 577245503 161 SVVLQ-SVPSYSTVVG 175
Cdd:cd05787   63 CTIPPgSLISFGVVIG 78
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
81-180 1.09e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 42.01  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  81 IHPGAKIGKRLFIDHGmgVVIGE------------TCTIGDNVTIYQGVTL-GGTGKERGKR---------------HpD 132
Cdd:PRK05289  47 IDGHTTIGKNNRIFPF--ASIGEdpqdlkykgeptRLVIGDNNTIREFVTInRGTVQGGGVTrigdnnllmayvhvaH-D 123

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577245503 133 --IGDNVLIAAGAKVLGNIKINSNVNIGAN------------------SVVLQSVPSYSTVVGIPGHI 180
Cdd:PRK05289 124 cvVGNHVILANNATLAGHVEVGDYAIIGGLtavhqfvrigahamvggmSGVSQDVPPYVLAEGNPARL 191
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 73-186 1.17e-04

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 42.44  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  73 SRFFTGIEIHPGAKIG-----KRLFIDHGMGV----VIGETcTIGDNVTIYQG-VTLGGTGKergKRHPD-IGDNVLIAA 141
Cdd:PRK14357 319 SRLREGTVLKKSVKIGnfveiKKSTIGENTKAqhltYLGDA-TVGKNVNIGAGtITCNYDGK---KKNPTfIEDGAFIGS 394

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 577245503 142 GAKVLGNIKINSNVNIGANSVVLQSVPSYSTVVGIPGHIVKQDGV 186
Cdd:PRK14357 395 NSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQIVKEGWV 439
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 81-158 1.26e-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: 41.25  E-value: 1.26e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577245503  81 IHPGAKIGKRLFIDHGmgVVIGETCTIGDNVTIYQGVTLGGTgkergkrhpDIGDNVLIAAGAkVLGNIKINSNVNIG 158
Cdd:cd03353   12 IDGDVEIGVDVVIDPG--VILEGKTVIGEDCVIGPNCVIKDS---------TIGDGVVIKASS-VIEGAVIGNGATVG 77
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 47-177 1.51e-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: 42.43  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503   47 AVWSHLIAHKLYNqkkyvaARAISQISRFFTGIEIHP------GAKIGKRLFIDhgmGVVIGET--CTIGDNVTIYQGVT 118
Cdd:TIGR02353 560 FVWLHELHWKLYE------SVAVPNFLRPFRGTPFLPailrllGVKIGRGVYID---GTDLTERdlVTIGDDSTLNEGSV 630

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 577245503  119 LGGTGKERGKRHPD---IGDNVLIAAGAKVLGNIKINSNVNIGANSVVL--QSVPSYSTVVGIP 177
Cdd:TIGR02353 631 IQTHLFEDRVMKSDtvtIGDGATLGPGAIVLYGVVMGEGSVLGPDSLVMkgEEVPAHTRWRGNP 694
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
81-163 1.72e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 41.62  E-value: 1.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  81 IHPGAKIGKrlfidhgmGVVIGETCTIGDNVTiyqgvtlggtgkergkrhpdIGDNVLIAAGAKVLGNIKINSNVNIGAN 160
Cdd:PRK05289  11 VEPGAKIGE--------NVEIGPFCVIGPNVV--------------------IGDGTVIGSHVVIDGHTTIGKNNRIFPF 62


                 ...
gi 577245503 161 SVV 163
Cdd:PRK05289  63 ASI 65
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 101-189 2.04e-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: 40.87  E-value: 2.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503 101 IGETCTIGDNVTIYQGVTLGGTGKergkrhpdIGDNVLIAAGAkVLGNIKINSNVNIGANSVVLQSVPSYSTVVGIPGHI 180
Cdd:cd03353   12 IDGDVEIGVDVVIDPGVILEGKTV--------IGEDCVIGPNC-VIKDSTIGDGVVIKASSVIEGAVIGNGATVGPFAHL 82

                         90
                 ....*....|...
gi 577245503 181 ----VKQDGVRVG 189
Cdd:cd03353   83 rpgtVLGEGVHIG 95
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 81-163 3.09e-04

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 40.77  E-value: 3.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  81 IHPGAKIGKrlfidhgmGVVIGETCTIGDNVTiyqgvtlggtgkergkrhpdIGDNVLIAAGAKVLGNIKINSNVNIGAN 160
Cdd:COG1043   10 VDPGAKLGE--------NVEIGPFCVIGPDVE--------------------IGDGTVIGSHVVIEGPTTIGKNNRIFPF 61


                 ...
gi 577245503 161 SVV 163
Cdd:COG1043   62 ASI 64
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 81-163 3.22e-04

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: 40.49  E-value: 3.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  81 IHPGAKIGKrlfidhgmGVVIGETCTIGDNVTiyqgvtlggtgkergkrhpdIGDNVLIAAGAKVLGNIKINSNVNIGAN 160
Cdd:cd03351    8 VDPGAKIGE--------NVEIGPFCVIGPNVE--------------------IGDGTVIGSHVVIDGPTTIGKNNRIFPF 59


                 ...
gi 577245503 161 SVV 163
Cdd:cd03351   60 ASI 62
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 107-185 6.06e-04

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


Pssm-ID: 441774 [Multi-domain]  Cd Length: 268  Bit Score: 39.72  E-value: 6.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503 107 IGDNVTIYQGVTLGGTgKERGKRHP-DIGDNVLIAAGAKVLGNIKINSNVNIGANSVVLQS---------------VPSY 170
Cdd:COG2171  147 IGKNVHLSGGAGIGGV-LEPLQAAPvIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLTAStkiydrvtgevyygrVPAG 225

                         90
                 ....*....|....*
gi 577245503 171 STVVgiPGHIVKQDG 185
Cdd:COG2171  226 SVVV--PGSLPGKDG 238
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 78-164 6.15e-04

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


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 39.94  E-value: 6.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503   78 GIEIHPGAKIGKRLFIDHGMG----VVIGETCTIGDNVTIYqgvtlGGTGKERGKRHpdIGDNVLIAAGAKVLGNIKINS 153
Cdd:TIGR01852  52 GTRIFPGAVIGGVPQDLKYKGektrLIIGDNNTIREFVTIN-----RGTASGGGVTR--IGNNNLLMAYSHIAHDCVVGN 124

                          90
                  ....*....|.
gi 577245503  154 NVnIGANSVVL 164
Cdd:TIGR01852 125 HV-ILANNATL 134
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 81-175 8.29e-04

Gamma carbonic anhydrases (CA): Carbonic anhydrases 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 distinct groups of carbonic anhydrases - alpha, beta and gamma - which show no significant sequence identity or structural similarity. Gamma CAs are homotrimeric enzymes, with each subunit containing a left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 38.76  E-value: 8.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503  81 IHPGA------KIGKRLFI--------DHGMGVVIGETCTIGDNVTIYqgvTLGGTGKErgkrhpdIGDNVLIAAGAKVL 146
Cdd:cd00710   11 VHPTAvvigdvIIGDNVFVgpgasiraDEGTPIIIGANVNIQDGVVIH---ALEGYSVW-------IGKNVSIAHGAIVH 80

                         90       100
                 ....*....|....*....|....*....
gi 577245503 147 GNIKINSNVNIGANSVVLQSVPSYSTVVG 175
Cdd:cd00710   81 GPAYIGDNCFIGFRSVVFNAKVGDNCVIG 109
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
133-159 2.60e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 34.23  E-value: 2.60e-03
                          10        20
                  ....*....|....*....|....*..
gi 577245503  133 IGDNVLIAAGAKVLGNIKINSNVNIGA 159
Cdd:pfam00132   4 IGDNVLIGPNAVIGGGVIIGDNVIIGA 30
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 101-189 3.02e-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: 38.08  E-value: 3.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 577245503 101 IGETCTIGDNVTIYQGVTLGGTGKergkrhpdIGDNVLIAAGAkVLgnikinSNVNIGANSVVLQSVPSYSTVvgipghi 180
Cdd:COG1207  263 IDGDVEIGRDVVIDPNVILEGKTV--------IGEGVVIGPNC-TL------KDSTIGDGVVIKYSVIEDAVV------- 320


                 ....*....
gi 577245503 181 vkQDGVRVG 189
Cdd:COG1207  321 --GAGATVG 327
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 99-167 3.51e-03

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 37.39  E-value: 3.51e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 577245503  99 VVIGETCTIGDNVTIYQGVTlggtgkergkrhpdIGDNVLIAAGAKVLGNIKINSNVNIGANSVVLQSV 167
Cdd:cd03352    2 AKIGENVSIGPNAVIGEGVV--------------IGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGC 56
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 81-146 4.90e-03

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: 34.92  E-value: 4.90e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 577245503  81 IHPGAKIGKRLFIDHGMGVVIGETCTIGDNVTIYQGVTlggtgkergkrhpdIGDNVLIAAGAKVL 146
Cdd:cd00208   27 IGPGAVIGAATGPNEKNPTIIGDNVEIGANAVIHGGVK--------------IGDNAVIGAGAVVT 78
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 81-158 8.25e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 36.65  E-value: 8.25e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 577245503  81 IHPGAKIGKRLFIDHGmgVVIGETCTIGDNVTIYQGVTLGGTgkergkrhpDIGDNVLIAAGAkVLGNIKINSNVNIG 158
Cdd:PRK14355 265 IDRGVVIGRDTTIYPG--VCISGDTRIGEGCTIEQGVVIKGC---------RIGDDVTVKAGS-VLEDSVVGDDVAIG 330
 
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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