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Conserved domains on  [gi|693233731|ref|WP_032345404|]
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serine acetyltransferase [Escherichia coli]

Protein Classification

serine acetyltransferase( domain architecture ID 10129656)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 87-185 1.21e-40

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: 133.33  E-value: 1.21e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  87 YGCDIGLGAQIGKGLVLPHHSGVVIHGNVKIGENVIIRQNTTIGEKESDSRENYIVIGDNVDVGAHTCIIGlNVKIGSNV 166
Cdd:cd03354    1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILG-NITIGDNV 79

                         90
                 ....*....|....*....
gi 693233731 167 KIGAMSFIMEEVPDNCTYV 185
Cdd:cd03354   80 KIGANAVVTKDVPANSTVV 98
 
Name Accession Description Interval E-value
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 87-185 1.21e-40

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: 133.33  E-value: 1.21e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  87 YGCDIGLGAQIGKGLVLPHHSGVVIHGNVKIGENVIIRQNTTIGEKESDSRENYIVIGDNVDVGAHTCIIGlNVKIGSNV 166
Cdd:cd03354    1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILG-NITIGDNV 79

                         90
                 ....*....|....*....
gi 693233731 167 KIGAMSFIMEEVPDNCTYV 185
Cdd:cd03354   80 KIGANAVVTKDVPANSTVV 98
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 53-185 2.18e-30

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: 109.40  E-value: 2.18e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  53 GF--LMWWRLANEMYisgNKKQRKCAIKIKNALMAKYGCDIGLGAQIGKGLVLPHHSGVVIHGNVKIGENVIIRQNTTIG 130
Cdd:COG1045   31 GFhaLALHRLAHWLW---KRGLPLLARLLSERARFLTGIDIHPGATIGRGFFIDHGTGVVIGETAVIGDNVTIYQGVTLG 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 693233731 131 EKESDSRENYIVIGDNVDVGAHTCIIGlNVKIGSNVKIGAMSFIMEEVPDNCTYV 185
Cdd:COG1045  108 GTGKEKGKRHPTIGDNVVIGAGAKILG-PITIGDNAKIGANSVVLKDVPPGSTVV 161
PLN02357 PLN02357
serine acetyltransferase
 52-185 7.86e-22

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 91.10  E-value: 7.86e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  52 RGFLMWW--RLANEMYISGNKKqrkCAIKIKNALMAKYGCDIGLGAQIGKGLVLPHHSGVVIHGNVKIGENVIIRQNTTI 129
Cdd:PLN02357 191 KGFLACQahRIAHKLWTQGRKI---LALLIQNRVSEAFAVDIHPGAKIGQGILLDHATGVVIGETAVVGNNVSILHNVTL 267

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 693233731 130 GEKESDSRENYIVIGDNVDVGAHTCIIGlNVKIGSNVKIGAMSFIMEEVPDNCTYV 185
Cdd:PLN02357 268 GGTGKQSGDRHPKIGDGVLIGAGTCILG-NITIGEGAKIGAGSVVLKDVPPRTTAV 322
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 95-185 8.52e-14

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: 66.75  E-value: 8.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731   95 AQIGKGLVLphHSGVVIHGNVKIGENVIIRQNTTIgekESDSR-ENY------------IVIGDNVDVGAHTCIIGlNVK 161
Cdd:TIGR03570 100 ASIGEGTVI--MAGAVINPDVRIGDNVIINTGAIV---EHDCViGDFvhiapgvtlsggVVIGEGVFIGAGATIIQ-GVT 173

                          90       100
                  ....*....|....*....|....
gi 693233731  162 IGSNVKIGAMSFIMEEVPDNCTYV 185
Cdd:TIGR03570 174 IGAGAIVGAGAVVTKDIPDGGVVV 197
 
Name Accession Description Interval E-value
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 87-185 1.21e-40

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: 133.33  E-value: 1.21e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  87 YGCDIGLGAQIGKGLVLPHHSGVVIHGNVKIGENVIIRQNTTIGEKESDSRENYIVIGDNVDVGAHTCIIGlNVKIGSNV 166
Cdd:cd03354    1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILG-NITIGDNV 79

                         90
                 ....*....|....*....
gi 693233731 167 KIGAMSFIMEEVPDNCTYV 185
Cdd:cd03354   80 KIGANAVVTKDVPANSTVV 98
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 53-185 2.18e-30

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: 109.40  E-value: 2.18e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  53 GF--LMWWRLANEMYisgNKKQRKCAIKIKNALMAKYGCDIGLGAQIGKGLVLPHHSGVVIHGNVKIGENVIIRQNTTIG 130
Cdd:COG1045   31 GFhaLALHRLAHWLW---KRGLPLLARLLSERARFLTGIDIHPGATIGRGFFIDHGTGVVIGETAVIGDNVTIYQGVTLG 107

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 693233731 131 EKESDSRENYIVIGDNVDVGAHTCIIGlNVKIGSNVKIGAMSFIMEEVPDNCTYV 185
Cdd:COG1045  108 GTGKEKGKRHPTIGDNVVIGAGAKILG-PITIGDNAKIGANSVVLKDVPPGSTVV 161
PLN02357 PLN02357
serine acetyltransferase
 52-185 7.86e-22

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 91.10  E-value: 7.86e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  52 RGFLMWW--RLANEMYISGNKKqrkCAIKIKNALMAKYGCDIGLGAQIGKGLVLPHHSGVVIHGNVKIGENVIIRQNTTI 129
Cdd:PLN02357 191 KGFLACQahRIAHKLWTQGRKI---LALLIQNRVSEAFAVDIHPGAKIGQGILLDHATGVVIGETAVVGNNVSILHNVTL 267

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 693233731 130 GEKESDSRENYIVIGDNVDVGAHTCIIGlNVKIGSNVKIGAMSFIMEEVPDNCTYV 185
Cdd:PLN02357 268 GGTGKQSGDRHPKIGDGVLIGAGTCILG-NITIGEGAKIGAGSVVLKDVPPRTTAV 322
PLN02694 PLN02694
serine O-acetyltransferase
 52-185 2.54e-17

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 77.76  E-value: 2.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  52 RGFLMWW--RLANEMYisgNKKQRKCAIKIKNALMAKYGCDIGLGAQIGKGLVLPHHSGVVIHGNVKIGENVIIRQNTTI 129
Cdd:PLN02694 125 KGFLACQahRVAHKLW---TQSRRPLALALHSRISDVFAVDIHPAAKIGKGILFDHATGVVIGETAVIGNNVSILHHVTL 201

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 693233731 130 GEKESDSRENYIVIGDNVDVGAHTCIIGlNVKIGSNVKIGAMSFIMEEVPDNCTYV 185
Cdd:PLN02694 202 GGTGKACGDRHPKIGDGVLIGAGATILG-NVKIGEGAKIGAGSVVLIDVPPRTTAV 256
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 88-174 3.86e-15

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: 71.97  E-value: 3.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  88 GCDIGLGAQIGKGLVLphHSGVVIHGNVKIGENVIIRQNTTIGekeSD-------SRENYI--------VIGDNVDVGAH 152
Cdd:COG1044  138 GVVIGDGVVIGDDCVL--HPNVTIYERCVIGDRVIIHSGAVIG---ADgfgfapdEDGGWVkipqlgrvVIGDDVEIGAN 212

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 693233731 153 TCI---------IGLNVK------IGSNVKIGAMSFI 174
Cdd:COG1044  213 TTIdrgalgdtvIGDGTKidnlvqIAHNVRIGEHTAI 249
PRK10191 PRK10191
putative acyl transferase; Provisional
 87-188 6.24e-15

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 68.38  E-value: 6.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  87 YGCDIGLGAQIGKGLVLPHHSGVVIHGNVKIGENVIIRQNTTIGEKESDSREnYIVIGDNVDVGAHTCIIGlNVKIGSNV 166
Cdd:PRK10191  40 FGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGVTIGNRGADNMA-CPHIGNGVELGANVIILG-DITIGNNV 117

                         90       100
                 ....*....|....*....|..
gi 693233731 167 KIGAMSFIMEEVPDNCTYVTRK 188
Cdd:PRK10191 118 TVGAGSVVLDSVPDNALVVGEK 139
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 91-185 9.67e-15

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: 69.05  E-value: 9.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  91 IGLGAQIGKGLVLphHSGVVIHGNVKIGENVIIRQNTTIGEkesDSR-ENY------------IVIGDNVDVGAHTCIIG 157
Cdd:cd03360   93 VSPSAVIGEGCVI--MAGAVINPDARIGDNVIINTGAVIGH---DCViGDFvhiapgvvlsggVTIGEGAFIGAGATIIQ 167

                         90       100
                 ....*....|....*....|....*...
gi 693233731 158 lNVKIGSNVKIGAMSFIMEEVPDNCTYV 185
Cdd:cd03360  168 -GVTIGAGAIIGAGAVVTKDVPDGSVVV 194
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 88-174 9.91e-15

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: 69.36  E-value: 9.91e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  88 GCDIGLGAQIGKGLVLphHSGVVIHGNVKIGENVIIRQNTTIGekeSD------SRENYI--------VIGDNVDVGAHT 153
Cdd:cd03352   31 GVVIGDGVVIGDDCVI--HPNVTIYEGCIIGDRVIIHSGAVIG---SDgfgfapDGGGWVkipqlggvIIGDDVEIGANT 105

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 693233731 154 CI---------IGLNVK------IGSNVKIGAMSFI 174
Cdd:cd03352  106 TIdrgalgdtvIGDGTKidnlvqIAHNVRIGENCLI 141
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 88-170 1.50e-14

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 70.55  E-value: 1.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  88 GCDIGLGAQIGKGLVLphHSGVVIHGNVKIGENVIIRQNTTIGekeSD------SRENYI--------VIGDNVDVGAHT 153
Cdd:PRK00892 142 GAVIGDGVKIGADCRL--HANVTIYHAVRIGNRVIIHSGAVIG---SDgfgfanDRGGWVkipqlgrvIIGDDVEIGANT 216

                         90       100       110
                 ....*....|....*....|....*....|..
gi 693233731 154 CI---------IGLNVK------IGSNVKIGA 170
Cdd:PRK00892 217 TIdrgalddtvIGEGVKidnlvqIAHNVVIGR 248
PLN02739 PLN02739
serine acetyltransferase
 55-179 2.31e-14

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 70.06  E-value: 2.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  55 LMWWRLANEMYISGNKKqrkCAIKIKNALMAKYGCDIGLGAQIGKGLVLPHHSGVVIHGNVKIGENVIIRQNTTIGEKES 134
Cdd:PLN02739 175 LQAYRVAHKLWKQGRKL---LALALQSRVSEVFGIDIHPAARIGKGILLDHGTGVVIGETAVIGDRVSILHGVTLGGTGK 251

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 693233731 135 DSRENYIVIGDNVDVGAHTCIIGlNVKIGSNVKIGAMSFIMEEVP 179
Cdd:PLN02739 252 ETGDRHPKIGDGALLGACVTILG-NISIGAGAMVAAGSLVLKDVP 295
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 95-185 8.52e-14

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: 66.75  E-value: 8.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731   95 AQIGKGLVLphHSGVVIHGNVKIGENVIIRQNTTIgekESDSR-ENY------------IVIGDNVDVGAHTCIIGlNVK 161
Cdd:TIGR03570 100 ASIGEGTVI--MAGAVINPDVRIGDNVIINTGAIV---EHDCViGDFvhiapgvtlsggVVIGEGVFIGAGATIIQ-GVT 173

                          90       100
                  ....*....|....*....|....
gi 693233731  162 IGSNVKIGAMSFIMEEVPDNCTYV 185
Cdd:TIGR03570 174 IGAGAIVGAGAVVTKDIPDGGVVV 197
cysE PRK11132
serine acetyltransferase; Provisional
 52-183 3.22e-13

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 66.26  E-value: 3.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  52 RGF--LMWWRLANEMYisgNKKQRKCAIKIKNALMAKYGCDIGLGAQIGKGLVLPHHSGVVIHGNVKIGENVIIRQNTTI 129
Cdd:PRK11132 106 KGFhaLQAYRIGHWLW---NQGRRALAIYLQNQISVAFQVDIHPAAKIGRGIMLDHATGIVIGETAVIENDVSILQSVTL 182

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 693233731 130 G--EKESDSRENYIVIGdnVDVGAHTCIIGlNVKIGSNVKIGAMSFIMEEVPDNCT 183
Cdd:PRK11132 183 GgtGKTSGDRHPKIREG--VMIGAGAKILG-NIEVGRGAKIGAGSVVLQPVPPHTT 235
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 91-185 4.87e-12

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: 59.78  E-value: 4.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  91 IGLGAQIGKGLVLPHHSGVVIHGNVKIGENVII-----RQNTTIGEKESDSRENYIVIGDNVDVGAHtCIIGLNVKIGSN 165
Cdd:cd04647    4 IGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIydhnhDIDDPERPIEQGVTSAPIVIGDDVWIGAN-VVILPGVTIGDG 82

                         90       100
                 ....*....|....*....|
gi 693233731 166 VKIGAMSFIMEEVPDNCTYV 185
Cdd:cd04647   83 AVVGAGSVVTKDVPPNSIVA 102
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
94-185 1.21e-11

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 59.50  E-value: 1.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  94 GAQIGKGLVLPHHSGVVIHGNVKIGENVIIRQNTTI--------GEKESDSRENYIVIGDNVDVGAHtCIIGLNVKIGSN 165
Cdd:COG0110   27 NITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTIltgnhpidDPATFPLRTGPVTIGDDVWIGAG-ATILPGVTIGDG 105

                         90       100
                 ....*....|....*....|
gi 693233731 166 VKIGAMSFIMEEVPDNCTYV 185
Cdd:COG0110  106 AVVGAGSVVTKDVPPYAIVA 125
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 106-175 5.24e-11

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: 56.10  E-value: 5.24e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731 106 HSGVVIHGNVKIGENVIIRQNTTIGEKESDSRENYIVIGDNVDVGAHTCIIGlNVKIGSNVKIGAMSFIM 175
Cdd:cd00208   10 HPKAVIRGPVVIGDNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGANAVIHG-GVKIGDNAVIGAGAVVT 78
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 106-178 1.24e-10

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: 59.26  E-value: 1.24e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 693233731 106 HSGVVIHGNVKIGENVIIRQNTTIGEKesdsrenyIVIGDNVDVGAHtCIIGLNVKIGSNVKIGAMSFIMEEV 178
Cdd:COG1044  100 HPSAVIDPSAKIGEGVSIGPFAVIGAG--------VVIGDGVVIGPG-VVIGDGVVIGDDCVLHPNVTIYERC 163
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 106-170 1.11e-09

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 56.69  E-value: 1.11e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 693233731 106 HSGVVIHGNVKIGENVIIRQNTTIGEKesdsrenyIVIGDNVDVGAHtCIIGLNVKIGSNVKIGA 170
Cdd:PRK00892 104 HPSAVIDPSAKIGEGVSIGPNAVIGAG--------VVIGDGVVIGAG-AVIGDGVKIGADCRLHA 159
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 91-170 1.39e-09

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 56.18  E-value: 1.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  91 IGLGAQIGKGLVLphHSGVVIHGNVKIGENVIIRQNTtigekesdsrenyiVIGDNVDVGAHtCIIGLNVKIGSNVKIGA 170
Cdd:COG1044  105 IDPSAKIGEGVSI--GPFAVIGAGVVIGDGVVIGPGV--------------VIGDGVVIGDD-CVLHPNVTIYERCVIGD 167
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 89-169 1.61e-09

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: 54.73  E-value: 1.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  89 CDIGLGAQIGKGLVLPHhsGVVIHGNVKIGENVIIRQNTTIGekesDSrenyiVIGDNVDVGAHT----CIIGLNVKIG- 163
Cdd:cd03353   10 TYIDGDVEIGVDVVIDP--GVILEGKTVIGEDCVIGPNCVIK----DS-----TIGDGVVIKASSviegAVIGNGATVGp 78

                         90
                 ....*....|....*..
gi 693233731 164 -----------SNVKIG 169
Cdd:cd03353   79 fahlrpgtvlgEGVHIG 95
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 95-173 7.37e-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: 53.18  E-value: 7.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  95 AQIGKGLVLphHSGVVIHGNVKIGENVIIRQNTTIGekesdsreNYIVIGDNVDVGAHT-----CIIGLNVKIGSNVKIG 169
Cdd:cd03352    2 AKIGENVSI--GPNAVIGEGVVIGDGVVIGPGVVIG--------DGVVIGDDCVIHPNVtiyegCIIGDRVIIHSGAVIG 71


                 ....
gi 693233731 170 AMSF 173
Cdd:cd03352   72 SDGF 75
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 90-169 9.71e-09

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: 53.88  E-value: 9.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  90 DIGLGAQIGKGLVLphHSGVVIHGNVKIGENVIIRQNTTIgekeSDSrenyiVIGDNVDVgaHTCIIgLNVKIGSNVKIG 169
Cdd:COG1207  262 YIDGDVEIGRDVVI--DPNVILEGKTVIGEGVVIGPNCTL----KDS-----TIGDGVVI--KYSVI-EDAVVGAGATVG 327
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 91-169 1.91e-08

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 52.83  E-value: 1.91e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 693233731  91 IGLGAQIGKGLVLPHHsgVVIHGNVKIGENVIIRQNTtigekesdsrenyiVIGDNVDVGAHtCIIGLNVKIGSNVKIG 169
Cdd:PRK00892 109 IDPSAKIGEGVSIGPN--AVIGAGVVIGDGVVIGAGA--------------VIGDGVKIGAD-CRLHANVTIYHAVRIG 170
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 91-168 1.36e-07

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 50.60  E-value: 1.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  91 IGLGAQIGKGLVLphHSGVVIHGNVKIGENVIIRQNT-----TIGEKES-------DSrenyiVIGDNVDVG--AH---T 153
Cdd:PRK14354 262 IDADVEIGSDTVI--EPGVVIKGNTVIGEDCVIGPGSrivdsTIGDGVTitnsvieES-----KVGDNVTVGpfAHlrpG 334

                         90
                 ....*....|....*
gi 693233731 154 CIIGLNVKIGSNVKI 168
Cdd:PRK14354 335 SVIGEEVKIGNFVEI 349
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 109-193 3.17e-07

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 49.54  E-value: 3.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731 109 VVIHGNVKIGENVIIRqNTTIGEKESDSRENYI---VIGDNVDVGA------------HTCIIGLNVKIGSN-------- 165
Cdd:PRK14360 332 AQIGSNCRIGNFVEIK-KSQLGEGSKVNHLSYIgdaTLGEQVNIGAgtitanydgvkkHRTVIGDRSKTGANsvlvapit 410

                         90       100       110
                 ....*....|....*....|....*....|..
gi 693233731 166 ----VKIGAMSFIMEEVPDNCTYVTRKESRII 193
Cdd:PRK14360 411 lgedVTVAAGSTITKDVPDNSLAIARSRQVIK 442
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 67-182 2.56e-06

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: 45.28  E-value: 2.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  67 SGNKKQRKCAIK-IKNALMAkygcdiglgaqiGKGLVlphHSGVVIHG---NVKIGENVIIRQNTTI---GEKESDSREN 139
Cdd:cd03359    6 SGNKVSRKSVICgSQNIVLN------------GKTII---QSDVIIRGdlaTVSIGRYCILSEGCVIrppFKKFSKGVAF 70

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 693233731 140 Y-IVIGDNVDVGAHtCIIGLnVKIGSNVKIGAMSFIME--EVPDNC 182
Cdd:cd03359   71 FpLHIGDYVFIGEN-CVVNA-AQIGSYVHIGKNCVIGRrcIIKDCV 114
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
106-180 7.13e-06

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 45.09  E-value: 7.13e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 693233731 106 HSGVVIHGNVKIGENVIIRQNTTIGEKesdsrenyIVIGDNVDVGAHTCIIGlNVKIGSNVKIGAMSFIMEEVPD 180
Cdd:PRK05289   6 HPTAIVEPGAKIGENVEIGPFCVIGPN--------VVIGDGTVIGSHVVIDG-HTTIGKNNRIFPFASIGEDPQD 71
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
110-174 9.67e-06

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 43.32  E-value: 9.67e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 693233731 110 VIHGNVKIGENVIIRQNTTIGEKEsdsrenyIVIGDNVDVGAHTCIIGL-NVKIGSNVKIGAMSFI 174
Cdd:COG0110    4 LLLFGARIGDGVVIGPGVRIYGGN-------ITIGDNVYIGPGVTIDDPgGITIGDNVLIGPGVTI 62
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 114-178 1.02e-05

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: 44.32  E-value: 1.02e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 693233731 114 NVKIGENVIIRQNTTIGEKesdsrenyIVIGDNVDVGAHtCIIGLNVKIGSNVKIGAMSFIMEEV 178
Cdd:cd03352    1 SAKIGENVSIGPNAVIGEG--------VVIGDGVVIGPG-VVIGDGVVIGDDCVIHPNVTIYEGC 56
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 87-181 1.29e-05

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 44.22  E-value: 1.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  87 YGCDIglgaQIGKGLVLPHHSGVVIHGNVKIGENVIIRQNTTIG----------EKESDSRENYIVIGDNVDVGAHTcII 156
Cdd:PRK09527  72 YGSNI----HIGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSvtghpvhhelRKNGEMYSFPITIGNNVWIGSHV-VI 146

                         90       100
                 ....*....|....*....|....*
gi 693233731 157 GLNVKIGSNVKIGAMSFIMEEVPDN 181
Cdd:PRK09527 147 NPGVTIGDNSVIGAGSVVTKDIPPN 171
PRK10502 PRK10502
putative acyl transferase; Provisional
 94-185 1.68e-05

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 43.40  E-value: 1.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  94 GAQIGKGLVL--------P------HHS----GVVIH--GNVKIGENVIIRQ-------NTTIGEKESDSRENYIVIGDN 146
Cdd:PRK10502  51 GAKIGKGVVIrpsvrityPwkltigDYAwigdDVWLYnlGEITIGAHCVISQksylctgSHDYSDPHFDLNTAPIVIGEG 130

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 693233731 147 VDVGAHtCIIGLNVKIGSNVKIGAMSFIMEEVPDNCTYV 185
Cdd:PRK10502 131 CWLAAD-VFVAPGVTIGSGAVVGARSSVFKSLPANTICR 168
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 88-181 1.75e-05

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 44.47  E-value: 1.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  88 GCDIGLGAQIGkglvlPH---HSGVVIHGNVKIGENVIIRqNTTIGEKESDSRENYI---VIGDNVDVGA---------- 151
Cdd:PRK14353 303 GAHVGEGAEVG-----PYarlRPGAELGEGAKVGNFVEVK-NAKLGEGAKVNHLTYIgdaTIGAGANIGAgtitcnydgf 376

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 693233731 152 --HTCIIGLNVKIGSN------VKIG--AM----SFIMEEVPDN 181
Cdd:PRK14353 377 nkHRTEIGAGAFIGSNsalvapVTIGdgAYiasgSVITEDVPDD 420
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 108-181 2.05e-05

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 43.98  E-value: 2.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731 108 GVVIHGNVKIGENVIIRqNTTIGEKESDSRENYI---VIGDNVDVGAHT------------------CIIGLN------V 160
Cdd:PRK14357 324 GTVLKKSVKIGNFVEIK-KSTIGENTKAQHLTYLgdaTVGKNVNIGAGTitcnydgkkknptfiedgAFIGSNsslvapV 402

                         90       100
                 ....*....|....*....|.
gi 693233731 161 KIGSNVKIGAMSFIMEEVPDN 181
Cdd:PRK14357 403 RIGKGALIGAGSVITEDVPPY 423
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 93-172 2.12e-05

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 44.36  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731   93 LGAQIGKGLVLpHHSGVVIHGNVKIGENVIIRQNTTIGEKESDS---RENYIVIGDNVDVGAHTcIIGLNVKIGSNVKIG 169
Cdd:TIGR02353 111 LGAKIGKGVDI-GSLPPVCTDLLTIGAGTIVRKEVMLLGYRAERgrlHTGPVTLGRDAFIGTRS-TLDIDTSIGDGAQLG 188


                  ...
gi 693233731  170 AMS 172
Cdd:TIGR02353 189 HGS 191
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 108-178 2.28e-05

Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix (LbH) domain: Proteins in this family show simlarity to glucose-1-phosphate adenylyltransferases in that they contain N-terminal catalytic domains that resemble a dinucleotide-binding Rossmann fold and C-terminal LbH fold domains. Members in this family are predicted to be glucose-1-phosphate thymidylyltransferases, which are involved in the dTDP-L-rhamnose biosynthetic pathway. Glucose-1-phosphate thymidylyltransferase catalyzes the synthesis of deoxy-thymidine di-phosphate (dTDP)-L-rhamnose, an important component of the cell wall of many microorganisms. The C-terminal LbH domain contains multiple 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.


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 42.96  E-value: 2.28e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 693233731 108 GVVIHGNVKIGENVIIRQNTTIgekesdsrENYIVIGDNVDVGAHT-----CIIGLNVKIGSNVKIGAmSFIMEEV 178
Cdd:cd05636   11 GVTIKGPVWIGEGAIVRSGAYI--------EGPVIIGKGCEIGPNAyirgyTVLGDGCVVGNSVEVKN-SIIMDGT 77
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 87-185 2.46e-05

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: 42.79  E-value: 2.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  87 YGCDIGLGAQ--IGKGLVLPHHSGVVIHGNVKIGENVIIrqnTTIGE----KESDSRENY---IVIGDNVDVGAHTCIIG 157
Cdd:cd03357   59 YGYNIHIGDNfyANFNCTILDVAPVTIGDNVLIGPNVQI---YTAGHpldpEERNRGLEYakpITIGDNVWIGGGVIILP 135

                         90       100
                 ....*....|....*....|....*...
gi 693233731 158 lNVKIGSNVKIGAMSFIMEEVPDNCTYV 185
Cdd:cd03357  136 -GVTIGDNSVIGAGSVVTKDIPANVVAA 162
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 89-169 3.03e-05

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: 43.19  E-value: 3.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  89 CDIGLGAQIGKGLVLphHSGVVIHGNVKIGENVIIRQNTTIGEKESDSR----ENYIVIGDN------------------ 146
Cdd:cd03351   24 CVIGPNVEIGDGTVI--GSHVVIDGPTTIGKNNRIFPFASIGEAPQDLKykgePTRLEIGDNntirefvtihrgtaqggg 101

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 693233731 147 -VDVG-----------AHTCIIGLNVKIGSNVKIG 169
Cdd:cd03351  102 vTRIGnnnllmayvhvAHDCVIGNNVILANNATLA 136
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
89-169 4.66e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 42.78  E-value: 4.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  89 CDIGLGAQIGKGLVLphHSGVVIHGNVKIGENVIIRQNTTIGEKESDSR----ENYIVIGDN-------------VD--- 148
Cdd:PRK05289  27 CVIGPNVVIGDGTVI--GSHVVIDGHTTIGKNNRIFPFASIGEDPQDLKykgePTRLVIGDNntirefvtinrgtVQggg 104

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 693233731 149 ---VG-----------AHTCIIGLNVKIGSNVKIG 169
Cdd:PRK05289 105 vtrIGdnnllmayvhvAHDCVVGNHVILANNATLA 139
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 106-169 5.44e-05

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 42.31  E-value: 5.44e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 693233731 106 HSGVVIHGNVKIGENVIIRQNTTIGEKesdsrenyIVIGDNVDVGAHTCIIGlNVKIGSNVKIG 169
Cdd:COG1043    5 HPTAIVDPGAKLGENVEIGPFCVIGPD--------VEIGDGTVIGSHVVIEG-PTTIGKNNRIF 59
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 89-169 5.49e-05

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 42.31  E-value: 5.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  89 CDIGLGAQIGKGLVLphHSGVVIHGNVKIGENVIIRQNTTIGE-------KESDSRenyIVIGDNVD------------- 148
Cdd:COG1043   26 CVIGPDVEIGDGTVI--GSHVVIEGPTTIGKNNRIFPFASIGEepqdlkyKGEPTR---LEIGDNNTirefvtihrgtvq 100

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 693233731 149 ------VG-----------AHTCIIGLNVKIGSNVKIG 169
Cdd:COG1043  101 gggvtrIGddnllmayvhvAHDCVVGNNVILANNATLA 138
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 78-169 1.07e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 41.78  E-value: 1.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  78 KIKNALMAKyGCDI---------GLGAQIGKGLVLPHHsgvVIHGNVKIGENVIIrQNTTIGEKesdsrenyIVIGDNVD 148
Cdd:PRK05293 290 KVKNSLVVE-GCVVygtvehsvlFQGVQVGEGSVVKDS---VIMPGAKIGENVVI-ERAIIGEN--------AVIGDGVI 356

                         90       100
                 ....*....|....*....|....
gi 693233731 149 VG---AHTCIIGLNVKIGSNVKIG 169
Cdd:PRK05293 357 IGggkEVITVIGENEVIGVGTVIG 380
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 105-174 1.16e-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: 40.69  E-value: 1.16e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 693233731 105 HHSGVVIhGNVKIGENVIIRQNTTIGEKESDSrenyIVIGDNVDV--GA--HtCIIGLNVKIGSNVKIGAMSFI 174
Cdd:cd00710   12 HPTAVVI-GDVIIGDNVFVGPGASIRADEGTP----IIIGANVNIqdGVviH-ALEGYSVWIGKNVSIAHGAIV 79
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 88-175 1.36e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 41.16  E-value: 1.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  88 GCDIGLGAQIGKGLVLPHHsgVVIHGNVKIGENVIIRQNTTIGEKESD----SRENYIVIGDNvdvgahtCIIGLNVKI- 162
Cdd:PRK12461  23 FAVIGANVEIGDGTWIGPH--AVILGPTRIGKNNKIHQGAVVGDEPQDftykGEESRLEIGDR-------NVIREGVTIh 93

                         90
                 ....*....|....*...
gi 693233731 163 -----GSNVKIGAMSFIM 175
Cdd:PRK12461  94 rgtkgGGVTRIGNDNLLM 111
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 91-169 1.52e-04

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: 38.71  E-value: 1.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  91 IGLGAQIGKGLVLphhSGVVIHGNVKIGENVIIR-----QNTTIGEkesDSRENYIVIGDNVDVGAHtCIIGLNVKIGSN 165
Cdd:cd05787    2 IGRGTSIGEGTTI---KNSVIGRNCKIGKNVVIDnsyiwDDVTIED---GCTIHHSIVADGAVIGKG-CTIPPGSLISFG 74


                 ....
gi 693233731 166 VKIG 169
Cdd:cd05787   75 VVIG 78
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 106-185 1.61e-04

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 40.40  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731 106 HSGVVIHGNVKIGENVIIRQNTTI-GEkesdsrENYIVIGDN----------------VDVGA----------HTCIIG- 157
Cdd:COG0663   20 APTAVVIGDVTIGEDVSVWPGAVLrGD------VGPIRIGEGsniqdgvvlhvdpgypLTIGDdvtighgailHGCTIGd 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 693233731 158 ----------LN-VKIGSNVKIGAMSFIME--EVPDNCTYV 185
Cdd:COG0663   94 nvligmgaivLDgAVIGDGSIVGAGALVTEgkVVPPGSLVV 134
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 142-183 1.74e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 41.28  E-value: 1.74e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 693233731 142 VIGDNVDVGAHtCIIGLNVKIGSNVKIGAMSFIMEEVP--DNCT 183
Cdd:PRK00892 114 KIGEGVSIGPN-AVIGAGVVIGDGVVIGAGAVIGDGVKigADCR 156
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 95-193 1.75e-04

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 41.55  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  95 AQIGKGLVLPHHSGVvihGNVKIGENVIIRQNTTIGekesdsreNY-------IVIGDNVDVGAHTCIIGlNVKIGSNVK 167
Cdd:PRK09451 353 ARLGKGSKAGHLTYL---GDAEIGDNVNIGAGTITC--------NYdgankfkTIIGDDVFVGSDTQLVA-PVTVGKGAT 420

                         90       100
                 ....*....|....*....|....*.
gi 693233731 168 IGAMSFIMEEVPDNCTYVTRKESRII 193
Cdd:PRK09451 421 IGAGTTVTRDVAENELVISRVPQRHI 446
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 97-170 1.80e-04

Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix (LbH) domain: Proteins in this family show simlarity to glucose-1-phosphate adenylyltransferases in that they contain N-terminal catalytic domains that resemble a dinucleotide-binding Rossmann fold and C-terminal LbH fold domains. Members in this family are predicted to be glucose-1-phosphate thymidylyltransferases, which are involved in the dTDP-L-rhamnose biosynthetic pathway. Glucose-1-phosphate thymidylyltransferase catalyzes the synthesis of deoxy-thymidine di-phosphate (dTDP)-L-rhamnose, an important component of the cell wall of many microorganisms. The C-terminal LbH domain contains multiple 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.


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 40.26  E-value: 1.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  97 IGKGLVLPhhSGVVIHGNVKIGENVIIRQNTTIgekesdsrENYIVIGDNVDVGAHT----CIIGLNVK----------- 161
Cdd:cd05636   20 IGEGAIVR--SGAYIEGPVIIGKGCEIGPNAYI--------RGYTVLGDGCVVGNSVevknSIIMDGTKvphlnyvgdsv 89


                 ....*....
gi 693233731 162 IGSNVKIGA 170
Cdd:cd05636   90 LGENVNLGA 98
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 143-182 2.86e-04

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: 39.02  E-value: 2.86e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 693233731 143 IGDNVDVGAHtCIIGLNVKIGSNVKIGAMSFIME--EVPDNC 182
Cdd:cd03358    1 IGDNCIIGTN-VFIENDVKIGDNVKIQSNVSIYEgvTIEDDV 41
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 106-174 2.94e-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: 2.94e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 693233731 106 HSGVVIHGNVKIGENVIIRQNTTIGEKesdsrenyIVIGDNVDVGAHTCIIGlNVKIGSNVKIGAMSFI 174
Cdd:cd03351    3 HPTAIVDPGAKIGENVEIGPFCVIGPN--------VEIGDGTVIGSHVVIDG-PTTIGKNNRIFPFASI 62
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 108-181 3.80e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 40.20  E-value: 3.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731 108 GVVIHGNVKIGENVIIRqNTTIGEKESDSRENYI---VIGDNVDVGA-------------HTCI-----IGLN------V 160
Cdd:PRK14354 334 GSVIGEEVKIGNFVEIK-KSTIGEGTKVSHLTYIgdaEVGENVNIGCgtitvnydgknkfKTIIgdnafIGCNsnlvapV 412

                         90       100
                 ....*....|....*....|.
gi 693233731 161 KIGSNVKIGAMSFIMEEVPDN 181
Cdd:PRK14354 413 TVGDNAYIAAGSTITKDVPED 433
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 91-163 8.48e-04

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: 36.84  E-value: 8.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  91 IGLGAQIGKGLVLPHhsgVVIHGNVKIGENV-----IIRQNTTIGEKesdSRENYIVIGDNVDVGAH-----TCIIGLNV 160
Cdd:cd03356    2 IGESTVIGENAIIKN---SVIGDNVRIGDGVtitnsILMDNVTIGAN---SVIVDSIIGDNAVIGENvrvvnLCIIGDDV 75


                 ...
gi 693233731 161 KIG 163
Cdd:cd03356   76 VVE 78
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 91-175 9.27e-04

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: 37.48  E-value: 9.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  91 IGLGAQIGKGlvlphhsgVVIHGNVKIGENVIIRQNTTIGEkesdsrenYIVIGDNVDVGAHTCIIGLN----------- 159
Cdd:cd03358    1 IGDNCIIGTN--------VFIENDVKIGDNVKIQSNVSIYE--------GVTIEDDVFIGPNVVFTNDLyprskiyrkwe 64

                         90
                 ....*....|....*....
gi 693233731 160 ---VKIGSNVKIGAMSFIM 175
Cdd:cd03358   65 lkgTTVKRGASIGANATIL 83
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 106-172 1.04e-03

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: 37.78  E-value: 1.04e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731 106 HSGVVIHGNVKIGENVIIRQNTTIgekesDSRENYIVIGDNVDVGAHTCI---IGLNVKIGSNVKIGAMS 172
Cdd:cd04645    9 APNATVIGDVTLGEGSSVWFGAVL-----RGDVNPIRIGERTNIQDGSVLhvdPGYPTIIGDNVTVGHGA 73
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 108-169 1.26e-03

Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Glucose-1-phosphate adenylyltransferase is also known as ADP-glucose synthase or ADP-glucose pyrophosphorylase. It catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for regulation of storage polysaccharide accumulation in plants and bacteria. The enzyme is a homotetramer, with each subunit containing an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain with at 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The LbH domain is involved in cooperative allosteric regulation and oligomerization.


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 36.67  E-value: 1.26e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731 108 GVVIH-GNVK---IGENVIIRQNTTIgeKESdsrenyiVIGDNVDVGAHT----CIIGLNVKIGSNVKIG 169
Cdd:cd04651   18 GCIISgGTVEnsvLFRGVRVGSGSVV--EDS-------VIMPNVGIGRNAvirrAIIDKNVVIPDGVVIG 78
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 87-168 1.66e-03

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 38.30  E-value: 1.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  87 YGCDIgLGAQIGKGLVLphhSGVVIHGNV-----KIGENVIIRQNTTIG--------EKESDSRENYIVIGdnvdVGAHT 153
Cdd:PLN02241 309 EDCRI-TDSIISHGCFL---RECKIEHSVvglrsRIGEGVEIEDTVMMGadyyeteeEIASLLAEGKVPIG----IGENT 380

                         90
                 ....*....|....*....
gi 693233731 154 ----CIIGLNVKIGSNVKI 168
Cdd:PLN02241 381 kirnAIIDKNARIGKNVVI 399
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 108-181 2.27e-03

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: 37.01  E-value: 2.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731 108 GVVI---HGNVKIGENVIIRQNTTIGEkesdSRENYIVIGDNVDVGA----HTCIIGLNV------------KIGSNVKI 168
Cdd:cd04645   29 GAVLrgdVNPIRIGERTNIQDGSVLHV----DPGYPTIIGDNVTVGHgavlHGCTIGDNCligmgaiildgaVIGKGSIV 104

                         90
                 ....*....|....*
gi 693233731 169 GAMSFIME--EVPDN 181
Cdd:cd04645  105 AAGSLVPPgkVIPPG 119
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
134-174 2.56e-03

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 36.77  E-value: 2.56e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 693233731 134 SDSRENYIVIGDNVDVGAHTCIIGLNVKIGSNVKIGAMSFI 174
Cdd:COG0110    2 KLLLLFGARIGDGVVIGPGVRIYGGNITIGDNVYIGPGVTI 42
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 88-156 4.04e-03

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: 36.20  E-value: 4.04e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 693233731  88 GCDIGLGAQIGKGLVLPHHSGVVIHGNVKIGENVIIRQNTTIGEKEsdsrenyiVIGDNVDVGAHTCII 156
Cdd:cd03350   55 NVHLSAGAVIGGVLEPLQATPVIIEDDVFIGANCEVVEGVIVGKGA--------VLAAGVVLTQSTPIY 115
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 141-175 5.05e-03

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: 35.12  E-value: 5.05e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 693233731 141 IVIGDNVDVGAHTCIIGLN-VKIGSNVKIGAMSFIM 175
Cdd:cd04647    2 ISIGDNVYIGPGCVISAGGgITIGDNVLIGPNVTIY 37
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 88-187 5.07e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 37.03  E-value: 5.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  88 GCDIGLGAQIGKGLVL--------------PH-HSGVVIHGNVKIGeNVIIRQNTTIGEKESDSRENYI---VIGDNVDV 149
Cdd:PRK14355 303 GCRIGDDVTVKAGSVLedsvvgddvaigpmAHlRPGTELSAHVKIG-NFVETKKIVMGEGSKASHLTYLgdaTIGRNVNI 381

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 693233731 150 GA------------HTCIIGLNVKIGSNVK------------IGAMSFIMEEVPDNCTYVTR 187
Cdd:PRK14355 382 GCgtitcnydgvkkHRTVIEDDVFVGSDVQfvapvtvgrnslIAAGTTVTKDVPPDSLAIAR 443
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 91-179 5.96e-03

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: 35.43  E-value: 5.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  91 IGLGAQIGKGLVLphHSGVVIHGNVKIGENVIIRQNTTIGEKESDSRENYIVIGDNVDVGAHtCIIGLNVKIGSNVKIGA 170
Cdd:cd03350   28 VNIGAYVDEGTMV--DSWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIEDDVFIGAN-CEVVEGVIVGKGAVLAA 104


                 ....*....
gi 693233731 171 MSFIMEEVP 179
Cdd:cd03350  105 GVVLTQSTP 113
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 92-180 7.45e-03

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 36.65  E-value: 7.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731   92 GLGAQIGKGLV-----LPHHSGVVIHGNVKIGENVIIRqntTIGEKESDSRENYIVIGDNVDVGAHTcIIGLNVKIGSNV 166
Cdd:TIGR02353 595 LLGVKIGRGVYidgtdLTERDLVTIGDDSTLNEGSVIQ---THLFEDRVMKSDTVTIGDGATLGPGA-IVLYGVVMGEGS 670

                          90
                  ....*....|....*.
gi 693233731  167 KIGAMSFIM--EEVPD 180
Cdd:TIGR02353 671 VLGPDSLVMkgEEVPA 686
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 89-169 8.38e-03

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 36.44  E-value: 8.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 693233731  89 CDIGLGAQIGKGLVLPhhsgvvihgNVKIGENVIIrQNTTIgekeSDSRenyivIGDNVDVGAHTCIIGlNVKIGSNVKI 168
Cdd:PRK14360 281 TVIGSGCRIGPGSLIE---------NSQIGENVTV-LYSVV----SDSQ-----IGDGVKIGPYAHLRP-EAQIGSNCRI 340


                 .
gi 693233731 169 G 169
Cdd:PRK14360 341 G 341
 
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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