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Conserved domains on  [gi|60493708|emb|CAH08497|]
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putative acetyltransferase [Bacteroides fragilis NCTC 9343]

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 ...
 77-175 2.25e-36

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: 122.16  E-value: 2.25e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708  77 ITIYP-NTIGAGLRIYHvGDFIHIGAQCHIGHNCTLLPGVVFGNKYEKATDTQIIAGNNCYFGLGAKIFGSIIIGNNVTI 155
Cdd:cd03354   3 IDIHPgAKIGPGLFIDH-GTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVKI 81

                        90       100
                ....*....|....*....|
gi 60493708 156 GANAVVTKDIPDNAIVGGIP 175
Cdd:cd03354  82 GANAVVTKDVPANSTVVGVP 101
 
Name Accession Description Interval E-value
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 77-175 2.25e-36

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: 122.16  E-value: 2.25e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708  77 ITIYP-NTIGAGLRIYHvGDFIHIGAQCHIGHNCTLLPGVVFGNKYEKATDTQIIAGNNCYFGLGAKIFGSIIIGNNVTI 155
Cdd:cd03354   3 IDIHPgAKIGPGLFIDH-GTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVKI 81

                        90       100
                ....*....|....*....|
gi 60493708 156 GANAVVTKDIPDNAIVGGIP 175
Cdd:cd03354  82 GANAVVTKDVPANSTVVGVP 101
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 11-184 3.77e-33

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: 116.34  E-value: 3.77e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708  11 YLSEDLKRFNNHKPNIKDWLlhnEIWYI---FHYIRHLRYVEYYKNTNknkiLFFYHFFRYKRLGFKLKITIYPN-TIGA 86
Cdd:COG1045   4 ALREDIQAVFERDPAARSLL---EVLLCypgFHALALHRLAHWLWKRG----LPLLARLLSERARFLTGIDIHPGaTIGR 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708  87 GLRIYHvGDFIHIGAQCHIGHNCTLLPGVVFGNKYEKATDTQIIAGNNCYFGLGAKIFGSIIIGNNVTIGANAVVTKDIP 166
Cdd:COG1045  77 GFFIDH-GTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVP 155

                       170
                ....*....|....*...
gi 60493708 167 DNAIVGGIPAKVLRFKEI 184
Cdd:COG1045 156 PGSTVVGVPARIVKRKGS 173
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 82-176 1.13e-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: 76.76  E-value: 1.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708    82 NTIGAGLRIyhvGDFIHI------GAQCHIGHNCTLLPGVVF-GNkyekatdtqIIAGNNCYFGLGAKIFGSIIIGNNVT 154
Cdd:TIGR03570 112 AVINPDVRI---GDNVIIntgaivEHDCVIGDFVHIAPGVTLsGG---------VVIGEGVFIGAGATIIQGVTIGAGAI 179

                          90       100
                  ....*....|....*....|..
gi 60493708   155 IGANAVVTKDIPDNAIVGGIPA 176
Cdd:TIGR03570 180 VGAGAVVTKDIPDGGVVVGVPA 201
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 104-180 1.48e-13

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 65.60  E-value: 1.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708  104 HIGHNCTLLPGV--------------VFGNKYEKAtdtqIIAGNNCYFGLGAKIFGSIIIGNNVTIGANAVVTKDIPDNA 169
Cdd:PRK10092  95 RIGDNCMLAPGVhiytathpldpvarNSGAELGKP----VTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNV 170

                         90
                 ....*....|.
gi 60493708  170 IVGGIPAKVLR 180
Cdd:PRK10092 171 VVGGNPARIIK 181
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
129-163 1.23e-03

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 35.11  E-value: 1.23e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 60493708   129 IIAGNNCYFGLGAKIfgSIIIGNNVTIGANAVVTK 163
Cdd:pfam14602   1 VIIGDNCLIGANSGI--GVSLGDNCVVGAGVVITA 33
 
Name Accession Description Interval E-value
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 77-175 2.25e-36

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: 122.16  E-value: 2.25e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708  77 ITIYP-NTIGAGLRIYHvGDFIHIGAQCHIGHNCTLLPGVVFGNKYEKATDTQIIAGNNCYFGLGAKIFGSIIIGNNVTI 155
Cdd:cd03354   3 IDIHPgAKIGPGLFIDH-GTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVKI 81

                        90       100
                ....*....|....*....|
gi 60493708 156 GANAVVTKDIPDNAIVGGIP 175
Cdd:cd03354  82 GANAVVTKDVPANSTVVGVP 101
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 11-184 3.77e-33

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: 116.34  E-value: 3.77e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708  11 YLSEDLKRFNNHKPNIKDWLlhnEIWYI---FHYIRHLRYVEYYKNTNknkiLFFYHFFRYKRLGFKLKITIYPN-TIGA 86
Cdd:COG1045   4 ALREDIQAVFERDPAARSLL---EVLLCypgFHALALHRLAHWLWKRG----LPLLARLLSERARFLTGIDIHPGaTIGR 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708  87 GLRIYHvGDFIHIGAQCHIGHNCTLLPGVVFGNKYEKATDTQIIAGNNCYFGLGAKIFGSIIIGNNVTIGANAVVTKDIP 166
Cdd:COG1045  77 GFFIDH-GTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVP 155

                       170
                ....*....|....*...
gi 60493708 167 DNAIVGGIPAKVLRFKEI 184
Cdd:COG1045 156 PGSTVVGVPARIVKRKGS 173
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
73-180 6.02e-23

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 88.77  E-value: 6.02e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708  73 FKLKITIYPNT-IGAGLRIY----HVGDFIHIGAQCH--------IGHNCTLLPGVVFGN----------KYEKATDTQI 129
Cdd:COG0110   5 LLFGARIGDGVvIGPGVRIYggniTIGDNVYIGPGVTiddpggitIGDNVLIGPGVTILTgnhpiddpatFPLRTGPVTI 84

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 60493708 130 iaGNNCYFGLGAKIFGSIIIGNNVTIGANAVVTKDIPDNAIVGGIPAKVLR 180
Cdd:COG0110  85 --GDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIR 133
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 94-179 3.75e-20

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: 82.47  E-value: 3.75e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708  94 GDFIHIGAQCHIGHNCTLL--------------PGVVFgnkY---------EKATDTQ----IIAGNNCYFGLGAKIFGS 146
Cdd:cd03357  60 GYNIHIGDNFYANFNCTILdvapvtigdnvligPNVQI---YtaghpldpeERNRGLEyakpITIGDNVWIGGGVIILPG 136

                        90       100       110
                ....*....|....*....|....*....|...
gi 60493708 147 IIIGNNVTIGANAVVTKDIPDNAIVGGIPAKVL 179
Cdd:cd03357 137 VTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 83-179 4.84e-19

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: 77.88  E-value: 4.84e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708  83 TIGAGLRIYHVGDfIHIGAQCHIGHNCTLLPG-----VVFGNKYEKATDTQIIAGNNCYFGLGAKIFGSIIIGNNVTIGA 157
Cdd:cd04647   9 YIGPGCVISAGGG-ITIGDNVLIGPNVTIYDHnhdidDPERPIEQGVTSAPIVIGDDVWIGANVVILPGVTIGDGAVVGA 87

                        90       100
                ....*....|....*....|..
gi 60493708 158 NAVVTKDIPDNAIVGGIPAKVL 179
Cdd:cd04647  88 GSVVTKDVPPNSIVAGNPAKVI 109
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 82-175 9.00e-18

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: 76.75  E-value: 9.00e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708  82 NTIGAGLRIyhvGDFIHIGAQCHIGHNC------TLLPGVVF-GNkyekatdTQIiaGNNCYFGLGAKIFGSIIIGNNVT 154
Cdd:cd03360 109 AVINPDARI---GDNVIINTGAVIGHDCvigdfvHIAPGVVLsGG-------VTI--GEGAFIGAGATIIQGVTIGAGAI 176

                        90       100
                ....*....|....*....|.
gi 60493708 155 IGANAVVTKDIPDNAIVGGIP 175
Cdd:cd03360 177 IGAGAVVTKDVPDGSVVVGNP 197
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 82-176 1.13e-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: 76.76  E-value: 1.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708    82 NTIGAGLRIyhvGDFIHI------GAQCHIGHNCTLLPGVVF-GNkyekatdtqIIAGNNCYFGLGAKIFGSIIIGNNVT 154
Cdd:TIGR03570 112 AVINPDVRI---GDNVIIntgaivEHDCVIGDFVHIAPGVTLsGG---------VVIGEGVFIGAGATIIQGVTIGAGAI 179

                          90       100
                  ....*....|....*....|..
gi 60493708   155 IGANAVVTKDIPDNAIVGGIPA 176
Cdd:TIGR03570 180 VGAGAVVTKDIPDGGVVVGVPA 201
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 94-181 6.54e-17

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: 73.35  E-value: 6.54e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708  94 GDFIHIGAQCHIGHNCTLLPGV----------------------VFGNKYEKATDTQIiaGNNCYFGLGAKIFGSIIIGN 151
Cdd:cd03349  19 GDKLSIGKFCSIAPGVKIGLGGnhptdwvstypfyifggeweddAKFDDWPSKGDVII--GNDVWIGHGATILPGVTIGD 96

                        90       100       110
                ....*....|....*....|....*....|
gi 60493708 152 NVTIGANAVVTKDIPDNAIVGGIPAKVLRF 181
Cdd:cd03349  97 GAVIAAGAVVTKDVPPYAIVGGNPAKVIRY 126
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 104-180 1.48e-13

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 65.60  E-value: 1.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708  104 HIGHNCTLLPGV--------------VFGNKYEKAtdtqIIAGNNCYFGLGAKIFGSIIIGNNVTIGANAVVTKDIPDNA 169
Cdd:PRK10092  95 RIGDNCMLAPGVhiytathpldpvarNSGAELGKP----VTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNV 170

                         90
                 ....*....|.
gi 60493708  170 IVGGIPAKVLR 180
Cdd:PRK10092 171 VVGGNPARIIK 181
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 97-180 2.71e-13

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 64.28  E-value: 2.71e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708  97 IHIGAQCHIGHNCTLLPGVVfgnkyekatdtqiiaGNNCYFGLGAKIFGSIIIGNNVTIGANAVVT--KDIPDNAIVGGI 174
Cdd:COG0663  72 LTIGDDVTIGHGAILHGCTI---------------GDNVLIGMGAIVLDGAVIGDGSIVGAGALVTegKVVPPGSLVVGS 136


                ....*.
gi 60493708 175 PAKVLR 180
Cdd:COG0663 137 PAKVVR 142
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 93-177 3.57e-13

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: 64.74  E-value: 3.57e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708  93 VGDFIHIGAQCHIGHNCTLLPGVVFGNKYEKATDTQIiaGNNCYFGLGAKIFGSIIIGNNVTIGANAVVTKDIPDNAIVG 172
Cdd:cd03352 117 IGDGTKIDNLVQIAHNVRIGENCLIAAQVGIAGSTTI--GDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVS 194


                ....*
gi 60493708 173 GIPAK 177
Cdd:cd03352 195 GTPAQ 199
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 84-180 1.52e-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: 61.36  E-value: 1.52e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708  84 IGAGLRIyhvGDFIHIGAQCHIGHNCTLL------------------PGVVFGN-------KYEKATDTQIIAGNNCYFG 138
Cdd:cd03358   1 IGDNCII---GTNVFIENDVKIGDNVKIQsnvsiyegvtieddvfigPNVVFTNdlyprskIYRKWELKGTTVKRGASIG 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 60493708 139 LGAKIFGSIIIGNNVTIGANAVVTKDIPDNAIVGGIPAKVLR 180
Cdd:cd03358  78 ANATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 125-184 4.48e-12

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 61.82  E-value: 4.48e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708  125 TDTQIIAGNNCYFGLGAKIFGSIIIGNNVTIGANAVVTKDIPDNAIVGGIPAKVLRFKEI 184
Cdd:PRK09677 127 ESSAVVIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKKYNH 186
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 78-177 4.99e-12

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: 63.11  E-value: 4.99e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708  78 TIYPNT-IGAGLRIyhvGD--FIH----IGAQCHIGHNCTLLPGVV-----FGN------KYEK---------------- 123
Cdd:COG1044 134 VIGPGVvIGDGVVI---GDdcVLHpnvtIYERCVIGDRVIIHSGAVigadgFGFapdedgGWVKipqlgrvvigddveig 210

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708 124 -------AT--DTQI-----------------------------IAG-----NNCYFGLGAKIFGSIIIGNNVTIGANAV 160
Cdd:COG1044 211 anttidrGAlgDTVIgdgtkidnlvqiahnvrigehtaiaaqvgIAGstkigDNVVIGGQVGIAGHLTIGDGVIIGAQSG 290

                       170
                ....*....|....*..
gi 60493708 161 VTKDIPDNAIVGGIPAK 177
Cdd:COG1044 291 VTKSIPEGGVYSGSPAQ 307
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 97-180 5.37e-12

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: 60.50  E-value: 5.37e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708  97 IHIGAQCHIGHNCTLLPGVVfgnkyekatdtqiiaGNNCYFGLGAKIFGSIIIGNNVTIGANAVVT--KDIPDNAIVGGI 174
Cdd:cd04645  61 TIIGDNVTVGHGAVLHGCTI---------------GDNCLIGMGAIILDGAVIGKGSIVAAGSLVPpgKVIPPGSLVAGS 125


                ....*.
gi 60493708 175 PAKVLR 180
Cdd:cd04645 126 PAKVVR 131
PLN02739 PLN02739
serine acetyltransferase
 77-183 2.25e-11

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 61.21  E-value: 2.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708   77 ITIYPNT-IGAGLRIYHvGDFIHIGAQCHIGHNCTLLPGVVFGNKYEKATDTQIIAGNNCYFGLGAKIFGSIIIGNNVTI 155
Cdd:PLN02739 206 IDIHPAArIGKGILLDH-GTGVVIGETAVIGDRVSILHGVTLGGTGKETGDRHPKIGDGALLGACVTILGNISIGAGAMV 284

                         90       100
                 ....*....|....*....|....*...
gi 60493708  156 GANAVVTKDIPDNAIVGGIPAKVLRFKE 183
Cdd:PLN02739 285 AAGSLVLKDVPSHSMVAGNPAKLIGFVD 312
PRK10191 PRK10191
putative acyl transferase; Provisional
 59-178 4.53e-11

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 57.98  E-value: 4.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708   59 ILFFYHFFRYKRLGFKLKITIypnTIGAGLRIYHvGDFIHIGAQCHIGHNCTLLPGVVFGNKYEKATDTQIIaGNNCYFG 138
Cdd:PRK10191  28 LLVLYRIITECFFGYEIQAAA---TIGRRFTIHH-GYAVVINKNVVAGDDFTIRHGVTIGNRGADNMACPHI-GNGVELG 102

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 60493708  139 LGAKIFGSIIIGNNVTIGANAVVTKDIPDNAIVGGIPAKV 178
Cdd:PRK10191 103 ANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKARV 142
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 129-185 4.24e-10

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 56.55  E-value: 4.24e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 60493708  129 IIAGNNCYFGLGAKIFGSIIIGNNVTIGANAVVTKDIPDNAIVGGIPAKVLRfkEIN 185
Cdd:PRK09527 132 ITIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIR--EIN 186
PLN02694 PLN02694
serine O-acetyltransferase
 68-183 5.09e-10

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 57.34  E-value: 5.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708   68 YKRLGFKLKITIYPNT-IGAGLRIYHVGDFIhIGAQCHIGHNCTLLPGVVFGNKYEKATDTQIIAGNNCYFGLGAKIFGS 146
Cdd:PLN02694 152 HSRISDVFAVDIHPAAkIGKGILFDHATGVV-IGETAVIGNNVSILHHVTLGGTGKACGDRHPKIGDGVLIGAGATILGN 230

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 60493708  147 IIIGNNVTIGANAVVTKDIPDNAIVGGIPAKVLRFKE 183
Cdd:PLN02694 231 VKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLVGGKE 267
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 80-187 1.47e-09

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 55.92  E-value: 1.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708   80 YPNTIGAGLRIYHVG-----DFIHIGA----------------------QCHIGHNC-----TLLPGVVfgnkyekatdt 127
Cdd:PRK00892 188 FANDRGGWVKIPQLGrviigDDVEIGAnttidrgalddtvigegvkidnLVQIAHNVvigrhTAIAAQV----------- 256

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 60493708  128 qIIAG-----NNCYFGLGAKIFGSIIIGNNVTIGANAVVTKDIPD-NAIVGGIPAKVLR--FKEINIL 187
Cdd:PRK00892 257 -GIAGstkigRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEpGEYSSGIPAQPNKewLRTAARL 323
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 97-180 1.76e-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: 1.76e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708  97 IHIGAQCHIGHNctllpGVVFGNKyekatdtqiiAGNNCYFGLGAKIFGSIIIGNNVTIGANAVVT--KDIPDNAIVGGI 174
Cdd:cd04650  62 TEIGDYVTIGHN-----AVVHGAK----------VGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTpgKEIPDYSLVLGV 126


                ....*.
gi 60493708 175 PAKVLR 180
Cdd:cd04650 127 PAKVVR 132
PRK10502 PRK10502
putative acyl transferase; Provisional
 84-180 3.04e-09

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 53.80  E-value: 3.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708   84 IGAGLRIYHVGDfIHIGAQCHIGHNCTLLPGvvfGNKYEKAT----DTQIIAGNNCYFGLGAKIFGSIIIGNNVTIGANA 159
Cdd:PRK10502  80 IGDDVWLYNLGE-ITIGAHCVISQKSYLCTG---SHDYSDPHfdlnTAPIVIGEGCWLAADVFVAPGVTIGSGAVVGARS 155

                         90       100
                 ....*....|....*....|.
gi 60493708  160 VVTKDIPDNAIVGGIPAKVLR 180
Cdd:PRK10502 156 SVFKSLPANTICRGNPAVPIR 176
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 83-161 3.75e-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: 54.64  E-value: 3.75e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 60493708  83 TIGAGLRIyhvGDFIHIGAQCHIGHNCTLLPGVVFGNkyekatDTQIiaGNNCYFGLGAKIFGSIIIGNNVTIGANAVV 161
Cdd:COG1044 110 KIGEGVSI---GPFAVIGAGVVIGDGVVIGPGVVIGD------GVVI--GDDCVLHPNVTIYERCVIGDRVIIHSGAVI 177
PLN02357 PLN02357
serine acetyltransferase
 77-183 6.74e-09

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 54.12  E-value: 6.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708   77 ITIYPNT-IGAGLRIYHVGDFIhIGAQCHIGHNCTLLPGVVFGNKYEKATDTQIIAGNNCYFGLGAKIFGSIIIGNNVTI 155
Cdd:PLN02357 227 VDIHPGAkIGQGILLDHATGVV-IGETAVVGNNVSILHNVTLGGTGKQSGDRHPKIGDGVLIGAGTCILGNITIGEGAKI 305

                         90       100
                 ....*....|....*....|....*...
gi 60493708  156 GANAVVTKDIPDNAIVGGIPAKVLRFKE 183
Cdd:PLN02357 306 GAGSVVLKDVPPRTTAVGNPARLIGGKE 333
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 82-161 2.28e-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: 51.64  E-value: 2.28e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708  82 NTIGAGLRIyhvGDFIHIGAQCHIGHNCTLLPGVVFGNkyekatDTQIiaGNNCYFGLGAKIFGSIIIGNNVTIGANAVV 161
Cdd:cd03352   2 AKIGENVSI---GPNAVIGEGVVIGDGVVIGPGVVIGD------GVVI--GDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 76-179 2.47e-08

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: 49.91  E-value: 2.47e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708  76 KITIYPNT-IGAGLRIYHVGDfIHIGAQCHIGHNCTLLPGvvfGNKYEKAT---DTQ-IIAGNNCYFGLGAKIFGSIIIG 150
Cdd:cd05825   3 NLTIGDNSwIGEGVWIYNLAP-VTIGSDACISQGAYLCTG---SHDYRSPAfplITApIVIGDGAWVAAEAFVGPGVTIG 78

                        90       100
                ....*....|....*....|....*....
gi 60493708 151 NNVTIGANAVVTKDIPDNAIVGGIPAKVL 179
Cdd:cd05825  79 EGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 93-162 5.61e-08

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: 48.01  E-value: 5.61e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708  93 VGDFIHIGAQCHIGHNCTLLPGVVFGNKYEKATDTQIIAGNNCYFGLGAKIFGSIIIGNNVTIGANAVVT 162
Cdd:cd00208   9 IHPKAVIRGPVVIGDNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 83-161 8.07e-08

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 50.91  E-value: 8.07e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 60493708   83 TIGAGLriyHVGDFIHIGAQCHIGHNCTLLPGVVFGNkyekatDTQIiaGNNCYFGLGAKIFGSIIIGNNVTIGANAVV 161
Cdd:PRK00892 114 KIGEGV---SIGPNAVIGAGVVIGDGVVIGAGAVIGD------GVKI--GADCRLHANVTIYHAVRIGNRVIIHSGAVI 181
cysE PRK11132
serine acetyltransferase; Provisional
 79-178 1.29e-07

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 50.08  E-value: 1.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708   79 IYPN-TIGAGLRIYHVGDfIHIGAQCHIGHNCTLLPGVVFGNKYEKATDTQIIAGNNCYFGLGAKIFGSIIIGNNVTIGA 157
Cdd:PRK11132 144 IHPAaKIGRGIMLDHATG-IVIGETAVIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGA 222

                         90       100
                 ....*....|....*....|.
gi 60493708  158 NAVVTKDIPDNAIVGGIPAKV 178
Cdd:PRK11132 223 GSVVLQPVPPHTTAAGVPARI 243
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 81-161 1.87e-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: 48.94  E-value: 1.87e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708  81 PNTIGAGLRIyhvGDFIHIGAQCHIGHNCTLLPGVVFGNkyekatDTQIiaGNNCYFGLGAKI----------------- 143
Cdd:cd03352  19 GVVIGDGVVI---GPGVVIGDGVVIGDDCVIHPNVTIYE------GCII--GDRVIIHSGAVIgsdgfgfapdgggwvki 87

                        90       100
                ....*....|....*....|
gi 60493708 144 --FGSIIIGNNVTIGANAVV 161
Cdd:cd03352  88 pqLGGVIIGDDVEIGANTTI 107
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 83-171 3.06e-07

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 49.25  E-value: 3.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708   83 TIGAGLRIYH---VGDfIHIGAQCHIGhnctllPGVVFGNkYEKATDTQIIAGNNCYFGLGAKIFGSIIIGNNVTIGANA 159
Cdd:PRK09451 354 RLGKGSKAGHltyLGD-AEIGDNVNIG------AGTITCN-YDGANKFKTIIGDDVFVGSDTQLVAPVTVGKGATIGAGT 425

                         90
                 ....*....|..
gi 60493708  160 VVTKDIPDNAIV 171
Cdd:PRK09451 426 TVTRDVAENELV 437
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 85-180 1.44e-06

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


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 45.82  E-value: 1.44e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708  85 GAGLRiyhvGDF--IHIGAQCHIGHNCTL--LPGV-----VFGNKYEKATDTQIIAGNNCYFGLGAKIFGSIIIGNNVTI 155
Cdd:cd04745  30 HASLR----GDFgrIVIRDGANVQDNCVIhgFPGQdtvleENGHIGHGAILHGCTIGRNALVGMNAVVMDGAVIGEESIV 105

                        90       100
                ....*....|....*....|....*..
gi 60493708 156 GANAVVTK--DIPDNAIVGGIPAKVLR 180
Cdd:cd04745 106 GAMAFVKAgtVIPPRSLIAGSPAKVIR 132
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 78-171 4.81e-06

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 45.69  E-value: 4.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708   78 TIYPNTIGAGLRIyhvGDFIHIGAQCHIGHNCTLlpgvvfGNKYEkATDTQIIAGNNC----YFG---LGAK-------- 142
Cdd:PRK14360 310 VVSDSQIGDGVKI---GPYAHLRPEAQIGSNCRI------GNFVE-IKKSQLGEGSKVnhlsYIGdatLGEQvnigagti 379

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 60493708  143 ------------IFGS-------------IIIGNNVTIGANAVVTKDIPDNAIV 171
Cdd:PRK14360 380 tanydgvkkhrtVIGDrsktgansvlvapITLGEDVTVAAGSTITKDVPDNSLA 433
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 77-178 7.23e-06

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: 44.94  E-value: 7.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708    77 ITIYPNTIGAGlRIYHVGDFIHIGAQCHIGHNCTLLPGVVFGNKYEKATDTQIiaGNNCYFGLGAKIFGSIIIGNNVTIG 156
Cdd:TIGR01852  89 VTINRGTASGG-GVTRIGNNNLLMAYSHIAHDCVVGNHVILANNATLAGHVEV--GDYAIIGGLVAVHQFVRIGRYAMIG 165

                          90       100
                  ....*....|....*....|..
gi 60493708   157 ANAVVTKDIPDNAIVGGIPAKV 178
Cdd:TIGR01852 166 GLSAVSKDVPPYCLAEGNRARL 187
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 101-178 9.86e-06

UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this family catalyze the transfer of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to UDP-GlcNAc. It is the first enzyme in the lipid A biosynthetic pathway and is also referred to as LpxA. Lipid A is essential for the growth of Escherichia coli and related bacteria. It is also essential for maintaining the integrity of the outer membrane. UDP-GlcNAc acyltransferase is a homotrimer of left-handed parallel beta helix (LbH) subunits. Each subunit contains an N-terminal LbH region with 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal alpha-helical region.


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 44.35  E-value: 9.86e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708 101 AQCHIGHNCTLlpgvvfgnkyekatdtqiiaGNNCYFGLGAKIFGSIIIGNNVTIGAN------------------AVVT 162
Cdd:cd03351 113 AYVHVAHDCVI--------------------GNNVILANNATLAGHVEIGDYAIIGGLsavhqfcrigrhamvgggSGVV 172

                        90
                ....*....|....*.
gi 60493708 163 KDIPDNAIVGGIPAKV 178
Cdd:cd03351 173 QDVPPYVIAAGNRARL 188
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 93-166 1.36e-05

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


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 43.14  E-value: 1.36e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60493708  93 VGDFIHIGAQCHIGHNCTLLPGVVFGNKYEKATDTQIIAGNNCYFGLGAKIFGSIIIGNNVTIGANAVVTKDIP 166
Cdd:cd03350  40 VDSWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTQSTP 113
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 83-171 1.40e-05

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: 43.56  E-value: 1.40e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708  83 TIGAGLRIYH---VGDfIHIGAQCHIGhnctllPGVVFGN-----KYEkatdTQIiaGNNCYFGLGAKIFGSIIIGNNVT 154
Cdd:cd03353 104 TIGEGSKANHlsyLGD-AEIGEGVNIG------AGTITCNydgvnKHR----TVI--GDNVFIGSNSQLVAPVTIGDGAT 170

                        90
                ....*....|....*..
gi 60493708 155 IGANAVVTKDIPDNAIV 171
Cdd:cd03353 171 IAAGSTITKDVPPGALA 187
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 78-171 8.98e-05

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: 41.94  E-value: 8.98e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708  78 TIYPNT------IGAGLRIYH-VGDFIHIGAQCHIGHNCTLLPGVVF------GNKYE--KAT--------------DTQ 128
Cdd:COG1207 292 VIGPNCtlkdstIGDGVVIKYsVIEDAVVGAGATVGPFARLRPGTVLgegvkiGNFVEvkNSTigegskvnhlsyigDAE 371

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 60493708 129 IiaGNNCYFGLG-------------------AKIfGS-------IIIGNNVTIGANAVVTKDIPDNAIV 171
Cdd:COG1207 372 I--GEGVNIGAGtitcnydgvnkhrtvigdgAFI-GSntnlvapVTIGDGATIGAGSTITKDVPAGALA 437
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 101-178 1.28e-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: 41.16  E-value: 1.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708 101 AQCHIGHNCTLlpgvvfgnkyekatdtqiiaGNNCYFGLGAKIFGSIIIGNNVTIGANA------------------VVT 162
Cdd:COG1043 115 AYVHVAHDCVV--------------------GNNVILANNATLAGHVEVGDHAIIGGLSavhqfvrigahamvgggsGVV 174

                        90
                ....*....|....*.
gi 60493708 163 KDIPDNAIVGGIPAKV 178
Cdd:COG1043 175 KDVPPYVLAAGNPARL 190
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 99-172 1.33e-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: 38.76  E-value: 1.33e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 60493708  99 IGAQCHIGHNCTLLPGVVFGNKY--EKATDTQIIAGNNCYFGLGAKIFGSIIiGNNVTIGANAvvtkDIPDNAIVG 172
Cdd:cd03356   2 IGESTVIGENAIIKNSVIGDNVRigDGVTITNSILMDNVTIGANSVIVDSII-GDNAVIGENV----RVVNLCIIG 72
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 83-170 2.43e-04

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 40.62  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708   83 TIGAGLRIYH---VGDfIHIGAQCHIGhnctllPGVVFGN-----KYEkatdTQIiagnncyfglGAKIFgsiiIGNN-- 152
Cdd:PRK14353 340 KLGEGAKVNHltyIGD-ATIGAGANIG------AGTITCNydgfnKHR----TEI----------GAGAF----IGSNsa 394

                         90       100
                 ....*....|....*....|....*...
gi 60493708  153 ----VTIGANA------VVTKDIPDNAI 170
Cdd:PRK14353 395 lvapVTIGDGAyiasgsVITEDVPDDAL 422
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
129-163 1.23e-03

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 35.11  E-value: 1.23e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 60493708   129 IIAGNNCYFGLGAKIfgSIIIGNNVTIGANAVVTK 163
Cdd:pfam14602   1 VIIGDNCLIGANSGI--GVSLGDNCVVGAGVVITA 33
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 78-156 1.51e-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: 38.47  E-value: 1.51e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708  78 TIYPNTIgagLRiyhvGDfIHIGAQCHIGHNCTLlpgvvfgnkyekaTDTQIiagnncyfGLGAKIFGSII----IGNNV 153
Cdd:COG1207 274 VIDPNVI---LE----GK-TVIGEGVVIGPNCTL-------------KDSTI--------GDGVVIKYSVIedavVGAGA 324


                ...
gi 60493708 154 TIG 156
Cdd:COG1207 325 TVG 327
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 83-170 1.62e-03

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 38.17  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708   83 TIGAGLRIYhvgDFIH-----IGAQCHIGHNCTLLPGVVF------GNKYE--KAT--------------DTQIIAGNN- 134
Cdd:PRK14356 306 VVSSGATIH---SFSHlegaeVGDGCSVGPYARLRPGAVLeegarvGNFVEmkKAVlgkgakanhltylgDAEIGAGANi 382

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 60493708  135 ------C-YFG-------LGAKIF-GS-------IIIGNNVTIGANAVVTKDIPDNAI 170
Cdd:PRK14356 383 gagtitCnYDGvnkhrtvIGEGAFiGSntalvapVTIGDGALVGAGSVITKDVPDGSL 440
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
101-178 1.89e-03

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 37.77  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708  101 AQCHIGHNCTLlpgvvfgnkyekatdtqiiaGNNCYFGLGAKIFGSIIIGNNVTIGANAVV------------------T 162
Cdd:PRK05289 116 AYVHVAHDCVV--------------------GNHVILANNATLAGHVEVGDYAIIGGLTAVhqfvrigahamvggmsgvS 175

                         90
                 ....*....|....*.
gi 60493708  163 KDIPDNAIVGGIPAKV 178
Cdd:PRK05289 176 QDVPPYVLAEGNPARL 191
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 83-170 2.64e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 37.50  E-value: 2.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708   83 TIGAGLRIYH---VGDfIHIGAQCHIGhnCtllpGVVFGNkYEKATDTQIIAGNNCYFGLGAKIFGSIIIGNNVTIGANA 159
Cdd:PRK14354 353 TIGEGTKVSHltyIGD-AEVGENVNIG--C----GTITVN-YDGKNKFKTIIGDNAFIGCNSNLVAPVTVGDNAYIAAGS 424

                         90
                 ....*....|.
gi 60493708  160 VVTKDIPDNAI 170
Cdd:PRK14354 425 TITKDVPEDAL 435
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 99-157 5.35e-03

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: 34.52  E-value: 5.35e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 60493708  99 IGAQCHIGHNCTLLPGVVFGNKY--EKATDTQIIAGNNCYFGLGAKIFGSIIIGNNVTIGA 157
Cdd:cd03356  19 IGDNVRIGDGVTITNSILMDNVTigANSVIVDSIIGDNAVIGENVRVVNLCIIGDDVVVED 79
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 99-172 6.95e-03

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: 34.09  E-value: 6.95e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 60493708  99 IGAQCHIGHNCTLlpgvvfgnkyekatdTQIIAGNNCYFGLGAKIFGSIIIgNNVTIGANAVVTKDI-PDNAIVG 172
Cdd:cd05787   2 IGRGTSIGEGTTI---------------KNSVIGRNCKIGKNVVIDNSYIW-DDVTIEDGCTIHHSIvADGAVIG 60
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 92-178 7.88e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 36.15  E-value: 7.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 60493708   92 HVGDFIHIGAQCHIGHNCTLlpgvvfgnkyekatdtqiiaGNNCYFGLGAKIFGSIIIGNNVTIGANAVV---------- 161
Cdd:PRK12461 103 RIGNDNLLMAYSHVAHDCQI--------------------GNNVILVNGALLAGHVTVGDRAIISGNCLVhqfcrigala 162

                         90       100
                 ....*....|....*....|....*
gi 60493708  162 --------TKDIPDNAIVGGIPAKV 178
Cdd:PRK12461 163 mmaggsriSKDVPPYCMMAGHPTNV 187
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 99-172 8.71e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 35.96  E-value: 8.71e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 60493708   99 IGAQCHIGHNCTLLPGVVFGNKyekatdTQIiaGNNCYFGLGAKIFGSIIiGNNVTIGANAVVTKDIPDNAIVG 172
Cdd:PRK14354 262 IDADVEIGSDTVIEPGVVIKGN------TVI--GEDCVIGPGSRIVDSTI-GDGVTITNSVIEESKVGDNVTVG 326
 
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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