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Conserved domains on  [gi|556251193|ref|WP_023286707|]
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MULTISPECIES: DapH/DapD/GlmU-related protein [Klebsiella]

Protein Classification

acyltransferase( domain architecture ID 11414744)

acyltransferase belonging to the transferase hexapeptide repeat family, catalyzes the transfer of an acyl group from an acyl-CoA to a substrate

CATH:  2.160.10.10
EC:  2.3.-.-
Gene Ontology:  GO:0046677|GO:0016746|GO:0120225
PubMed:  15500694
SCOP:  4002841

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
52-190 1.97e-38

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


:

Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 128.84  E-value: 1.97e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  52 KGNVKVGNNVRFGPFARIGateGAKIIIGDNVSVNQGSFIISRESIVIGNNTRVGEYVSIRDNDHEWRDKNTPILKQGFI 131
Cdd:COG0110    6 LFGARIGDGVVIGPGVRIY---GGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPATFPLRTGPV 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 556251193 132 TnsveIGSDVWIGRNVVICKGVKIGDGAVIGANAVITKNVNQYEVVVGNPGRVIKVRGE 190
Cdd:COG0110   83 T----IGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDE 137
 
Name Accession Description Interval E-value
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
52-190 1.97e-38

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 128.84  E-value: 1.97e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  52 KGNVKVGNNVRFGPFARIGateGAKIIIGDNVSVNQGSFIISRESIVIGNNTRVGEYVSIRDNDHEWRDKNTPILKQGFI 131
Cdd:COG0110    6 LFGARIGDGVVIGPGVRIY---GGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPATFPLRTGPV 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 556251193 132 TnsveIGSDVWIGRNVVICKGVKIGDGAVIGANAVITKNVNQYEVVVGNPGRVIKVRGE 190
Cdd:COG0110   83 T----IGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDE 137
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 76-185 2.22e-36

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: 122.57  E-value: 2.22e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  76 KIIIGDNVSVNQGSFIISRESIVIGNNTRVGEYVSIRDNDHEWRDKNTPIlKQGFITNSVEIGSDVWIGRNVVICKGVKI 155
Cdd:cd04647    1 NISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDHNHDIDDPERPI-EQGVTSAPIVIGDDVWIGANVVILPGVTI 79

                         90       100       110
                 ....*....|....*....|....*....|
gi 556251193 156 GDGAVIGANAVITKNVNQYEVVVGNPGRVI 185
Cdd:cd04647   80 GDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 53-188 5.81e-27

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 101.11  E-value: 5.81e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  53 GNVKVGNNVRFGPFARIGATEGAKIIIGDNVSVNQGSFIISRESIVIGNNTRVGEYVSIRDNDHEWRDKNTPIL------ 126
Cdd:PRK09677  42 GSINFGEGFTSGVGLRLDAFGRGKLFFGDNVQVNDYVHIACIESITIGRDTLIASKVFITDHNHGSFKHSDDFSspnlpp 121

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556251193 127 -KQGFITNSVEIGSDVWIGRNVVICKGVKIGDGAVIGANAVITKNVNQYEVVVGNPGRVIKVR 188
Cdd:PRK09677 122 dMRTLESSAVVIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKKY 184
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 54-181 1.83e-13

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: 65.59  E-value: 1.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193   54 NVKVGNNVRFGPFARIGAteGAKIiiGDNVSVNQGSfiisresiVIGNNTRVGEYVSIRDNDHewrdkntpilkqgfITN 133
Cdd:TIGR03570  99 SASIGEGTVIMAGAVINP--DVRI--GDNVIINTGA--------IVEHDCVIGDFVHIAPGVT--------------LSG 152

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 556251193  134 SVEIGSDVWIGRNVVICKGVKIGDGAVIGANAVITKNVNQYEVVVGNP 181
Cdd:TIGR03570 153 GVVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVP 200
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
134-163 1.16e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 37.70  E-value: 1.16e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 556251193  134 SVEIGSDVWIGRNVVICKGVKIGDGAVIGA 163
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
52-190 1.97e-38

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 128.84  E-value: 1.97e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  52 KGNVKVGNNVRFGPFARIGateGAKIIIGDNVSVNQGSFIISRESIVIGNNTRVGEYVSIRDNDHEWRDKNTPILKQGFI 131
Cdd:COG0110    6 LFGARIGDGVVIGPGVRIY---GGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPATFPLRTGPV 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 556251193 132 TnsveIGSDVWIGRNVVICKGVKIGDGAVIGANAVITKNVNQYEVVVGNPGRVIKVRGE 190
Cdd:COG0110   83 T----IGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDE 137
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 76-185 2.22e-36

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: 122.57  E-value: 2.22e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  76 KIIIGDNVSVNQGSFIISRESIVIGNNTRVGEYVSIRDNDHEWRDKNTPIlKQGFITNSVEIGSDVWIGRNVVICKGVKI 155
Cdd:cd04647    1 NISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDHNHDIDDPERPI-EQGVTSAPIVIGDDVWIGANVVILPGVTI 79

                         90       100       110
                 ....*....|....*....|....*....|
gi 556251193 156 GDGAVIGANAVITKNVNQYEVVVGNPGRVI 185
Cdd:cd04647   80 GDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 53-188 5.81e-27

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 101.11  E-value: 5.81e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  53 GNVKVGNNVRFGPFARIGATEGAKIIIGDNVSVNQGSFIISRESIVIGNNTRVGEYVSIRDNDHEWRDKNTPIL------ 126
Cdd:PRK09677  42 GSINFGEGFTSGVGLRLDAFGRGKLFFGDNVQVNDYVHIACIESITIGRDTLIASKVFITDHNHGSFKHSDDFSspnlpp 121

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556251193 127 -KQGFITNSVEIGSDVWIGRNVVICKGVKIGDGAVIGANAVITKNVNQYEVVVGNPGRVIKVR 188
Cdd:PRK09677 122 dMRTLESSAVVIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKKY 184
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 82-188 2.56e-26

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: 98.00  E-value: 2.56e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  82 NVSVNQGSFIISRESIVIGNNTRVGEYVSIRDN-------------------DHEWRDKNTPILKQGFITNS-VEIGSDV 141
Cdd:cd03349    1 NISVGDYSYGSGPDCDVGGDKLSIGKFCSIAPGvkiglggnhptdwvstypfYIFGGEWEDDAKFDDWPSKGdVIIGNDV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 556251193 142 WIGRNVVICKGVKIGDGAVIGANAVITKNVNQYEVVVGNPGRVIKVR 188
Cdd:cd03349   81 WIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRYR 127
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 74-185 1.92e-23

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: 90.94  E-value: 1.92e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  74 GAKIIIGDNVSVNQGSFIISRESIVIGNNTRVGEYVSIRDNDH--EWRDKNTPILkqgfITNSVEIGSDVWIGRNVVICK 151
Cdd:cd03357   60 GYNIHIGDNFYANFNCTILDVAPVTIGDNVLIGPNVQIYTAGHplDPEERNRGLE----YAKPITIGDNVWIGGGVIILP 135

                         90       100       110
                 ....*....|....*....|....*....|....
gi 556251193 152 GVKIGDGAVIGANAVITKNVNQYEVVVGNPGRVI 185
Cdd:cd03357  136 GVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 76-185 2.30e-19

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: 78.80  E-value: 2.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  76 KIIIGDNVSVNQGSFIISRESIVIGNNTRVGEYVSIRDNDHEWRDKNTPilkqgFITNSVEIGSDVWIGRNVVICKGVKI 155
Cdd:cd05825    3 NLTIGDNSWIGEGVWIYNLAPVTIGSDACISQGAYLCTGSHDYRSPAFP-----LITAPIVIGDGAWVAAEAFVGPGVTI 77

                         90       100       110
                 ....*....|....*....|....*....|
gi 556251193 156 GDGAVIGANAVITKNVNQYEVVVGNPGRVI 185
Cdd:cd05825   78 GEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
PRK10502 PRK10502
putative acyl transferase; Provisional
 56-188 1.30e-18

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 78.84  E-value: 1.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  56 KVGNNVRFGPFARIgaTEGAKIIIGDNVSVNQGSFIISRESIVIGNNTRVGEYVSIRDNDHEWRDKNTpilkqGFITNSV 135
Cdd:PRK10502  53 KIGKGVVIRPSVRI--TYPWKLTIGDYAWIGDDVWLYNLGEITIGAHCVISQKSYLCTGSHDYSDPHF-----DLNTAPI 125

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 556251193 136 EIGSDVWIGRNVVICKGVKIGDGAVIGANAVITKNVNQYEVVVGNPGRVIKVR 188
Cdd:PRK10502 126 VIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIRPR 178
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 56-186 2.21e-17

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 76.20  E-value: 2.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  56 KVGNNVRFGPfaRIGATEGAKIIIGDNVSVNQGSFIISRESIVIGNNTRVGEYVSIRDNDHEwrdKNTPILKQG-FITNS 134
Cdd:PRK09527  57 TVGENAWVEP--PVYFSYGSNIHIGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGHP---VHHELRKNGeMYSFP 131

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 556251193 135 VEIGSDVWIGRNVVICKGVKIGDGAVIGANAVITKNVNQYEVVVGNPGRVIK 186
Cdd:PRK09527 132 ITIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIR 183
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 54-181 1.25e-14

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 68.67  E-value: 1.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  54 NVKVGNNVRFGPFARIGAtegaKIIIGDNVSVNQGSfiisresiVIGNNTRVGEYVSIrdndhewrdknTPilkQGFITN 133
Cdd:cd03360   96 SAVIGEGCVIMAGAVINP----DARIGDNVIINTGA--------VIGHDCVIGDFVHI-----------AP---GVVLSG 149

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 556251193 134 SVEIGSDVWIGRNVVICKGVKIGDGAVIGANAVITKNVNQYEVVVGNP 181
Cdd:cd03360  150 GVTIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 57-186 2.09e-14

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: 66.37  E-value: 2.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  57 VGNNVRFGPFARIGAtegaKIIIGDNVSVNQGSFIIsrESIVIGNNTRVGEYVSIRdNDHEWRDKNTPILKQGfitnSVE 136
Cdd:cd03358    1 IGDNCIIGTNVFIEN----DVKIGDNVKIQSNVSIY--EGVTIEDDVFIGPNVVFT-NDLYPRSKIYRKWELK----GTT 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 556251193 137 IGSDVWIGRNVVICKGVKIGDGAVIGANAVITKNVNQYEVVVGNPGRVIK 186
Cdd:cd03358   70 VKRGASIGANATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 74-186 1.77e-13

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 65.22  E-value: 1.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  74 GAKIIIGDNVSVNQGSFIISRESIVIGNNTRVGEYVSIRDNDH----EWRDKNTPILKqgfitnSVEIGSDVWIGRNVVI 149
Cdd:PRK10092  71 GYNIFLGNNFYANFDCVMLDVCPIRIGDNCMLAPGVHIYTATHpldpVARNSGAELGK------PVTIGNNVWIGGRAVI 144

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 556251193 150 CKGVKIGDGAVIGANAVITKNVNQYEVVVGNPGRVIK 186
Cdd:PRK10092 145 NPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIK 181
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 54-181 1.83e-13

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: 65.59  E-value: 1.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193   54 NVKVGNNVRFGPFARIGAteGAKIiiGDNVSVNQGSfiisresiVIGNNTRVGEYVSIRDNDHewrdkntpilkqgfITN 133
Cdd:TIGR03570  99 SASIGEGTVIMAGAVINP--DVRI--GDNVIINTGA--------IVEHDCVIGDFVHIAPGVT--------------LSG 152

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 556251193  134 SVEIGSDVWIGRNVVICKGVKIGDGAVIGANAVITKNVNQYEVVVGNP 181
Cdd:TIGR03570 153 GVVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVP 200
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 97-189 4.59e-13

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: 63.95  E-value: 4.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  97 IVIGNNTRVGEYVSI------------RDNDHewrdkntPIlkqgfitnsveIGSDVWIGRNVVICKGVKIGDGAVIGAN 164
Cdd:COG1045   86 VVIGETAVIGDNVTIyqgvtlggtgkeKGKRH-------PT-----------IGDNVVIGAGAKILGPITIGDNAKIGAN 147

                         90       100
                 ....*....|....*....|....*
gi 556251193 165 AVITKNVNQYEVVVGNPGRVIKVRG 189
Cdd:COG1045  148 SVVLKDVPPGSTVVGVPARIVKRKG 172
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 50-186 7.18e-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: 7.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  50 AVKGNVKVGNNVRFGPFARIGAtEGAKIIIGDNVSVNQGSFIISREsiviGNNTRVGEYVSIrdndhewrdkntpilKQG 129
Cdd:cd04645   13 TVIGDVTLGEGSSVWFGAVLRG-DVNPIRIGERTNIQDGSVLHVDP----GYPTIIGDNVTV---------------GHG 72

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 556251193 130 FITNSVEIGSDVWIGRNVVICKGVKIGDGAVIGANAVITKN--VNQYEVVVGNPGRVIK 186
Cdd:cd04645   73 AVLHGCTIGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGkvIPPGSLVAGSPAKVVR 131
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 53-186 2.29e-11

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 59.27  E-value: 2.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  53 GNVKVGNNVRFGPFARIGATEGaKIIIGDNVSVNQGSfiisresiVI----GNNTRVGEYVSIrdnDHewrdkntpilkq 128
Cdd:COG0663   27 GDVTIGEDVSVWPGAVLRGDVG-PIRIGEGSNIQDGV--------VLhvdpGYPLTIGDDVTI---GH------------ 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556251193 129 gfitNSV----EIGSDVWIGRNVVICKGVKIGDGAVIGANAVITKN--VNQYEVVVGNPGRVIK 186
Cdd:COG0663   83 ----GAIlhgcTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGkvVPPGSLVVGSPAKVVR 142
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 52-179 4.54e-11

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: 58.97  E-value: 4.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  52 KGNVKVGNNVRFGPFARIGATegakiIIGDNVSVNQGSFIisrESIVIGNNTRVGEYVSIRDNDHEWRD---------KN 122
Cdd:cd03353   31 EGKTVIGEDCVIGPNCVIKDS-----TIGDGVVIKASSVI---EGAVIGNGATVGPFAHLRPGTVLGEGvhignfveiKK 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193 123 TPILKQ----------------------GFIT--------NSVEIGSDVWIGRNVVICKGVKIGDGAVIGANAVITKNVN 172
Cdd:cd03353  103 STIGEGskanhlsylgdaeigegvnigaGTITcnydgvnkHRTVIGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVP 182


                 ....*..
gi 556251193 173 QYEVVVG 179
Cdd:cd03353  183 PGALAIA 189
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 97-181 1.87e-10

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: 55.14  E-value: 1.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  97 IVIGNNTRVGEYVSIRDN-----DHEWRDKNTPIlkqgfitnsveIGSDVWIGRNVVICKGVKIGDGAVIGANAVITKNV 171
Cdd:cd03354   23 IVIGETAVIGDNCTIYQGvtlggKGKGGGKRHPT-----------IGDNVVIGAGAKILGNITIGDNVKIGANAVVTKDV 91

                         90
                 ....*....|
gi 556251193 172 NQYEVVVGNP 181
Cdd:cd03354   92 PANSTVVGVP 101
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 51-167 4.48e-10

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: 55.71  E-value: 4.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  51 VKGNVKVGNNVRFGPFARIGATEGAKIIIGDNVSVNQGSFIISRE--SIVIGNntrvgeyvsirdndhewrdkNTPILKQ 128
Cdd:cd00710   17 VIGDVIIGDNVFVGPGASIRADEGTPIIIGANVNIQDGVVIHALEgySVWIGK--------------------NVSIAHG 76

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 556251193 129 GFITNSVEIGSDVWIGRNVVICKGvKIGDGAVIGANAVI 167
Cdd:cd00710   77 AIVHGPAYIGDNCFIGFRSVVFNA-KVGDNCVIGHNAVV 114
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 130-171 2.40e-09

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 55.41  E-value: 2.40e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 556251193 130 FITNSVEIGSDVWIGRNVVICKGVKIGDGAVIGANAVITKNV 171
Cdd:COG1044  104 VIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGV 145
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 54-181 4.49e-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: 53.57  E-value: 4.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  54 NVKVGNNVRFGPFARIGA-------TEGA--KI------IIGDNV------SVNQGSF---IISRESIV-----IGNNTR 104
Cdd:cd03352   55 GCIIGDRVIIHSGAVIGSdgfgfapDGGGwvKIpqlggvIIGDDVeigantTIDRGALgdtVIGDGTKIdnlvqIAHNVR 134

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556251193 105 VGEyvsirdndhewrdkNTPILKQGFITNSVEIGSDVWIGRNVVICKGVKIGDGAVIGANAVITKNVNQYEVVVGNP 181
Cdd:cd03352  135 IGE--------------NCLIAAQVGIAGSTTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTP 197
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 54-167 6.73e-09

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 54.25  E-value: 6.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  54 NVKVGNNVRFGPFArigategakiIIGDNVsvnqgsfiisresiVIGNNTRVGEYVSIRDNdhewrdkntpilkqgfitn 133
Cdd:COG1044  108 SAKIGEGVSIGPFA----------VIGAGV--------------VIGDGVVIGPGVVIGDG------------------- 144

                         90       100       110
                 ....*....|....*....|....*....|....
gi 556251193 134 sVEIGSDVWIGRNVVICKGVKIGDGAVIGANAVI 167
Cdd:COG1044  145 -VVIGDDCVLHPNVTIYERCVIGDRVIIHSGAVI 177
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 51-186 7.77e-09

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 54.00  E-value: 7.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  51 VKGNVKVGNNVRFGPFARIG-----------ATEGAKIIIGDNVSVnqGSFIISRESIVIGNNTRVGEYVSIRDNDhewR 119
Cdd:PRK14357 270 IEGKTRIGEDCEIGPMTRIVdceignnvkiiRSECEKSVIEDDVSV--GPFSRLREGTVLKKSVKIGNFVEIKKST---I 344

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193 120 DKNTPI-----LKQGFITNSVEIGS-------------------DVWIGRNVVICKGVKIGDGAVIGANAVITKNVNQYE 175
Cdd:PRK14357 345 GENTKAqhltyLGDATVGKNVNIGAgtitcnydgkkknptfiedGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYS 424

                        170
                 ....*....|.
gi 556251193 176 VVVGNPGRVIK 186
Cdd:PRK14357 425 LALGRARQIVK 435
PLN02357 PLN02357
serine acetyltransferase
 74-185 9.98e-09

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 53.73  E-value: 9.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  74 GAKIiiGDNVSVNQGSFIISRESIVIGNNTRVGEYVSIRDNDHEWRDKNTpilkqgfitnsvEIGSDVWIGRNVVICKGV 153
Cdd:PLN02357 232 GAKI--GQGILLDHATGVVIGETAVVGNNVSILHNVTLGGTGKQSGDRHP------------KIGDGVLIGAGTCILGNI 297

                         90       100       110
                 ....*....|....*....|....*....|..
gi 556251193 154 KIGDGAVIGANAVITKNVNQYEVVVGNPGRVI 185
Cdd:PLN02357 298 TIGEGAKIGAGSVVLKDVPPRTTAVGNPARLI 329
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 95-185 1.07e-08

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: 53.48  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  95 ESIVIGNNTRVGEYVSIRDNdhewrdkntpilkqgfitnsVEIGSDVWIGRNVVICKGVKIGDGAVIGANAVItknvnQY 174
Cdd:COG1044  107 PSAKIGEGVSIGPFAVIGAG--------------------VVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTI-----YE 161

                         90
                 ....*....|.
gi 556251193 175 EVVVGNpgRVI 185
Cdd:COG1044  162 RCVIGD--RVI 170
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 46-179 1.36e-08

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: 53.49  E-value: 1.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  46 IYVPAV-KGNVKVGNNVRFGPF-----ARIGatEGAKI--------IIGDNVSVnqGSFIISRESIVIGNNTRVGEYVSI 111
Cdd:COG1207  275 IDPNVIlEGKTVIGEGVVIGPNctlkdSTIG--DGVVIkysviedaVVGAGATV--GPFARLRPGTVLGEGVKIGNFVEV 350

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193 112 rdndhewrdKNTPILKQ----------------------GFIT--------NSVEIGSDVWIGRNVVICKGVKIGDGAVI 161
Cdd:COG1207  351 ---------KNSTIGEGskvnhlsyigdaeigegvnigaGTITcnydgvnkHRTVIGDGAFIGSNTNLVAPVTIGDGATI 421

                        170
                 ....*....|....*...
gi 556251193 162 GANAVITKNVNQYEVVVG 179
Cdd:COG1207  422 GAGSTITKDVPAGALAIA 439
PLN02694 PLN02694
serine O-acetyltransferase
 79-185 2.23e-08

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 52.34  E-value: 2.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  79 IGDNVSVNQGSFIISRESIVIGNNTRVGEYVSIRDNDHEWRDKNTpilkqgfitnsvEIGSDVWIGRNVVICKGVKIGDG 158
Cdd:PLN02694 169 IGKGILFDHATGVVIGETAVIGNNVSILHHVTLGGTGKACGDRHP------------KIGDGVLIGAGATILGNVKIGEG 236

                         90       100
                 ....*....|....*....|....*..
gi 556251193 159 AVIGANAVITKNVNQYEVVVGNPGRVI 185
Cdd:PLN02694 237 AKIGAGSVVLIDVPPRTTAVGNPARLV 263
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 77-168 2.27e-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: 49.17  E-value: 2.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  77 IIIGDNVSVNQGSFIisRESIVIGNNTRVGEYVSIRDNDHEWRDkntpilkqgfitNSVEIGSDVWIGRNVVICKGVKIG 156
Cdd:cd00208    1 VFIGEGVKIHPKAVI--RGPVVIGDNVNIGPGAVIGAATGPNEK------------NPTIIGDNVEIGANAVIHGGVKIG 66

                         90
                 ....*....|..
gi 556251193 157 DGAVIGANAVIT 168
Cdd:cd00208   67 DNAVIGAGAVVT 78
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 130-171 3.16e-08

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 52.06  E-value: 3.16e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 556251193 130 FITNSVEIGSDVWIGRNVVICKGVKIGDGAVIGANAVITKNV 171
Cdd:PRK00892 108 VIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGV 149
PLN02739 PLN02739
serine acetyltransferase
 79-190 3.48e-08

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 51.96  E-value: 3.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  79 IGDNVSVNQGSFIISRESIVIGNNTRVGEYVSIRDNDHEWRDKNTpilkqgfitnsvEIGSDVWIGRNVVICKGVKIGDG 158
Cdd:PLN02739 214 IGKGILLDHGTGVVIGETAVIGDRVSILHGVTLGGTGKETGDRHP------------KIGDGALLGACVTILGNISIGAG 281

                         90       100       110
                 ....*....|....*....|....*....|..
gi 556251193 159 AVIGANAVITKNVNQYEVVVGNPGRVIKVRGE 190
Cdd:PLN02739 282 AMVAAGSLVLKDVPSHSMVAGNPAKLIGFVDE 313
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 77-186 7.53e-08

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: 49.49  E-value: 7.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  77 IIIGDNVSVNQGSFIISRESIVI----GNNTRVGEYVSIRDNDhewrdkntpilkqgfITNSVEIGSDVWIGRNVVICKG 152
Cdd:cd04650   32 VIRGDNDSIYIGKYSNVQENVSIhtdhGYPTEIGDYVTIGHNA---------------VVHGAKVGNYVIVGMGAILLNG 96

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 556251193 153 VKIGDGAVIGANAVITKN--VNQYEVVVGNPGRVIK 186
Cdd:cd04650   97 AKIGDHVIIGAGAVVTPGkeIPDYSLVLGVPAKVVR 132
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 55-186 1.06e-07

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 50.63  E-value: 1.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  55 VKVGNNVRFGPFARI--GAT-------EGAKIiiGDNVSVnqGSFIISRESIVIGNNTRVGEYVSIrdndhewrdKNTPI 125
Cdd:PRK14353 275 VVIEPNVVFGPGVTVasGAVihafshlEGAHV--GEGAEV--GPYARLRPGAELGEGAKVGNFVEV---------KNAKL 341

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193 126 LK------------------------------QGFITNSVEIGSDVWIGRNVVICKGVKIGDGAVIGANAVITKNVNQYE 175
Cdd:PRK14353 342 GEgakvnhltyigdatigaganigagtitcnyDGFNKHRTEIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDA 421

                        170
                 ....*....|.
gi 556251193 176 VVVGNPGRVIK 186
Cdd:PRK14353 422 LALGRARQETK 432
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 51-184 1.26e-07

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


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 50.12  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  51 VKGNVKVGNNVRFGPFARIGAT--------EGAKIIIGDN------VSVNQGSFiISRESIVIGNN------TRVGEYVS 110
Cdd:cd03351   44 IDGPTTIGKNNRIFPFASIGEApqdlkykgEPTRLEIGDNntirefVTIHRGTA-QGGGVTRIGNNnllmayVHVAHDCV 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193 111 IRDNDHewrdkntpilkqgfITNS------VEIGSDVWIGRNVVICKGVKIGDGAVIGANAVITKNVNQYEVVVGNPGRV 184
Cdd:cd03351  123 IGNNVI--------------LANNatlaghVEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARL 188
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 78-167 2.21e-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: 2.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  78 IIGDNVSVnqGSFIISRESIVIGNNTRVGEYVSIRDNdhewrdkntpilkqgfitnsVEIGSDVWIGRNVVICKGVKIGD 157
Cdd:cd03352    3 KIGENVSI--GPNAVIGEGVVIGDGVVIGPGVVIGDG--------------------VVIGDDCVIHPNVTIYEGCIIGD 60

                         90
                 ....*....|
gi 556251193 158 GAVIGANAVI 167
Cdd:cd03352   61 RVIIHSGAVI 70
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 134-171 2.83e-07

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 48.56  E-value: 2.83e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 556251193 134 SVEIGSDVWIGRNVVICKGVKIGDGAVIGANAVITKNV 171
Cdd:cd03352    1 SAKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGV 38
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 51-184 4.50e-07

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 48.48  E-value: 4.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  51 VKGNVKVGNNVRFGPFARIGAT--------EGAKIIIGDN------VSVNQGSfIISRESIVIGNN------------TR 104
Cdd:COG1043   46 IEGPTTIGKNNRIFPFASIGEEpqdlkykgEPTRLEIGDNntirefVTIHRGT-VQGGGVTRIGDDnllmayvhvahdCV 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193 105 VGEYVsirdndhewrdkntpilkqgFITNS------VEIGSDVWIGRNVVICKGVKIGDGAVIGANAVITKNVNQYEVVV 178
Cdd:COG1043  125 VGNNV--------------------ILANNatlaghVEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDVPPYVLAA 184


                 ....*.
gi 556251193 179 GNPGRV 184
Cdd:COG1043  185 GNPARL 190
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 77-190 4.95e-07

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: 47.21  E-value: 4.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  77 IIIGDNVSVNQGSF-IISRESIVI--GNNTRVGEYVS-IRDNDHEWRDKNTpilkqgfITNSVEIGSDVWIGRNVVICKG 152
Cdd:cd03359   35 IIRGDLATVSIGRYcILSEGCVIRppFKKFSKGVAFFpLHIGDYVFIGENC-------VVNAAQIGSYVHIGKNCVIGRR 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 556251193 153 VKIGDGAVIGANAVITKN--VNQYEVVVGNPGRVIKVRGE 190
Cdd:cd03359  108 CIIKDCVKILDGTVVPPDtvIPPYSVVSGRPARFIGELPE 147
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 56-179 6.92e-07

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 48.29  E-value: 6.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  56 KVGNNVRFGPFA--RIGATEGAKIIIGDNVSVNQGsfiisresiVIGNNTRVGEYVSIRDNDhewRDKNTPI-------- 125
Cdd:PRK14354 318 KVGDNVTVGPFAhlRPGSVIGEEVKIGNFVEIKKS---------TIGEGTKVSHLTYIGDAE---VGENVNIgcgtitvn 385

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 556251193 126 --LKQGFITNsveIGSDVWIGRNVVICKGVKIGDGAVIGANAVITKNVNQYEVVVG 179
Cdd:PRK14354 386 ydGKNKFKTI---IGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDALAIA 438
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 54-181 3.04e-06

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 46.16  E-value: 3.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  54 NVKVGNNVRFGPFARIGA--------TEGA--KI------IIGDNV------SVNQGSF---IISRESIV-----IGNNT 103
Cdd:COG1044  162 RCVIGDRVIIHSGAVIGAdgfgfapdEDGGwvKIpqlgrvVIGDDVeigantTIDRGALgdtVIGDGTKIdnlvqIAHNV 241

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556251193 104 RVGEyvsirdndhewrdkNTPILKQGFITNSVEIGSDVWIGRNVVICKGVKIGDGAVIGANAVITKNVNQYEVVVGNP 181
Cdd:COG1044  242 RIGE--------------HTAIAAQVGIAGSTKIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSGSP 305
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 53-186 4.75e-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: 44.67  E-value: 4.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  53 GNVKVGNNVRFGPFARIGAtEGAKIIIGDNVSVNQGSFIISResivIGNNTRVGEYVSIrdndhewrdkntpilKQGFIT 132
Cdd:cd04745   17 GDVIIGKNCYIGPHASLRG-DFGRIVIRDGANVQDNCVIHGF----PGQDTVLEENGHI---------------GHGAIL 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 556251193 133 NSVEIGSDVWIGRNVVICKGVKIGDGAVIGANAVITKNVN--QYEVVVGNPGRVIK 186
Cdd:cd04745   77 HGCTIGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAGTVipPRSLIAGSPAKVIR 132
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 96-185 5.64e-06

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 45.09  E-value: 5.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  96 SIVIGNNTRVGEYVSIRDNdhewrdkntpilkqgfitnsVEIGSDVWIGRNVVICKGVKIGDGAVIGANAVItknvnQYE 175
Cdd:cd03352    1 SAKIGENVSIGPNAVIGEG--------------------VVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTI-----YEG 55

                         90
                 ....*....|
gi 556251193 176 VVVGNpgRVI 185
Cdd:cd03352   56 CIIGD--RVI 63
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 54-163 1.01e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 44.74  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  54 NVKVGNNVRFGPFArigategakiIIGDNVsvnqgsfiisresiVIGNNTRVGEYVSIRDNdhewrdkntpilkqgfitn 133
Cdd:PRK00892 112 SAKIGEGVSIGPNA----------VIGAGV--------------VIGDGVVIGAGAVIGDG------------------- 148

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 556251193 134 sVEIGSDVWIGRNVVICKGVKIGD------GAVIGA 163
Cdd:PRK00892 149 -VKIGADCRLHANVTIYHAVRIGNrviihsGAVIGS 183
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 51-178 1.08e-05

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 45.02  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  51 VKGNVKVGNNVRfgpfarIGAteGAKI---IIGDNVSVNQGSFIisrESIVIGNNTRVGEYVSIR------DNDH----- 116
Cdd:PRK09451 280 IEGNVTLGNRVK------IGA--GCVLkncVIGDDCEISPYSVV---EDANLGAACTIGPFARLRpgaelaEGAHvgnfv 348

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193 117 EWrdKNTPI---LKQGFIT--NSVEIGSDVWIGRNVVICK-------------------------GVKIGDGAVIGANAV 166
Cdd:PRK09451 349 EM--KKARLgkgSKAGHLTylGDAEIGDNVNIGAGTITCNydgankfktiigddvfvgsdtqlvaPVTVGKGATIGAGTT 426

                        170
                 ....*....|..
gi 556251193 167 ITKNVNQYEVVV 178
Cdd:PRK09451 427 VTRDVAENELVI 438
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
51-184 1.91e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 43.93  E-value: 1.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  51 VKGNVKVGNNVRFGPFARIGAT--------EGAKIIIGDN------VSVNQGSfIISRESIVIGNNTRVGEYVSIrdnDH 116
Cdd:PRK05289  47 IDGHTTIGKNNRIFPFASIGEDpqdlkykgEPTRLVIGDNntirefVTINRGT-VQGGGVTRIGDNNLLMAYVHV---AH 122

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556251193 117 EWRDKNTPIlkqgfITNS------VEIGSDVWIGRNVVICKGVKIGDGAVIGANAVITKNVNQYEVVVGNPGRV 184
Cdd:PRK05289 123 DCVVGNHVI-----LANNatlaghVEVGDYAIIGGLTAVHQFVRIGAHAMVGGMSGVSQDVPPYVLAEGNPARL 191
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 137-179 3.58e-05

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 43.17  E-value: 3.58e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 556251193 137 IGSDVWIGRNVVICKGVKIGDGAVIGANAVITKNVNQYEVVVG 179
Cdd:PRK14356 401 IGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSLAIA 443
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 52-186 4.65e-05

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 42.99  E-value: 4.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  52 KGNVKVGNNVRFGPF-----ARIGatEGAKII--------IGDNVSVnqGSFIISRESIVIGNNTRVGEYVSIRDNDHEW 118
Cdd:PRK14360 278 RGNTVIGSGCRIGPGslienSQIG--ENVTVLysvvsdsqIGDGVKI--GPYAHLRPEAQIGSNCRIGNFVEIKKSQLGE 353

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193 119 RDK--------NTPILKQ-----GFIT--------NSVEIGSDVWIGRNVVICKGVKIGDGAVIGANAVITKNVNQYEVV 177
Cdd:PRK14360 354 GSKvnhlsyigDATLGEQvnigaGTITanydgvkkHRTVIGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLA 433


                 ....*....
gi 556251193 178 VGNPGRVIK 186
Cdd:PRK14360 434 IARSRQVIK 442
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 130-168 4.95e-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: 42.71  E-value: 4.95e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 556251193 130 FITNSVEIGSDVWIGRNVVICKGVKIGDGAVIGANAVIT 168
Cdd:COG1207  262 YIDGDVEIGRDVVIDPNVILEGKTVIGEGVVIGPNCTLK 300
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 54-171 6.35e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 42.43  E-value: 6.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  54 NVKVGNNVRFGPFARIG------ATEGA---KI------IIGDNV------SVNQGSFiisrESIVIGNNTRVGEYVSIR 112
Cdd:PRK00892 166 AVRIGNRVIIHSGAVIGsdgfgfANDRGgwvKIpqlgrvIIGDDVeigantTIDRGAL----DDTVIGEGVKIDNLVQIA 241

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 556251193 113 DNDHEWRdkNTPILKQGFITNSVEIGSDVWIGRNVVICKGVKIGDGAVIGANAVITKNV 171
Cdd:PRK00892 242 HNVVIGR--HTAIAAQVGIAGSTKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSI 298
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 134-168 6.85e-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: 41.93  E-value: 6.85e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 556251193 134 SVEIGSDVWIGRNVVICKGVKIGDGAVIGANAVIT 168
Cdd:COG1043   13 GAKLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIE 47
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 98-167 1.09e-04

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 41.54  E-value: 1.09e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  98 VIGNNTRVGEYVSIRDNdhewrdkntpilkqgfitnsVEIGSDVWIGRNVVICKGVKIGDGAVIGANAVI 167
Cdd:COG1043   15 KLGENVEIGPFCVIGPD--------------------VEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASI 64
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
134-163 1.16e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 37.70  E-value: 1.16e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 556251193  134 SVEIGSDVWIGRNVVICKGVKIGDGAVIGA 163
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 51-180 1.53e-04

Dynactin 6 (or subunit p27): 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 p27 is part of the pointed-end subcomplex in dynactin that also includes p25, p26, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain the 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: 100052 [Multi-domain]  Cd Length: 164  Bit Score: 40.39  E-value: 1.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  51 VKGNVKVGNNVRFGPFARIGATEGAkIIIGDNVSVNQGSFIISRESivigNNTRVGEYVSIRDNDHewrdkntpiLKQGF 130
Cdd:cd04646   14 IRGDVTIGPGTVVHPRATIIAEAGP-IIIGENNIIEEQVTIVNKKP----KDPAEPKPMIIGSNNV---------FEVGC 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 556251193 131 ITNSVEIGSDVWIGRNVVICKGVKIGDGAVIGANAVIT--KNVNQYEVVVGN 180
Cdd:cd04646   80 KCEALKIGNNNVFESKSFVGKNVIITDGCIIGAGCKLPssEILPENTVIYGA 131
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 134-168 2.00e-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: 40.88  E-value: 2.00e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 556251193 134 SVEIGSDVWIGRNVVICKGVKIGDGAVIGANAVIT 168
Cdd:cd03351   11 GAKIGENVEIGPFCVIGPNVEIGDGTVIGSHVVID 45
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 131-167 2.95e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 40.39  E-value: 2.95e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 556251193 131 ITNSVEIGSDVWIGRNVVICKGVKIGDGAVIGANAVI 167
Cdd:PRK12461   8 IDPSAKLGSGVEIGPFAVIGANVEIGDGTWIGPHAVI 44
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
95-167 4.33e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 39.70  E-value: 4.33e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556251193  95 ESIVIGNNTRVGEYVSIRDNdhewrdkntpilkqgfitnsVEIGSDVWIGRNVVICKGVKIGDGAVIGANAVI 167
Cdd:PRK05289  13 PGAKIGENVEIGPFCVIGPN--------------------VVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASI 65
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 51-181 7.59e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 38.85  E-value: 7.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  51 VKGNVKVGNNVRFGPFARIGAT--------EGAKIIIGDNVSVnqgsfiisRESIVI------GNNTRVGEYVSIRDNDH 116
Cdd:PRK12461  44 ILGPTRIGKNNKIHQGAVVGDEpqdftykgEESRLEIGDRNVI--------REGVTIhrgtkgGGVTRIGNDNLLMAYSH 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556251193 117 EWRD---KNTPILKQG-FITNSVEIGSDVWIGRNVVICKGVKIGDGAVIGANAVITKNVNQYEVVVGNP 181
Cdd:PRK12461 116 VAHDcqiGNNVILVNGaLLAGHVTVGDRAIISGNCLVHQFCRIGALAMMAGGSRISKDVPPYCMMAGHP 184
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 95-167 8.39e-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: 38.95  E-value: 8.39e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556251193  95 ESIVIGNNTRVGEYVSIRDNdhewrdkntpilkqgfitnsVEIGSDVWIGRNVVICKGVKIGDGAVIGANAVI 167
Cdd:cd03351   10 PGAKIGENVEIGPFCVIGPN--------------------VEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASI 62
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 130-168 1.09e-03

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: 38.17  E-value: 1.09e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 556251193 130 FITNSVEIGSDVWIGRNVVICKGVKIGDGAVIGANAVIT 168
Cdd:cd03353   11 YIDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIK 49
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 136-163 1.37e-03

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 38.69  E-value: 1.37e-03
                         10        20
                 ....*....|....*....|....*...
gi 556251193 136 EIGSDVWIGRNVVICKGVKIGDGAVIGA 163
Cdd:PRK14353 270 VIGRDVVIEPNVVFGPGVTVASGAVIHA 297
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 91-166 2.49e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 37.90  E-value: 2.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  91 IISRESI---VIGNNTRVGEYVSIRDndhewrdkntpilkqgfitnSVeIGSDVWIGR-----NVVICKGVKIGDGAVIG 162
Cdd:PRK00725 335 IISGAVVrrsVLFSRVRVNSFSNVED--------------------SV-LLPDVNVGRscrlrRCVIDRGCVIPEGMVIG 393


                 ....
gi 556251193 163 ANAV 166
Cdd:PRK00725 394 EDPE 397
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
134-168 3.44e-03

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 37.00  E-value: 3.44e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 556251193 134 SVEIGSDVWIGRNVVICKGVKIGDGAVIGANAVIT 168
Cdd:PRK05289  14 GAKIGENVEIGPFCVIGPNVVIGDGTVIGSHVVID 48
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 78-171 3.75e-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: 34.91  E-value: 3.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  78 IIGDNVSVNQGSFIisrESIVIGNNTRVGEYVSIrdndhewrdkntpilKQGFITNSVEIGSDVWIgRNVVICKGVKIGD 157
Cdd:cd03356    1 LIGESTVIGENAII---KNSVIGDNVRIGDGVTI---------------TNSILMDNVTIGANSVI-VDSIIGDNAVIGE 61

                         90
                 ....*....|....
gi 556251193 158 GAVIGANAVITKNV 171
Cdd:cd03356   62 NVRVVNLCIIGDDV 75
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 137-185 3.76e-03

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 37.22  E-value: 3.76e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 556251193 137 IGSDVWIGRNVVICKGVKIGDGAVIGANAVITKNVNQYEVVV-GNPGRVI 185
Cdd:PRK14352 402 IGSHVRTGSDTMFVAPVTVGDGAYTGAGTVIREDVPPGALAVsEGPQRNI 451
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 125-167 4.31e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 37.15  E-value: 4.31e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 556251193 125 ILKQGFITNSVEIGSDVWI-----GRNVVICKGVKIGDG----AVIGANAVI 167
Cdd:PRK05293 322 VVKDSVIMPGAKIGENVVIeraiiGENAVIGDGVIIGGGkeviTVIGENEVI 373
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 130-178 4.77e-03

bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 36.88  E-value: 4.77e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 556251193 130 FITNSVEIGSDVWIGRNVVICKGVKIGDGAVIGANAVITKNVNQYEVVV 178
Cdd:PRK14358 266 LIEDTVTLGRDVTIEPGVLLRGQTRVADGVTIGAYSVVTDSVLHEGAVI 314
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 121-180 5.39e-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: 34.48  E-value: 5.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193 121 KNTPILKQGFITNSVeIGSDVWIGRNVVIcKGVKIGDGAVIGANAVITKNVNQYEVVVGN 180
Cdd:cd05787    4 RGTSIGEGTTIKNSV-IGRNCKIGKNVVI-DNSYIWDDVTIEDGCTIHHSIVADGAVIGK 61
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 51-168 5.47e-03

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: 36.03  E-value: 5.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  51 VKGNVKVGNNVRFGPFARI-GATegakiIIGDNVSVNQGSFIisRESIvIGNNTRVGEYVSIRDN--------------- 114
Cdd:cd05636   32 IEGPVIIGKGCEIGPNAYIrGYT-----VLGDGCVVGNSVEV--KNSI-IMDGTKVPHLNYVGDSvlgenvnlgagtita 103

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193 115 DHEWRDKNTPILKQGFITNS------VEIGSDVWIGRNVVICKGVKIGDGAVIGANAVIT 168
Cdd:cd05636  104 NLRFDDKPVKVRLKGERVDTgrrklgAIIGDGVKTGINVSLNPGVKIGPGSWVYPGCVVR 163
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
51-167 6.78e-03

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 36.23  E-value: 6.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  51 VKGNVKVGNNVRFGPFARIGA--TEGAKIIIGDNVSVNQGSFIISRESI----------------------VIGNNTRVG 106
Cdd:PRK05289  11 VEPGAKIGENVEIGPFCVIGPnvVIGDGTVIGSHVVIDGHTTIGKNNRIfpfasigedpqdlkykgeptrlVIGDNNTIR 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556251193 107 EYVSIrdndhewrdkNTPILKQGFITnsvEIGSDVW------------IGRNVVICKG------VKIGDGAVIGANAVI 167
Cdd:PRK05289  91 EFVTI----------NRGTVQGGGVT---RIGDNNLlmayvhvahdcvVGNHVILANNatlaghVEVGDYAIIGGLTAV 156
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 78-171 6.85e-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: 6.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556251193  78 IIGDNVSVNQGSFIISResiVIGNNTRVGEYVSIRDNdhewrdkntpilkqgFITNSVEIGSDVWIgRNVVICKGVKIGD 157
Cdd:cd05787    1 VIGRGTSIGEGTTIKNS---VIGRNCKIGKNVVIDNS---------------YIWDDVTIEDGCTI-HHSIVADGAVIGK 61

                         90
                 ....*....|....
gi 556251193 158 GAVIGANAVITKNV 171
Cdd:cd05787   62 GCTIPPGSLISFGV 75
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 120-167 8.57e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 35.77  E-value: 8.57e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 556251193 120 DKNTPILKQGFITNSVEIGSDVWIGRNVVICKGVKIGDGAVIGANAVI 167
Cdd:PRK12461  15 GSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVV 62
 
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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