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Conserved domains on  [gi|490329276|ref|WP_004218733|]
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MULTISPECIES: sugar O-acetyltransferase [Bifidobacterium]

Protein Classification

sugar O-acetyltransferase( domain architecture ID 10129706)

sugar O-acetyltransferase similar to maltose O-acetyltransferase and galactoside O-acetyltransferase, which catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates

CATH:  2.160.10.10
EC:  2.3.1.-
Gene Ontology:  GO:0016407
PubMed:  11747907

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 20-188 5.17e-99

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: 284.31  E-value: 5.17e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276  20 LYIADDPYLKEHSLKRRRLVQEINRSDYDEFDKREALFRELFGSFGEGSYIEPPFRADYGCNTYIGRNFYANTDCIFLDV 99
Cdd:cd03357    1 LYNASDPELVAERARARRLLHEYNQTPPSDAEERRELLKELFGSVGENVYIEPPFHCDYGYNIHIGDNFYANFNCTILDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276 100 ARIDIGDNVFCGPRVSLLTPYHPIDAQVRNEQLEGGKPISIGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVVKDIPSHCI 179
Cdd:cd03357   81 APVTIGDNVLIGPNVQIYTAGHPLDPEERNRGLEYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVV 160


                 ....*....
gi 490329276 180 AVGNPCRPI 188
Cdd:cd03357  161 AAGNPARVI 169
 
Name Accession Description Interval E-value
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 20-188 5.17e-99

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: 284.31  E-value: 5.17e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276  20 LYIADDPYLKEHSLKRRRLVQEINRSDYDEFDKREALFRELFGSFGEGSYIEPPFRADYGCNTYIGRNFYANTDCIFLDV 99
Cdd:cd03357    1 LYNASDPELVAERARARRLLHEYNQTPPSDAEERRELLKELFGSVGENVYIEPPFHCDYGYNIHIGDNFYANFNCTILDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276 100 ARIDIGDNVFCGPRVSLLTPYHPIDAQVRNEQLEGGKPISIGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVVKDIPSHCI 179
Cdd:cd03357   81 APVTIGDNVLIGPNVQIYTAGHPLDPEERNRGLEYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVV 160


                 ....*....
gi 490329276 180 AVGNPCRPI 188
Cdd:cd03357  161 AAGNPARVI 169
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 11-189 6.00e-72

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 216.60  E-value: 6.00e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276  11 EYERMLSGELYIADDPYLKEHSLKRRRLVQEINRSDYDEFDKREALFRELFGSFgEGSYIEPPFRADYGCNTYIGRNFYA 90
Cdd:PRK10092   4 EKEKMIAGELYRSADETLSRDRLRARQLIHRYNHSLPDEHTLRQQILADLFGQV-TEAYIEPTFRCDYGYNIFLGNNFYA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276  91 NTDCIFLDVARIDIGDNVFCGPRVSLLTPYHPIDAQVRNEQLEGGKPISIGNDVWFGGNVTVCPGVTIGDDVVIGAGSVV 170
Cdd:PRK10092  83 NFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPLDPVARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVV 162

                        170
                 ....*....|....*....
gi 490329276 171 VKDIPSHCIAVGNPCRPIR 189
Cdd:PRK10092 163 TKDVPDNVVVGGNPARIIK 181
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
55-195 1.29e-52

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 165.81  E-value: 1.29e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276  55 ALFRELFGSFGEGSYIEPPFRAdYGCNTYIGRNFYANTDCIFLDVARIDIGDNVFCGPRVSLLTPYHPIDAQVRNEqlEG 134
Cdd:COG0110    2 KLLLLFGARIGDGVVIGPGVRI-YGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPATFP--LR 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490329276 135 GKPISIGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVVKDIPSHCIAVGNPCRPIRAITDAD 195
Cdd:COG0110   79 TGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEEE 139
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 63-184 4.59e-19

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: 81.00  E-value: 4.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276   63 SFGEGSYIEPpfRADYGCNTYIGRNFYANTDCIfldvarID----IGDNVFCGPRVSLLtpyhpidaqvrneqleGGkpI 138
Cdd:TIGR03570 101 SIGEGTVIMA--GAVINPDVRIGDNVIINTGAI------VEhdcvIGDFVHIAPGVTLS----------------GG--V 154

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 490329276  139 SIGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVVKDIPSHCIAVGNP 184
Cdd:TIGR03570 155 VIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVP 200
Mac pfam12464
Maltose acetyltransferase; This domain family is found in bacteria, archaea and eukaryotes, ...
 14-65 1.23e-17

Maltose acetyltransferase; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 50 amino acids in length. The family is found in association with pfam00132. Mac uses acetyl-CoA as acetyl donor to acetylated cytoplasmic maltose.


Pssm-ID: 463596 [Multi-domain]  Cd Length: 52  Bit Score: 73.29  E-value: 1.23e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 490329276   14 RMLSGELYIADDPYLKEHSLKRRRLVQEINRSDYDEFDKREALFRELFGSFG 65
Cdd:pfam12464   1 KMLAGELYDASDPELVAERLRARRLLRRYNNTPPEDAEEREELLKELFGSVG 52
 
Name Accession Description Interval E-value
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 20-188 5.17e-99

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: 284.31  E-value: 5.17e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276  20 LYIADDPYLKEHSLKRRRLVQEINRSDYDEFDKREALFRELFGSFGEGSYIEPPFRADYGCNTYIGRNFYANTDCIFLDV 99
Cdd:cd03357    1 LYNASDPELVAERARARRLLHEYNQTPPSDAEERRELLKELFGSVGENVYIEPPFHCDYGYNIHIGDNFYANFNCTILDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276 100 ARIDIGDNVFCGPRVSLLTPYHPIDAQVRNEQLEGGKPISIGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVVKDIPSHCI 179
Cdd:cd03357   81 APVTIGDNVLIGPNVQIYTAGHPLDPEERNRGLEYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVV 160


                 ....*....
gi 490329276 180 AVGNPCRPI 188
Cdd:cd03357  161 AAGNPARVI 169
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 11-189 6.00e-72

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 216.60  E-value: 6.00e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276  11 EYERMLSGELYIADDPYLKEHSLKRRRLVQEINRSDYDEFDKREALFRELFGSFgEGSYIEPPFRADYGCNTYIGRNFYA 90
Cdd:PRK10092   4 EKEKMIAGELYRSADETLSRDRLRARQLIHRYNHSLPDEHTLRQQILADLFGQV-TEAYIEPTFRCDYGYNIFLGNNFYA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276  91 NTDCIFLDVARIDIGDNVFCGPRVSLLTPYHPIDAQVRNEQLEGGKPISIGNDVWFGGNVTVCPGVTIGDDVVIGAGSVV 170
Cdd:PRK10092  83 NFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPLDPVARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVV 162

                        170
                 ....*....|....*....
gi 490329276 171 VKDIPSHCIAVGNPCRPIR 189
Cdd:PRK10092 163 TKDVPDNVVVGGNPARIIK 181
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 13-201 1.54e-59

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 185.59  E-value: 1.54e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276  13 ERMLSGELYIADDPYLKEHSLKRRRLVQEINRSDYDEFDKREALFRELFGSFGEGSYIEPPFRADYGCNTYIGRNFYANT 92
Cdd:PRK09527   7 ERIKAGKLFTDMCEGLPEKRLRGKTLMYEFNHSHPSEVEKRESLIKEMFATVGENAWVEPPVYFSYGSNIHIGRNFYANF 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276  93 DCIFLDVARIDIGDNVFCGPRVSLLTPYHPIDAQVRNEQLEGGKPISIGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVVK 172
Cdd:PRK09527  87 NLTIVDDYTVTIGDNVLIAPNVTLSVTGHPVHHELRKNGEMYSFPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTK 166

                        170       180
                 ....*....|....*....|....*....
gi 490329276 173 DIPSHCIAVGNPCRPIRAITDADHEQWQR 201
Cdd:PRK09527 167 DIPPNVVAAGVPCRVIREINDRDKQYYFK 195
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
55-195 1.29e-52

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 165.81  E-value: 1.29e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276  55 ALFRELFGSFGEGSYIEPPFRAdYGCNTYIGRNFYANTDCIFLDVARIDIGDNVFCGPRVSLLTPYHPIDAQVRNEqlEG 134
Cdd:COG0110    2 KLLLLFGARIGDGVVIGPGVRI-YGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPATFP--LR 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490329276 135 GKPISIGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVVKDIPSHCIAVGNPCRPIRAITDAD 195
Cdd:COG0110   79 TGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEEE 139
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 84-188 1.26e-40

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: 134.12  E-value: 1.26e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276  84 IGRNFYANTDCIFLDVARIDIGDNVFCGPRVSLLTPYHPIDAQ-VRNEQLEGGKPISIGNDVWFGGNVTVCPGVTIGDDV 162
Cdd:cd04647    4 IGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDHNHDIDDPeRPIEQGVTSAPIVIGDDVWIGANVVILPGVTIGDGA 83

                         90       100
                 ....*....|....*....|....*.
gi 490329276 163 VIGAGSVVVKDIPSHCIAVGNPCRPI 188
Cdd:cd04647   84 VVGAGSVVTKDVPPNSIVAGNPAKVI 109
PRK10502 PRK10502
putative acyl transferase; Provisional
 53-190 5.53e-25

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 96.17  E-value: 5.53e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276  53 REALFReLFG-SFGEGSYIEPPFRADYGCNTYIGRNFYANTDCIFLDVARIDIGDNVFCGPRVSLLTPYHpiDAQVRNEQ 131
Cdd:PRK10502  43 RAFLLR-LFGaKIGKGVVIRPSVRITYPWKLTIGDYAWIGDDVWLYNLGEITIGAHCVISQKSYLCTGSH--DYSDPHFD 119

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490329276 132 LEGgKPISIGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVVKDIPSHCIAVGNPCRPIRA 190
Cdd:PRK10502 120 LNT-APIVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIRP 177
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 79-189 2.02e-24

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: 92.95  E-value: 2.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276  79 GCNTYIGRNFYANTDCIFLDVARID----------IGDNVFCGPRVSLLTPYHPIDAQVRNEQLeggKPISIGNDVWFGG 148
Cdd:cd03358    2 GDNCIIGTNVFIENDVKIGDNVKIQsnvsiyegvtIEDDVFIGPNVVFTNDLYPRSKIYRKWEL---KGTTVKRGASIGA 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 490329276 149 NVTVCPGVTIGDDVVIGAGSVVVKDIPSHCIAVGNPCRPIR 189
Cdd:cd03358   79 NATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 63-189 1.37e-23

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: 91.45  E-value: 1.37e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276  63 SFGEGSYIEPPFRADYGCNTYIGRnfyantDCIfldvaridIGDNVfcgprVSLLTPYHPIDA------QVRNEQLEGG- 135
Cdd:cd03349    3 SVGDYSYGSGPDCDVGGDKLSIGK------FCS--------IAPGV-----KIGLGGNHPTDWvstypfYIFGGEWEDDa 63

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490329276 136 --------KPISIGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVVKDIPSHCIAVGNPCRPIR 189
Cdd:cd03349   64 kfddwpskGDVIIGNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIR 125
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 63-184 7.68e-22

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: 88.31  E-value: 7.68e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276  63 SFGEGSYIEPpfRADYGCNTYIGRNFYANT------DCIfldvaridIGDNVFCGPRVSLLtpyhpidaqvrneqleGGk 136
Cdd:cd03360   98 VIGEGCVIMA--GAVINPDARIGDNVIINTgavighDCV--------IGDFVHIAPGVVLS----------------GG- 150

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 490329276 137 pISIGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVVKDIPSHCIAVGNP 184
Cdd:cd03360  151 -VTIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 73-188 2.43e-21

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: 84.58  E-value: 2.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276  73 PFRADYGCNTYIGRnfyantDCIFLDVARIDIGDNVFCGPRVSLLT-------PYHPIDAqvrneqleggKPISIGNDVW 145
Cdd:cd05825    1 PWNLTIGDNSWIGE------GVWIYNLAPVTIGSDACISQGAYLCTgshdyrsPAFPLIT----------APIVIGDGAW 64

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 490329276 146 FGGNVTVCPGVTIGDDVVIGAGSVVVKDIPSHCIAVGNPCRPI 188
Cdd:cd05825   65 VAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 63-184 4.59e-19

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: 81.00  E-value: 4.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276   63 SFGEGSYIEPpfRADYGCNTYIGRNFYANTDCIfldvarID----IGDNVFCGPRVSLLtpyhpidaqvrneqleGGkpI 138
Cdd:TIGR03570 101 SIGEGTVIMA--GAVINPDVRIGDNVIINTGAI------VEhdcvIGDFVHIAPGVTLS----------------GG--V 154

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 490329276  139 SIGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVVKDIPSHCIAVGNP 184
Cdd:TIGR03570 155 VIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVP 200
Mac pfam12464
Maltose acetyltransferase; This domain family is found in bacteria, archaea and eukaryotes, ...
 14-65 1.23e-17

Maltose acetyltransferase; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 50 amino acids in length. The family is found in association with pfam00132. Mac uses acetyl-CoA as acetyl donor to acetylated cytoplasmic maltose.


Pssm-ID: 463596 [Multi-domain]  Cd Length: 52  Bit Score: 73.29  E-value: 1.23e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 490329276   14 RMLSGELYIADDPYLKEHSLKRRRLVQEINRSDYDEFDKREALFRELFGSFG 65
Cdd:pfam12464   1 KMLAGELYDASDPELVAERLRARRLLRRYNNTPPEDAEEREELLKELFGSVG 52
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 104-184 6.66e-17

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: 72.86  E-value: 6.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276 104 IGDNVFCGPRVSL------LTPYHPIdaqvrneqleggkpisIGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVVKDIPSH 177
Cdd:cd03354   31 IGDNCTIYQGVTLggkgkgGGKRHPT----------------IGDNVVIGAGAKILGNITIGDNVKIGANAVVTKDVPAN 94


                 ....*..
gi 490329276 178 CIAVGNP 184
Cdd:cd03354   95 STVVGVP 101
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 102-200 9.96e-16

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 72.22  E-value: 9.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276 102 IDIGDNVFCGPRVsLLTPYHPIDAQVRNEQLEG----------GKPISIGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVV 171
Cdd:PRK09677  86 ITIGRDTLIASKV-FITDHNHGSFKHSDDFSSPnlppdmrtleSSAVVIGQRVWIGENVTILPGVSIGNGCIVGANSVVT 164

                         90       100
                 ....*....|....*....|....*....
gi 490329276 172 KDIPSHCIAVGNPCRPIRaITDADHEQWQ 200
Cdd:PRK09677 165 KSIPENTVIAGNPAKIIK-KYNHETKLWE 192
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 132-189 2.45e-15

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: 70.50  E-value: 2.45e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276 132 LEGGK--PIsIGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVVKDIPSHCIAVGNPCRPIR 189
Cdd:COG1045  111 KEKGKrhPT-IGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVK 169
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 140-212 1.21e-14

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 68.52  E-value: 1.21e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490329276 140 IGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVV--KDIPSHCIAVGNPCRPIRAITDADHEQWQRKAREYRAWKEG 212
Cdd:COG0663   91 IGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTegKVVPPGSLVVGSPAKVVRELTEEEIAFLRESAENYVELARR 165
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 102-211 6.92e-14

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: 66.28  E-value: 6.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276 102 IDIGDNVFCGPRVslltpyhpidaqvrneQLEGGKpisIGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVV--KDIPSHCI 179
Cdd:cd04645   61 TIIGDNVTVGHGA----------------VLHGCT---IGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPpgKVIPPGSL 121

                         90       100       110
                 ....*....|....*....|....*....|..
gi 490329276 180 AVGNPCRPIRAITDADHEQWQRKAREYRAWKE 211
Cdd:cd04645  122 VAGSPAKVVRELTDEEIAELRESAEHYVELAK 153
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 83-170 2.09e-12

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 60.34  E-value: 2.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276  83 YIGRNFYANTDCIFLDvaRIDIGDNVFCGPRVSLLTPYHPidaqvrneqlEGGKPISIGNDVWFGGNVTVCPGVTIGDDV 162
Cdd:cd00208    2 FIGEGVKIHPKAVIRG--PVVIGDNVNIGPGAVIGAATGP----------NEKNPTIIGDNVEIGANAVIHGGVKIGDNA 69


                 ....*...
gi 490329276 163 VIGAGSVV 170
Cdd:cd00208   70 VIGAGAVV 77
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 140-189 5.89e-12

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: 62.04  E-value: 5.89e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 490329276 140 IGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVVKDIPSHCIAVGNPCRPIR 189
Cdd:cd03352  153 IGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQPHR 202
PLN02739 PLN02739
serine acetyltransferase
 104-207 1.45e-09

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 56.58  E-value: 1.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276 104 IGDNVFCGPRVSLLtpyHPIDAQVRNEQlEGGKPISIGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVVKDIPSHCIAVGN 183
Cdd:PLN02739 228 IGETAVIGDRVSIL---HGVTLGGTGKE-TGDRHPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGN 303

                         90       100       110
                 ....*....|....*....|....*....|....
gi 490329276 184 PCRPIRAIT----------DADHEQWQRKAREYR 207
Cdd:PLN02739 304 PAKLIGFVDeqdpsltmeyDATREFFQNVAVAYR 337
PLN02357 PLN02357
serine acetyltransferase
 95-188 5.23e-09

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 54.89  E-value: 5.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276  95 IFLDVAR-IDIGDNVFCGPRVSLLtpyHPIDAQVRNEQlEGGKPISIGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVVKD 173
Cdd:PLN02357 239 ILLDHATgVVIGETAVVGNNVSIL---HNVTLGGTGKQ-SGDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKD 314

                         90
                 ....*....|....*
gi 490329276 174 IPSHCIAVGNPCRPI 188
Cdd:PLN02357 315 VPPRTTAVGNPARLI 329
PRK10191 PRK10191
putative acyl transferase; Provisional
 140-186 5.70e-09

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 52.97  E-value: 5.70e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 490329276 140 IGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVVKDIPSHCIAVGNPCR 186
Cdd:PRK10191  95 IGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKAR 141
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 138-187 1.98e-08

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: 52.82  E-value: 1.98e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 490329276 138 ISIGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVVKDIPSHCIAVGNPCRP 187
Cdd:cd03351  139 VEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARL 188
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 129-206 2.77e-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: 51.03  E-value: 2.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276 129 NEQLEGGKpisIGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVV--KDIPSHCIAVGNPCRPIRAITDADHEQWQRKAREY 206
Cdd:cd04650   73 NAVVHGAK---VGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTpgKEIPDYSLVLGVPAKVVRKLTEEEIEWIKKNAEEY 149
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 140-182 3.84e-08

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: 51.27  E-value: 3.84e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 490329276 140 IGNDVWFGGNVT-VCPgVTIGDDVVIGAGSVVVKDIPSHCIAVG 182
Cdd:cd03353  147 IGDNVFIGSNSQlVAP-VTIGDGATIAAGSTITKDVPPGALAIA 189
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 140-187 4.84e-08

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: 51.56  E-value: 4.84e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 490329276 140 IGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVVKDIPSHCIAVGNPCRP 187
Cdd:COG1043  143 VGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDVPPYVLAAGNPARL 190
PLN02694 PLN02694
serine O-acetyltransferase
 134-186 2.50e-07

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 50.03  E-value: 2.50e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490329276 134 GGKPISIGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVVKDIPSHCIAVGNPCR 186
Cdd:PLN02694 209 GDRHPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPAR 261
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 65-170 6.72e-07

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: 48.86  E-value: 6.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276  65 GEGSYIEPpfradygcNTYIGRNfyantdcifldvARIdiGDNVFCGPRVSlltpyhpIDAQVRneqleggkpisIGNDV 144
Cdd:COG1044  112 GEGVSIGP--------FAVIGAG------------VVI--GDGVVIGPGVV-------IGDGVV-----------IGDDC 151

                         90       100
                 ....*....|....*....|....*.
gi 490329276 145 WFGGNVTVCPGVTIGDDVVIGAGSVV 170
Cdd:COG1044  152 VLHPNVTIYERCVIGDRVIIHSGAVI 177
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 140-182 7.83e-07

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: 48.87  E-value: 7.83e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 490329276 140 IGNDVWFGGNVT-VCPgVTIGDDVVIGAGSVVVKDIPSHCIAVG 182
Cdd:COG1207  397 IGDGAFIGSNTNlVAP-VTIGDGATIGAGSTITKDVPAGALAIA 439
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 140-201 1.18e-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: 48.09  E-value: 1.18e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490329276 140 IGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVVKDIPSHCIAVGNPCRPiraitdadHEQWQR 201
Cdd:COG1044  261 IGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSGSPAQP--------HREWLR 314
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 104-170 1.25e-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: 47.02  E-value: 1.25e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490329276 104 IGDNVFCGPRVSlltpyhpIDAQVRneqleggkpisIGNDVWFGGNVTVCPGVTIGDDVVIGAGSVV 170
Cdd:cd03352   22 IGDGVVIGPGVV-------IGDGVV-----------IGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 140-203 1.27e-06

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 48.00  E-value: 1.27e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490329276 140 IGNDVWFGGN-VTVCPgVTIGDDVVIGAGSVVVKDIPSHCIAVGnpcRPIRAItdadHEQWQRKA 203
Cdd:PRK14360 393 IGDRSKTGANsVLVAP-ITLGEDVTVAAGSTITKDVPDNSLAIA---RSRQVI----KENWKKKS 449
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
137-166 1.55e-06

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 43.09  E-value: 1.55e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 490329276  137 PISIGNDVWFGGNVTVCPGVTIGDDVVIGA 166
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
140-187 1.60e-06

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 47.40  E-value: 1.60e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490329276 140 IGNDVWFGGNVTVCPGVTIGDDVVIG------------------AGSVVVKDIPSHCIAVGNPCRP 187
Cdd:PRK05289 126 VGNHVILANNATLAGHVEVGDYAIIGgltavhqfvrigahamvgGMSGVSQDVPPYVLAEGNPARL 191
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 140-182 9.40e-06

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 45.59  E-value: 9.40e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 490329276 140 IGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVVKDIPSHCIAVG 182
Cdd:PRK14354 396 IGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDALAIA 438
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 140-182 2.03e-05

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 44.33  E-value: 2.03e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 490329276 140 IGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVVKDIPSHCIAVG 182
Cdd:PRK14356 401 IGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSLAIA 443
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 140-182 2.28e-05

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 44.47  E-value: 2.28e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 490329276 140 IGNDVWFGGNVT-VCPgVTIGDDVVIGAGSVVVKDIPSHCIAVG 182
Cdd:PRK14353 383 IGAGAFIGSNSAlVAP-VTIGDGAYIASGSVITEDVPDDALALG 425
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
138-170 2.73e-05

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 39.73  E-value: 2.73e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 490329276  138 ISIGNDVWFGGNVTVcpGVTIGDDVVIGAGSVV 170
Cdd:pfam14602   1 VIIGDNCLIGANSGI--GVSLGDNCVVGAGVVI 31
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 140-179 3.17e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 43.59  E-value: 3.17e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 490329276 140 IGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVVKD--IPSHCI 179
Cdd:PRK00892 115 IGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGvkIGADCR 156
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 140-204 3.39e-05

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 43.77  E-value: 3.39e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490329276 140 IGNDVWFG-GNVTVCPgVTIGDDVVIGAGSVVVKDIPSHCIAV-GNPCRPIraitdadhEQWQRKAR 204
Cdd:PRK14352 402 IGSHVRTGsDTMFVAP-VTVGDGAYTGAGTVIREDVPPGALAVsEGPQRNI--------EGWVQRKR 459
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 140-207 3.48e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 43.59  E-value: 3.48e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490329276 140 IGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVVKDIPSHCIAVGN-PCRPIRaitdadheQWQRKAREYR 207
Cdd:PRK00892 264 IGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEPGEYSSGiPAQPNK--------EWLRTAARLR 324
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 135-176 4.72e-05

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 43.44  E-value: 4.72e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 490329276 135 GKPISIGNDVWFggnvtVCPgVTIGDDVVIGAGSVVVKDIPS 176
Cdd:PRK14359 371 GKNVFIGSDTQL-----VAP-VNIEDNVLIAAGSTVTKDVPK 406
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 65-170 7.78e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 42.43  E-value: 7.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276  65 GEGSYIEPpfradygcNTYIGRNfyantdcifldvARIdiGDNVFCGPRVSlltpyhpIDAQVRneqleggkpisIGNDV 144
Cdd:PRK00892 116 GEGVSIGP--------NAVIGAG------------VVI--GDGVVIGAGAV-------IGDGVK-----------IGADC 155

                         90       100
                 ....*....|....*....|....*.
gi 490329276 145 WFGGNVTVCPGVTIGDDVVIGAGSVV 170
Cdd:PRK00892 156 RLHANVTIYHAVRIGNRVIIHSGAVI 181
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 139-170 1.35e-04

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: 41.93  E-value: 1.35e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 490329276 139 SIGNDVWFGGNVTVCPGVTIGDDVVIGAGSVV 170
Cdd:COG1044  110 KIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVI 141
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 140-181 2.12e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 41.27  E-value: 2.12e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 490329276 140 IGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVVKDIPSHCIAV 181
Cdd:PRK14355 400 IEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPPDSLAI 441
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 140-170 3.05e-04

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 40.08  E-value: 3.05e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 490329276 140 IGNDVWFGGNVTVCPGVTIGDDVVIGAGSVV 170
Cdd:cd03352    4 IGENVSIGPNAVIGEGVVIGDGVVIGPGVVI 34
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 98-206 4.05e-04

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: 39.51  E-value: 4.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276  98 DVARIDIGDNVFCGPRVSLLTPYhpidaqVRNEQLEGGKPISIGNDVWFGGNvTVCPGVTIGDDVVIGAGSV-----VVK 172
Cdd:cd03359   39 DLATVSIGRYCILSEGCVIRPPF------KKFSKGVAFFPLHIGDYVFIGEN-CVVNAAQIGSYVHIGKNCVigrrcIIK 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 490329276 173 D---------------IPSHCIAVGNPCRPIRAITDAdHEQWQR-KAREY 206
Cdd:cd03359  112 DcvkildgtvvppdtvIPPYSVVSGRPARFIGELPEC-TQELMEeETKEY 160
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 104-186 4.66e-04

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 39.70  E-value: 4.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276 104 IGDNVFCGPRVSLltpyhpidaqvrneqlegGKPISIGNDVWFGGNVTVCPGVTIGDDVVIGAGsVVVKDipsHCIaVGN 183
Cdd:cd03352    4 IGENVSIGPNAVI------------------GEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPN-VTIYE---GCI-IGD 60


                 ...
gi 490329276 184 PCR 186
Cdd:cd03352   61 RVI 63
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 138-184 8.40e-04

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 39.73  E-value: 8.40e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 490329276  138 ISIGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVVK--DIPSHCIAVGNP 184
Cdd:TIGR02353 646 VTIGDGATLGPGAIVLYGVVMGEGSVLGPDSLVMKgeEVPAHTRWRGNP 694
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 102-207 9.90e-04

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 39.73  E-value: 9.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490329276  102 IDIGDNVFCGPRVSLLTpyhpidAQVRNEQLEGGkPISIGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVVKD--IPSHCI 179
Cdd:TIGR02353 132 LTIGAGTIVRKEVMLLG------YRAERGRLHTG-PVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSALQGGqsIPDGER 204

                          90       100
                  ....*....|....*....|....*...
gi 490329276  180 AVGNPCRPiraiTDADHEQWQRkAREYR 207
Cdd:TIGR02353 205 WHGSPAQK----TGADYRKVQP-ARPYT 227
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 140-170 1.18e-03

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 38.85  E-value: 1.18e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 490329276 140 IGNDVWFGGNVTVCPGVTIGDDVVIGAGSVV 170
Cdd:COG1044  105 IDPSAKIGEGVSIGPFAVIGAGVVIGDGVVI 135
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 140-174 1.18e-03

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 39.24  E-value: 1.18e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 490329276 140 IGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVVKDI 174
Cdd:PRK09451 397 IGDDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDV 431
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 137-182 2.08e-03

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 38.59  E-value: 2.08e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 490329276 137 PISIGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVVKDIPSHCIAVG 182
Cdd:PRK14357 383 PTFIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALG 428
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 140-211 3.01e-03

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: 36.96  E-value: 3.01e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490329276 140 IGNDVWFGGNVTVCPGVTIGDDVVIGAGSVVVK--DIPSHCIAVGNPCRPIRAITDadhEQWQRKAREYRAWKE 211
Cdd:cd04745   81 IGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAgtVIPPRSLIAGSPAKVIRELSD---EEVAWKTRGTKEYQQ 151
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 140-170 7.03e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 36.66  E-value: 7.03e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 490329276 140 IGNDVWFGGNVTVCPGVTIGDDVVIGAGSVV 170
Cdd:PRK00892 109 IDPSAKIGEGVSIGPNAVIGAGVVIGDGVVI 139
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 140-207 7.35e-03

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 36.32  E-value: 7.35e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490329276 140 IGNDVWFGGNVTVCPGVTIGDDVVIGAGSVV---VKDIPSHCIaVGNPCRPIRAITDADHeQWQR-KAREYR 207
Cdd:PRK13627  91 IGRDALVGMNSVIMDGAVIGEESIVAAMSFVkagFQGEKRQLL-MGTPARAVRSVSDDEL-HWKRlNTKEYQ 160
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
100-170 8.65e-03

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 36.23  E-value: 8.65e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490329276 100 ARID----IGDNVFCGPrvslltpYHPIDAQVRneqleggkpisIGNDVWFGGNVTVCPGVTIGDDVVIGAGSVV 170
Cdd:PRK05289   9 AIVEpgakIGENVEIGP-------FCVIGPNVV-----------IGDGTVIGSHVVIDGHTTIGKNNRIFPFASI 65
 
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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