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Conserved domains on  [gi|616690642|gb|KAE88211|]
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hypothetical protein W632_00535 [Staphylococcus aureus VET0402R]

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 ...
 12-181 5.54e-93

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: 268.52  E-value: 5.54e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  12 WYDANfDQDLINERARAKDICFELNHTKPSDKNKRKELIDELFQTTTDNVSISIPFDTDYGWNVKLGKNVYVNTNCYFMD 91
Cdd:cd03357    1 LYNAS-DPELVAERARARRLLHEYNQTPPSDAEERRELLKELFGSVGENVYIEPPFHCDYGYNIHIGDNFYANFNCTILD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  92 GGQITIGDNVFIGPNCGFYTATHPLNFHHRNEGFEKAGPINIGSNTWFGGHVAVLPGVTIGEGSVIGAGSVVTKDIPPHS 171
Cdd:cd03357   80 VAPVTIGDNVLIGPNVQIYTAGHPLDPEERNRGLEYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANV 159

                        170
                 ....*....|
gi 616690642 172 LAVGNPCKVV 181
Cdd:cd03357  160 VAAGNPARVI 169
 
Name Accession Description Interval E-value
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 12-181 5.54e-93

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: 268.52  E-value: 5.54e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  12 WYDANfDQDLINERARAKDICFELNHTKPSDKNKRKELIDELFQTTTDNVSISIPFDTDYGWNVKLGKNVYVNTNCYFMD 91
Cdd:cd03357    1 LYNAS-DPELVAERARARRLLHEYNQTPPSDAEERRELLKELFGSVGENVYIEPPFHCDYGYNIHIGDNFYANFNCTILD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  92 GGQITIGDNVFIGPNCGFYTATHPLNFHHRNEGFEKAGPINIGSNTWFGGHVAVLPGVTIGEGSVIGAGSVVTKDIPPHS 171
Cdd:cd03357   80 VAPVTIGDNVLIGPNVQIYTAGHPLDPEERNRGLEYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANV 159

                        170
                 ....*....|
gi 616690642 172 LAVGNPCKVV 181
Cdd:cd03357  160 VAAGNPARVI 169
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 1-186 2.85e-59

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 184.44  E-value: 2.85e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642   1 MTEKEKMLAEKWYdANFDQDLINERARAKDICFELNHTKPSDKNKRKELIDELFQTTTDNVSISIPFDTDYGWNVKLGKN 80
Cdd:PRK09527   3 MSMTERIKAGKLF-TDMCEGLPEKRLRGKTLMYEFNHSHPSEVEKRESLIKEMFATVGENAWVEPPVYFSYGSNIHIGRN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  81 VYVNTNCYFMDGGQITIGDNVFIGPNCGFYTATHPLNFHHRNEGFEKAGPINIGSNTWFGGHVAVLPGVTIGEGSVIGAG 160
Cdd:PRK09527  82 FYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGHPVHHELRKNGEMYSFPITIGNNVWIGSHVVINPGVTIGDNSVIGAG 161

                        170       180
                 ....*....|....*....|....*.
gi 616690642 161 SVVTKDIPPHSLAVGNPCKVVRKIDN 186
Cdd:PRK09527 162 SVVTKDIPPNVVAAGVPCRVIREIND 187
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
59-187 2.65e-55

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 171.98  E-value: 2.65e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  59 DNVSISIPFdTDYGWNVKLGKNVYVNTNCYFMDGGQITIGDNVFIGPNCGFYTATHPlnFHHRNEGFEKAGPINIGSNTW 138
Cdd:COG0110   13 DGVVIGPGV-RIYGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHP--IDDPATFPLRTGPVTIGDDVW 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 616690642 139 FGGHVAVLPGVTIGEGSVIGAGSVVTKDIPPHSLAVGNPCKVVRKIDNE 187
Cdd:COG0110   90 IGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEE 138
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 74-177 7.91e-22

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: 87.93  E-value: 7.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642   74 NVKLGKNVYVNTNCYFmdGGQITIGDNVFIGPNCGFytathplnfhhrnegfekAGPINIGSNTWFGGHVAVLPGVTIGE 153
Cdd:TIGR03570 117 DVRIGDNVIINTGAIV--EHDCVIGDFVHIAPGVTL------------------SGGVVIGEGVFIGAGATIIQGVTIGA 176

                          90       100
                  ....*....|....*....|....
gi 616690642  154 GSVIGAGSVVTKDIPPHSLAVGNP 177
Cdd:TIGR03570 177 GAIVGAGAVVTKDIPDGGVVVGVP 200
Mac pfam12464
Maltose acetyltransferase; This domain family is found in bacteria, archaea and eukaryotes, ...
 6-57 1.19e-16

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: 70.21  E-value: 1.19e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 616690642    6 KMLAEKWYDAnFDQDLINERARAKDICFELNHTKPSDKNKRKELIDELFQTT 57
Cdd:pfam12464   1 KMLAGELYDA-SDPELVAERLRARRLLRRYNNTPPEDAEEREELLKELFGSV 51
 
Name Accession Description Interval E-value
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 12-181 5.54e-93

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: 268.52  E-value: 5.54e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  12 WYDANfDQDLINERARAKDICFELNHTKPSDKNKRKELIDELFQTTTDNVSISIPFDTDYGWNVKLGKNVYVNTNCYFMD 91
Cdd:cd03357    1 LYNAS-DPELVAERARARRLLHEYNQTPPSDAEERRELLKELFGSVGENVYIEPPFHCDYGYNIHIGDNFYANFNCTILD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  92 GGQITIGDNVFIGPNCGFYTATHPLNFHHRNEGFEKAGPINIGSNTWFGGHVAVLPGVTIGEGSVIGAGSVVTKDIPPHS 171
Cdd:cd03357   80 VAPVTIGDNVLIGPNVQIYTAGHPLDPEERNRGLEYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANV 159

                        170
                 ....*....|
gi 616690642 172 LAVGNPCKVV 181
Cdd:cd03357  160 VAAGNPARVI 169
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 1-186 2.85e-59

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 184.44  E-value: 2.85e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642   1 MTEKEKMLAEKWYdANFDQDLINERARAKDICFELNHTKPSDKNKRKELIDELFQTTTDNVSISIPFDTDYGWNVKLGKN 80
Cdd:PRK09527   3 MSMTERIKAGKLF-TDMCEGLPEKRLRGKTLMYEFNHSHPSEVEKRESLIKEMFATVGENAWVEPPVYFSYGSNIHIGRN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  81 VYVNTNCYFMDGGQITIGDNVFIGPNCGFYTATHPLNFHHRNEGFEKAGPINIGSNTWFGGHVAVLPGVTIGEGSVIGAG 160
Cdd:PRK09527  82 FYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGHPVHHELRKNGEMYSFPITIGNNVWIGSHVVINPGVTIGDNSVIGAG 161

                        170       180
                 ....*....|....*....|....*.
gi 616690642 161 SVVTKDIPPHSLAVGNPCKVVRKIDN 186
Cdd:PRK09527 162 SVVTKDIPPNVVAAGVPCRVIREIND 187
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 2-184 6.83e-57

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 177.70  E-value: 6.83e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642   2 TEKEKMLAEKWYDANfDQDLINERARAKDICFELNHTKPSDKNKRKELIDELFQTTTDnVSISIPFDTDYGWNVKLGKNV 81
Cdd:PRK10092   3 TEKEKMIAGELYRSA-DETLSRDRLRARQLIHRYNHSLPDEHTLRQQILADLFGQVTE-AYIEPTFRCDYGYNIFLGNNF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  82 YVNTNCYFMDGGQITIGDNVFIGPNCGFYTATHPLNFHHRNEGFEKAGPINIGSNTWFGGHVAVLPGVTIGEGSVIGAGS 161
Cdd:PRK10092  81 YANFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPLDPVARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGA 160

                        170       180
                 ....*....|....*....|...
gi 616690642 162 VVTKDIPPHSLAVGNPCKVVRKI 184
Cdd:PRK10092 161 VVTKDVPDNVVVGGNPARIIKKL 183
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
59-187 2.65e-55

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 171.98  E-value: 2.65e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  59 DNVSISIPFdTDYGWNVKLGKNVYVNTNCYFMDGGQITIGDNVFIGPNCGFYTATHPlnFHHRNEGFEKAGPINIGSNTW 138
Cdd:COG0110   13 DGVVIGPGV-RIYGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHP--IDDPATFPLRTGPVTIGDDVW 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 616690642 139 FGGHVAVLPGVTIGEGSVIGAGSVVTKDIPPHSLAVGNPCKVVRKIDNE 187
Cdd:COG0110   90 IGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEE 138
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 74-181 2.98e-48

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: 153.00  E-value: 2.98e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  74 NVKLGKNVYVNTNCYFMDGGQITIGDNVFIGPNCGFYTATHPLNFHHR-NEGFEKAGPINIGSNTWFGGHVAVLPGVTIG 152
Cdd:cd04647    1 NISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDHNHDIDDPERpIEQGVTSAPIVIGDDVWIGANVVILPGVTIG 80

                         90       100
                 ....*....|....*....|....*....
gi 616690642 153 EGSVIGAGSVVTKDIPPHSLAVGNPCKVV 181
Cdd:cd04647   81 DGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 74-183 1.85e-29

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: 106.09  E-value: 1.85e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  74 NVKLGKNVYVNTNCYFMDGGQITIGDNVFIGPNCGFYT-ATHPLN------FHHRNE---------GFEKAGPINIGSNT 137
Cdd:cd03349    1 NISVGDYSYGSGPDCDVGGDKLSIGKFCSIAPGVKIGLgGNHPTDwvstypFYIFGGeweddakfdDWPSKGDVIIGNDV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 616690642 138 WFGGHVAVLPGVTIGEGSVIGAGSVVTKDIPPHSLAVGNPCKVVRK 183
Cdd:cd03349   81 WIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRY 126
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 74-182 7.26e-28

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: 101.42  E-value: 7.26e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  74 NVKLGKNVYVNTNCYFMDGgqITIGDNVFIGPNCGFytaTHPLNFHHRNEGFEKAGPINIGSNTWFGGHVAVLPGVTIGE 153
Cdd:cd03358   16 DVKIGDNVKIQSNVSIYEG--VTIEDDVFIGPNVVF---TNDLYPRSKIYRKWELKGTTVKRGASIGANATILPGVTIGE 90

                         90       100
                 ....*....|....*....|....*....
gi 616690642 154 GSVIGAGSVVTKDIPPHSLAVGNPCKVVR 182
Cdd:cd03358   91 YALVGAGAVVTKDVPPYALVVGNPARIIG 119
PRK10502 PRK10502
putative acyl transferase; Provisional
 71-182 1.84e-26

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 99.64  E-value: 1.84e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  71 YGWNVKLGKNVYVNTNCYFMDGGQITIGDNVFIGPNCGFYTATHplnfHHRNEGFE-KAGPINIGSNTWFGGHVAVLPGV 149
Cdd:PRK10502  68 YPWKLTIGDYAWIGDDVWLYNLGEITIGAHCVISQKSYLCTGSH----DYSDPHFDlNTAPIVIGEGCWLAADVFVAPGV 143

                         90       100       110
                 ....*....|....*....|....*....|...
gi 616690642 150 TIGEGSVIGAGSVVTKDIPPHSLAVGNPCKVVR 182
Cdd:PRK10502 144 TIGSGAVVGARSSVFKSLPANTICRGNPAVPIR 176
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 73-181 6.17e-26

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: 96.14  E-value: 6.17e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  73 WNVKLGKNVYV--NTNCYFMDggQITIGDNVFIGPNCGFYTATHplnfHHRNEGFE-KAGPINIGSNTWFGGHVAVLPGV 149
Cdd:cd05825    2 WNLTIGDNSWIgeGVWIYNLA--PVTIGSDACISQGAYLCTGSH----DYRSPAFPlITAPIVIGDGAWVAAEAFVGPGV 75

                         90       100       110
                 ....*....|....*....|....*....|..
gi 616690642 150 TIGEGSVIGAGSVVTKDIPPHSLAVGNPCKVV 181
Cdd:cd05825   76 TIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 74-177 1.26e-23

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: 92.55  E-value: 1.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  74 NVKLGKNVYVNTNCYFM-DGgqiTIGDNVFIGPNCGFytathplnfhhrnegfekAGPINIGSNTWFGGHVAVLPGVTIG 152
Cdd:cd03360  114 DARIGDNVIINTGAVIGhDC---VIGDFVHIAPGVVL------------------SGGVTIGEGAFIGAGATIIQGVTIG 172

                         90       100
                 ....*....|....*....|....*
gi 616690642 153 EGSVIGAGSVVTKDIPPHSLAVGNP 177
Cdd:cd03360  173 AGAIIGAGAVVTKDVPDGSVVVGNP 197
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 74-177 7.91e-22

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: 87.93  E-value: 7.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642   74 NVKLGKNVYVNTNCYFmdGGQITIGDNVFIGPNCGFytathplnfhhrnegfekAGPINIGSNTWFGGHVAVLPGVTIGE 153
Cdd:TIGR03570 117 DVRIGDNVIINTGAIV--EHDCVIGDFVHIAPGVTL------------------SGGVVIGEGVFIGAGATIIQGVTIGA 176

                          90       100
                  ....*....|....*....|....
gi 616690642  154 GSVIGAGSVVTKDIPPHSLAVGNP 177
Cdd:TIGR03570 177 GAIVGAGAVVTKDIPDGGVVVGVP 200
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 75-187 1.71e-19

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 81.85  E-value: 1.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  75 VKLGKNVYVNTNCYFMDGGQITIGDNVFIGPNCgFYTATHPLNFHHRNEGFE----------KAGPINIGSNTWFGGHVA 144
Cdd:PRK09677  66 LFFGDNVQVNDYVHIACIESITIGRDTLIASKV-FITDHNHGSFKHSDDFSSpnlppdmrtlESSAVVIGQRVWIGENVT 144

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 616690642 145 VLPGVTIGEGSVIGAGSVVTKDIPPHSLAVGNPCKVVRKIDNE 187
Cdd:PRK09677 145 ILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKKYNHE 187
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 87-177 1.03e-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: 74.40  E-value: 1.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  87 CYFMDGGQITIGDNVFIGPNCGFYtatHPLNFHHRNEGFEKAGPInIGSNTWFGGHVAVLPGVTIGEGSVIGAGSVVTKD 166
Cdd:cd03354   15 LFIDHGTGIVIGETAVIGDNCTIY---QGVTLGGKGKGGGKRHPT-IGDNVVIGAGAKILGNITIGDNVKIGANAVVTKD 90

                         90
                 ....*....|.
gi 616690642 167 IPPHSLAVGNP 177
Cdd:cd03354   91 VPANSTVVGVP 101
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 89-187 7.26e-17

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: 74.35  E-value: 7.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  89 FMD-GGQITIGDNVFIGPNCGFY---T--AThplnfhhrneGFEKAG--PInIGSNTWFGGHVAVLPGVTIGEGSVIGAG 160
Cdd:COG1045   79 FIDhGTGVVIGETAVIGDNVTIYqgvTlgGT----------GKEKGKrhPT-IGDNVVIGAGAKILGPITIGDNAKIGAN 147

                         90       100
                 ....*....|....*....|....*..
gi 616690642 161 SVVTKDIPPHSLAVGNPCKVVRKIDNE 187
Cdd:COG1045  148 SVVLKDVPPGSTVVGVPARIVKRKGSK 174
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 92-187 1.06e-16

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: 73.21  E-value: 1.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  92 GGQITIGDNVFIGPNCGFYTAThplnfhhrnegfekagpinIGSNTWFGGHVAVLPGVTIGEGSVIGAGSVVT--KDIPP 169
Cdd:cd04645   58 GYPTIIGDNVTVGHGAVLHGCT-------------------IGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPpgKVIPP 118

                         90
                 ....*....|....*...
gi 616690642 170 HSLAVGNPCKVVRKIDNE 187
Cdd:cd04645  119 GSLVAGSPAKVVRELTDE 136
Mac pfam12464
Maltose acetyltransferase; This domain family is found in bacteria, archaea and eukaryotes, ...
 6-57 1.19e-16

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: 70.21  E-value: 1.19e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 616690642    6 KMLAEKWYDAnFDQDLINERARAKDICFELNHTKPSDKNKRKELIDELFQTT 57
Cdd:pfam12464   1 KMLAGELYDA-SDPELVAERLRARRLLRRYNNTPPEDAEEREELLKELFGSV 51
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 75-164 2.56e-15

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: 67.66  E-value: 2.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  75 VKLGKNVYVNTNCYFmdGGQITIGDNVFIGPNCGFYTATHPlnfhhrnegfEKAGPINIGSNTWFGGHVAVLPGVTIGEG 154
Cdd:cd00208    1 VFIGEGVKIHPKAVI--RGPVVIGDNVNIGPGAVIGAATGP----------NEKNPTIIGDNVEIGANAVIHGGVKIGDN 68

                         90
                 ....*....|
gi 616690642 155 SVIGAGSVVT 164
Cdd:cd00208   69 AVIGAGAVVT 78
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 74-187 4.66e-15

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 69.29  E-value: 4.66e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  74 NVKLGKNVYV-----------------NTN--------CyfMDGGQITIGDNVFIGPNCGFYTAThplnfhhrnegfeka 128
Cdd:COG0663   28 DVTIGEDVSVwpgavlrgdvgpirigeGSNiqdgvvlhV--DPGYPLTIGDDVTIGHGAILHGCT--------------- 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 616690642 129 gpinIGSNTWFGGHVAVLPGVTIGEGSVIGAGSVVT--KDIPPHSLAVGNPCKVVRKIDNE 187
Cdd:COG0663   91 ----IGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTegKVVPPGSLVVGSPAKVVRELTEE 147
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 86-181 5.11e-13

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: 65.42  E-value: 5.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  86 NCYFMDGGQI----TIGDNVFIGPNCGFytathplnfhhrnegfekAGPINIGSNTWFGGHVAVLPGVTIGEGSVIGAGS 161
Cdd:COG1043  110 DNLLMAYVHVahdcVVGNNVILANNATL------------------AGHVEVGDHAIIGGLSAVHQFVRIGAHAMVGGGS 171

                         90       100
                 ....*....|....*....|
gi 616690642 162 VVTKDIPPHSLAVGNPCKVV 181
Cdd:COG1043  172 GVVKDVPPYVLAAGNPARLR 191
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 74-188 1.10e-12

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: 62.77  E-value: 1.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  74 NVKLGKNVYVNTN-CYFMDGGQITIGDNVFIGPNC---GF--YTATHPLNFH--HrnegfekaGPI----NIGSNTWFGG 141
Cdd:cd04745   18 DVIIGKNCYIGPHaSLRGDFGRIVIRDGANVQDNCvihGFpgQDTVLEENGHigH--------GAIlhgcTIGRNALVGM 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 616690642 142 HVAVLPGVTIGEGSVIGAGSVVTK--DIPPHSLAVGNPCKVVRKI-DNEV 188
Cdd:cd04745   90 NAVVMDGAVIGEESIVGAMAFVKAgtVIPPRSLIAGSPAKVIRELsDEEV 139
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 86-181 2.96e-12

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: 63.22  E-value: 2.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  86 NCYFMDGGQI----TIGDNVFIGPNCGFytathplnfhhrnegfekAGPINIGSNTWFGGHVAVLPGVTIGEGSVIGAGS 161
Cdd:cd03351  108 NNLLMAYVHVahdcVIGNNVILANNATL------------------AGHVEIGDYAIIGGLSAVHQFCRIGRHAMVGGGS 169

                         90       100
                 ....*....|....*....|
gi 616690642 162 VVTKDIPPHSLAVGNPCKVV 181
Cdd:cd03351  170 GVVQDVPPYVIAAGNRARLR 189
PLN02739 PLN02739
serine acetyltransferase
 132-193 6.09e-12

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 63.13  E-value: 6.09e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616690642 132 NIGSNTWFGGHVAVLPGVTIGEGSVIGAGSVVTKDIPPHSLAVGNPCKVVRKIDNEVPSEAL 193
Cdd:PLN02739 259 KIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFVDEQDPSLTM 320
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 74-187 9.85e-12

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: 60.28  E-value: 9.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  74 NVKLGK--NVYVNTNCYFMDGGQITIGDNVFIGPNCGFYTAthplnfhhrnegfekagpiNIGSNTWFGGHVAVLPGVTI 151
Cdd:cd04650   39 SIYIGKysNVQENVSIHTDHGYPTEIGDYVTIGHNAVVHGA-------------------KVGNYVIVGMGAILLNGAKI 99

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 616690642 152 GEGSVIGAGSVVT--KDIPPHSLAVGNPCKVVRKIDNE 187
Cdd:cd04650  100 GDHVIIGAGAVVTpgKEIPDYSLVLGVPAKVVRKLTEE 137
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 94-177 1.06e-11

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: 61.27  E-value: 1.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  94 QITIGDNVFIGPNCGFYTAThplnfhhrneGFekAGPINIGSNTWFGGHVAVLPGVTIGEGSVIGAGSVVTKDIPPHSLA 173
Cdd:cd03352  126 LVQIAHNVRIGENCLIAAQV----------GI--AGSTTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYV 193


                 ....
gi 616690642 174 VGNP 177
Cdd:cd03352  194 SGTP 197
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 96-175 2.90e-11

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: 61.58  E-value: 2.90e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  96 TIGDNVFIGpncgfytathplnfhhrnegfekagpinigSNTWFgghVAvlPgVTIGEGSVIGAGSVVTKDIPPHSLAVG 175
Cdd:COG1207  396 VIGDGAFIG------------------------------SNTNL---VA--P-VTIGDGATIGAGSTITKDVPAGALAIA 439
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 75-177 4.07e-11

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: 61.31  E-value: 4.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642   75 VKLGKNVYVNTnCYFMDGGQITIGDNVFIGPNCGFYTathplnfHHRNEGFEKAGPINIGSNTWFGGHVAVLPGVTIGEG 154
Cdd:TIGR02353 598 VKIGRGVYIDG-TDLTERDLVTIGDDSTLNEGSVIQT-------HLFEDRVMKSDTVTIGDGATLGPGAIVLYGVVMGEG 669

                          90       100
                  ....*....|....*....|....*
gi 616690642  155 SVIGAGSVVTK--DIPPHSLAVGNP 177
Cdd:TIGR02353 670 SVLGPDSLVMKgeEVPAHTRWRGNP 694
PLN02694 PLN02694
serine O-acetyltransferase
 63-194 8.29e-11

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 59.66  E-value: 8.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  63 ISIPFDTDYGWNVKLGKNVYVNTNCYFMDGGQITIGDNVFIgpncgfytathplnFHHRN-EGFEKAG----PiNIGSNT 137
Cdd:PLN02694 155 ISDVFAVDIHPAAKIGKGILFDHATGVVIGETAVIGNNVSI--------------LHHVTlGGTGKACgdrhP-KIGDGV 219

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 616690642 138 WFGGHVAVLPGVTIGEGSVIGAGSVVTKDIPPHSLAVGNPCKVV-----RKIDNEVPSEALN 194
Cdd:PLN02694 220 LIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLVggkekPAKHEECPGESMD 281
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 74-182 1.35e-10

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 59.49  E-value: 1.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  74 NVKLGKNVYVNTNCYFMDGgqiTIGDNVFIGP---NC---GFytathplnFHHRNEGFEKAgpiNIGSNTwfgghVAVLP 147
Cdd:PRK14353 338 NAKLGEGAKVNHLTYIGDA---TIGAGANIGAgtiTCnydGF--------NKHRTEIGAGA---FIGSNS-----ALVAP 398

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 616690642 148 gVTIGEGSVIGAGSVVTKDIPPHSLAVGNPCKVVR 182
Cdd:PRK14353 399 -VTIGDGAYIASGSVITEDVPDDALALGRARQETK 432
PLN02357 PLN02357
serine acetyltransferase
 63-186 3.72e-10

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 57.97  E-value: 3.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  63 ISIPFDTDYGWNVKLGKNVYVNTNCYFMDGGQITIGDNVFI---------GPNCGfytATHPlnfhhrnegfekagpiNI 133
Cdd:PLN02357 221 VSEAFAVDIHPGAKIGQGILLDHATGVVIGETAVVGNNVSIlhnvtlggtGKQSG---DRHP----------------KI 281

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 616690642 134 GSNTWFGGHVAVLPGVTIGEGSVIGAGSVVTKDIPPHSLAVGNPCKVVRKIDN 186
Cdd:PLN02357 282 GDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLIGGKEN 334
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 74-175 5.24e-10

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: 56.27  E-value: 5.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  74 NVKLGKNVYVNTNCYFmdgGQITIGDNVFIGpnCGFYTAthplNFhhrnEGFEKAGPI-----NIGSNTWFgghVAvlPg 148
Cdd:cd03353  102 KSTIGEGSKANHLSYL---GDAEIGEGVNIG--AGTITC----NY----DGVNKHRTVigdnvFIGSNSQL---VA--P- 162

                         90       100
                 ....*....|....*....|....*..
gi 616690642 149 VTIGEGSVIGAGSVVTKDIPPHSLAVG 175
Cdd:cd03353  163 VTIGDGATIAAGSTITKDVPPGALAIA 189
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 93-182 2.63e-09

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 55.91  E-value: 2.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  93 GQITIGDNVFIGpnCGFYTATHPLNFHHRNEgfekagpinIGSNTWFGGHVAVLPGVTIGEGSVIGAGSVVTKDIPPHSL 172
Cdd:PRK14355 371 GDATIGRNVNIG--CGTITCNYDGVKKHRTV---------IEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPPDSL 439

                         90
                 ....*....|
gi 616690642 173 AVGNPCKVVR 182
Cdd:PRK14355 440 AIARSPQVNK 449
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 77-175 3.67e-09

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 55.50  E-value: 3.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  77 LGKNVYVNTNCYFmdgGQITIGDNVFIGpnCGFYTATHP-LNFHHRNEGfEKAgpiNIGSNTwfgghvAVLPGVTIGEGS 155
Cdd:PRK14356 359 LGKGAKANHLTYL---GDAEIGAGANIG--AGTITCNYDgVNKHRTVIG-EGA---FIGSNT------ALVAPVTIGDGA 423

                         90       100
                 ....*....|....*....|
gi 616690642 156 VIGAGSVVTKDIPPHSLAVG 175
Cdd:PRK14356 424 LVGAGSVITKDVPDGSLAIA 443
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 74-183 1.02e-08

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 54.16  E-value: 1.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  74 NVKLGKNVYVNTNCYFmdgGQITIGDNVFIGpnCGFYTAthplNFhhrnEGFEKAgPINIGSNTWFGGH-VAVLPgVTIG 152
Cdd:PRK14360 348 KSQLGEGSKVNHLSYI---GDATLGEQVNIG--AGTITA----NY----DGVKKH-RTVIGDRSKTGANsVLVAP-ITLG 412

                         90       100       110
                 ....*....|....*....|....*....|.
gi 616690642 153 EGSVIGAGSVVTKDIPPHSLAVGNPCKVVRK 183
Cdd:PRK14360 413 EDVTVAAGSTITKDVPDNSLAIARSRQVIKE 443
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
86-180 1.31e-08

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 53.18  E-value: 1.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  86 NCYFMDGGQI----TIGDNVFIGPNCGFytathplnfhhrnegfekAGPINIGSNTWFGGHVAVLPGVTIGEGSVIGAGS 161
Cdd:PRK05289 111 NNLLMAYVHVahdcVVGNHVILANNATL------------------AGHVEVGDYAIIGGLTAVHQFVRIGAHAMVGGMS 172

                         90
                 ....*....|....*....
gi 616690642 162 VVTKDIPPHSLAVGNPCKV 180
Cdd:PRK05289 173 GVSQDVPPYVLAEGNPARL 191
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 93-183 1.88e-08

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 53.23  E-value: 1.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  93 GQITIGDNVFIGpncgfyTATHPLNFhhrnEGFEKaGPINIGSNTWFGGHVAVLPGVTIGEGSVIGAGSVVTKDIPPHSL 172
Cdd:PRK14357 357 GDATVGKNVNIG------AGTITCNY----DGKKK-NPTFIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSL 425

                         90
                 ....*....|.
gi 616690642 173 AVGNPCKVVRK 183
Cdd:PRK14357 426 ALGRARQIVKE 436
cysE PRK11132
serine acetyltransferase; Provisional
 145-194 4.76e-08

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 51.62  E-value: 4.76e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 616690642 145 VLPGVTIGEGSVIGAGSVVTKDIPPHSLAVGNPCKVVRKIDNEVPSEALN 194
Cdd:PRK11132 208 ILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVGKPESDKPSMDMD 257
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 74-163 9.57e-08

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 50.10  E-value: 9.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  74 NVKLGKNVYVNTNCYFMDGGQI----TIGDNVFIGPNCgfytathplnfhhrnegfekagpiNIGSNTWFGGHVAVLPGV 149
Cdd:cd03352    1 SAKIGENVSIGPNAVIGEGVVIgdgvVIGPGVVIGDGV------------------------VIGDDCVIHPNVTIYEGC 56

                         90
                 ....*....|....
gi 616690642 150 TIGEGSVIGAGSVV 163
Cdd:cd03352   57 IIGDRVIIHSGAVI 70
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 74-163 7.02e-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: 48.48  E-value: 7.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  74 NVKLGKNVYVNTNCYFMDGgqITIGDNVFIGPNCGFYTATHplnfhhrnegfekagpinIGSNTWFGGHVAVLPGVTIGE 153
Cdd:COG1044  108 SAKIGEGVSIGPFAVIGAG--VVIGDGVVIGPGVVIGDGVV------------------IGDDCVLHPNVTIYERCVIGD 167

                         90
                 ....*....|
gi 616690642 154 GSVIGAGSVV 163
Cdd:COG1044  168 RVIIHSGAVI 177
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 133-174 8.68e-07

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 48.40  E-value: 8.68e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 616690642 133 IGSNTWFgghvaVLPgVTIGEGSVIGAGSVVTKDIPPHSLAV 174
Cdd:PRK14352 408 TGSDTMF-----VAP-VTVGDGAYTGAGTVIREDVPPGALAV 443
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 74-197 1.21e-06

Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p25 is part of the pointed-end subcomplex in dynactin that also includes p26, p27, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100049 [Multi-domain]  Cd Length: 161  Bit Score: 46.44  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  74 NVKLGKNVYVNTNC-------------YFMDggqITIGDNVFIGPNCGFYTAthplnfhhrnegfekagpiNIGSNTWFG 140
Cdd:cd03359   42 TVSIGRYCILSEGCvirppfkkfskgvAFFP---LHIGDYVFIGENCVVNAA-------------------QIGSYVHIG 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 616690642 141 GHVAVLPGVTIGEGSVIGAGSVVTKD--IPPHSLAVGNPCKVVrKIDNEVPSEALNDET 197
Cdd:cd03359  100 KNCVIGRRCIIKDCVKILDGTVVPPDtvIPPYSVVSGRPARFI-GELPECTQELMEEET 157
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 94-169 2.08e-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: 46.93  E-value: 2.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  94 QITIGDNVFIGPNC------GFytathplnfhhrnegfekAGPINIGSNTWFGGHVAVLPGVTIGEGSVIGAGSVVTKDI 167
Cdd:COG1044  234 LVQIAHNVRIGEHTaiaaqvGI------------------AGSTKIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSI 295


                 ..
gi 616690642 168 PP 169
Cdd:COG1044  296 PE 297
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 74-163 2.09e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 47.06  E-value: 2.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  74 NVKLGKNVYVNTNCYFMDGgqITIGDNVFIGPNCGFYTATHplnfhhrnegfekagpinIGSNTWFGGHVAVLPGVTIGE 153
Cdd:PRK00892 112 SAKIGEGVSIGPNAVIGAG--VVIGDGVVIGAGAVIGDGVK------------------IGADCRLHANVTIYHAVRIGN 171

                         90
                 ....*....|
gi 616690642 154 GSVIGAGSVV 163
Cdd:PRK00892 172 RVIIHSGAVI 181
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 94-169 2.28e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 47.06  E-value: 2.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  94 QITIGDNVFIGPNC------GFytathplnfhhrnegfekAGPINIGSNTWFGGHVAVLPGVTIGEGSVIGAGSVVTKDI 167
Cdd:PRK00892 237 LVQIAHNVVIGRHTaiaaqvGI------------------AGSTKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSI 298


                 ..
gi 616690642 168 PP 169
Cdd:PRK00892 299 PE 300
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 133-175 3.27e-06

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 46.75  E-value: 3.27e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 616690642 133 IGSNTWFgghvaVLPgVTIGEGSVIGAGSVVTKDIPPHSLAVG 175
Cdd:PRK14354 402 IGCNSNL-----VAP-VTVGDNAYIAAGSTITKDVPEDALAIA 438
PRK10191 PRK10191
putative acyl transferase; Provisional
 92-180 7.07e-06

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 44.11  E-value: 7.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  92 GGQITIGDNVFIGPNcgfYTATHPLNFHHRNeGFEKAGPInIGSNTWFGGHVAVLPGVTIGEGSVIGAGSVVTKDIPPHS 171
Cdd:PRK10191  59 GYAVVINKNVVAGDD---FTIRHGVTIGNRG-ADNMACPH-IGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNA 133


                 ....*....
gi 616690642 172 LAVGNPCKV 180
Cdd:PRK10191 134 LVVGEKARV 142
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 75-168 1.51e-05

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


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 43.14  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  75 VKLGKNV------YVNTNCYFMDGGQI----------TIGDNVFIGPNCGFYTATHPLNfhhrnegfekAGPINIGSNTW 138
Cdd:cd03350   14 AFIGPGAvlmmpsYVNIGAYVDEGTMVdswatvgscaQIGKNVHLSAGAVIGGVLEPLQ----------ATPVIIEDDVF 83

                         90       100       110
                 ....*....|....*....|....*....|
gi 616690642 139 FGGHVAVLPGVTIGEGSVIGAGSVVTKDIP 168
Cdd:cd03350   84 IGANCEVVEGVIVGKGAVLAAGVVLTQSTP 113
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 74-174 7.63e-05

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 42.71  E-value: 7.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  74 NVKLGKNVYVNTNCYFmdgGQITIGDNVFIGpnCGFYTATHplnfhhrnEGFEKAGPInIGSNTWFGGHVAVLPGVTIGE 153
Cdd:PRK09451 352 KARLGKGSKAGHLTYL---GDAEIGDNVNIG--AGTITCNY--------DGANKFKTI-IGDDVFVGSDTQLVAPVTVGK 417

                         90       100
                 ....*....|....*....|.
gi 616690642 154 GSVIGAGSVVTKDIPPHSLAV 174
Cdd:PRK09451 418 GATIGAGTTVTRDVAENELVI 438
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 96-163 8.46e-05

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 41.93  E-value: 8.46e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 616690642  96 TIGDNVFIGPNCGFytathplnfhhrnegfekAGPINIGSNTWFGGHVAVLPGVTIGEGSVIGAGSVV 163
Cdd:PRK12461  13 KLGSGVEIGPFAVI------------------GANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVV 62
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 75-192 9.33e-05

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 42.43  E-value: 9.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642   75 VKLGKNVYVNT---NCYfmdgGQITIGDNVFIGPNCGFYTathplnfhHRNE-GFEKAGPINIGSNTWFGGHVAVLPGVT 150
Cdd:TIGR02353 113 AKIGKGVDIGSlppVCT----DLLTIGAGTIVRKEVMLLG--------YRAErGRLHTGPVTLGRDAFIGTRSTLDIDTS 180

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 616690642  151 IGEGSVIGAGSVVTKD--IPPHSLAVGNPCKVVRKIDNEVPSEA 192
Cdd:TIGR02353 181 IGDGAQLGHGSALQGGqsIPDGERWHGSPAQKTGADYRKVQPAR 224
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
97-163 1.26e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 41.62  E-value: 1.26e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 616690642  97 IGDNVFIGPncgfYTATHPlnfhhrnegfekagPINIGSNTWFGGHVAVLPGVTIGEGSVIGAGSVV 163
Cdd:PRK05289  17 IGENVEIGP----FCVIGP--------------NVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASI 65
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
130-159 2.31e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 36.93  E-value: 2.31e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 616690642  130 PINIGSNTWFGGHVAVLPGVTIGEGSVIGA 159
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 97-163 3.02e-04

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 40.39  E-value: 3.02e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616690642  97 IGDNVFIGPNC--GfytathplnfhhrnegfekaGPINIGSNTWFGGHVAVLPGVTIGEGSVIGAGSVV 163
Cdd:COG1043   16 LGENVEIGPFCviG--------------------PDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASI 64
PLN02296 PLN02296
carbonate dehydratase
 96-187 4.66e-04

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 39.72  E-value: 4.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  96 TIGDNVFIGPNCGFYTATHplnfhhRNEGFekagpINIGSNtwfgghvaVLPGVTIGEGSVIGAGSVVTKD--IPPHSLA 173
Cdd:PLN02296 121 IIGDNVTIGHSAVLHGCTV------EDEAF-----VGMGAT--------LLDGVVVEKHAMVAAGALVRQNtrIPSGEVW 181

                         90
                 ....*....|....
gi 616690642 174 VGNPCKVVRKIDNE 187
Cdd:PLN02296 182 AGNPAKFLRKLTEE 195
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 97-163 6.97e-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: 39.34  E-value: 6.97e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 616690642  97 IGDNVFIGPNC--GfytathplnfhhrnegfekaGPINIGSNTWFGGHVAVLPGVTIGEGSVIGAGSVV 163
Cdd:cd03351   14 IGENVEIGPFCviG--------------------PNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASI 62
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 78-180 9.60e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 38.85  E-value: 9.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  78 GKNVYVNTNCYFMDGGQItiGDNVFIGPNC--GFYTAThplnfhhrnegfekAGPINIGSNTWFGGHVAVLPGVTIGEGS 155
Cdd:PRK12461  99 GGVTRIGNDNLLMAYSHV--AHDCQIGNNVilVNGALL--------------AGHVTVGDRAIISGNCLVHQFCRIGALA 162

                         90       100
                 ....*....|....*....|....*
gi 616690642 156 VIGAGSVVTKDIPPHSLAVGNPCKV 180
Cdd:PRK12461 163 MMAGGSRISKDVPPYCMMAGHPTNV 187
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 72-164 1.49e-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: 37.57  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  72 GWNVKLGKNVYVNtNCYFMDGGQIT----IGDNVfIGPNCGFYTATHPLNFHH-------------RNEGFEKAGPInIG 134
Cdd:cd05636   57 GDGCVVGNSVEVK-NSIIMDGTKVPhlnyVGDSV-LGENVNLGAGTITANLRFddkpvkvrlkgerVDTGRRKLGAI-IG 133

                         90       100       110
                 ....*....|....*....|....*....|
gi 616690642 135 SNTWFGGHVAVLPGVTIGEGSVIGAGSVVT 164
Cdd:cd05636  134 DGVKTGINVSLNPGVKIGPGSWVYPGCVVR 163
PLN02472 PLN02472
uncharacterized protein
 140-195 2.18e-03

uncharacterized protein


Pssm-ID: 215263 [Multi-domain]  Cd Length: 246  Bit Score: 37.63  E-value: 2.18e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 616690642 140 GGHVAVLPGVTIGEGSVIGAGSVVT--KDIPPHSLAVGNPCKVVRKIDNE----VP--SEALND 195
Cdd:PLN02472 153 GQHSILMEGSLVETHSILEAGSVLPpgRRIPTGELWAGNPARFVRTLTNEetleIPklAVAIND 216
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 94-174 2.62e-03

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 38.05  E-value: 2.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  94 QITIGDNVFIGPNCGFytathplnfhhrnegfekAGPINIGSNTwfgghvavlpgvtigegsVIGAGSVVTKDIPPHSLA 173
Cdd:PRK14359 367 KTIIGKNVFIGSDTQL------------------VAPVNIEDNV------------------LIAAGSTVTKDVPKGSLA 410


                 .
gi 616690642 174 V 174
Cdd:PRK14359 411 I 411
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 72-168 3.01e-03

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


Pssm-ID: 441774 [Multi-domain]  Cd Length: 268  Bit Score: 37.40  E-value: 3.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616690642  72 GWNVKLGKNVY---VntncyfMDGGQ---ITIGDNVFIGPNCGfytathplnfhhrnegfekagpinigsntwfgghvaV 145
Cdd:COG2171  148 GKNVHLSGGAGiggV------LEPLQaapVIIEDNCFIGARSG------------------------------------V 185

                         90       100
                 ....*....|....*....|...
gi 616690642 146 LPGVTIGEGSVIGAGSVVTKDIP 168
Cdd:COG2171  186 VEGVIVGEGAVLGAGVYLTASTK 208
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 133-194 3.67e-03

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 36.71  E-value: 3.67e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 616690642 133 IGSNTWFGGHVAVLPGVTIGEGSVIGAGSVVTKDI--PPHSLAVGNPCKVVRKI-DNEVPSEALN 194
Cdd:PRK13627  91 IGRDALVGMNSVIMDGAVIGEESIVAAMSFVKAGFqgEKRQLLMGTPARAVRSVsDDELHWKRLN 155
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
133-165 4.94e-03

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 33.57  E-value: 4.94e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 616690642  133 IGSNTWFGGHVAVlpGVTIGEGSVIGAGSVVTK 165
Cdd:pfam14602   3 IGDNCLIGANSGI--GVSLGDNCVVGAGVVITA 33
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
74-105 5.53e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.46  E-value: 5.53e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 616690642   74 NVKLGKNVYVNTNCYFMDGgqITIGDNVFIGP 105
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGG--VIIGDNVIIGA 30
 
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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