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Conserved domains on  [gi|835335140|ref|WP_047460835|]
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sugar O-acetyltransferase [Vibrio fluvialis]

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 ...
 13-180 4.67e-95

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: 273.14  E-value: 4.67e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  13 YDPADTELKAMRASTREKLDRFNRSQSDEQALQERIITELFGAAGSNISVNRHFRCDYGVNIKVGNNFYTNYDCVILDCA 92
Cdd:cd03357    2 YNASDPELVAERARARRLLHEYNQTPPSDAEERRELLKELFGSVGENVYIEPPFHCDYGYNIHIGDNFYANFNCTILDVA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  93 EVIIGDDCLIGPQVGLYTACHPLDPVERASGKEFAKPITIGNNCWIGGHATINPGVTLGNNVVVASGAVVTKSFGANVVI 172
Cdd:cd03357   82 PVTIGDNVLIGPNVQIYTAGHPLDPEERNRGLEYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVA 161


                 ....*...
gi 835335140 173 AGNPARVI 180
Cdd:cd03357  162 AGNPARVI 169
 
Name Accession Description Interval E-value
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 13-180 4.67e-95

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: 273.14  E-value: 4.67e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  13 YDPADTELKAMRASTREKLDRFNRSQSDEQALQERIITELFGAAGSNISVNRHFRCDYGVNIKVGNNFYTNYDCVILDCA 92
Cdd:cd03357    2 YNASDPELVAERARARRLLHEYNQTPPSDAEERRELLKELFGSVGENVYIEPPFHCDYGYNIHIGDNFYANFNCTILDVA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  93 EVIIGDDCLIGPQVGLYTACHPLDPVERASGKEFAKPITIGNNCWIGGHATINPGVTLGNNVVVASGAVVTKSFGANVVI 172
Cdd:cd03357   82 PVTIGDNVLIGPNVQIYTAGHPLDPEERNRGLEYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVA 161


                 ....*...
gi 835335140 173 AGNPARVI 180
Cdd:cd03357  162 AGNPARVI 169
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 3-183 3.72e-85

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 248.57  E-value: 3.72e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140   3 EFKKMVTGEIYDPADTELKAMRASTREKLDRFNRSQSDEQALQERIITELFGAAGsNISVNRHFRCDYGVNIKVGNNFYT 82
Cdd:PRK10092   4 EKEKMIAGELYRSADETLSRDRLRARQLIHRYNHSLPDEHTLRQQILADLFGQVT-EAYIEPTFRCDYGYNIFLGNNFYA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  83 NYDCVILDCAEVIIGDDCLIGPQVGLYTACHPLDPVERASGKEFAKPITIGNNCWIGGHATINPGVTLGNNVVVASGAVV 162
Cdd:PRK10092  83 NFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPLDPVARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVV 162

                        170       180
                 ....*....|....*....|.
gi 835335140 163 TKSFGANVVIAGNPARVIKSL 183
Cdd:PRK10092 163 TKDVPDNVVVGGNPARIIKKL 183
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
47-184 7.31e-49

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 155.03  E-value: 7.31e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  47 RIITELFGAAGSNISVNRHFRCdYGVNIKVGNNFYTNYDCVILDCAEVIIGDDCLIGPQVGLYTACHPLDPVERasGKEF 126
Cdd:COG0110    2 KLLLLFGARIGDGVVIGPGVRI-YGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPAT--FPLR 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 835335140 127 AKPITIGNNCWIGGHATINPGVTLGNNVVVASGAVVTKSFGANVVIAGNPARVIKSLE 184
Cdd:COG0110   79 TGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRD 136
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 71-177 3.40e-15

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: 70.21  E-value: 3.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140   71 GVNIKVGNNFYTNYDCVIlDCaEVIIGDDCLIGPQVGLytachpldpveraSGKefakpITIGNNCWIGGHATINPGVTL 150
Cdd:TIGR03570 115 NPDVRIGDNVIINTGAIV-EH-DCVIGDFVHIAPGVTL-------------SGG-----VVIGEGVFIGAGATIIQGVTI 174

                          90       100
                  ....*....|....*....|....*..
gi 835335140  151 GNNVVVASGAVVTKSFGANVVIAGNPA 177
Cdd:TIGR03570 175 GAGAIVGAGAVVTKDIPDGGVVVGVPA 201
Mac pfam12464
Maltose acetyltransferase; This domain family is found in bacteria, archaea and eukaryotes, ...
 6-57 3.94e-14

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: 63.28  E-value: 3.94e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 835335140    6 KMVTGEIYDPADTELKAMRASTREKLDRFNRSQSDEQALQERIITELFGAAG 57
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 ...
 13-180 4.67e-95

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: 273.14  E-value: 4.67e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  13 YDPADTELKAMRASTREKLDRFNRSQSDEQALQERIITELFGAAGSNISVNRHFRCDYGVNIKVGNNFYTNYDCVILDCA 92
Cdd:cd03357    2 YNASDPELVAERARARRLLHEYNQTPPSDAEERRELLKELFGSVGENVYIEPPFHCDYGYNIHIGDNFYANFNCTILDVA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  93 EVIIGDDCLIGPQVGLYTACHPLDPVERASGKEFAKPITIGNNCWIGGHATINPGVTLGNNVVVASGAVVTKSFGANVVI 172
Cdd:cd03357   82 PVTIGDNVLIGPNVQIYTAGHPLDPEERNRGLEYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVA 161


                 ....*...
gi 835335140 173 AGNPARVI 180
Cdd:cd03357  162 AGNPARVI 169
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 3-183 3.72e-85

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 248.57  E-value: 3.72e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140   3 EFKKMVTGEIYDPADTELKAMRASTREKLDRFNRSQSDEQALQERIITELFGAAGsNISVNRHFRCDYGVNIKVGNNFYT 82
Cdd:PRK10092   4 EKEKMIAGELYRSADETLSRDRLRARQLIHRYNHSLPDEHTLRQQILADLFGQVT-EAYIEPTFRCDYGYNIFLGNNFYA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  83 NYDCVILDCAEVIIGDDCLIGPQVGLYTACHPLDPVERASGKEFAKPITIGNNCWIGGHATINPGVTLGNNVVVASGAVV 162
Cdd:PRK10092  83 NFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPLDPVARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVV 162

                        170       180
                 ....*....|....*....|.
gi 835335140 163 TKSFGANVVIAGNPARVIKSL 183
Cdd:PRK10092 163 TKDVPDNVVVGGNPARIIKKL 183
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
47-184 7.31e-49

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 155.03  E-value: 7.31e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  47 RIITELFGAAGSNISVNRHFRCdYGVNIKVGNNFYTNYDCVILDCAEVIIGDDCLIGPQVGLYTACHPLDPVERasGKEF 126
Cdd:COG0110    2 KLLLLFGARIGDGVVIGPGVRI-YGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPAT--FPLR 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 835335140 127 AKPITIGNNCWIGGHATINPGVTLGNNVVVASGAVVTKSFGANVVIAGNPARVIKSLE 184
Cdd:COG0110   79 TGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRD 136
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 1-183 4.63e-46

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 150.15  E-value: 4.63e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140   1 MNEFKKMVTGEIYDPADTELKAMRASTREKLDRFNRSQSDEQALQERIITELFGAAGSNISVNRHFRCDYGVNIKVGNNF 80
Cdd:PRK09527   3 MSMTERIKAGKLFTDMCEGLPEKRLRGKTLMYEFNHSHPSEVEKRESLIKEMFATVGENAWVEPPVYFSYGSNIHIGRNF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  81 YTNYDCVILDCAEVIIGDDCLIGPQVGLYTACHPLDPVERASGKEFAKPITIGNNCWIGGHATINPGVTLGNNVVVASGA 160
Cdd:PRK09527  83 YANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGHPVHHELRKNGEMYSFPITIGNNVWIGSHVVINPGVTIGDNSVIGAGS 162

                        170       180
                 ....*....|....*....|...
gi 835335140 161 VVTKSFGANVVIAGNPARVIKSL 183
Cdd:PRK09527 163 VVTKDIPPNVVAAGVPCRVIREI 185
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 73-180 6.46e-42

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: 136.43  E-value: 6.46e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  73 NIKVGNNFYTNYDCVILDCAEVIIGDDCLIGPQVGLYTACHPLDPVERA-SGKEFAKPITIGNNCWIGGHATINPGVTLG 151
Cdd:cd04647    1 NISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDHNHDIDDPERPiEQGVTSAPIVIGDDVWIGANVVILPGVTIG 80

                         90       100
                 ....*....|....*....|....*....
gi 835335140 152 NNVVVASGAVVTKSFGANVVIAGNPARVI 180
Cdd:cd04647   81 DGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 73-181 9.61e-22

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: 86.06  E-value: 9.61e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  73 NIKVGNNFYTNYDCVILDCAEVIIGDDCLIGPQV--GLYTAcHPLDPV-------------ERASGKEF--AKPITIGNN 135
Cdd:cd03349    1 NISVGDYSYGSGPDCDVGGDKLSIGKFCSIAPGVkiGLGGN-HPTDWVstypfyifggeweDDAKFDDWpsKGDVIIGND 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 835335140 136 CWIGGHATINPGVTLGNNVVVASGAVVTKSFGANVVIAGNPARVIK 181
Cdd:cd03349   80 VWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIR 125
PRK10502 PRK10502
putative acyl transferase; Provisional
 52-181 1.17e-21

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 86.54  E-value: 1.17e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  52 LFGAagsniSVNRHFRCDYGVNIK------VGNNFYTNYDCVILDCAEVIIGDDCLIGPQVGLYTACHplDPvERASGKE 125
Cdd:PRK10502  49 LFGA-----KIGKGVVIRPSVRITypwkltIGDYAWIGDDVWLYNLGEITIGAHCVISQKSYLCTGSH--DY-SDPHFDL 120

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 835335140 126 FAKPITIGNNCWIGGHATINPGVTLGNNVVVASGAVVTKSFGANVVIAGNPARVIK 181
Cdd:PRK10502 121 NTAPIVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIR 176
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 71-181 3.25e-21

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: 83.70  E-value: 3.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  71 GVNIKVGNNFYTNYDCVILD----------CAEVIIGDDCLIGPQVGLYTACHPLDPVERasgKEFAKPITIGNNCWIGG 140
Cdd:cd03358    2 GDNCIIGTNVFIENDVKIGDnvkiqsnvsiYEGVTIEDDVFIGPNVVFTNDLYPRSKIYR---KWELKGTTVKRGASIGA 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 835335140 141 HATINPGVTLGNNVVVASGAVVTKSFGANVVIAGNPARVIK 181
Cdd:cd03358   79 NATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 74-181 8.38e-20

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 82.23  E-value: 8.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  74 IKVGNNFYTNyDCVILDCAEVI-IGDDCLIGPQVGLYTACH------------PLDPVERASGkefAKPITIGNNCWIGG 140
Cdd:PRK09677  66 LFFGDNVQVN-DYVHIACIESItIGRDTLIASKVFITDHNHgsfkhsddfsspNLPPDMRTLE---SSAVVIGQRVWIGE 141

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 835335140 141 HATINPGVTLGNNVVVASGAVVTKSFGANVVIAGNPARVIK 181
Cdd:PRK09677 142 NVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIK 182
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 73-180 8.63e-20

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: 79.57  E-value: 8.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  73 NIKVGNNFYTNYDCVILDCAEVIIGDDCLIGPQVGLYTACH-------PLDpverasgkefAKPITIGNNCWIGGHATIN 145
Cdd:cd05825    3 NLTIGDNSWIGEGVWIYNLAPVTIGSDACISQGAYLCTGSHdyrspafPLI----------TAPIVIGDGAWVAAEAFVG 72

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 835335140 146 PGVTLGNNVVVASGAVVTKSFGANVVIAGNPARVI 180
Cdd:cd05825   73 PGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 71-176 1.32e-16

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: 73.67  E-value: 1.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  71 GVNIKVGNNFYTNYDCVI-LDCaevIIGDDCLIGPQVGLytachpldpveraSGKefakpITIGNNCWIGGHATINPGVT 149
Cdd:cd03360  112 NPDARIGDNVIINTGAVIgHDC---VIGDFVHIAPGVVL-------------SGG-----VTIGEGAFIGAGATIIQGVT 170

                         90       100
                 ....*....|....*....|....*..
gi 835335140 150 LGNNVVVASGAVVTKSFGANVVIAGNP 176
Cdd:cd03360  171 IGAGAIIGAGAVVTKDVPDGSVVVGNP 197
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 94-181 1.53e-16

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: 73.19  E-value: 1.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  94 VIIGDDCLIGPQVGLytachpldpveRASGKEFAK--PiTIGNNCWIGGHATINPGVTLGNNVVVASGAVVTKSFGANVV 171
Cdd:COG1045   92 AVIGDNVTIYQGVTL-----------GGTGKEKGKrhP-TIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGST 159

                         90
                 ....*....|
gi 835335140 172 IAGNPARVIK 181
Cdd:COG1045  160 VVGVPARIVK 169
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 74-163 1.43e-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: 68.04  E-value: 1.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  74 IKVGNNFYTNYDCVILDCaeVIIGDDCLIGPQVGLYTACHPldpverasgkEFAKPITIGNNCWIGGHATINPGVTLGNN 153
Cdd:cd00208    1 VFIGEGVKIHPKAVIRGP--VVIGDNVNIGPGAVIGAATGP----------NEKNPTIIGDNVEIGANAVIHGGVKIGDN 68

                         90
                 ....*....|
gi 835335140 154 VVVASGAVVT 163
Cdd:cd00208   69 AVIGAGAVVT 78
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 67-183 1.61e-15

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: 69.75  E-value: 1.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  67 RCDYGVnIKVGNNfyTNY-DCVILDCAE---VIIGDDCLIGPQVGLYtAChpldpverasgkefakpiTIGNNCWIGGHA 142
Cdd:cd04645   33 RGDVNP-IRIGER--TNIqDGSVLHVDPgypTIIGDNVTVGHGAVLH-GC------------------TIGDNCLIGMGA 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 835335140 143 TINPGVTLGNNVVVASGAVVT--KSFGANVVIAGNPARVIKSL 183
Cdd:cd04645   91 IILDGAVIGKGSIVAAGSLVPpgKVIPPGSLVAGSPAKVVREL 133
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 71-177 3.40e-15

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: 70.21  E-value: 3.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140   71 GVNIKVGNNFYTNYDCVIlDCaEVIIGDDCLIGPQVGLytachpldpveraSGKefakpITIGNNCWIGGHATINPGVTL 150
Cdd:TIGR03570 115 NPDVRIGDNVIINTGAIV-EH-DCVIGDFVHIAPGVTL-------------SGG-----VVIGEGVFIGAGATIIQGVTI 174

                          90       100
                  ....*....|....*....|....*..
gi 835335140  151 GNNVVVASGAVVTKSFGANVVIAGNPA 177
Cdd:TIGR03570 175 GAGAIVGAGAVVTKDIPDGGVVVGVPA 201
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 92-176 1.11e-14

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: 66.31  E-value: 1.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  92 AEVIIGDDCLIGPQVGLytachpldpvERASGKEFAKPITIGNNCWIGGHATINPGVTLGNNVVVASGAVVTKSFGANVV 171
Cdd:cd03354   27 ETAVIGDNCTIYQGVTL----------GGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVKIGANAVVTKDVPANST 96


                 ....*
gi 835335140 172 IAGNP 176
Cdd:cd03354   97 VVGVP 101
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 74-184 1.66e-14

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 67.74  E-value: 1.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  74 IKVGNNfyTN-YDCVILDCAE---VIIGDDCLIGPQVGLYtAChpldpverasgkefakpiTIGNNCWIGGHATINPGVT 149
Cdd:COG0663   50 IRIGEG--SNiQDGVVLHVDPgypLTIGDDVTIGHGAILH-GC------------------TIGDNVLIGMGAIVLDGAV 108

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 835335140 150 LGNNVVVASGAVVT--KSFGANVVIAGNPARVIKSLE 184
Cdd:COG0663  109 IGDGSIVGAGALVTegKVVPPGSLVVGSPAKVVRELT 145
Mac pfam12464
Maltose acetyltransferase; This domain family is found in bacteria, archaea and eukaryotes, ...
 6-57 3.94e-14

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: 63.28  E-value: 3.94e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 835335140    6 KMVTGEIYDPADTELKAMRASTREKLDRFNRSQSDEQALQERIITELFGAAG 57
Cdd:pfam12464   1 KMLAGELYDASDPELVAERLRARRLLRRYNNTPPEDAEEREELLKELFGSVG 52
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 94-178 1.30e-13

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 65.89  E-value: 1.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  94 VIIGDDCLIGPQVGLytachpldpverasgkefAKPITIGNNCWIGGHATINPGVTLGNNVVVASGAVVTKSFGANVVIA 173
Cdd:cd03352  133 VRIGENCLIAAQVGI------------------AGSTTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVS 194


                 ....*
gi 835335140 174 GNPAR 178
Cdd:cd03352  195 GTPAQ 199
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 94-178 6.95e-09

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 53.87  E-value: 6.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  94 VIIGDDCLIGPQVGLytachpldpveraSGKefakpITIGNNCWIGGHATINPGVTLGNNVVVASGAVVTKSFGANVVIA 173
Cdd:COG1044  241 VRIGEHTAIAAQVGI-------------AGS-----TKIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYS 302


                 ....*
gi 835335140 174 GNPAR 178
Cdd:COG1044  303 GSPAQ 307
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 75-162 1.33e-08

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 53.22  E-value: 1.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  75 KVGNNFYTNYDCVIldCAEVIIGDDCLIGPQVGLYTAChpldpverasgkefakpiTIGNNCWIGGHATINPGVTLGNNV 154
Cdd:PRK00892 114 KIGEGVSIGPNAVI--GAGVVIGDGVVIGAGAVIGDGV------------------KIGADCRLHANVTIYHAVRIGNRV 173


                 ....*...
gi 835335140 155 VVASGAVV 162
Cdd:PRK00892 174 IIHSGAVI 181
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 86-162 1.42e-08

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 53.10  E-value: 1.42e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 835335140  86 CVIldCAEVIIGDDCLIGPQVGLYTAChpldpverasgkefakpiTIGNNCWIGGHATINPGVTLGNNVVVASGAVV 162
Cdd:COG1044  121 AVI--GAGVVIGDGVVIGPGVVIGDGV------------------VIGDDCVLHPNVTIYERCVIGDRVIIHSGAVI 177
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 75-162 1.65e-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: 52.03  E-value: 1.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  75 KVGNNFYTNYDCVIldCAEVIIGDDCLIGPQVGLYTAChpldpverasgkefakpiTIGNNCWIGGHATINPGVTLGNNV 154
Cdd:cd03352    3 KIGENVSIGPNAVI--GEGVVIGDGVVIGPGVVIGDGV------------------VIGDDCVIHPNVTIYEGCIIGDRV 62


                 ....*...
gi 835335140 155 VVASGAVV 162
Cdd:cd03352   63 IIHSGAVI 70
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 94-181 3.67e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 48.98  E-value: 3.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  94 VIIGDDCLIGPQVGLytachpldpverasgkefAKPITIGNNCWIGGHATINPGVTLGNNVVVASGAVVTKSF-GANVVI 172
Cdd:PRK00892 244 VVIGRHTAIAAQVGI------------------AGSTKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIpEPGEYS 305


                 ....*....
gi 835335140 173 AGNPARVIK 181
Cdd:PRK00892 306 SGIPAQPNK 314
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 131-172 2.06e-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: 46.55  E-value: 2.06e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 835335140 131 TIGNNCWIGGHATINPGVTLGNNVVVASGAVVtksfGANVVI 172
Cdd:COG1044  110 KIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVI----GDGVVI 147
PLN02739 PLN02739
serine acetyltransferase
 43-184 3.52e-06

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 46.18  E-value: 3.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  43 ALQERIiTELFGaagsnISVNRHFRCDYGVNIKVGNNfytnydcvildcaeVIIGDDCLIGPQVGLYTAChPLDPVERAS 122
Cdd:PLN02739 195 ALQSRV-SEVFG-----IDIHPAARIGKGILLDHGTG--------------VVIGETAVIGDRVSILHGV-TLGGTGKET 253

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 835335140 123 GKEFAKpitIGNNCWIGGHATINPGVTLGNNVVVASGAVVTKSFGANVVIAGNPARVIKSLE 184
Cdd:PLN02739 254 GDRHPK---IGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFVD 312
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
94-162 7.12e-06

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 44.70  E-value: 7.12e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 835335140  94 VIIGDDCLIGPQVglytachpldpverasgkefakpiTIGNNCWIGGHATINPGVTLGNNVVVASGAVV 162
Cdd:PRK05289  21 VEIGPFCVIGPNV------------------------VIGDGTVIGSHVVIDGHTTIGKNNRIFPFASI 65
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 131-184 1.02e-05

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: 43.51  E-value: 1.02e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 835335140 131 TIGNNCWIGGHATINPGVTLGNNVVVASGAVVTKS--FGANVVIAGNPARVIKSLE 184
Cdd:cd04745   80 TIGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAGtvIPPRSLIAGSPAKVIRELS 135
PLN02694 PLN02694
serine O-acetyltransferase
 87-184 2.26e-05

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 43.48  E-value: 2.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  87 VILDCAE-VIIGDDCLIGPQVGLYTAChPLDPVERASGKEFAKpitIGNNCWIGGHATINPGVTLGNNVVVASGAVVTKS 165
Cdd:PLN02694 173 ILFDHATgVVIGETAVIGNNVSILHHV-TLGGTGKACGDRHPK---IGDGVLIGAGATILGNVKIGEGAKIGAGSVVLID 248

                         90
                 ....*....|....*....
gi 835335140 166 FGANVVIAGNPARVIKSLE 184
Cdd:PLN02694 249 VPPRTTAVGNPARLVGGKE 267
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
129-158 3.12e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 39.24  E-value: 3.12e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 835335140  129 PITIGNNCWIGGHATINPGVTLGNNVVVAS 158
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 10-50 3.79e-05

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.28  E-value: 3.79e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 835335140  10 GEIYDPADTELKAMR-------ASTREKLDRFNRSQSDEQALQERIIT 50
Cdd:PRK00409 143 GEVKDSASEKLRGIRrqlrrkkSRIREKLESIIRSKSLQKYLQDTIIT 190
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
130-164 4.08e-05

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 38.96  E-value: 4.08e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 835335140  130 ITIGNNCWIGGHATInpGVTLGNNVVVASGAVVTK 164
Cdd:pfam14602   1 VIIGDNCLIGANSGI--GVSLGDNCVVGAGVVITA 33
PRK10191 PRK10191
putative acyl transferase; Provisional
 68-179 4.54e-05

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 41.41  E-value: 4.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  68 CDYGVNIK----VGNNFYTNYDCVILDCAEVIIGDDCLI--GPQVGLYTACHPLDPVerasgkefakpitIGNNCWIGGH 141
Cdd:PRK10191  38 CFFGYEIQaaatIGRRFTIHHGYAVVINKNVVAGDDFTIrhGVTIGNRGADNMACPH-------------IGNGVELGAN 104

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 835335140 142 ATINPGVTLGNNVVVASGAVVTKSFGANVVIAGNPARV 179
Cdd:PRK10191 105 VIILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKARV 142
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 73-183 4.55e-05

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: 41.82  E-value: 4.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  73 NIKVGNNFYTNYDCVIL-DCAEVIIGDDCLIGPQVGLytacHPldPVERASGKEFAKPITIGNNCWI------------- 138
Cdd:cd03359   21 NIVLNGKTIIQSDVIIRgDLATVSIGRYCILSEGCVI----RP--PFKKFSKGVAFFPLHIGDYVFIgencvvnaaqigs 94

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 835335140 139 ----GGHATINPGVTLGNNVVVASGAVV---TKsFGANVVIAGNPARVIKSL 183
Cdd:cd03359   95 yvhiGKNCVIGRRCIIKDCVKILDGTVVppdTV-IPPYSVVSGRPARFIGEL 145
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 94-162 4.90e-05

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


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 42.42  E-value: 4.90e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 835335140  94 VIIGDDCLIGPQVglytachpldpverasgkefakpiTIGNNCWIGGHATINPGVTLGNNVVVASGAVV 162
Cdd:cd03351   18 VEIGPFCVIGPNV------------------------EIGDGTVIGSHVVIDGPTTIGKNNRIFPFASI 62
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 94-162 5.70e-05

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 42.31  E-value: 5.70e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 835335140  94 VIIGDDCLIGPQVglytachpldpverasgkefakpiTIGNNCWIGGHATINPGVTLGNNVVVASGAVV 162
Cdd:COG1043   20 VEIGPFCVIGPDV------------------------EIGDGTVIGSHVVIEGPTTIGKNNRIFPFASI 64
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 130-175 7.20e-05

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: 41.70  E-value: 7.20e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 835335140 130 ITIGNNCWIGGHATINPGVTLGNNVVVASGAVV---TK-----SFGANVVIAGN 175
Cdd:cd03360   97 AVIGEGCVIMAGAVINPDARIGDNVIINTGAVIghdCVigdfvHIAPGVVLSGG 150
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 127-162 8.36e-05

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 41.93  E-value: 8.36e-05
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 835335140 127 AKPITIGNNCWIGGHATINPGVTLGNNVVVASGAVV 162
Cdd:PRK12461  27 GANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVV 62
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 94-180 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: 41.16  E-value: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  94 VIIGDDCLIGPQVglytachpldpV--ERAsgkefakpiTIGNNCWIGGHATINPGVTLGNNVVVASGAVVtksfGANVV 171
Cdd:COG1044  109 AKIGEGVSIGPFA-----------VigAGV---------VIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTI----YERCV 164


                 ....*....
gi 835335140 172 IaGNpaRVI 180
Cdd:COG1044  165 I-GD--RVI 170
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 75-177 3.21e-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: 40.50  E-value: 3.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140   75 KVGNNFYTN-YDCVILDCAEviIGDDCLIGPQVGLytACHPL-DPVERASGkefakpITIGNNCWIGGHATINPGVTLGN 152
Cdd:TIGR02353 599 KIGRGVYIDgTDLTERDLVT--IGDDSTLNEGSVI--QTHLFeDRVMKSDT------VTIGDGATLGPGAIVLYGVVMGE 668

                          90       100
                  ....*....|....*....|....*..
gi 835335140  153 NVVVASGAVVTK--SFGANVVIAGNPA 177
Cdd:TIGR02353 669 GSVLGPDSLVMKgeEVPAHTRWRGNPA 695
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 132-183 4.90e-04

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: 38.71  E-value: 4.90e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 835335140 132 IGNNCWIGGHATINPGVTLGNNVVVASGAVVT--KSFGANVVIAGNPARVIKSL 183
Cdd:cd04650   81 VGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTpgKEIPDYSLVLGVPAKVVRKL 134
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 91-165 5.90e-04

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: 38.52  E-value: 5.90e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 835335140  91 CAEviIGDDCLIGPQVGLYTAchpLDPVErasgkefAKPITIGNNCWIGGHATINPGVTLGNNVVVASGAVVTKS 165
Cdd:cd03350   49 CAQ--IGKNVHLSAGAVIGGV---LEPLQ-------ATPVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTQS 111
MutS2 COG1193
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
10-51 6.77e-04

dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];


Pssm-ID: 440806 [Multi-domain]  Cd Length: 784  Bit Score: 39.35  E-value: 6.77e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 835335140  10 GEIYDPADTELKAMR-------ASTREKLDRFNRSQSDEQALQERIITE 51
Cdd:COG1193  141 GEVKDSASPELRRIRreirsleQRIREKLESILRSASYQKYLQDAIITI 189
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 73-153 8.89e-04

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 38.85  E-value: 8.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  73 NIKVGNNFYTNYDCVILDCaevIIGDDCLIGPqvglYTAchpldpVERAsgkefakpiTIGNNCWIGGHATINPGVTLGN 152
Cdd:PRK09451 283 NVTLGNRVKIGAGCVLKNC---VIGDDCEISP----YSV------VEDA---------NLGAACTIGPFARLRPGAELAE 340


                 .
gi 835335140 153 N 153
Cdd:PRK09451 341 G 341
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 86-151 4.34e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 36.66  E-value: 4.34e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 835335140  86 CVILDcaEVIIGDDCLIGPQVGLYTACHpldpverasgkefakpitIGNNCwigghaTINPGVTLG 151
Cdd:PRK00892 143 AVIGD--GVKIGADCRLHANVTIYHAVR------------------IGNRV------IIHSGAVIG 182
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 90-179 4.84e-03

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: 36.64  E-value: 4.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  90 DCaevIIGDDCLIGPQVGLytACHpldpverasgkefakpITIGNNCWIGGHATINPGVTLGNNVVVASGAVVTKSFGAN 169
Cdd:cd03351  120 DC---VIGNNVILANNATL--AGH----------------VEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPY 178

                         90
                 ....*....|
gi 835335140 170 VVIAGNPARV 179
Cdd:cd03351  179 VIAAGNRARL 188
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 92-172 6.70e-03

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 36.54  E-value: 6.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 835335140  92 AEVIIGDDCLIGPQVGLYtachpldpverasGKefakpITIGNNCWIGGHATINpGVTLGNNVVV----ASGAVVtksfG 167
Cdd:COG1207  265 GDVEIGRDVVIDPNVILE-------------GK-----TVIGEGVVIGPNCTLK-DSTIGDGVVIkysvIEDAVV----G 321


                 ....*
gi 835335140 168 ANVVI 172
Cdd:COG1207  322 AGATV 326
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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