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Conserved domains on  [gi|1650123362|gb|QCQ31468|]
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sugar O-acetyltransferase [Bacteroides fragilis]

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 ...
 13-192 8.29e-98

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: 280.85  E-value: 8.29e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  13 WYDCHNQVFLDLKPRTHKLLMKYNSLPYENKEEKNSLLKKMLGSIGMKVSVASPFICDYGCNIHIGDNVTVNTGCTFVDC 92
Cdd:cd03357     1 LYNASDPELVAERARARRLLHEYNQTPPSDAEERRELLKELFGSVGENVYIEPPFHCDYGYNIHIGDNFYANFNCTILDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  93 NKITIGSNVLIAPNVQLYTATHPIDLDERLAPVEtedgikrvrrtYALPITIEDGCWIGGGVIILPGITIGYGSVIGAGS 172
Cdd:cd03357    81 APVTIGDNVLIGPNVQIYTAGHPLDPEERNRGLE-----------YAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGS 149

                         170       180
                  ....*....|....*....|
gi 1650123362 173 VVTKDIPANSLAIGNPCKVI 192
Cdd:cd03357   150 VVTKDIPANVVAAGNPARVI 169
 
Name Accession Description Interval E-value
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 13-192 8.29e-98

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: 280.85  E-value: 8.29e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  13 WYDCHNQVFLDLKPRTHKLLMKYNSLPYENKEEKNSLLKKMLGSIGMKVSVASPFICDYGCNIHIGDNVTVNTGCTFVDC 92
Cdd:cd03357     1 LYNASDPELVAERARARRLLHEYNQTPPSDAEERRELLKELFGSVGENVYIEPPFHCDYGYNIHIGDNFYANFNCTILDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  93 NKITIGSNVLIAPNVQLYTATHPIDLDERLAPVEtedgikrvrrtYALPITIEDGCWIGGGVIILPGITIGYGSVIGAGS 172
Cdd:cd03357    81 APVTIGDNVLIGPNVQIYTAGHPLDPEERNRGLE-----------YAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGS 149

                         170       180
                  ....*....|....*....|
gi 1650123362 173 VVTKDIPANSLAIGNPCKVI 192
Cdd:cd03357   150 VVTKDIPANVVAAGNPARVI 169
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
48-196 1.08e-55

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 173.13  E-value: 1.08e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  48 SLLKKMLGSIGMKVSVASPFICdYGCNIHIGDNVTVNTGCTFVDCNKITIGSNVLIAPNVQLYTATHPIDLDERlapvet 127
Cdd:COG0110     2 KLLLLFGARIGDGVVIGPGVRI-YGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPAT------ 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1650123362 128 edgikrvRRTYALPITIEDGCWIGGGVIILPGITIGYGSVIGAGSVVTKDIPANSLAIGNPCKVIRQIN 196
Cdd:COG0110    75 -------FPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRD 136
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 27-200 2.57e-49

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 159.01  E-value: 2.57e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  27 RTHKLLMKYNSLPYENKEEKNSLLKKMLGSIGMKVSVASPFICDYGCNIHIGDNVTVNTGCTFVDCNKITIGSNVLIAPN 106
Cdd:PRK09527   28 RGKTLMYEFNHSHPSEVEKRESLIKEMFATVGENAWVEPPVYFSYGSNIHIGRNFYANFNLTIVDDYTVTIGDNVLIAPN 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362 107 VQLYTATHPIDLDERLapveteDGikrvrRTYALPITIEDGCWIGGGVIILPGITIGYGSVIGAGSVVTKDIPANSLAIG 186
Cdd:PRK09527  108 VTLSVTGHPVHHELRK------NG-----EMYSFPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAG 176

                         170
                  ....*....|....
gi 1650123362 187 NPCKVIRQINQTKK 200
Cdd:PRK09527  177 VPCRVIREINDRDK 190
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 67-188 2.98e-23

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: 91.79  E-value: 2.98e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  67 FICDY---GCNIHIGDNVTVNTGCTFV-DCnkiTIGSNVLIAPNVQLYTATHpidlderlapvetedgikrvrrtyalpi 142
Cdd:TIGR03570 107 VIMAGaviNPDVRIGDNVIINTGAIVEhDC---VIGDFVHIAPGVTLSGGVV---------------------------- 155

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1650123362 143 tIEDGCWIGGGVIILPGITIGYGSVIGAGSVVTKDIPANSLAIGNP 188
Cdd:TIGR03570 156 -IGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVP 200
Mac pfam12464
Maltose acetyltransferase; This domain family is found in bacteria, archaea and eukaryotes, ...
 7-58 1.38e-13

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: 62.51  E-value: 1.38e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1650123362   7 KCLAGEWYDCHNQVFLDLKPRTHKLLMKYNSLPYENKEEKNSLLKKMLGSIG 58
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 ...
 13-192 8.29e-98

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: 280.85  E-value: 8.29e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  13 WYDCHNQVFLDLKPRTHKLLMKYNSLPYENKEEKNSLLKKMLGSIGMKVSVASPFICDYGCNIHIGDNVTVNTGCTFVDC 92
Cdd:cd03357     1 LYNASDPELVAERARARRLLHEYNQTPPSDAEERRELLKELFGSVGENVYIEPPFHCDYGYNIHIGDNFYANFNCTILDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  93 NKITIGSNVLIAPNVQLYTATHPIDLDERLAPVEtedgikrvrrtYALPITIEDGCWIGGGVIILPGITIGYGSVIGAGS 172
Cdd:cd03357    81 APVTIGDNVLIGPNVQIYTAGHPLDPEERNRGLE-----------YAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGS 149

                         170       180
                  ....*....|....*....|
gi 1650123362 173 VVTKDIPANSLAIGNPCKVI 192
Cdd:cd03357   150 VVTKDIPANVVAAGNPARVI 169
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
48-196 1.08e-55

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 173.13  E-value: 1.08e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  48 SLLKKMLGSIGMKVSVASPFICdYGCNIHIGDNVTVNTGCTFVDCNKITIGSNVLIAPNVQLYTATHPIDLDERlapvet 127
Cdd:COG0110     2 KLLLLFGARIGDGVVIGPGVRI-YGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPAT------ 74

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1650123362 128 edgikrvRRTYALPITIEDGCWIGGGVIILPGITIGYGSVIGAGSVVTKDIPANSLAIGNPCKVIRQIN 196
Cdd:COG0110    75 -------FPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRD 136
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 27-200 2.57e-49

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 159.01  E-value: 2.57e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  27 RTHKLLMKYNSLPYENKEEKNSLLKKMLGSIGMKVSVASPFICDYGCNIHIGDNVTVNTGCTFVDCNKITIGSNVLIAPN 106
Cdd:PRK09527   28 RGKTLMYEFNHSHPSEVEKRESLIKEMFATVGENAWVEPPVYFSYGSNIHIGRNFYANFNLTIVDDYTVTIGDNVLIAPN 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362 107 VQLYTATHPIDLDERLapveteDGikrvrRTYALPITIEDGCWIGGGVIILPGITIGYGSVIGAGSVVTKDIPANSLAIG 186
Cdd:PRK09527  108 VTLSVTGHPVHHELRK------NG-----EMYSFPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAG 176

                         170
                  ....*....|....
gi 1650123362 187 NPCKVIRQINQTKK 200
Cdd:PRK09527  177 VPCRVIREINDRDK 190
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 74-192 5.05e-49

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: 154.92  E-value: 5.05e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  74 NIHIGDNVTVNTGCTFVDCNKITIGSNVLIAPNVQLYTATHPIDLDERLAPVETEDGikrvrrtyalPITIEDGCWIGGG 153
Cdd:cd04647     1 NISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDHNHDIDDPERPIEQGVTSA----------PIVIGDDVWIGAN 70

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1650123362 154 VIILPGITIGYGSVIGAGSVVTKDIPANSLAIGNPCKVI 192
Cdd:cd04647    71 VVILPGVTIGDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 1-195 2.21e-48

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 156.13  E-value: 2.21e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362   1 MKTEMEKCLAGEWYDCHNQVFLDLKPRTHKLLMKYNSLPYENKEEKNSLLKKMLGSIGmKVSVASPFICDYGCNIHIGDN 80
Cdd:PRK10092    1 MSTEKEKMIAGELYRSADETLSRDRLRARQLIHRYNHSLPDEHTLRQQILADLFGQVT-EAYIEPTFRCDYGYNIFLGNN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  81 VTVNTGCTFVDCNKITIGSNVLIAPNVQLYTATHPIDLDERLAPVEtedgikrvrrtYALPITIEDGCWIGGGVIILPGI 160
Cdd:PRK10092   80 FYANFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPLDPVARNSGAE-----------LGKPVTIGNNVWIGGRAVINPGV 148

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1650123362 161 TIGYGSVIGAGSVVTKDIPANSLAIGNPCKVIRQI 195
Cdd:PRK10092  149 TIGDNVVVASGAVVTKDVPDNVVVGGNPARIIKKL 183
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 74-194 1.07e-28

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: 104.55  E-value: 1.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  74 NIHIGDNVTVNTGCTFVDCNKITIGSNVLIAPNVQLYT-ATHPID---------LDERLAPVETEDGIKRVRrtyalPIT 143
Cdd:cd03349     1 NISVGDYSYGSGPDCDVGGDKLSIGKFCSIAPGVKIGLgGNHPTDwvstypfyiFGGEWEDDAKFDDWPSKG-----DVI 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1650123362 144 IEDGCWIGGGVIILPGITIGYGSVIGAGSVVTKDIPANSLAIGNPCKVIRQ 194
Cdd:cd03349    76 IGNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRY 126
PRK10502 PRK10502
putative acyl transferase; Provisional
 74-194 1.45e-27

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 102.72  E-value: 1.45e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  74 NIHIGDNVTVNTGCTFVDCNKITIGSNVLIAPNVQLYTATHPIDlderlapvetedgikrvRRTYAL---PITIEDGCWI 150
Cdd:PRK10502   71 KLTIGDYAWIGDDVWLYNLGEITIGAHCVISQKSYLCTGSHDYS-----------------DPHFDLntaPIVIGEGCWL 133

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1650123362 151 GGGVIILPGITIGYGSVIGAGSVVTKDIPANSLAIGNPCKVIRQ 194
Cdd:PRK10502  134 AADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIRP 177
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 74-192 2.16e-27

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: 99.99  E-value: 2.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  74 NIHIGDNVTVNTGCTFVDCNKITIGSNVLIAPNVQLYTATHPIDLDERlapvetedgikrvrRTYALPITIEDGCWIGGG 153
Cdd:cd05825     3 NLTIGDNSWIGEGVWIYNLAPVTIGSDACISQGAYLCTGSHDYRSPAF--------------PLITAPIVIGDGAWVAAE 68

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1650123362 154 VIILPGITIGYGSVIGAGSVVTKDIPANSLAIGNPCKVI 192
Cdd:cd05825    69 AFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 57-193 1.94e-25

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: 95.26  E-value: 1.94e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  57 IGMKVSVASPFICDYGCNIhiGDNVTVNTGCtFVdCNKITIGSNVLIAPNVQLYTATHPIDLDERLAPVetedgikrvrr 136
Cdd:cd03358     1 IGDNCIIGTNVFIENDVKI--GDNVKIQSNV-SI-YEGVTIEDDVFIGPNVVFTNDLYPRSKIYRKWEL----------- 65

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1650123362 137 tyaLPITIEDGCWIGGGVIILPGITIGYGSVIGAGSVVTKDIPANSLAIGNPCKVIR 193
Cdd:cd03358    66 ---KGTTVKRGASIGANATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 72-188 1.79e-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: 92.16  E-value: 1.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  72 GCNIHIGDNVTVNTGCTfV--DCnkiTIGSNVLIAPNVQLytATHpidlderlapvetedgikrvrrtyalpITIEDGCW 149
Cdd:cd03360   112 NPDARIGDNVIINTGAV-IghDC---VIGDFVHIAPGVVL--SGG---------------------------VTIGEGAF 158

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1650123362 150 IGGGVIILPGITIGYGSVIGAGSVVTKDIPANSLAIGNP 188
Cdd:cd03360   159 IGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 67-188 2.98e-23

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: 91.79  E-value: 2.98e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  67 FICDY---GCNIHIGDNVTVNTGCTFV-DCnkiTIGSNVLIAPNVQLYTATHpidlderlapvetedgikrvrrtyalpi 142
Cdd:TIGR03570 107 VIMAGaviNPDVRIGDNVIINTGAIVEhDC---VIGDFVHIAPGVTLSGGVV---------------------------- 155

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1650123362 143 tIEDGCWIGGGVIILPGITIGYGSVIGAGSVVTKDIPANSLAIGNP 188
Cdd:TIGR03570 156 -IGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVP 200
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 75-201 6.83e-22

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 88.01  E-value: 6.83e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  75 IHIGDNVTVNTGCTFVDCNKITIGSNVLIAPNVQLYTATHPiDLDErlAPVETEDGIKRVRRTY-ALPITIEDGCWIGGG 153
Cdd:PRK09677   66 LFFGDNVQVNDYVHIACIESITIGRDTLIASKVFITDHNHG-SFKH--SDDFSSPNLPPDMRTLeSSAVVIGQRVWIGEN 142

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1650123362 154 VIILPGITIGYGSVIGAGSVVTKDIPANSLAIGNPCKVIRQINQTKKL 201
Cdd:PRK09677  143 VTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKKYNHETKL 190
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 143-194 6.92e-19

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: 79.74  E-value: 6.92e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1650123362 143 TIEDGCWIGGGVIILPGITIGYGSVIGAGSVVTKDIPANSLAIGNPCKVIRQ 194
Cdd:COG1045   119 TIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVKR 170
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 72-195 1.53e-18

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: 78.22  E-value: 1.53e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  72 GCNIHIGDNVTVNTGCTFvdcnKITIGSNVLIAPNVQLYTAThpidlderlapvetedgikrvrrtyalpitIEDGCWIG 151
Cdd:cd04645    42 GERTNIQDGSVLHVDPGY----PTIIGDNVTVGHGAVLHGCT------------------------------IGDNCLIG 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1650123362 152 GGVIILPGITIGYGSVIGAGSVVT--KDIPANSLAIGNPCKVIRQI 195
Cdd:cd04645    88 MGAIILDGAVIGKGSIVAAGSLVPpgKVIPPGSLVAGSPAKVVREL 133
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 75-197 2.48e-16

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 72.75  E-value: 2.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  75 IHIGDNVTVNTGCTF-VDCNK-ITIGSNVLIAPNVQLYTAThpidlderlapvetedgikrvrrtyalpitIEDGCWIGG 152
Cdd:COG0663    50 IRIGEGSNIQDGVVLhVDPGYpLTIGDDVTIGHGAILHGCT------------------------------IGDNVLIGM 99

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1650123362 153 GVIILPGITIGYGSVIGAGSVVT--KDIPANSLAIGNPCKVIRQINQ 197
Cdd:COG0663   100 GAIVLDGAVIGDGSIVGAGALVTegKVVPPGSLVVGSPAKVVRELTE 146
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 67-188 4.79e-16

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: 70.16  E-value: 4.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  67 FICDYGCNIHIGDNVTvntgctfvdcnkitIGSNVLIAPNVQLytathpidlderlapvetedGIKRVRRTYALPiTIED 146
Cdd:cd03354    15 LFIDHGTGIVIGETAV--------------IGDNCTIYQGVTL--------------------GGKGKGGGKRHP-TIGD 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1650123362 147 GCWIGGGVIILPGITIGYGSVIGAGSVVTKDIPANSLAIGNP 188
Cdd:cd03354    60 NVVIGAGAKILGNITIGDNVKIGANAVVTKDVPANSTVVGVP 101
Mac pfam12464
Maltose acetyltransferase; This domain family is found in bacteria, archaea and eukaryotes, ...
 7-58 1.38e-13

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: 62.51  E-value: 1.38e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1650123362   7 KCLAGEWYDCHNQVFLDLKPRTHKLLMKYNSLPYENKEEKNSLLKKMLGSIG 58
Cdd:pfam12464   1 KMLAGELYDASDPELVAERLRARRLLRRYNNTPPEDAEEREELLKELFGSVG 52
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 75-175 2.88e-12

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 59.57  E-value: 2.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  75 IHIGDNVTVNTGCTFVDCnkITIGSNVLIAPNVQLYTATHPidlderlapvetedgikrvrrTYALPITIEDGCWIGGGV 154
Cdd:cd00208     1 VFIGEGVKIHPKAVIRGP--VVIGDNVNIGPGAVIGAATGP---------------------NEKNPTIIGDNVEIGANA 57

                          90       100
                  ....*....|....*....|.
gi 1650123362 155 IILPGITIGYGSVIGAGSVVT 175
Cdd:cd00208    58 VIHGGVKIGDNAVIGAGAVVT 78
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 143-194 3.58e-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: 59.73  E-value: 3.58e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1650123362 143 TIEDGCWIGGGVIILPGITIGYGSVIGAGSVVTKDIPANSLAIGNPCKVIRQ 194
Cdd:cd03352   152 TIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQPHRE 203
PLN02357 PLN02357
serine acetyltransferase
 144-192 6.66e-11

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 60.28  E-value: 6.66e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1650123362 144 IEDGCWIGGGVIILPGITIGYGSVIGAGSVVTKDIPANSLAIGNPCKVI 192
Cdd:PLN02357  281 IGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLI 329
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 74-186 1.15e-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: 58.20  E-value: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  74 NIHIGDNVTVNTGCTFVDCnkiTIGSNVLIAPNVQLYTAThpIDLDERLAP-------------------VET-----ED 129
Cdd:cd03353    33 KTVIGEDCVIGPNCVIKDS---TIGDGVVIKASSVIEGAV--IGNGATVGPfahlrpgtvlgegvhignfVEIkkstiGE 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362 130 GIKRVRRTY-------------ALPIT------------IEDGCWIGGGVIILPGITIGYGSVIGAGSVVTKDIPANSLA 184
Cdd:cd03353   108 GSKANHLSYlgdaeigegvnigAGTITcnydgvnkhrtvIGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGALA 187


                  ..
gi 1650123362 185 IG 186
Cdd:cd03353   188 IA 189
PLN02694 PLN02694
serine O-acetyltransferase
 144-192 1.68e-10

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 58.89  E-value: 1.68e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1650123362 144 IEDGCWIGGGVIILPGITIGYGSVIGAGSVVTKDIPANSLAIGNPCKVI 192
Cdd:PLN02694  215 IGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLV 263
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 143-196 2.83e-10

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: 58.50  E-value: 2.83e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1650123362 143 TIEDGCWIG-GGVIILPgITIGYGSVIGAGSVVTKDIPANSLAIGnpckVIRQIN 196
Cdd:COG1207   396 VIGDGAFIGsNTNLVAP-VTIGDGATIGAGSTITKDVPAGALAIA----RARQRN 445
PLN02739 PLN02739
serine acetyltransferase
 144-197 6.15e-10

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 57.35  E-value: 6.15e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1650123362 144 IEDGCWIGGGVIILPGITIGYGSVIGAGSVVTKDIPANSLAIGNPCKVIRQINQ 197
Cdd:PLN02739  260 IGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFVDE 313
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 77-196 4.17e-09

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: 54.64  E-value: 4.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  77 IGDN------VTVNTG-------------CTFV-------DCnkiTIGSNVLIAPNVQLytATHpidlderlapvetedg 130
Cdd:COG1043    82 IGDNntirefVTIHRGtvqgggvtrigddNLLMayvhvahDC---VVGNNVILANNATL--AGH---------------- 140

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1650123362 131 ikrvrrtyalpITIEDGCWIGGGVIILPGITIGYGSVIGAGSVVTKDIPANSLAIGNPCKViRQIN 196
Cdd:COG1043   141 -----------VEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDVPPYVLAAGNPARL-RGLN 194
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 144-200 8.19e-09

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 54.34  E-value: 8.19e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1650123362 144 IEDGCWIGGGVIILPGITIGYGSVIGAGSVVTKDIPANSLAIGNpckvIRQINQTKK 200
Cdd:PRK14356  401 IGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSLAIAR----GRQKNLPRK 453
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 52-188 8.63e-09

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: 54.37  E-value: 8.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  52 KMLGS-IGMKVSVASPFICDYGCnIHIGDNVTVNTGCTfvdcnkitigsnvliapnVQlytaTHPIdlderlapvetEDG 130
Cdd:TIGR02353 594 RLLGVkIGRGVYIDGTDLTERDL-VTIGDDSTLNEGSV------------------IQ----THLF-----------EDR 639

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362 131 IKRVRRtyalpITIEDGCWIGGGVIILPGITIGYGSVIGAGSVVTK--DIPANSLAIGNP 188
Cdd:TIGR02353 640 VMKSDT-----VTIGDGATLGPGAIVLYGVVMGEGSVLGPDSLVMKgeEVPAHTRWRGNP 694
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 141-197 1.09e-08

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 54.00  E-value: 1.09e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1650123362 141 PITIEDGCWIGGGVIILPGITIGYGSVIGAGSVVTKDIPANSLAIGNPckviRQINQ 197
Cdd:PRK14357  383 PTFIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRA----RQIVK 435
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 150-197 1.15e-08

Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in iron acquisition. It binds iron when it is complexed with pyochelin. It adopts the left-handed parallel beta-helix (LbH) structure, and contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Acyltransferase activity has not been observed in this group.


Pssm-ID: 100055 [Multi-domain]  Cd Length: 154  Bit Score: 52.19  E-value: 1.15e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1650123362 150 IGGGVIILPGITIGYGSVIGAGSVVT--KDIPANSLAIGNPCKVIRQINQ 197
Cdd:cd04650    87 VGMGAILLNGAKIGDHVIIGAGAVVTpgKEIPDYSLVLGVPAKVVRKLTE 136
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 129-185 2.07e-08

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 53.21  E-value: 2.07e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1650123362 129 DGIKRvRRTyalpiTIEDGCWIGGGVIILPGITIGYGSVIGAGSVVTKDIPANSLAI 185
Cdd:PRK14355  391 DGVKK-HRT-----VIEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPPDSLAI 441
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 76-196 2.57e-08

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


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 52.43  E-value: 2.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  76 HIGDN------VTVNTG------CTFV--------------DCnkiTIGSNVLIAPNVQLytATHpidlderlapveted 129
Cdd:cd03351    79 EIGDNntirefVTIHRGtaqgggVTRIgnnnllmayvhvahDC---VIGNNVILANNATL--AGH--------------- 138

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1650123362 130 gikrvrrtyalpITIEDGCWIGGGVIILPGITIGYGSVIGAGSVVTKDIPANSLAIGNPCKvIRQIN 196
Cdd:cd03351   139 ------------VEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRAR-LRGLN 192
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 143-196 4.86e-08

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 52.17  E-value: 4.86e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1650123362 143 TIEDGCWIGGGVIILPGITIGYGSVIGAGSVVTKDIPANSLAIGNPckviRQIN 196
Cdd:PRK14353  382 EIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALGRA----RQET 431
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 74-185 1.25e-07

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 50.80  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  74 NIHIGDNVTVNTGCTFVDCnkiTIGSNVLIAPnvqlYTATHPIDLDE--------RLAP-VETEDG--------IKRVR- 135
Cdd:PRK09451  283 NVTLGNRVKIGAGCVLKNC---VIGDDCEISP----YSVVEDANLGAactigpfaRLRPgAELAEGahvgnfveMKKARl 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362 136 --------RTYALPITIEDGCWIGGGVI--------------------------ILPgITIGYGSVIGAGSVVTKDIPAN 181
Cdd:PRK09451  356 gkgskaghLTYLGDAEIGDNVNIGAGTItcnydgankfktiigddvfvgsdtqlVAP-VTVGKGATIGAGTTVTRDVAEN 434


                  ....
gi 1650123362 182 SLAI 185
Cdd:PRK09451  435 ELVI 438
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 143-196 1.27e-07

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 50.99  E-value: 1.27e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1650123362 143 TIEDGCWIGGGVIILPGITIGYGSVIGAGSVVTKDIPANSLAIGNPckviRQIN 196
Cdd:PRK14354  395 IIGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDALAIARA----RQVN 444
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 57-179 1.27e-07

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: 48.92  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  57 IGMKVSVASPFICDYGCniHIGDNVTVNTGCTFVDCnkITIGSNVLIAPNVQLYTAthpidlderLAPVEtedgikrvrr 136
Cdd:cd03350    16 IGPGAVLMMPSYVNIGA--YVDEGTMVDSWATVGSC--AQIGKNVHLSAGAVIGGV---------LEPLQ---------- 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1650123362 137 tyALPITIEDGCWIGGGVIILPGITIGYGSVIGAGSVVTKDIP 179
Cdd:cd03350    73 --ATPVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTQSTP 113
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 143-195 5.66e-07

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: 47.36  E-value: 5.66e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1650123362 143 TIEDGCWIGGGVIILPGITIGYGSVIGAGSVVTK--DIPANSLAIGNPCKVIRQI 195
Cdd:cd04745    80 TIGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAgtVIPPRSLIAGSPAKVIREL 134
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 143-188 6.42e-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: 6.42e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1650123362 143 TIEDGCWIGGGVIILPGITIGYGSVIGAGSVVTKDIPANSLAIGNP 188
Cdd:COG1044   260 KIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSGSP 305
cysE PRK11132
serine acetyltransferase; Provisional
 144-192 7.41e-07

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 48.15  E-value: 7.41e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1650123362 144 IEDGCWIGGGVIILPGITIGYGSVIGAGSVVTKDIPANSLAIGNPCKVI 192
Cdd:PRK11132  196 IREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIV 244
PLN02472 PLN02472
uncharacterized protein
 74-195 1.84e-06

uncharacterized protein


Pssm-ID: 215263 [Multi-domain]  Cd Length: 246  Bit Score: 46.88  E-value: 1.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  74 NIHIGDNVTVNTGCTFV-------DCNKITIGsnvlIAPNVQLYTATHPIDLDERLAPVETEDGIKRVRRTYAL--PITI 144
Cdd:PLN02472   71 NVVLAGQVTVWDGASVWngavlrgDLNKITVG----FCSNVQERCVLHAAWNSPTGLPAETLIDRYVTIGAYSLlrSCTI 146

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1650123362 145 EDGCWIGGGVIILPGITIGYGSVIGAGSVVT--KDIPANSLAIGNPCKVIRQI 195
Cdd:PLN02472  147 EPECIIGQHSILMEGSLVETHSILEAGSVLPpgRRIPTGELWAGNPARFVRTL 199
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 139-179 1.85e-06

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: 47.03  E-value: 1.85e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1650123362 139 ALPITIEDGCWIGGGVIILPGITIGYGSVIGAGSVVTKDIP 179
Cdd:COG2171   168 AAPVIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLTASTK 208
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 75-197 2.23e-06

acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes LpxA, an enzyme for the biosynthesis of lipid A, a component oflipopolysaccharide (LPS) in the outer membrane outer leaflet of most Gram-negative bacteria. Some differences are found between lipid A of different species, but this protein represents the first step (from UDP-N-acetyl-D-glucosamine) and appears to be conserved in function. Proteins from this family contain many copies of the bacterial transferase hexapeptide repeat (pfam00132). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 46.48  E-value: 2.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  75 IHIGDN------VTVNTG-------------CTFV-------DCnkiTIGSNVLIAPNVQLytATHpidlderlapvete 128
Cdd:TIGR01852  77 LIIGDNntirefVTINRGtasgggvtrignnNLLMayshiahDC---VVGNHVILANNATL--AGH-------------- 137

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1650123362 129 dgikrvrrtyalpITIEDGCWIGGGVIILPGITIGYGSVIGAGSVVTKDIPANSLAIGNPcKVIRQINQ 197
Cdd:TIGR01852 138 -------------VEVGDYAIIGGLVAVHQFVRIGRYAMIGGLSAVSKDVPPYCLAEGNR-ARLRGLNI 192
PLN02296 PLN02296
carbonate dehydratase
 74-195 2.38e-06

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 46.66  E-value: 2.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  74 NIHIGDNVTVNTGCTFV-DCNKITIGSNVLIAPNVQLYTATHpiDLDERLAPVETEDgikRVRRTYALPI---TIEDGCW 149
Cdd:PLN02296   70 DVQVGRGSSIWYGCVLRgDVNSISVGSGTNIQDNSLVHVAKT--NLSGKVLPTIIGD---NVTIGHSAVLhgcTVEDEAF 144

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1650123362 150 IGGGVIILPGITIGYGSVIGAGSVVTKD--IPANSLAIGNPCKVIRQI 195
Cdd:PLN02296  145 VGMGATLLDGVVVEKHAMVAAGALVRQNtrIPSGEVWAGNPAKFLRKL 192
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
77-196 3.36e-06

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 46.24  E-value: 3.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  77 IGDN------VTVNTG-------------CTFV-------DCnkiTIGSNVLIAPNVQLytATHpidlderlapvetedg 130
Cdd:PRK05289   83 IGDNntirefVTINRGtvqgggvtrigdnNLLMayvhvahDC---VVGNHVILANNATL--AGH---------------- 141

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1650123362 131 ikrvrrtyalpITIEDGCWIGGGVIILPGITIGYGSVIGAGSVVTKDIPANSLAIGNPCKvIRQIN 196
Cdd:PRK05289  142 -----------VEVGDYAIIGGLTAVHQFVRIGAHAMVGGMSGVSQDVPPYVLAEGNPAR-LRGLN 195
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 143-181 3.48e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 46.29  E-value: 3.48e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1650123362 143 TIEDGCWIGGGVIILPGITIGYGSVIGAGSVVTKDIPAN 181
Cdd:PRK00892  263 KIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEP 301
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 139-179 4.53e-06

2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 45.95  E-value: 4.53e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1650123362 139 ALPITIEDGCWIGGGVIILPGITIGYGSVIGAGSVVTKDIP 179
Cdd:PRK11830  174 ANPVIIEDNCFIGARSEVVEGVIVEEGSVLGMGVFLGQSTK 214
PRK10191 PRK10191
putative acyl transferase; Provisional
 139-191 1.17e-05

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 43.34  E-value: 1.17e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1650123362 139 ALPItIEDGCWIGGGVIILPGITIGYGSVIGAGSVVTKDIPANSLAIGNPCKV 191
Cdd:PRK10191   91 ACPH-IGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKARV 142
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 154-193 1.46e-05

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 44.53  E-value: 1.46e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1650123362 154 VIILPgITIGYGSVIGAGSVVTKDIPANSLAIGNPCKVIR 193
Cdd:PRK14360  404 VLVAP-ITLGEDVTVAAGSTITKDVPDNSLAIARSRQVIK 442
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 129-192 3.30e-05

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 43.77  E-value: 3.30e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1650123362 129 DGIKRvRRTyalpiTIEDGCWIGGGVIILPGITIGYGSVIGAGSVVTKDIPANSLAI-GNPCKVI 192
Cdd:PRK14352  393 DGVNK-HRT-----TIGSHVRTGSDTMFVAPVTVGDGAYTGAGTVIREDVPPGALAVsEGPQRNI 451
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
142-176 1.37e-04

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 37.80  E-value: 1.37e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1650123362 142 ITIEDGCWIGGGVIIlpGITIGYGSVIGAGSVVTK 176
Cdd:pfam14602   1 VIIGDNCLIGANSGI--GVSLGDNCVVGAGVVITA 33
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 73-185 2.63e-04

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 40.74  E-value: 2.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  73 CNIHIGDNVtvntGCTFVDCN-------KITIGSNVLIAPNVQLytathpidlderLAPVETEDGIkrvrrtyalpitie 145
Cdd:PRK14359  343 CEIDEGTNI----GAGTITCNydgkkkhKTIIGKNVFIGSDTQL------------VAPVNIEDNV-------------- 392

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1650123362 146 dgcwigggviilpgitigygsVIGAGSVVTKDIPANSLAI 185
Cdd:PRK14359  393 ---------------------LIAAGSTVTKDVPKGSLAI 411
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 81-191 4.13e-04

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 40.31  E-value: 4.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1650123362  81 VT-VNTGCTFVDCNkITIGSNVLIAPNVQLYTATH-----PIDLDERLAPVETEDGiKRVRRTYALPITIEDGCWIGGGV 154
Cdd:PRK14352  258 VTiVDPATTWIDVD-VTIGRDVVIHPGTQLLGRTTigedaVVGPDTTLTDVTVGEG-ASVVRTHGSESEIGAGATVGPFT 335

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1650123362 155 IILPGITIGYGSVIGAgSVVTKdipaNSlAIGNPCKV 191
Cdd:PRK14352  336 YLRPGTVLGEEGKLGA-FVETK----NA-TIGRGTKV 366
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 144-173 4.31e-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: 40.00  E-value: 4.31e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1650123362 144 IEDGCWIGGGVIILPGITIGYGSVIGAGSV 173
Cdd:COG1044   123 IGAGVVIGDGVVIGPGVVIGDGVVIGDDCV 152
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
141-170 5.18e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 36.16  E-value: 5.18e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1650123362 141 PITIEDGCWIGGGVIILPGITIGYGSVIGA 170
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 143-174 1.42e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 38.58  E-value: 1.42e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1650123362 143 TIEDGCWIGGGVIILPGITIGYGSVIGAGSVV 174
Cdd:PRK00892  114 KIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVI 145
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 143-174 1.56e-03

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 38.46  E-value: 1.56e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1650123362 143 TIEDGCWIGGGVIILPGITIGYGSVIGAGSVV 174
Cdd:COG1044   128 VIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTI 159
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 143-191 1.57e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 38.58  E-value: 1.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1650123362 143 TIEDGCWIGGGVIILPGITIGYGSVIGAGSVvtkdIPAN-----SLAIGNPCKV 191
Cdd:PRK00892  126 VIGAGVVIGDGVVIGAGAVIGDGVKIGADCR----LHANvtiyhAVRIGNRVII 175
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 144-174 4.44e-03

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: 36.62  E-value: 4.44e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1650123362 144 IEDGCWIGGGVIILPGITIGYGSVIGAGSVV 174
Cdd:cd03352    16 IGEGVVIGDGVVIGPGVVIGDGVVIGDDCVI 46
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 143-174 6.15e-03

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 36.53  E-value: 6.15e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1650123362 143 TIEDGCWIGGGVIILPGITIGYGSVIGAGSVV 174
Cdd:COG1044   110 KIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVI 141
 
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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