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Conserved domains on  [gi|15829649|ref|NP_308422|]
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galactoside O-acetyltransferase [Escherichia coli O157:H7 str. Sakai]

Protein Classification

LbetaH domain-containing protein; acyltransferase( domain architecture ID 11484326)

LbetaH (left-handed parallel beta-helix) domain-containing protein| acyltransferase belonging to the transferase hexapeptide repeat family, catalyzes the transfer of an acyl group from an acyl-CoA to a substrate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 1-203 1.03e-157

galactoside O-acetyltransferase; Reviewed


:

Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 433.66  E-value: 1.03e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649    1 MNMSMTERIKAGKLFTDMCEGLPEKRLRRKTLMYEFNHSHPSEVDKRESLIKEMFATVGENAWVEPPVYFSYGSNIHIGR 80
Cdd:PRK09527   1 MNMSMTERIKAGKLFTDMCEGLPEKRLRGKTLMYEFNHSHPSEVEKRESLIKEMFATVGENAWVEPPVYFSYGSNIHIGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649   81 NFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGHPVHHELRKNGEMYSFPITIGNNVWIGSHVVINPGVTIGDNSVIGA 160
Cdd:PRK09527  81 NFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGHPVHHELRKNGEMYSFPITIGNNVWIGSHVVINPGVTIGDNSVIGA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 15829649  161 GSIVTKDIPPNVVAAGVPCRVIREINDRDKQYYFRDYKVESSV 203
Cdd:PRK09527 161 GSVVTKDIPPNVVAAGVPCRVIREINDRDKQYYFKDYKVESSV 203
 
Name Accession Description Interval E-value
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 1-203 1.03e-157

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 433.66  E-value: 1.03e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649    1 MNMSMTERIKAGKLFTDMCEGLPEKRLRRKTLMYEFNHSHPSEVDKRESLIKEMFATVGENAWVEPPVYFSYGSNIHIGR 80
Cdd:PRK09527   1 MNMSMTERIKAGKLFTDMCEGLPEKRLRGKTLMYEFNHSHPSEVEKRESLIKEMFATVGENAWVEPPVYFSYGSNIHIGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649   81 NFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGHPVHHELRKNGEMYSFPITIGNNVWIGSHVVINPGVTIGDNSVIGA 160
Cdd:PRK09527  81 NFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGHPVHHELRKNGEMYSFPITIGNNVWIGSHVVINPGVTIGDNSVIGA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 15829649  161 GSIVTKDIPPNVVAAGVPCRVIREINDRDKQYYFRDYKVESSV 203
Cdd:PRK09527 161 GSVVTKDIPPNVVAAGVPCRVIREINDRDKQYYFKDYKVESSV 203
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 14-182 3.57e-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: 281.62  E-value: 3.57e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649  14 LFTDMCEGLPEKRLRRKTLMYEFNHSHPSEVDKRESLIKEMFATVGENAWVEPPVYFSYGSNIHIGRNFYANFNLTIVDD 93
Cdd:cd03357   1 LYNASDPELVAERARARRLLHEYNQTPPSDAEERRELLKELFGSVGENVYIEPPFHCDYGYNIHIGDNFYANFNCTILDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649  94 YTVTIGDNVLIAPNVTLSVTGHPVHHELRKNGEMYSFPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSIVTKDIPPNVV 173
Cdd:cd03357  81 APVTIGDNVLIGPNVQIYTAGHPLDPEERNRGLEYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVV 160


                ....*....
gi 15829649 174 AAGVPCRVI 182
Cdd:cd03357 161 AAGNPARVI 169
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
49-190 1.57e-56

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 175.44  E-value: 1.57e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649  49 SLIKEMFATVGENAWVEPPVYFsYGSNIHIGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGHPVHHELRknGEMY 128
Cdd:COG0110   2 KLLLLFGARIGDGVVIGPGVRI-YGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPAT--FPLR 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829649 129 SFPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSIVTKDIPPNVVAAGVPCRVIREINDRDK 190
Cdd:COG0110  79 TGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEEER 140
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 73-178 2.95e-24

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: 94.48  E-value: 2.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649    73 GSNIHIGRNFYANFNLTIvdDYTVTIGDNVLIAPNVTLSvtGHpvhhelrkngemysfpITIGNNVWIGSHVVINPGVTI 152
Cdd:TIGR03570 115 NPDVRIGDNVIINTGAIV--EHDCVIGDFVHIAPGVTLS--GG----------------VVIGEGVFIGAGATIIQGVTI 174

                          90       100
                  ....*....|....*....|....*.
gi 15829649   153 GDNSVIGAGSIVTKDIPPNVVAAGVP 178
Cdd:TIGR03570 175 GAGAIVGAGAVVTKDIPDGGVVVGVP 200
Mac pfam12464
Maltose acetyltransferase; This domain family is found in bacteria, archaea and eukaryotes, ...
 8-59 8.12e-12

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: 57.89  E-value: 8.12e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15829649     8 RIKAGKLFTDMCEGLPEKRLRRKTLMYEFNHSHPSEVDKRESLIKEMFATVG 59
Cdd:pfam12464   1 KMLAGELYDASDPELVAERLRARRLLRRYNNTPPEDAEEREELLKELFGSVG 52
 
Name Accession Description Interval E-value
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 1-203 1.03e-157

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 433.66  E-value: 1.03e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649    1 MNMSMTERIKAGKLFTDMCEGLPEKRLRRKTLMYEFNHSHPSEVDKRESLIKEMFATVGENAWVEPPVYFSYGSNIHIGR 80
Cdd:PRK09527   1 MNMSMTERIKAGKLFTDMCEGLPEKRLRGKTLMYEFNHSHPSEVEKRESLIKEMFATVGENAWVEPPVYFSYGSNIHIGR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649   81 NFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGHPVHHELRKNGEMYSFPITIGNNVWIGSHVVINPGVTIGDNSVIGA 160
Cdd:PRK09527  81 NFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGHPVHHELRKNGEMYSFPITIGNNVWIGSHVVINPGVTIGDNSVIGA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 15829649  161 GSIVTKDIPPNVVAAGVPCRVIREINDRDKQYYFRDYKVESSV 203
Cdd:PRK09527 161 GSVVTKDIPPNVVAAGVPCRVIREINDRDKQYYFKDYKVESSV 203
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 14-182 3.57e-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: 281.62  E-value: 3.57e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649  14 LFTDMCEGLPEKRLRRKTLMYEFNHSHPSEVDKRESLIKEMFATVGENAWVEPPVYFSYGSNIHIGRNFYANFNLTIVDD 93
Cdd:cd03357   1 LYNASDPELVAERARARRLLHEYNQTPPSDAEERRELLKELFGSVGENVYIEPPFHCDYGYNIHIGDNFYANFNCTILDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649  94 YTVTIGDNVLIAPNVTLSVTGHPVHHELRKNGEMYSFPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSIVTKDIPPNVV 173
Cdd:cd03357  81 APVTIGDNVLIGPNVQIYTAGHPLDPEERNRGLEYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVV 160


                ....*....
gi 15829649 174 AAGVPCRVI 182
Cdd:cd03357 161 AAGNPARVI 169
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 7-185 2.37e-61

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 189.25  E-value: 2.37e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649    7 ERIKAGKLFTDMCEGLPEKRLRRKTLMYEFNHSHPSEVDKRESLIKEMFATVgENAWVEPPVYFSYGSNIHIGRNFYANF 86
Cdd:PRK10092   6 EKMIAGELYRSADETLSRDRLRARQLIHRYNHSLPDEHTLRQQILADLFGQV-TEAYIEPTFRCDYGYNIFLGNNFYANF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649   87 NLTIVDDYTVTIGDNVLIAPNVTLSVTGHPVHHELRKNGEMYSFPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSIVTK 166
Cdd:PRK10092  85 DCVMLDVCPIRIGDNCMLAPGVHIYTATHPLDPVARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTK 164

                        170
                 ....*....|....*....
gi 15829649  167 DIPPNVVAAGVPCRVIREI 185
Cdd:PRK10092 165 DVPDNVVVGGNPARIIKKL 183
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
49-190 1.57e-56

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 175.44  E-value: 1.57e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649  49 SLIKEMFATVGENAWVEPPVYFsYGSNIHIGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGHPVHHELRknGEMY 128
Cdd:COG0110   2 KLLLLFGARIGDGVVIGPGVRI-YGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPAT--FPLR 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829649 129 SFPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSIVTKDIPPNVVAAGVPCRVIREINDRDK 190
Cdd:COG0110  79 TGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEEER 140
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 75-182 4.10e-46

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: 147.60  E-value: 4.10e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649  75 NIHIGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGHPVHHELRKNGEMYSF-PITIGNNVWIGSHVVINPGVTIG 153
Cdd:cd04647   1 NISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDHNHDIDDPERPIEQGVTSaPIVIGDDVWIGANVVILPGVTIG 80

                        90       100
                ....*....|....*....|....*....
gi 15829649 154 DNSVIGAGSIVTKDIPPNVVAAGVPCRVI 182
Cdd:cd04647  81 DGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 75-183 1.87e-31

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: 111.48  E-value: 1.87e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649  75 NIHIGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTL---------SVTGHPVHHELRKNGEMYSF-------PITIGNNV 138
Cdd:cd03349   1 NISVGDYSYGSGPDCDVGGDKLSIGKFCSIAPGVKIglggnhptdWVSTYPFYIFGGEWEDDAKFddwpskgDVIIGNDV 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 15829649 139 WIGSHVVINPGVTIGDNSVIGAGSIVTKDIPPNVVAAGVPCRVIR 183
Cdd:cd03349  81 WIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIR 125
PRK10502 PRK10502
putative acyl transferase; Provisional
 56-184 4.23e-26

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 98.87  E-value: 4.23e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649   56 ATVGENAWVEPPVYFSYGSNIHIGRNFYanfnltIVDD---YT---VTIGDNVLIAPNVTLsVTGHpvHHELRKNGEMYS 129
Cdd:PRK10502  52 AKIGKGVVIRPSVRITYPWKLTIGDYAW------IGDDvwlYNlgeITIGAHCVISQKSYL-CTGS--HDYSDPHFDLNT 122

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15829649  130 FPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSIVTKDIPPNVVAAGVPCRVIRE 184
Cdd:PRK10502 123 APIVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIRP 177
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 73-178 1.32e-25

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: 97.94  E-value: 1.32e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649  73 GSNIHIGRNFYANFNLTIvdDYTVTIGDNVLIAPNVTLSvtGHpvhhelrkngemysfpITIGNNVWIGSHVVINPGVTI 152
Cdd:cd03360 112 NPDARIGDNVIINTGAVI--GHDCVIGDFVHIAPGVVLS--GG----------------VTIGEGAFIGAGATIIQGVTI 171

                        90       100
                ....*....|....*....|....*.
gi 15829649 153 GDNSVIGAGSIVTKDIPPNVVAAGVP 178
Cdd:cd03360 172 GAGAIIGAGAVVTKDVPDGSVVVGNP 197
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 70-188 1.33e-25

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: 97.46  E-value: 1.33e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649  70 FSYGSNIH----IGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTG------HPvhhelrkngemysfpiTIGNNVW 139
Cdd:COG1045  62 FLTGIDIHpgatIGRGFFIDHGTGVVIGETAVIGDNVTIYQGVTLGGTGkekgkrHP----------------TIGDNVV 125

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 15829649 140 IGSHVVINPGVTIGDNSVIGAGSIVTKDIPPNVVAAGVPCRVIREINDR 188
Cdd:COG1045 126 IGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVKRKGSK 174
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 73-178 2.95e-24

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: 94.48  E-value: 2.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649    73 GSNIHIGRNFYANFNLTIvdDYTVTIGDNVLIAPNVTLSvtGHpvhhelrkngemysfpITIGNNVWIGSHVVINPGVTI 152
Cdd:TIGR03570 115 NPDVRIGDNVIINTGAIV--EHDCVIGDFVHIAPGVTLS--GG----------------VVIGEGVFIGAGATIIQGVTI 174

                          90       100
                  ....*....|....*....|....*.
gi 15829649   153 GDNSVIGAGSIVTKDIPPNVVAAGVP 178
Cdd:TIGR03570 175 GAGAIVGAGAVVTKDIPDGGVVVGVP 200
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 73-183 3.44e-23

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: 89.48  E-value: 3.44e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649  73 GSNIHIGRNFYANFNLTIVDDYT----------VTIGDNVLIAPNVTLSVTGHPVHHELRKNgEMysFPITIGNNVWIGS 142
Cdd:cd03358   2 GDNCIIGTNVFIENDVKIGDNVKiqsnvsiyegVTIEDDVFIGPNVVFTNDLYPRSKIYRKW-EL--KGTTVKRGASIGA 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15829649 143 HVVINPGVTIGDNSVIGAGSIVTKDIPPNVVAAGVPCRVIR 183
Cdd:cd03358  79 NATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 72-178 4.84e-23

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: 88.65  E-value: 4.84e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649  72 YGSNIH----IGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTL------SVTGHPvhhelrkngemysfpiTIGNNVWIG 141
Cdd:cd03354   1 TGIDIHpgakIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLggkgkgGGKRHP----------------TIGDNVVIG 64

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15829649 142 SHVVINPGVTIGDNSVIGAGSIVTKDIPPNVVAAGVP 178
Cdd:cd03354  65 AGAKILGNITIGDNVKIGANAVVTKDVPANSTVVGVP 101
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 57-182 3.19e-22

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: 86.51  E-value: 3.19e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649  57 TVGENAWVEPPVYFsygsnihigrnfyanFNLTivddyTVTIGDNVLIAPNVTLSvTGHpvhHELRK-NGEMYSFPITIG 135
Cdd:cd05825   5 TIGDNSWIGEGVWI---------------YNLA-----PVTIGSDACISQGAYLC-TGS---HDYRSpAFPLITAPIVIG 60

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15829649 136 NNVWIGSHVVINPGVTIGDNSVIGAGSIVTKDIPPNVVAAGVPCRVI 182
Cdd:cd05825  61 DGAWVAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 76-186 4.78e-21

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 86.08  E-value: 4.78e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649   76 IHIGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLsvTGHPvHHELRKNGEMYSF------------PITIGNNVWIGSH 143
Cdd:PRK09677  66 LFFGDNVQVNDYVHIACIESITIGRDTLIASKVFI--TDHN-HGSFKHSDDFSSPnlppdmrtlessAVVIGQRVWIGEN 142

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 15829649  144 VVINPGVTIGDNSVIGAGSIVTKDIPPNVVAAGVPCRVIREIN 186
Cdd:PRK09677 143 VTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKKYN 185
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 57-192 1.75e-19

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: 80.92  E-value: 1.75e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649  57 TVGENAWVeppvyfSYGS-------NIHIGrnfyANFN------LTIVDDYTVTIGDNVLIAPNVTLsvtgHPVhhelrk 123
Cdd:cd04645  19 TLGEGSSV------WFGAvlrgdvnPIRIG----ERTNiqdgsvLHVDPGYPTIIGDNVTVGHGAVL----HGC------ 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15829649 124 ngemysfpiTIGNNVWIGSHVVINPGVTIGDNSVIGAGSIVT--KDIPPNVVAAGVPCRVIREINDRDKQY 192
Cdd:cd04645  79 ---------TIGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPpgKVIPPGSLVAGSPAKVVRELTDEEIAE 140
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 92-192 5.14e-19

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 80.07  E-value: 5.14e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649  92 DDYTVTIGDNVLIAPNVTLsvtghpvhHelrknGemysfpITIGNNVWIGSHVVINPGVTIGDNSVIGAGSIVT--KDIP 169
Cdd:COG0663  68 PGYPLTIGDDVTIGHGAIL--------H-----G------CTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTegKVVP 128

                        90       100
                ....*....|....*....|...
gi 15829649 170 PNVVAAGVPCRVIREINDRDKQY 192
Cdd:COG0663 129 PGSLVVGSPAKVVRELTEEEIAF 151
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 76-165 3.13e-18

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: 75.36  E-value: 3.13e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649  76 IHIGRNFYANFNLTIVDdyTVTIGDNVLIAPNVTLSVTGHPVHhelrkngemySFPITIGNNVWIGSHVVINPGVTIGDN 155
Cdd:cd00208   1 VFIGEGVKIHPKAVIRG--PVVIGDNVNIGPGAVIGAATGPNE----------KNPTIIGDNVEIGANAVIHGGVKIGDN 68

                        90
                ....*....|
gi 15829649 156 SVIGAGSIVT 165
Cdd:cd00208  69 AVIGAGAVVT 78
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 76-184 2.15e-14

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: 68.59  E-value: 2.15e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649  76 IHIGRNfyanfnltivddytVTIGDNVLIAPNVTLSvtGHpvhhelrkngemysfpITIGNNVWIGSHVVINPGVTIGDN 155
Cdd:cd03352 127 VQIAHN--------------VRIGENCLIAAQVGIA--GS----------------TTIGDNVIIGGQVGIAGHLTIGDG 174

                        90       100
                ....*....|....*....|....*....
gi 15829649 156 SVIGAGSIVTKDIPPNVVAAGVPCRVIRE 184
Cdd:cd03352 175 VVIGAGSGVTSIVPPGEYVSGTPAQPHRE 203
PLN02357 PLN02357
serine acetyltransferase
 71-182 3.51e-13

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 66.83  E-value: 3.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649   71 SYGSNIH----IGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGhpvhhelRKNGEMYSfpiTIGNNVWIGSHVVI 146
Cdd:PLN02357 224 AFAVDIHpgakIGQGILLDHATGVVIGETAVVGNNVSILHNVTLGGTG-------KQSGDRHP---KIGDGVLIGAGTCI 293

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 15829649  147 NPGVTIGDNSVIGAGSIVTKDIPPNVVAAGVPCRVI 182
Cdd:PLN02357 294 LGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLI 329
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 96-181 4.35e-13

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: 65.92  E-value: 4.35e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649  96 VTIGDNVLIAPNVTLSvtGHpvhhelrkngemysfpITIGNNVWIGSHVVINPGVTIGDNSVIGAGSIVTKDIPPNVVAA 175
Cdd:cd03351 121 CVIGNNVILANNATLA--GH----------------VEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAA 182


                ....*.
gi 15829649 176 GVPCRV 181
Cdd:cd03351 183 GNRARL 188
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 98-181 1.07e-12

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: 64.65  E-value: 1.07e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649  98 IGDNVLIAPNVTLSvtGHpvhhelrkngemysfpITIGNNVWIGSHVVINPGVTIGDNSVIGAGSIVTKDIPPNVVAAGV 177
Cdd:COG1043 125 VGNNVILANNATLA--GH----------------VEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDVPPYVLAAGN 186


                ....
gi 15829649 178 PCRV 181
Cdd:COG1043 187 PARL 190
Mac pfam12464
Maltose acetyltransferase; This domain family is found in bacteria, archaea and eukaryotes, ...
 8-59 8.12e-12

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: 57.89  E-value: 8.12e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15829649     8 RIKAGKLFTDMCEGLPEKRLRRKTLMYEFNHSHPSEVDKRESLIKEMFATVG 59
Cdd:pfam12464   1 KMLAGELYDASDPELVAERLRARRLLRRYNNTPPEDAEEREELLKELFGSVG 52
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 75-189 4.20e-11

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: 58.74  E-value: 4.20e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649  75 NIHIGRNFYANFNLTIVDD--YTVTIGDNVLIAPNVtlsvtghpVHHELRkngemysfpitIGNNVWIGSHVVINPGVTI 152
Cdd:cd04650  39 SIYIGKYSNVQENVSIHTDhgYPTEIGDYVTIGHNA--------VVHGAK-----------VGNYVIVGMGAILLNGAKI 99

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15829649 153 GDNSVIGAGSIVT--KDIPPNVVAAGVPCRVIREINDRD 189
Cdd:cd04650 100 GDHVIIGAGAVVTpgKEIPDYSLVLGVPAKVVRKLTEEE 138
PLN02739 PLN02739
serine acetyltransferase
 72-189 5.98e-11

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 60.43  E-value: 5.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649   72 YGSNIH----IGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGhpvhhelRKNGEMYSfpiTIGNNVWIGSHVVIN 147
Cdd:PLN02739 204 FGIDIHpaarIGKGILLDHGTGVVIGETAVIGDRVSILHGVTLGGTG-------KETGDRHP---KIGDGALLGACVTIL 273

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 15829649  148 PGVTIGDNSVIGAGSIVTKDIPPNVVAAGVPCRVIREINDRD 189
Cdd:PLN02739 274 GNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFVDEQD 315
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 96-187 7.73e-11

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: 57.76  E-value: 7.73e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649  96 VTIGDNVLIAPNVTLSVTGHPVHHE----LRKNGEMYSFP--------------------ITIGNNVWIGSHVVINPGVT 151
Cdd:cd04745  19 VIIGKNCYIGPHASLRGDFGRIVIRdganVQDNCVIHGFPgqdtvleenghighgailhgCTIGRNALVGMNAVVMDGAV 98

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15829649 152 IGDNSVIGAGSIVTK--DIPPNVVAAGVPCRVIREIND 187
Cdd:cd04745  99 IGEESIVGAMAFVKAgtVIPPRSLIAGSPAKVIRELSD 136
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 130-184 2.24e-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: 58.88  E-value: 2.24e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15829649 130 FPITIGNNVWIGSHVV-INPgVTIGDNSVIGAGSIVTKDIPPNVVAAGVPCRVIRE 184
Cdd:COG1207 393 HRTVIGDGAFIGSNTNlVAP-VTIGDGATIGAGSTITKDVPAGALAIARARQRNIE 447
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 76-184 2.38e-10

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: 58.49  E-value: 2.38e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649  76 IHIGRNfyanfnltivddytVTIGDNVLIAPNVTL--SVTghpvhhelrkngemysfpitIGNNVWIGSHVVINPGVTIG 153
Cdd:COG1044 235 VQIAHN--------------VRIGEHTAIAAQVGIagSTK--------------------IGDNVVIGGQVGIAGHLTIG 280

                        90       100       110
                ....*....|....*....|....*....|.
gi 15829649 154 DNSVIGAGSIVTKDIPPNVVAAGVPCRVIRE 184
Cdd:COG1044 281 DGVIIGAQSGVTKSIPEGGVYSGSPAQPHRE 311
PLN02694 PLN02694
serine O-acetyltransferase
 72-182 3.06e-10

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 58.12  E-value: 3.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649   72 YGSNIH----IGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGhpvhhelRKNGEMYSfpiTIGNNVWIGSHVVIN 147
Cdd:PLN02694 159 FAVDIHpaakIGKGILFDHATGVVIGETAVIGNNVSILHHVTLGGTG-------KACGDRHP---KIGDGVLIGAGATIL 228

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 15829649  148 PGVTIGDNSVIGAGSIVTKDIPPNVVAAGVPCRVI 182
Cdd:PLN02694 229 GNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLV 263
PRK10191 PRK10191
putative acyl transferase; Provisional
 78-181 9.97e-10

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 54.90  E-value: 9.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649   78 IGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGhpvhhelrknGEMYSFPItIGNNVWIGSHVVINPGVTIGDNSV 157
Cdd:PRK10191  50 IGRRFTIHHGYAVVINKNVVAGDDFTIRHGVTIGNRG----------ADNMACPH-IGNGVELGANVIILGDITIGNNVT 118

                         90       100
                 ....*....|....*....|....
gi 15829649  158 IGAGSIVTKDIPPNVVAAGVPCRV 181
Cdd:PRK10191 119 VGAGSVVLDSVPDNALVVGEKARV 142
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 92-187 1.09e-09

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: 54.91  E-value: 1.09e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649  92 DDYTVTIGDNVLIAPNVTL--SVTGHpvhhelrkNGEMYSFPITIGNNVWIGSHVVINPG-----VTIGDNSVIGAGSIV 164
Cdd:cd03359  39 DLATVSIGRYCILSEGCVIrpPFKKF--------SKGVAFFPLHIGDYVFIGENCVVNAAqigsyVHIGKNCVIGRRCII 110

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 15829649 165 tKD---------------IPPNVVAAGVPCRVIREIND 187
Cdd:cd03359 111 -KDcvkildgtvvppdtvIPPYSVVSGRPARFIGELPE 147
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 90-164 1.12e-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: 56.56  E-value: 1.12e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829649  90 IVDDyTVTIGDNVLIAPNVtlsVTGHPVhhelrkngemysfpiTIGNNVWIGSHVVINPGVTIGDNSVIGAGSIV 164
Cdd:COG1044 104 VIDP-SAKIGEGVSIGPFA---VIGAGV---------------VIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTI 159
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 56-164 1.23e-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: 56.56  E-value: 1.23e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649  56 ATVGENAWVEPPVYfsygsnihIGRNfyanfnltivddytVTIGDNVLIAPNVTLsvtGHPVhhelrkngemysfpiTIG 135
Cdd:COG1044 109 AKIGEGVSIGPFAV--------IGAG--------------VVIGDGVVIGPGVVI---GDGV---------------VIG 148

                        90       100
                ....*....|....*....|....*....
gi 15829649 136 NNVWIGSHVVINPGVTIGDNSVIGAGSIV 164
Cdd:COG1044 149 DDCVLHPNVTIYERCVIGDRVIIHSGAVI 177
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 133-174 2.36e-09

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: 54.35  E-value: 2.36e-09
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 15829649 133 TIGNNVWIGSHVVINPGVTIGDNSVIGAGSIVTKDIPPNVVA 174
Cdd:cd03353 146 VIGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGALA 187
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 55-164 2.44e-09

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 54.72  E-value: 2.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649  55 FATVGENAWVEPPVYfsygsnihIGRNfyanfnltivddytVTIGDNVLIAPNVTLsvtGHPVhhelrkngemysfpiTI 134
Cdd:cd03352   1 SAKIGENVSIGPNAV--------IGEG--------------VVIGDGVVIGPGVVI---GDGV---------------VI 40

                        90       100       110
                ....*....|....*....|....*....|
gi 15829649 135 GNNVWIGSHVVINPGVTIGDNSVIGAGSIV 164
Cdd:cd03352  41 GDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 95-173 3.95e-09

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 55.15  E-value: 3.95e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15829649   95 TVTIGDNVLIAPNVtlsvtghpvhhelrkngemysfpiTIGNNVWIGSHVVINPGVTIGDNSVIGAGSIvtkdIPPNVV 173
Cdd:PRK00892 112 SAKIGEGVSIGPNA------------------------VIGAGVVIGDGVVIGAGAVIGDGVKIGADCR----LHANVT 162
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
97-186 4.07e-09

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 54.72  E-value: 4.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649   97 TIGDNVLIAPNVTLsvTGHpvhhelrkngemysfpITIGNNVWIGSHVVINPGVTIGDNSVIGAGSIVTKDIPPNVVAAG 176
Cdd:PRK05289 125 VVGNHVILANNATL--AGH----------------VEVGDYAIIGGLTAVHQFVRIGAHAMVGGMSGVSQDVPPYVLAEG 186

                         90
                 ....*....|
gi 15829649  177 VPCRvIREIN 186
Cdd:PRK05289 187 NPAR-LRGLN 195
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 96-184 1.06e-08

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 53.99  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649   96 VTIGDNVLIAPNVTL--SVTghpvhhelrkngemysfpitIGNNVWIGSHVVINPGVTIGDNSVIGAGSIVTKDIP-PNV 172
Cdd:PRK00892 244 VVIGRHTAIAAQVGIagSTK--------------------IGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPePGE 303

                         90
                 ....*....|..
gi 15829649  173 VAAGVPCRVIRE 184
Cdd:PRK00892 304 YSSGIPAQPNKE 315
cysE PRK11132
serine acetyltransferase; Provisional
 71-182 1.28e-08

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 53.16  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649   71 SYGSNIH----IGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTG------HPvhhelrkngemysfpiTIGNNVWI 140
Cdd:PRK11132 139 AFQVDIHpaakIGRGIMLDHATGIVIGETAVIENDVSILQSVTLGGTGktsgdrHP----------------KIREGVMI 202

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 15829649  141 GSHVVINPGVTIGDNSVIGAGSIVTKDIPPNVVAAGVPCRVI 182
Cdd:PRK11132 203 GAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIV 244
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 134-174 2.65e-08

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 52.82  E-value: 2.65e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 15829649  134 IGNNVWIGSHVVINPGVTIGDNSVIGAGSIVTKDIPPNVVA 174
Cdd:PRK14355 400 IEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPPDSLA 440
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 56-162 3.54e-08

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 52.45  E-value: 3.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649   56 ATVGENAWVEPPVYFsyGSNIHIGRN--FYANfnlTIVDDYtVTIGDNVLIAPNVTlsvtghpVHHELRkngemysfpit 133
Cdd:PRK00892 113 AKIGEGVSIGPNAVI--GAGVVIGDGvvIGAG---AVIGDG-VKIGADCRLHANVT-------IYHAVR----------- 168

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 15829649  134 IGNNVWIGSHVVI--------NP-----------GVTIGDNSVIGAGS 162
Cdd:PRK00892 169 IGNRVIIHSGAVIgsdgfgfaNDrggwvkipqlgRVIIGDDVEIGANT 216
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 133-184 5.75e-08

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 51.79  E-value: 5.75e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15829649  133 TIGNNVWIGSHVVINPGVTIGDNSVIGAGSIVTKDIPPNVVAAGVPCRVIRE 184
Cdd:PRK14353 382 EIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALGRARQETKP 433
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
131-160 8.74e-08

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 46.56  E-value: 8.74e-08
                          10        20        30
                  ....*....|....*....|....*....|
gi 15829649   131 PITIGNNVWIGSHVVINPGVTIGDNSVIGA 160
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 134-174 8.99e-08

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 51.26  E-value: 8.99e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 15829649  134 IGNNVWIGSHVVINPGVTIGDNSVIGAGSIVTKDIPPNVVA 174
Cdd:PRK14356 401 IGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSLA 441
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 78-184 1.36e-07

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 50.92  E-value: 1.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649   78 IGRNFYANfNLTIVDDytVTIGDNVLI-APNVTLSVTGHpvhhelRKNgemysfPITIGNNVWIGSHVVINPGVTIGDNS 156
Cdd:PRK14357 344 IGENTKAQ-HLTYLGD--ATVGKNVNIgAGTITCNYDGK------KKN------PTFIEDGAFIGSNSSLVAPVRIGKGA 408

                         90       100
                 ....*....|....*....|....*...
gi 15829649  157 VIGAGSIVTKDIPPNVVAAGVPCRVIRE 184
Cdd:PRK14357 409 LIGAGSVITEDVPPYSLALGRARQIVKE 436
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 96-178 1.70e-07

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: 50.52  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649    96 VTIGDNVLIAPNVTLSvtGHPVHHELRKNGemysfPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSIVTKD--IPPNVV 173
Cdd:TIGR02353 132 LTIGAGTIVRKEVMLL--GYRAERGRLHTG-----PVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSALQGGqsIPDGER 204


                  ....*
gi 15829649   174 AAGVP 178
Cdd:TIGR02353 205 WHGSP 209
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
90-184 2.66e-07

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 49.33  E-value: 2.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649   90 IVDDyTVTIGDNVLIAPnvtLSVTGHPVhhelrkngemysfpiTIGNNVWIGSHVVINPGVTIGDNSVIGAGSIVTkDIP 169
Cdd:PRK05289  10 IVEP-GAKIGENVEIGP---FCVIGPNV---------------VIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIG-EDP 69

                         90       100
                 ....*....|....*....|..
gi 15829649  170 PNVVAAGVPCRV-------IRE 184
Cdd:PRK05289  70 QDLKYKGEPTRLvigdnntIRE 91
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 130-174 2.76e-07

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 49.83  E-value: 2.76e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 15829649  130 FPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSIVTKDIPPNVVA 174
Cdd:PRK14354 392 FKTIIGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDALA 436
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 77-178 3.13e-07

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: 49.75  E-value: 3.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649    77 HIGRNFYanfnltiVDDYTVTIGDNVLIAPNVTLSVTGHPVHHeLRKNGEMYSFPITIGNNVWIGSHVVINPGVTIGDNS 156
Cdd:TIGR02353 599 KIGRGVY-------IDGTDLTERDLVTIGDDSTLNEGSVIQTH-LFEDRVMKSDTVTIGDGATLGPGAIVLYGVVMGEGS 670

                          90       100
                  ....*....|....*....|....
gi 15829649   157 VIGAGSIVTK--DIPPNVVAAGVP 178
Cdd:TIGR02353 671 VLGPDSLVMKgeEVPAHTRWRGNP 694
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 133-173 3.92e-07

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 48.56  E-value: 3.92e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 15829649 133 TIGNNVWIGSHVVINPGVTIGDNSVIGAGSIVTKD--------IPPNVV 173
Cdd:cd03352   3 KIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGvvigddcvIHPNVT 51
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 56-178 4.68e-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: 47.38  E-value: 4.68e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649  56 ATVGENAWVEPPVYFSYGSNIHIGrnfyanfnlTIVDDYTV-----TIGDNVLIAPNVTLSVTGHPVHhelrkngemySF 130
Cdd:cd03350  14 AFIGPGAVLMMPSYVNIGAYVDEG---------TMVDSWATvgscaQIGKNVHLSAGAVIGGVLEPLQ----------AT 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15829649 131 PITIGNNVWIGSHVVINPGVTIGDNSVIGAGSIVTK---------------DIPPN-VVAAGVP 178
Cdd:cd03350  75 PVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTQstpiydretgeiyygRVPPGsVVVAGSL 138
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 90-164 5.33e-07

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 48.48  E-value: 5.33e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829649  90 IVDDyTVTIGDNVLIAPNvtlSVTGHPVhhelrkngemysfpiTIGNNVWIGSHVVINPGVTIGDNSVIGAGSIV 164
Cdd:COG1043   9 IVDP-GAKLGENVEIGPF---CVIGPDV---------------EIGDGTVIGSHVVIEGPTTIGKNNRIFPFASI 64
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 130-169 1.31e-06

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 47.68  E-value: 1.31e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 15829649  130 FPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSIVTKDIP 169
Cdd:PRK14359 366 HKTIIGKNVFIGSDTQLVAPVNIEDNVLIAAGSTVTKDVP 405
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 56-182 1.96e-06

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 47.24  E-value: 1.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649   56 ATVGENAWVEPPVYFSYGS---------------NIHIGRNFYANfNLTIVDDytVTIGDNVLI-APNVTLSVTGHPVHH 119
Cdd:PRK14352 323 SEIGAGATVGPFTYLRPGTvlgeegklgafvetkNATIGRGTKVP-HLTYVGD--ADIGEHSNIgASSVFVNYDGVNKHR 399

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829649  120 elrkngemysfpITIGNNVWIGSHVVINPGVTIGDNSVIGAGSIVTKDIPPN--VVAAGvPCRVI 182
Cdd:PRK14352 400 ------------TTIGSHVRTGSDTMFVAPVTVGDGAYTGAGTVIREDVPPGalAVSEG-PQRNI 451
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 75-182 1.99e-06

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 47.33  E-value: 1.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649   75 NIHIGRNFYANfNLTIVDDytVTIGDNVLI-APNVTLSVTGhpvhhelrKNgemySFPITIGNNVWIGSHVVINPGVTIG 153
Cdd:PRK09451 352 KARLGKGSKAG-HLTYLGD--AEIGDNVNIgAGTITCNYDG--------AN----KFKTIIGDDVFVGSDTQLVAPVTVG 416

                         90       100       110
                 ....*....|....*....|....*....|
gi 15829649  154 DNSVIGAGSIVTKDIPPN-VVAAGVPCRVI 182
Cdd:PRK09451 417 KGATIGAGTTVTRDVAENeLVISRVPQRHI 446
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 128-190 3.29e-06

Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p27 is part of the pointed-end subcomplex in dynactin that also includes p25, p26, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain the imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100052 [Multi-domain]  Cd Length: 164  Bit Score: 45.39  E-value: 3.29e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829649 128 YSFPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSIVTKD--IPPNVVAAGVPCrVIREINDRDK 190
Cdd:cd04646  80 KCEALKIGNNNVFESKSFVGKNVIITDGCIIGAGCKLPSSeiLPENTVIYGADC-LRRTQTDRPK 143
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 90-164 3.78e-06

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: 45.89  E-value: 3.78e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829649  90 IVDDyTVTIGDNVLIAPNvtlSVTGHPVhhelrkngemysfpiTIGNNVWIGSHVVINPGVTIGDNSVIGAGSIV 164
Cdd:cd03351   7 IVDP-GAKIGENVEIGPF---CVIGPNV---------------EIGDGTVIGSHVVIDGPTTIGKNNRIFPFASI 62
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 89-164 6.23e-06

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: 45.79  E-value: 6.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649  89 TIVD------DYTVTIGDNVLIAPNVTLsvTGHpvhhelrkngemysfpITIGNNVWIGSHVVINpGVTIGDN------- 155
Cdd:COG1207 254 TIIDpattyiDGDVEIGRDVVIDPNVIL--EGK----------------TVIGEGVVIGPNCTLK-DSTIGDGvvikysv 314

                        90
                ....*....|..
gi 15829649 156 ---SVIGAGSIV 164
Cdd:COG1207 315 iedAVVGAGATV 326
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
132-166 6.39e-06

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 41.66  E-value: 6.39e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 15829649   132 ITIGNNVWIGSHVVInpGVTIGDNSVIGAGSIVTK 166
Cdd:pfam14602   1 VIIGDNCLIGANSGI--GVSLGDNCVVGAGVVITA 33
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 56-184 3.51e-05

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 43.76  E-value: 3.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649   56 ATVGENAWVEPpvyFSY-------GSNIHIGrNFYANFNLTIVDDYTV---------TIGDNVLI-APNVTLSVTGHPVH 118
Cdd:PRK14360 314 SQIGDGVKIGP---YAHlrpeaqiGSNCRIG-NFVEIKKSQLGEGSKVnhlsyigdaTLGEQVNIgAGTITANYDGVKKH 389

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829649  119 helrkngemysfPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSIVTKDIPPNVVAAGVPCRVIRE 184
Cdd:PRK14360 390 ------------RTVIGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLAIARSRQVIKE 443
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 89-164 1.51e-04

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: 40.87  E-value: 1.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649  89 TIVD------DYTVTIGDNVLIAPNVTLSvtGHpvhhelrkngemysfpITIGNNVWIGSHVVINPGvTIGDNSVIGAGS 162
Cdd:cd03353   3 TLIDpettyiDGDVEIGVDVVIDPGVILE--GK----------------TVIGEDCVIGPNCVIKDS-TIGDGVVIKASS 63


                ..
gi 15829649 163 IV 164
Cdd:cd03353  64 VI 65
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 89-188 1.53e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 41.16  E-value: 1.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649   89 TIVDDYTVTIGDNVLIAPNVtlsVTGHPVhhelrkngemysfpiTIGNNVWIGSHVVINPGVTIGDNSVIGAGSIVTKDi 168
Cdd:PRK12461   5 TAVIDPSAKLGSGVEIGPFA---VIGANV---------------EIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGDE- 65

                         90       100
                 ....*....|....*....|
gi 15829649  169 PPNVVAAGVPCRVIreINDR 188
Cdd:PRK12461  66 PQDFTYKGEESRLE--IGDR 83
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 131-191 1.65e-04

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: 41.26  E-value: 1.65e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649 131 PITIGNNVWIGSHVVINPGVTIGDNSVIGAGSIVTK---------------DIPPN-VVAAG----------VPCRVIre 184
Cdd:COG2171 170 PVIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLTAstkiydrvtgevyygRVPAGsVVVPGslpgkdgdygLYCAVI-- 247


                ....*..
gi 15829649 185 INDRDKQ 191
Cdd:COG2171 248 VKRRDEK 254
PLN02296 PLN02296
carbonate dehydratase
 130-192 2.57e-04

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 40.88  E-value: 2.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649  130 FPITIGNNVWIGSHVVINpGVTIGDNSVIG------------------AGSIVTKD--IPPNVVAAGVPCRVIREINDRD 189
Cdd:PLN02296 118 LPTIIGDNVTIGHSAVLH-GCTVEDEAFVGmgatlldgvvvekhamvaAGALVRQNtrIPSGEVWAGNPAKFLRKLTEEE 196


                 ...
gi 15829649  190 KQY 192
Cdd:PLN02296 197 IAF 199
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 134-192 4.98e-04

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 39.41  E-value: 4.98e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15829649  134 IGNNVWIGSHVVINPGVTIGDNSVIGAGSIVTKDI--PPNVVAAGVPCRVIREINDRDKQY 192
Cdd:PRK13627  91 IGRDALVGMNSVIMDGAVIGEESIVAAMSFVKAGFqgEKRQLLMGTPARAVRSVSDDELHW 151
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 58-164 7.51e-04

Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three distinct groups of carbonic anhydrases - alpha, beta and gamma - which show no significant sequence identity or structural similarity. Gamma CAs are homotrimeric enzymes, with each subunit containing a left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 38.76  E-value: 7.51e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649  58 VGENAWVEPpvYFSYGSNIHIGRNFYANFNLTIVDDYT--VTIGDNVLIAPNVtlsvtghpVHHELrkngEMYSfpITIG 135
Cdd:cd00710   5 IDPSAYVHP--TAVVIGDVIIGDNVFVGPGASIRADEGtpIIIGANVNIQDGV--------VIHAL----EGYS--VWIG 68

                        90       100
                ....*....|....*....|....*....
gi 15829649 136 NNVWIGSHVVINPGVTIGDNSVIGAGSIV 164
Cdd:cd00710  69 KNVSIAHGAIVHGPAYIGDNCFIGFRSVV 97
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 56-165 1.33e-03

Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix (LbH) domain: Proteins in this family show simlarity to glucose-1-phosphate adenylyltransferases in that they contain N-terminal catalytic domains that resemble a dinucleotide-binding Rossmann fold and C-terminal LbH fold domains. Members in this family are predicted to be glucose-1-phosphate thymidylyltransferases, which are involved in the dTDP-L-rhamnose biosynthetic pathway. Glucose-1-phosphate thymidylyltransferase catalyzes the synthesis of deoxy-thymidine di-phosphate (dTDP)-L-rhamnose, an important component of the cell wall of many microorganisms. The C-terminal LbH domain contains multiple turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 37.95  E-value: 1.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649  56 ATVGENAWVEPPVYFsyGSNIHIGRNFYANFNLTIVDDytVTIGD-----NVLIAPNVTL--------SVTGHPVH---- 118
Cdd:cd05636  24 AIVRSGAYIEGPVII--GKGCEIGPNAYIRGYTVLGDG--CVVGNsvevkNSIIMDGTKVphlnyvgdSVLGENVNlgag 99

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15829649 119 ------------HELRKNGEMYS-----FPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSIVT 165
Cdd:cd05636 100 titanlrfddkpVKVRLKGERVDtgrrkLGAIIGDGVKTGINVSLNPGVKIGPGSWVYPGCVVR 163
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 73-181 1.64e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 38.08  E-value: 1.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649   73 GSNIHIGRNFYANFNLTIVDDytVTIGDNVLIAPNVTLSvtGHpvhhelrkngemysfpITIGNNVWIGSHVVINPGVTI 152
Cdd:PRK12461  99 GGVTRIGNDNLLMAYSHVAHD--CQIGNNVILVNGALLA--GH----------------VTVGDRAIISGNCLVHQFCRI 158

                         90       100
                 ....*....|....*....|....*....
gi 15829649  153 GDNSVIGAGSIVTKDIPPNVVAAGVPCRV 181
Cdd:PRK12461 159 GALAMMAGGSRISKDVPPYCMMAGHPTNV 187
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 94-190 1.71e-03

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: 38.58  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649    94 YTVTIGDNVLIAPNVTLSvtghPVHHElrkNGEMYSFPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSIVTKDIP--PN 171
Cdd:TIGR02353 371 DLTDIGEETFIADGLLMG----NARLS---GGWFRLGRTRIGRRSFLGNSGYYPPGAKTGDNVLLGVLSMTPKDGKvrEG 443

                          90
                  ....*....|....*....
gi 15829649   172 VVAAGVPCRVIREINDRDK 190
Cdd:TIGR02353 444 VGWLGSPPFELPRRVNRDD 462
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 134-173 2.05e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 38.20  E-value: 2.05e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 15829649  134 IGNNVWIGSHVVINPGVTIGDNSVIGAGSIvtkdIPPNVV 173
Cdd:PRK00892 109 IDPSAKIGEGVSIGPNAVIGAGVVIGDGVV----IGAGAV 144
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 134-165 3.06e-03

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: 37.31  E-value: 3.06e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 15829649 134 IGNNVWIGSHVVINPGVTIGDNSVIGAGSIVT 165
Cdd:COG1043  16 LGENVEIGPFCVIGPDVEIGDGTVIGSHVVIE 47
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
137-164 3.15e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.85  E-value: 3.15e-03
                          10        20
                  ....*....|....*....|....*...
gi 15829649   137 NVWIGSHVVINPGVTIGDNSVIGAGSIV 164
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVII 28
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 132-182 3.89e-03

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: 37.24  E-value: 3.89e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 15829649   132 ITIGNNVWIGSHVVINPGVTIGDNSVIGAGSIVtKDIPPNVVAAGVPCRVI 182
Cdd:TIGR01852  29 VKIGDGVELKSHVVILGHTTIGEGTRIFPGAVI-GGVPQDLKYKGEKTRLI 78
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 95-186 4.23e-03

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: 36.85  E-value: 4.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829649    95 TVTIGDNVLIAPNVtlsvtgHPVHHelrkngemysfpITIGNNVWIGSHVVINPGVTIGDN------------------S 156
Cdd:TIGR01852 101 VTRIGNNNLLMAYS------HIAHD------------CVVGNHVILANNATLAGHVEVGDYaiigglvavhqfvrigryA 162

                          90       100       110
                  ....*....|....*....|....*....|
gi 15829649   157 VIGAGSIVTKDIPPNVVAAGVPCRvIREIN 186
Cdd:TIGR01852 163 MIGGLSAVSKDVPPYCLAEGNRAR-LRGLN 191
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 133-162 5.52e-03

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 37.15  E-value: 5.52e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 15829649  133 TIGNNVWIGSHVVINPGVTIGDNSVIGAGS 162
Cdd:PRK14353 270 VIGRDVVIEPNVVFGPGVTVASGAVIHAFS 299
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 131-169 5.72e-03

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


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 36.71  E-value: 5.72e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 15829649  131 PITIGNNVWIGSHVVINPGVTIGDNSVIGAGSIVTKDIP 169
Cdd:PRK11830 176 PVIIEDNCFIGARSEVVEGVIVEEGSVLGMGVFLGQSTK 214
 
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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