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Conserved domains on  [gi|2731393433|ref|WP_345495404|]
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MULTISPECIES: DapH/DapD/GlmU-related protein [Brucella]

Protein Classification

LbetaH domain-containing protein( domain architecture ID 372)

LbetaH (left-handed parallel beta-helix) domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LbetaH super family cl00160
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 12-209 1.43e-103

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.


The actual alignment was detected with superfamily member TIGR03308:

Pssm-ID: 469633 [Multi-domain]  Cd Length: 204  Bit Score: 297.07  E-value: 1.43e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731393433  12 SEPHIHSTAQLKSVKLGRYADIGERMILREVTVGDFTYFERNGEGIYAEIGKFCSIAANVRINALEHPMERLTTHKVSYR 91
Cdd:TIGR03308   7 PEPTLHPTAELTESKLGRYTEIGERTRLREVALGDYSYVMRDCDIIYTTIGKFCSIAAMVRINATNHPMERPTLHHFTYR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731393433  92 PNEYFRYLGVDGDFRARRQARRVVIGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDVAPYLVVGGVPARLIRKRFSDA 171
Cdd:TIGR03308  87 AAMYFDDASDDADFFAWRRAKRVTIGHDVWIGHGAVILPGVTIGNGAVIAAGAVVTKDVAPYTIVAGVPAKLIRRRFPPE 166

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2731393433 172 VIARLLALSWWDWPVEKLYEAVPDIQALEIEAFLEKWG 209
Cdd:TIGR03308 167 IAARIEALAWWDWDHETLREALPDFRDLPAEAFLDKYE 204
 
Name Accession Description Interval E-value
phn_thr-fam TIGR03308
phosphonate metabolism protein, transferase hexapeptide repeat family; This family of proteins ...
 12-209 1.43e-103

phosphonate metabolism protein, transferase hexapeptide repeat family; This family of proteins contains copies of the Bacterial transferase hexapeptide repeat family (pfam00132) and is only found in operons encoding the phosphonate C-P lyase system (GenProp0232). Many C-P lyase operons, however, lack a homolog of this protein.


Pssm-ID: 132351 [Multi-domain]  Cd Length: 204  Bit Score: 297.07  E-value: 1.43e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731393433  12 SEPHIHSTAQLKSVKLGRYADIGERMILREVTVGDFTYFERNGEGIYAEIGKFCSIAANVRINALEHPMERLTTHKVSYR 91
Cdd:TIGR03308   7 PEPTLHPTAELTESKLGRYTEIGERTRLREVALGDYSYVMRDCDIIYTTIGKFCSIAAMVRINATNHPMERPTLHHFTYR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731393433  92 PNEYFRYLGVDGDFRARRQARRVVIGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDVAPYLVVGGVPARLIRKRFSDA 171
Cdd:TIGR03308  87 AAMYFDDASDDADFFAWRRAKRVTIGHDVWIGHGAVILPGVTIGNGAVIAAGAVVTKDVAPYTIVAGVPAKLIRRRFPPE 166

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2731393433 172 VIARLLALSWWDWPVEKLYEAVPDIQALEIEAFLEKWG 209
Cdd:TIGR03308 167 IAARIEALAWWDWDHETLREALPDFRDLPAEAFLDKYE 204
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 41-185 7.20e-63

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: 191.99  E-value: 7.20e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731393433  41 EVTVGDFTYFERNG---EGIYAEIGKFCSIAANVRINA-LEHPMERLTTHKVSYRPNEYFRylgvDGDFRARRQARRVVI 116
Cdd:cd03349     1 NISVGDYSYGSGPDcdvGGDKLSIGKFCSIAPGVKIGLgGNHPTDWVSTYPFYIFGGEWED----DAKFDDWPSKGDVII 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2731393433 117 GNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDVAPYLVVGGVPARLIRKRFSDAVIARLLALSWWDWP 185
Cdd:cd03349    77 GNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRYRFDEETIERLLALKWWDWP 145
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
25-170 2.17e-38

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 129.22  E-value: 2.17e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731393433  25 VKLGRYADIGERMILR--EVTVGDFTYFERN-----GEGIyaEIGKFCSIAANVRINALEHPMERLTTHKVSYRPneyfr 97
Cdd:COG0110     9 ARIGDGVVIGPGVRIYggNITIGDNVYIGPGvtiddPGGI--TIGDNVLIGPGVTILTGNHPIDDPATFPLRTGP----- 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2731393433  98 ylgvdgdfrarrqarrVVIGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDVAPYLVVGGVPARLIRKRFSD 170
Cdd:COG0110    82 ----------------VTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEE 138
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 61-166 2.90e-17

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 76.58  E-value: 2.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731393433  61 IGKFCSIAANVRINALEHPMerlttHKVSYRPNEYFRYlgvdgdfrarrqarRVVIGNDVWIGHGAVITPGVVIGHGAVI 140
Cdd:PRK09527   98 IGDNVLIAPNVTLSVTGHPV-----HHELRKNGEMYSF--------------PITIGNNVWIGSHVVINPGVTIGDNSVI 158

                          90       100
                  ....*....|....*....|....*.
gi 2731393433 141 GANAVVTRDVAPYLVVGGVPARLIRK 166
Cdd:PRK09527  159 GAGSVVTKDIPPNVVAAGVPCRVIRE 184
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
116-142 1.11e-06

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 43.48  E-value: 1.11e-06
                          10        20
                  ....*....|....*....|....*..
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGA 142
Cdd:pfam00132   4 IGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
phn_thr-fam TIGR03308
phosphonate metabolism protein, transferase hexapeptide repeat family; This family of proteins ...
 12-209 1.43e-103

phosphonate metabolism protein, transferase hexapeptide repeat family; This family of proteins contains copies of the Bacterial transferase hexapeptide repeat family (pfam00132) and is only found in operons encoding the phosphonate C-P lyase system (GenProp0232). Many C-P lyase operons, however, lack a homolog of this protein.


Pssm-ID: 132351 [Multi-domain]  Cd Length: 204  Bit Score: 297.07  E-value: 1.43e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731393433  12 SEPHIHSTAQLKSVKLGRYADIGERMILREVTVGDFTYFERNGEGIYAEIGKFCSIAANVRINALEHPMERLTTHKVSYR 91
Cdd:TIGR03308   7 PEPTLHPTAELTESKLGRYTEIGERTRLREVALGDYSYVMRDCDIIYTTIGKFCSIAAMVRINATNHPMERPTLHHFTYR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731393433  92 PNEYFRYLGVDGDFRARRQARRVVIGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDVAPYLVVGGVPARLIRKRFSDA 171
Cdd:TIGR03308  87 AAMYFDDASDDADFFAWRRAKRVTIGHDVWIGHGAVILPGVTIGNGAVIAAGAVVTKDVAPYTIVAGVPAKLIRRRFPPE 166

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2731393433 172 VIARLLALSWWDWPVEKLYEAVPDIQALEIEAFLEKWG 209
Cdd:TIGR03308 167 IAARIEALAWWDWDHETLREALPDFRDLPAEAFLDKYE 204
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 41-185 7.20e-63

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: 191.99  E-value: 7.20e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731393433  41 EVTVGDFTYFERNG---EGIYAEIGKFCSIAANVRINA-LEHPMERLTTHKVSYRPNEYFRylgvDGDFRARRQARRVVI 116
Cdd:cd03349     1 NISVGDYSYGSGPDcdvGGDKLSIGKFCSIAPGVKIGLgGNHPTDWVSTYPFYIFGGEWED----DAKFDDWPSKGDVII 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2731393433 117 GNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDVAPYLVVGGVPARLIRKRFSDAVIARLLALSWWDWP 185
Cdd:cd03349    77 GNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRYRFDEETIERLLALKWWDWP 145
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
25-170 2.17e-38

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 129.22  E-value: 2.17e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731393433  25 VKLGRYADIGERMILR--EVTVGDFTYFERN-----GEGIyaEIGKFCSIAANVRINALEHPMERLTTHKVSYRPneyfr 97
Cdd:COG0110     9 ARIGDGVVIGPGVRIYggNITIGDNVYIGPGvtiddPGGI--TIGDNVLIGPGVTILTGNHPIDDPATFPLRTGP----- 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2731393433  98 ylgvdgdfrarrqarrVVIGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDVAPYLVVGGVPARLIRKRFSD 170
Cdd:COG0110    82 ----------------VTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEE 138
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 33-164 1.50e-28

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: 103.31  E-value: 1.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731393433  33 IGERmilreVTVGDFTYFErNGEGIyaEIGKFCSIAANVRINALEHPM---ERLTTHKVSYRPneyfrylgvdgdfrarr 109
Cdd:cd04647     4 IGDN-----VYIGPGCVIS-AGGGI--TIGDNVLIGPNVTIYDHNHDIddpERPIEQGVTSAP----------------- 58

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2731393433 110 qarrVVIGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDVAPYLVVGGVPARLI 164
Cdd:cd04647    59 ----IVIGDDVWIGANVVILPGVTIGDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 29-164 8.65e-23

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: 90.17  E-value: 8.65e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731393433  29 RYADIGERM-ILREV--TVGDFTYFE--------RN---GEGIYA------------EIGKFCSIAANVRINALEHPMEr 82
Cdd:cd03357    27 PPSDAEERReLLKELfgSVGENVYIEppfhcdygYNihiGDNFYAnfnctildvapvTIGDNVLIGPNVQIYTAGHPLD- 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731393433  83 lttHKVSYRPNEYFRylgvdgdfrarrqarRVVIGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDVAPYLVVGGVPAR 162
Cdd:cd03357   106 ---PEERNRGLEYAK---------------PITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPAR 167


                  ..
gi 2731393433 163 LI 164
Cdd:cd03357   168 VI 169
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 116-167 1.04e-17

Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440667 [Multi-domain]  Cd Length: 174  Bit Score: 76.66  E-value: 1.04e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDVAPYLVVGGVPARLIRKR 167
Cdd:COG1045   120 IGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVKRK 171
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 61-166 2.90e-17

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 76.58  E-value: 2.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731393433  61 IGKFCSIAANVRINALEHPMerlttHKVSYRPNEYFRYlgvdgdfrarrqarRVVIGNDVWIGHGAVITPGVVIGHGAVI 140
Cdd:PRK09527   98 IGDNVLIAPNVTLSVTGHPV-----HHELRKNGEMYSF--------------PITIGNNVWIGSHVVINPGVTIGDNSVI 158

                          90       100
                  ....*....|....*....|....*.
gi 2731393433 141 GANAVVTRDVAPYLVVGGVPARLIRK 166
Cdd:PRK09527  159 GAGSVVTKDIPPNVVAAGVPCRVIRE 184
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 61-166 3.35e-17

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 76.01  E-value: 3.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731393433  61 IGKFCSIAANVRINALEHPMErlTTHKVSYRpnEYFRYLgvdgdfrarrqarrvVIGNDVWIGHGAVITPGVVIGHGAVI 140
Cdd:PRK10092   96 IGDNCMLAPGVHIYTATHPLD--PVARNSGA--ELGKPV---------------TIGNNVWIGGRAVINPGVTIGDNVVV 156

                          90       100
                  ....*....|....*....|....*.
gi 2731393433 141 GANAVVTRDVAPYLVVGGVPARLIRK 166
Cdd:PRK10092  157 ASGAVVTKDVPDNVVVGGNPARIIKK 182
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 116-165 1.69e-15

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: 69.45  E-value: 1.69e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDVAPYLVVGGVPARLIR 165
Cdd:cd03358    70 VKRGASIGANATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 116-160 6.17e-14

Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetylserine, as the first step of a two-step biosynthetic pathway in bacteria and plants leading to the formation of L-cysteine. This reaction represents a key metabolic point of regulation for the cysteine biosynthetic pathway due to its feedback inhibition by cysteine. The enzyme is a 175 kDa homohexamer, composed of a dimer of homotrimers. Each subunit contains an N-terminal alpha helical region and a C-terminal left-handed beta-helix (LbH) subdomain with 5 turns, each containing a hexapeptide repeat motif characteristic of the acyltransferase superfamily of enzymes. The trimer interface mainly involves the C-terminal LbH subdomain while the dimer (of trimers) interface is mediated by the N-terminal alpha helical subdomain.


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 64.77  E-value: 6.17e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDVAPYLVVGGVP 160
Cdd:cd03354    57 IGDNVVIGAGAKILGNITIGDNVKIGANAVVTKDVPANSTVVGVP 101
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 16-161 1.49e-13

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: 66.36  E-value: 1.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731393433  16 IHSTAQL-KSVKLGRYADIGER-MILREVTVGDF------TYFERNgegiyAEIGKFCSIAANVRINAlehpmerltthk 87
Cdd:TIGR03570  90 IHPSAIVsPSASIGEGTVIMAGaVINPDVRIGDNviintgAIVEHD-----CVIGDFVHIAPGVTLSG------------ 152

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2731393433  88 vsyrpneyfrylGVdgdfrarrqarrvVIGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDVAPYLVVGGVPA 161
Cdd:TIGR03570 153 ------------GV-------------VIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 116-167 2.19e-13

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 65.67  E-value: 2.19e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDVAPYLVVGGVPARLIRKR 167
Cdd:PRK09677  133 IGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKKY 184
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 116-164 2.65e-13

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: 63.39  E-value: 2.65e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDVAPYLVVGGVPARLI 164
Cdd:cd05825    59 IGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 16-160 1.61e-12

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: 63.27  E-value: 1.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731393433  16 IHSTAQL-KSVKLGRYADIGER-MILREVTVGDFTYFerNgegIYA------EIGKFCSIAANVRINAlehpmerltthk 87
Cdd:cd03360    87 IHPSAVVsPSAVIGEGCVIMAGaVINPDARIGDNVII--N---TGAvighdcVIGDFVHIAPGVVLSG------------ 149

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2731393433  88 vsyrpneyfrylGVdgdfrarrqarrvVIGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDVAPYLVVGGVP 160
Cdd:cd03360   150 ------------GV-------------TIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
PRK10502 PRK10502
putative acyl transferase; Provisional
 116-168 2.11e-12

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 63.04  E-value: 2.11e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDVAPYLVVGGVPARLIRKRF 168
Cdd:PRK10502  127 IGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIRPRV 179
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 116-166 7.52e-11

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: 58.19  E-value: 7.52e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVT--RDVAPYLVVGGVPARLIRK 166
Cdd:cd04645    80 IGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPpgKVIPPGSLVAGSPAKVVRE 132
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 116-176 1.02e-10

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 58.11  E-value: 1.02e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVT--RDVAPYLVVGGVPARLIRKRfSDAVIARL 176
Cdd:COG0663    91 IGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTegKVVPPGSLVVGSPAKVVREL-TEEEIAFL 152
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 59-147 2.34e-09

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: 52.25  E-value: 2.34e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731393433  59 AEIGKFCSIAANVRINALEHPMERLTTHkvsyrpneyfrylgvdgdfrarrqarrvvIGNDVWIGHGAVITPGVVIGHGA 138
Cdd:cd00208    19 VVIGDNVNIGPGAVIGAATGPNEKNPTI-----------------------------IGDNVEIGANAVIHGGVKIGDNA 69


                  ....*....
gi 2731393433 139 VIGANAVVT 147
Cdd:cd00208    70 VIGAGAVVT 78
cysE PRK11132
serine acetyltransferase; Provisional
 120-170 2.78e-08

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 52.39  E-value: 2.78e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2731393433 120 VWIGHGAVITPGVVIGHGAVIGANAVVTRDVAPYLVVGGVPARLIRKRFSD 170
Cdd:PRK11132  200 VMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVGKPESD 250
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 116-176 7.46e-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: 51.28  E-value: 7.46e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDVAPYLVVGGVPARLI--------RKRFSDAVIARL 176
Cdd:cd03351   141 IGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARLRglnlvglkRRGFSREEIRAL 209
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 116-176 7.61e-08

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 51.17  E-value: 7.61e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDVAPYLVVGGVPARLI--------RKRFSDAVIARL 176
Cdd:COG1043   143 VGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDVPPYVLAAGNPARLRglnlvglkRRGFSREQIRAL 211
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 116-166 9.09e-08

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 50.48  E-value: 9.09e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDVAPYLVVGGVPARLIRK 166
Cdd:cd03352   153 IGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQPHRE 203
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 116-150 9.86e-08

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 51.17  E-value: 9.86e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDV 150
Cdd:COG1044   111 IGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGV 145
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 116-166 1.17e-07

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: 49.49  E-value: 1.17e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVT--RDVAPYLVVGGVPARLIRK 166
Cdd:cd04650    81 VGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTpgKEIPDYSLVLGVPAKVVRK 133
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 116-150 2.24e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 50.14  E-value: 2.24e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDV 150
Cdd:PRK00892  115 IGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGV 149
PLN02357 PLN02357
serine acetyltransferase
 116-164 4.92e-07

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 49.11  E-value: 4.92e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDVAPYLVVGGVPARLI 164
Cdd:PLN02357  281 IGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLI 329
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 116-150 6.49e-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: 47.79  E-value: 6.49e-07
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDV 150
Cdd:cd03352     4 IGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGV 38
PLN02694 PLN02694
serine O-acetyltransferase
 116-164 6.68e-07

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 48.49  E-value: 6.68e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDVAPYLVVGGVPARLI 164
Cdd:PLN02694  215 IGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLV 263
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
116-142 1.11e-06

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 43.48  E-value: 1.11e-06
                          10        20
                  ....*....|....*....|....*..
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGA 142
Cdd:pfam00132   4 IGDNVLIGPNAVIGGGVIIGDNVIIGA 30
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
116-176 3.95e-06

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 46.24  E-value: 3.95e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDVAPYLVVGGVPARLI--------RKRFSDAVIARL 176
Cdd:PRK05289  144 VGDYAIIGGLTAVHQFVRIGAHAMVGGMSGVSQDVPPYVLAEGNPARLRglnlvglkRRGFSREEIHAL 212
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 116-164 3.98e-06

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


Pssm-ID: 100049 [Multi-domain]  Cd Length: 161  Bit Score: 45.28  E-value: 3.98e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVvtrdVAPYLVVGGVPARLI 164
Cdd:cd03359    98 IGKNCVIGRRCIIKDCVKILDGTVVPPDTV----IPPYSVVSGRPARFI 142
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 116-150 1.05e-05

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: 45.01  E-value: 1.05e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDV 150
Cdd:COG1044   129 IGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERC 163
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 116-145 1.16e-05

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: 45.01  E-value: 1.16e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAV 145
Cdd:COG1044   123 IGAGVVIGDGVVIGPGVVIGDGVVIGDDCV 152
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 116-164 1.31e-05

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 45.02  E-value: 1.31e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDVAP-YLVVGGVPARLI 164
Cdd:PRK09451  397 IGDDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDVAEnELVISRVPQRHI 446
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 116-150 3.00e-05

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: 43.17  E-value: 3.00e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDV 150
Cdd:cd03352    22 IGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGC 56
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
116-160 4.24e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 43.16  E-value: 4.24e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRD--------VAPYLVVGGVP 160
Cdd:PRK05289   17 IGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHttigknnrIFPFASIGEDP 69
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 116-160 4.30e-05

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 43.08  E-value: 4.30e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRD--------VAPYLVVGGVP 160
Cdd:COG1043    16 LGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPttigknnrIFPFASIGEEP 68
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 116-146 5.21e-05

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: 42.40  E-value: 5.21e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVV 146
Cdd:cd03352    16 IGEGVVIGDGVVIGPGVVIGDGVVIGDDCVI 46
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 116-150 7.28e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 42.43  E-value: 7.28e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDV 150
Cdd:PRK00892  133 IGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAV 167
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 116-160 8.64e-05

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


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 42.03  E-value: 8.64e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRD--------VAPYLVVGGVP 160
Cdd:cd03351    14 IGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPttigknnrIFPFASIGEAP 66
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 13-146 1.09e-04

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 41.93  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731393433  13 EPHIHSTAQL-KSVKLGRyadigermilrEVTVGDFTYFERNgegiyAEIGKFCSIAANVrinalehpmerltthkvsyr 91
Cdd:COG1044    96 APGIHPSAVIdPSAKIGE-----------GVSIGPFAVIGAG-----VVIGDGVVIGPGV-------------------- 139

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2731393433  92 pneyfrylgvdgdfrarrqarrvVIGNDVWIGHGAVITPGVVIGHGAVIGANAVV 146
Cdd:COG1044   140 -----------------------VIGDGVVIGDDCVLHPNVTIYERCVIGDRVII 171
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 116-157 1.14e-04

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 41.93  E-value: 1.14e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVvtrdVAPYLVVG 157
Cdd:COG1044   105 IDPSAKIGEGVSIGPFAVIGAGVVIGDGVV----IGPGVVIG 142
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 116-176 1.22e-04

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 41.93  E-value: 1.22e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDVAPYLVVGGVPARLIRK-RFSDAVIARL 176
Cdd:COG1044   261 IGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSGSPAQPHREwLRNAAALRRL 322
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 116-175 1.65e-04

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: 40.43  E-value: 1.65e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVTR--DVAPYLVVGGVPARLIRkRFSDAVIAR 175
Cdd:cd04745    81 IGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAgtVIPPRSLIAGSPAKVIR-ELSDEEVAW 141
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 116-178 3.25e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 40.51  E-value: 3.25e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDV-APYLVVGGVPARLIRKRFSDAVIARLLA 178
Cdd:PRK00892  264 IGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIpEPGEYSSGIPAQPNKEWLRTAARLRRLD 327
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 116-146 5.50e-04

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 39.31  E-value: 5.50e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVV 146
Cdd:cd03352    34 IGDGVVIGDDCVIHPNVTIYEGCIIGDRVII 64
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 116-164 5.68e-04

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: 40.01  E-value: 5.68e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2731393433 116 IGNDVWIG-HGAVITPgVVIGHGAVIGANAVVTRDVAPY-LVVGGVPARLI 164
Cdd:COG1207   397 IGDGAFIGsNTNLVAP-VTIGDGATIGAGSTITKDVPAGaLAIARARQRNI 446
PLN02739 PLN02739
serine acetyltransferase
 116-165 6.28e-04

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 40.02  E-value: 6.28e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDVAPYLVVGGVPARLIR 165
Cdd:PLN02739  260 IGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIG 309
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 59-162 6.34e-04

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


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 38.52  E-value: 6.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731393433  59 AEIGKFCSIAANVRINALEHPMERLTThkvsyrpneyfrylgvdgdfrarrqarrvVIGNDVWIGHGAVITPGVVIGHGA 138
Cdd:cd03350    50 AQIGKNVHLSAGAVIGGVLEPLQATPV-----------------------------IIEDDVFIGANCEVVEGVIVGKGA 100

                          90       100       110
                  ....*....|....*....|....*....|
gi 2731393433 139 VIGANAVVTRDVAPYLVVGG------VPAR 162
Cdd:cd03350   101 VLAAGVVLTQSTPIYDRETGeiyygrVPPG 130
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 116-146 1.06e-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: 38.54  E-value: 1.06e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVV 146
Cdd:cd03352    40 IGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 116-157 1.24e-03

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: 38.17  E-value: 1.24e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDVAPY-LVVG 157
Cdd:cd03353   147 IGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGaLAIA 189
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 116-162 1.46e-03

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


Pssm-ID: 441774 [Multi-domain]  Cd Length: 268  Bit Score: 38.56  E-value: 1.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDVAPYLVVGG------VPAR 162
Cdd:COG2171   173 IEDNCFIGARSGVVEGVIVGEGAVLGAGVYLTASTKIYDRVTGevyygrVPAG 225
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 116-146 2.07e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 38.20  E-value: 2.07e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVV 146
Cdd:PRK00892  109 IDPSAKIGEGVSIGPNAVIGAGVVIGDGVVI 139
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
116-148 2.58e-03

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 34.34  E-value: 2.58e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2731393433 116 IGNDVWIGHGAVItpGVVIGHGAVIGANAVVTR 148
Cdd:pfam14602   3 IGDNCLIGANSGI--GVSLGDNCVVGAGVVITA 33
PLN02296 PLN02296
carbonate dehydratase
 116-166 2.72e-03

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 37.80  E-value: 2.72e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731393433 116 IGNDVWIGHGAVI-----------------TPGVVIGHGAVIGANAVVTRD--VAPYLVVGGVPARLIRK 166
Cdd:PLN02296  122 IGDNVTIGHSAVLhgctvedeafvgmgatlLDGVVVEKHAMVAAGALVRQNtrIPSGEVWAGNPAKFLRK 191
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 116-173 4.77e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 36.92  E-value: 4.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVV------------------TRDVAPYLVVGGVPAR--------LIRKRFS 169
Cdd:PRK12461  122 IGNNVILVNGALLAGHVTVGDRAIISGNCLVhqfcrigalammaggsriSKDVPPYCMMAGHPTNvhglnavgLRRRGFS 201


                  ....
gi 2731393433 170 DAVI 173
Cdd:PRK12461  202 SRAI 205
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 116-162 5.03e-03

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


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 37.09  E-value: 5.03e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDVAPYLVV------GGVPAR 162
Cdd:PRK11830  179 IEDNCFIGARSEVVEGVIVEEGSVLGMGVFLGQSTKIYDREtgevhyGRVPAG 231
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 122-157 5.88e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 37.04  E-value: 5.88e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2731393433 122 IGHGAVITPGVVIGHGAVIGANAVVTRDV--APYLVVG 157
Cdd:PRK00892  109 IDPSAKIGEGVSIGPNAVIGAGVVIGDGVviGAGAVIG 146
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 116-150 8.17e-03

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 36.63  E-value: 8.17e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2731393433 116 IGNDVWIGHGAVITPGVVIGHGAVIGANAVVTRDV 150
Cdd:PRK14356  401 IGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDV 435
 
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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