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Conserved domains on  [gi|2475280252|emb|CAI8295817|]
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MAG: Putative acetyltransferase [Acidimicrobiaceae bacterium]

Protein Classification

acyltransferase( domain architecture ID 10140306)

acyltransferase belonging to the transferase hexapeptide repeat family, catalyzes the transfer of an acyl group from an acyl-CoA to a substrate; similar to Neisseria meningitidis polysialic acid O-acetyltransferase

CATH:  2.160.10.10
EC:  2.3.1.-
Gene Ontology:  GO:0016746|GO:0120225
PubMed:  15500694

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 91-199 9.93e-39

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: 129.50  E-value: 9.93e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  91 VRIGDRCLIGRGTSIIGHLAIEIGDDVFTGMNVYITDQNHGYENLDEPIgKQLPNEQPVSIGEGAWIGSGAIILPGSKIG 170
Cdd:cd04647     2 ISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDHNHDIDDPERPI-EQGVTSAPIVIGDDVWIGANVVILPGVTIG 80

                          90       100
                  ....*....|....*....|....*....
gi 2475280252 171 NHVVIGANSVVTGEIPSYSVAVGSPAKVV 199
Cdd:cd04647    81 DGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
 
Name Accession Description Interval E-value
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 91-199 9.93e-39

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: 129.50  E-value: 9.93e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  91 VRIGDRCLIGRGTSIIGHLAIEIGDDVFTGMNVYITDQNHGYENLDEPIgKQLPNEQPVSIGEGAWIGSGAIILPGSKIG 170
Cdd:cd04647     2 ISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDHNHDIDDPERPI-EQGVTSAPIVIGDDVWIGANVVILPGVTIG 80

                          90       100
                  ....*....|....*....|....*....
gi 2475280252 171 NHVVIGANSVVTGEIPSYSVAVGSPAKVV 199
Cdd:cd04647    81 DGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
63-200 7.14e-38

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 128.45  E-value: 7.14e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  63 IGEDVLIAADVTlsagmgpgqemITDPVVRIGDRCLIGRGTSIIGHLAIEIGDDVFTGMNVYITDQNHGYENLDEPIGKq 142
Cdd:COG0110    11 IGDGVVIGPGVR-----------IYGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPATFPLR- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2475280252 143 lpnEQPVSIGEGAWIGSGAIILPGSKIGNHVVIGANSVVTGEIPSYSVAVGSPAKVVR 200
Cdd:COG0110    79 ---TGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIR 133
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 69-208 1.19e-27

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 103.80  E-value: 1.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  69 IAADVTLSAGMGPGQEMITDPVVRIGDRCLIGRGTSIIGHLAIEIGDDVFTGMNVYITDQNHGyeNLDEPIGKQLPN--- 145
Cdd:PRK09677   44 INFGEGFTSGVGLRLDAFGRGKLFFGDNVQVNDYVHIACIESITIGRDTLIASKVFITDHNHG--SFKHSDDFSSPNlpp 121

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2475280252 146 ------EQPVSIGEGAWIGSGAIILPGSKIGNHVVIGANSVVTGEIPSYSVAVGSPAKVVRLYD--GNSWE 208
Cdd:PRK09677  122 dmrtleSSAVVIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKKYNheTKLWE 192
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 63-196 1.86e-16

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: 74.45  E-value: 1.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  63 IGEDVLIAADVTLSAGmgpgqemitdpvVRIGDRCLIgRGTSIIGHLAIeIGDDVFTGMNVYITdqnhGYenldepigkq 142
Cdd:TIGR03570 102 IGEGTVIMAGAVINPD------------VRIGDNVII-NTGAIVEHDCV-IGDFVHIAPGVTLS----GG---------- 153

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2475280252 143 lpneqpVSIGEGAWIGSGAIILPGSKIGNHVVIGANSVVTGEIPSYSVAVGSPA 196
Cdd:TIGR03570 154 ------VVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
148-177 2.07e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 40.40  E-value: 2.07e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 2475280252 148 PVSIGEGAWIGSGAIILPGSKIGNHVVIGA 177
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 91-199 9.93e-39

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: 129.50  E-value: 9.93e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  91 VRIGDRCLIGRGTSIIGHLAIEIGDDVFTGMNVYITDQNHGYENLDEPIgKQLPNEQPVSIGEGAWIGSGAIILPGSKIG 170
Cdd:cd04647     2 ISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDHNHDIDDPERPI-EQGVTSAPIVIGDDVWIGANVVILPGVTIG 80

                          90       100
                  ....*....|....*....|....*....
gi 2475280252 171 NHVVIGANSVVTGEIPSYSVAVGSPAKVV 199
Cdd:cd04647    81 DGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
63-200 7.14e-38

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 128.45  E-value: 7.14e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  63 IGEDVLIAADVTlsagmgpgqemITDPVVRIGDRCLIGRGTSIIGHLAIEIGDDVFTGMNVYITDQNHGYENLDEPIGKq 142
Cdd:COG0110    11 IGDGVVIGPGVR-----------IYGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPATFPLR- 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2475280252 143 lpnEQPVSIGEGAWIGSGAIILPGSKIGNHVVIGANSVVTGEIPSYSVAVGSPAKVVR 200
Cdd:COG0110    79 ---TGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIR 133
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 69-208 1.19e-27

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 103.80  E-value: 1.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  69 IAADVTLSAGMGPGQEMITDPVVRIGDRCLIGRGTSIIGHLAIEIGDDVFTGMNVYITDQNHGyeNLDEPIGKQLPN--- 145
Cdd:PRK09677   44 INFGEGFTSGVGLRLDAFGRGKLFFGDNVQVNDYVHIACIESITIGRDTLIASKVFITDHNHG--SFKHSDDFSSPNlpp 121

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2475280252 146 ------EQPVSIGEGAWIGSGAIILPGSKIGNHVVIGANSVVTGEIPSYSVAVGSPAKVVRLYD--GNSWE 208
Cdd:PRK09677  122 dmrtleSSAVVIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKKYNheTKLWE 192
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 91-199 5.86e-27

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: 101.34  E-value: 5.86e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  91 VRIGDRCLIGRGTSIIGHLAIEIGDDVFTGMNVYITDQNH---------GYEnldepIGKqlpneqPVSIGEGAWIGSGA 161
Cdd:cd03357    63 IHIGDNFYANFNCTILDVAPVTIGDNVLIGPNVQIYTAGHpldpeernrGLE-----YAK------PITIGDNVWIGGGV 131

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2475280252 162 IILPGSKIGNHVVIGANSVVTGEIPSYSVAVGSPAKVV 199
Cdd:cd03357   132 IILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 91-200 4.44e-23

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: 90.30  E-value: 4.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  91 VRIGDRCLIGRGTSIIGHLAIEIGDDVFTGMNVYI-TDQNH-------------GYENLDEPIGKQLPNEQPVSIGEGAW 156
Cdd:cd03349     2 ISVGDYSYGSGPDCDVGGDKLSIGKFCSIAPGVKIgLGGNHptdwvstypfyifGGEWEDDAKFDDWPSKGDVIIGNDVW 81

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2475280252 157 IGSGAIILPGSKIGNHVVIGANSVVTGEIPSYSVAVGSPAKVVR 200
Cdd:cd03349    82 IGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIR 125
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 63-200 1.83e-22

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: 87.94  E-value: 1.83e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  63 IGEDVLIAADVTLSAGmgpgqemitdpvVRIGDRCLIGRGTSIIGHLaiEIGDDVFTGMNVYITDQNHgyenldePIGKQ 142
Cdd:cd03358     1 IGDNCIIGTNVFIEND------------VKIGDNVKIQSNVSIYEGV--TIEDDVFIGPNVVFTNDLY-------PRSKI 59

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252 143 LPNE--QPVSIGEGAWIGSGAIILPGSKIGNHVVIGANSVVTGEIPSYSVAVGSPAKVVR 200
Cdd:cd03358    60 YRKWelKGTTVKRGASIGANATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 91-199 1.18e-19

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: 80.34  E-value: 1.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  91 VRIGDRCLIGRGTSIIGHLAIEIGDDVFTGMNVYITDQNHGYENLDEPIgkqlpNEQPVSIGEGAWIGSGAIILPGSKIG 170
Cdd:cd05825     4 LTIGDNSWIGEGVWIYNLAPVTIGSDACISQGAYLCTGSHDYRSPAFPL-----ITAPIVIGDGAWVAAEAFVGPGVTIG 78

                          90       100
                  ....*....|....*....|....*....
gi 2475280252 171 NHVVIGANSVVTGEIPSYSVAVGSPAKVV 199
Cdd:cd05825    79 EGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 63-195 8.74e-19

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: 80.61  E-value: 8.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  63 IGEDVLIAADVTLSAGmgpgqemitdpvVRIGDRCLIGRGtSIIGHLAIeIGDDVFTGMNVYITdqnhGYenldepigkq 142
Cdd:cd03360    99 IGEGCVIMAGAVINPD------------ARIGDNVIINTG-AVIGHDCV-IGDFVHIAPGVVLS----GG---------- 150

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2475280252 143 lpneqpVSIGEGAWIGSGAIILPGSKIGNHVVIGANSVVTGEIPSYSVAVGSP 195
Cdd:cd03360   151 ------VTIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 63-200 1.00e-18

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 79.69  E-value: 1.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  63 IGEDVLIAADVTLSAGMGPgqemitdpvVRIGDRCLIGRGTSIigH----LAIEIGDDVFTGMNVYItdqnHGyenldep 138
Cdd:COG0663    31 IGEDVSVWPGAVLRGDVGP---------IRIGEGSNIQDGVVL--HvdpgYPLTIGDDVTIGHGAIL----HG------- 88

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2475280252 139 igkqlpneqpVSIGEGAWIGSGAIILPGSKIGNHVVIGANSVVTG--EIPSYSVAVGSPAKVVR 200
Cdd:COG0663    89 ----------CTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEgkVVPPGSLVVGSPAKVVR 142
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 63-200 1.74e-18

Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 78.61  E-value: 1.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  63 IGEDVLIAADVTLSAGMGPgqemitdpvVRIGDRCLIGRGTSIigHLA----IEIGDDVFTGMNVYItdqnHGyenldep 138
Cdd:cd04645    20 LGEGSSVWFGAVLRGDVNP---------IRIGERTNIQDGSVL--HVDpgypTIIGDNVTVGHGAVL----HG------- 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2475280252 139 igkqlpneqpVSIGEGAWIGSGAIILPGSKIGNHVVIGANSVVTG--EIPSYSVAVGSPAKVVR 200
Cdd:cd04645    78 ----------CTIGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPgkVIPPGSLVAGSPAKVVR 131
PRK10502 PRK10502
putative acyl transferase; Provisional
 56-200 2.07e-18

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 79.22  E-value: 2.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  56 FGEKwiwIGEDVLIAADVTlsagmgpgqemITDP-VVRIGDRCLIGRGTSIIGHLAIEIGDDVFTGMNVYITDQNHGYEN 134
Cdd:PRK10502   50 FGAK---IGKGVVIRPSVR-----------ITYPwKLTIGDYAWIGDDVWLYNLGEITIGAHCVISQKSYLCTGSHDYSD 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2475280252 135 LDEPIgkqlpNEQPVSIGEGAWIGSGAIILPGSKIGNHVVIGANSVVTGEIPSYSVAVGSPAKVVR 200
Cdd:PRK10502  116 PHFDL-----NTAPIVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIR 176
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 63-200 4.81e-17

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 76.20  E-value: 4.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  63 IGEDVLIAADVTLSAGMGpgqemitdpvVRIGDRCLIGRGTSIIGHLAIEIGDDVFTGMNVYITDQNHgyenldePIGKQ 142
Cdd:PRK09527   58 VGENAWVEPPVYFSYGSN----------IHIGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGH-------PVHHE 120

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2475280252 143 LPNEQ-----PVSIGEGAWIGSGAIILPGSKIGNHVVIGANSVVTGEIPSYSVAVGSPAKVVR 200
Cdd:PRK09527  121 LRKNGemysfPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIR 183
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 63-196 1.86e-16

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: 74.45  E-value: 1.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  63 IGEDVLIAADVTLSAGmgpgqemitdpvVRIGDRCLIgRGTSIIGHLAIeIGDDVFTGMNVYITdqnhGYenldepigkq 142
Cdd:TIGR03570 102 IGEGTVIMAGAVINPD------------VRIGDNVII-NTGAIVEHDCV-IGDFVHIAPGVTLS----GG---------- 153

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2475280252 143 lpneqpVSIGEGAWIGSGAIILPGSKIGNHVVIGANSVVTGEIPSYSVAVGSPA 196
Cdd:TIGR03570 154 ------VVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 89-200 1.98e-16

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


Pssm-ID: 440667 [Multi-domain]  Cd Length: 174  Bit Score: 73.58  E-value: 1.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  89 PVVRIGDRCLIGRGTSI-IGHLAiEIGDDVftgmNVYitdQN-----HGYENldepiGKQLPNeqpvsIGEGAWIGSGAI 162
Cdd:COG1045    70 PGATIGRGFFIDHGTGVvIGETA-VIGDNV----TIY---QGvtlggTGKEK-----GKRHPT-----IGDNVVIGAGAK 131

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2475280252 163 ILPGSKIGNHVVIGANSVVTGEIPSYSVAVGSPAKVVR 200
Cdd:COG1045   132 ILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVK 169
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 89-195 2.41e-15

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: 69.01  E-value: 2.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  89 PVVRIGDRCLIGRGTSIIGHLAIEIGDDVFTGMNVYItdqnhgyENLDEPIGKQLPneqpvSIGEGAWIGSGAIILPGSK 168
Cdd:cd03354     7 PGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTL-------GGKGKGGGKRHP-----TIGDNVVIGAGAKILGNIT 74

                          90       100
                  ....*....|....*....|....*..
gi 2475280252 169 IGNHVVIGANSVVTGEIPSYSVAVGSP 195
Cdd:cd03354    75 IGDNVKIGANAVVTKDVPANSTVVGVP 101
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 111-200 2.58e-14

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 68.30  E-value: 2.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252 111 IEIGDDVFTGMNVYITDQNHGYENLDEPIGKQLPneQPVSIGEGAWIGSGAIILPGSKIGNHVVIGANSVVTGEIPSYSV 190
Cdd:PRK10092   94 IRIGDNCMLAPGVHIYTATHPLDPVARNSGAELG--KPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVV 171

                          90
                  ....*....|
gi 2475280252 191 AVGSPAKVVR 200
Cdd:PRK10092  172 VGGNPARIIK 181
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 91-200 8.94e-13

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: 63.74  E-value: 8.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  91 VRIGDRCLIGRGTSIigHLA----IEIGDDVFTGMNVYItdqnHGyenldepigkqlpneqpVSIGEGAWIGSGAIILPG 166
Cdd:cd04650    40 IYIGKYSNVQENVSI--HTDhgypTEIGDYVTIGHNAVV----HG-----------------AKVGNYVIVGMGAILLNG 96

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2475280252 167 SKIGNHVVIGANSVVT--GEIPSYSVAVGSPAKVVR 200
Cdd:cd04650    97 AKIGDHVIIGAGAVVTpgKEIPDYSLVLGVPAKVVR 132
PLN02739 PLN02739
serine acetyltransferase
 89-203 6.75e-11

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 60.82  E-value: 6.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  89 PVVRIGDRCLIGRGTSI-IGHLAIeIGDDVFTGMNVYITDQnhgyenldepiGKQLPNEQPvSIGEGAWIGSGAIILPGS 167
Cdd:PLN02739  210 PAARIGKGILLDHGTGVvIGETAV-IGDRVSILHGVTLGGT-----------GKETGDRHP-KIGDGALLGACVTILGNI 276

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2475280252 168 KIGNHVVIGANSVVTGEIPSYSVAVGSPAKVVRLYD 203
Cdd:PLN02739  277 SIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFVD 312
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 91-182 6.90e-10

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: 53.79  E-value: 6.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  91 VRIGDRCLIGRGTSIIGHlaIEIGDDVFTGMNVYITDQNHGYENldepigkqlpneQPVSIGEGAWIGSGAIILPGSKIG 170
Cdd:cd00208     1 VFIGEGVKIHPKAVIRGP--VVIGDNVNIGPGAVIGAATGPNEK------------NPTIIGDNVEIGANAVIHGGVKIG 66

                          90
                  ....*....|..
gi 2475280252 171 NHVVIGANSVVT 182
Cdd:cd00208    67 DNAVIGAGAVVT 78
PLN02694 PLN02694
serine O-acetyltransferase
 89-199 1.02e-09

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 56.96  E-value: 1.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  89 PVVRIGDRCLIGRGTSIIghlaieIGDDVFTGMNVYITdqnhgYENLDEPIGKQLPNEQPvSIGEGAWIGSGAIILPGSK 168
Cdd:PLN02694  165 PAAKIGKGILFDHATGVV------IGETAVIGNNVSIL-----HHVTLGGTGKACGDRHP-KIGDGVLIGAGATILGNVK 232

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2475280252 169 IGNHVVIGANSVVTGEIPSYSVAVGSPAKVV 199
Cdd:PLN02694  233 IGEGAKIGAGSVVLIDVPPRTTAVGNPARLV 263
PLN02357 PLN02357
serine acetyltransferase
 89-199 2.27e-09

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 56.43  E-value: 2.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  89 PVVRIGDRCLIGRGTSI-IGHLAIeIGDDVFTGMNVYITDQnhgyenldepiGKQLPNEQPvSIGEGAWIGSGAIILPGS 167
Cdd:PLN02357  231 PGAKIGQGILLDHATGVvIGETAV-VGNNVSILHNVTLGGT-----------GKQSGDRHP-KIGDGVLIGAGTCILGNI 297

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2475280252 168 KIGNHVVIGANSVVTGEIPSYSVAVGSPAKVV 199
Cdd:PLN02357  298 TIGEGAKIGAGSVVLKDVPPRTTAVGNPARLI 329
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 91-213 1.38e-08

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: 51.99  E-value: 1.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  91 VRIGDRCLIGRGTSIIGHL-AIEIGDdvftGMNVYITDQNHGYENLDEPIGK--QLPNEQPV---SIGEGAWIGSGAIIL 164
Cdd:cd04745    19 VIIGKNCYIGPHASLRGDFgRIVIRD----GANVQDNCVIHGFPGQDTVLEEngHIGHGAILhgcTIGRNALVGMNAVVM 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2475280252 165 PGSKIGNHVVIGANSVVTGE--IPSYSVAVGSPAKVVRLYDGN--SWERQGIK 213
Cdd:cd04745    95 DGAVIGEESIVGAMAFVKAGtvIPPRSLIAGSPAKVIRELSDEevAWKTRGTK 147
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 91-196 6.04e-08

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: 52.45  E-value: 6.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  91 VRIGDRCLIGrGTSIIGHLAIEIGDDVftGMNVYITDQNHGYEN----LDEpigkqlpneqpVSIGEGAWIGSGAIILPG 166
Cdd:TIGR02353 598 VKIGRGVYID-GTDLTERDLVTIGDDS--TLNEGSVIQTHLFEDrvmkSDT-----------VTIGDGATLGPGAIVLYG 663

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2475280252 167 SKIGNHVVIGANSVVTG--EIPSYSVAVGSPA 196
Cdd:TIGR02353 664 VVMGEGSVLGPDSLVMKgeEVPAHTRWRGNPA 695
cysE PRK11132
serine acetyltransferase; Provisional
 89-199 1.16e-07

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 50.85  E-value: 1.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  89 PVVRIGDRCLIGRGTSI-IGHLAIeIGDDVFTGMNVYITDQnhgyenldepiGKQLPNEQPvSIGEGAWIGSGAIILPGS 167
Cdd:PRK11132  146 PAAKIGRGIMLDHATGIvIGETAV-IENDVSILQSVTLGGT-----------GKTSGDRHP-KIREGVMIGAGAKILGNI 212

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2475280252 168 KIGNHVVIGANSVVTGEIPSYSVAVGSPAKVV 199
Cdd:PRK11132  213 EVGRGAKIGAGSVVLQPVPPHTTAAGVPARIV 244
PRK10191 PRK10191
putative acyl transferase; Provisional
 93-198 6.28e-07

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 47.19  E-value: 6.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  93 IGDRCLIGRGTSIIGHLAIEIGDDvFTgMNVYITDQNHGYENLDEPIgkqlpneqpvsIGEGAWIGSGAIILPGSKIGNH 172
Cdd:PRK10191   50 IGRRFTIHHGYAVVINKNVVAGDD-FT-IRHGVTIGNRGADNMACPH-----------IGNGVELGANVIILGDITIGNN 116

                          90       100
                  ....*....|....*....|....*.
gi 2475280252 173 VVIGANSVVTGEIPSYSVAVGSPAKV 198
Cdd:PRK10191  117 VTVGAGSVVLDSVPDNALVVGEKARV 142
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 91-181 1.03e-06

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 48.48  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  91 VRIGDRCLIGRGTsiighlaiEIGDDVFTGMNVYItdqnhgYENldepigkqlpneqpVSIGEGAWIGSGAIILPGSKIG 170
Cdd:COG1044   115 VSIGPFAVIGAGV--------VIGDGVVIGPGVVI------GDG--------------VVIGDDCVLHPNVTIYERCVIG 166

                          90
                  ....*....|.
gi 2475280252 171 NHVVIGANSVV 181
Cdd:COG1044   167 DRVIIHSGAVI 177
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 91-192 3.81e-06

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


Pssm-ID: 441774 [Multi-domain]  Cd Length: 268  Bit Score: 46.26  E-value: 3.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  91 VRIGDRCLIGRGTSIIGHLaieigddvftgmnvyitdqnhgyenldEPIGKQlpneqPVSIGEGAWIGSGAIILPGSKIG 170
Cdd:COG2171   145 AQIGKNVHLSGGAGIGGVL---------------------------EPLQAA-----PVIIEDNCFIGARSGVVEGVIVG 192

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2475280252 171 NHVVIGANSVVT---------------GEIPSYSVAV 192
Cdd:COG2171   193 EGAVLGAGVYLTastkiydrvtgevyyGRVPAGSVVV 229
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 57-201 8.88e-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: 45.12  E-value: 8.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  57 GEK-WIWIGEDVLIAADVTLSAGMGPGQeMITdpvvRIGDRCLIgRGTSIIGHLAIeIGDDVFTGMNVYITdqnhGYenl 135
Cdd:cd03351    73 GEPtRLEIGDNNTIREFVTIHRGTAQGG-GVT----RIGNNNLL-MAYVHVAHDCV-IGNNVILANNATLA----GH--- 138

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2475280252 136 depigkqlpneqpVSIGEGAWIGSGAIILPGSKIGNHVVIGANSVVTGEIPSYSVAVGSPAKVVRL 201
Cdd:cd03351   139 -------------VEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARLRGL 191
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 112-181 1.12e-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: 1.12e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252 112 EIGDDVFTGMNVYItdqnhgyenldepigkqlpnEQPVSIGEGAWIGSGAIILPGSKIGNHVVIGANSVV 181
Cdd:COG1044   110 KIGEGVSIGPFAVI--------------------GAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTI 159
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 113-181 1.30e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 45.13  E-value: 1.30e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2475280252 113 IGDDVFTGMNVYItdqnhgyenldepigkqlpnEQPVSIGEGAWIGSGAIILPGSKIGNHVVIGANSVV 181
Cdd:PRK00892  115 IGEGVSIGPNAVI--------------------GAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTI 163
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 149-181 1.70e-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: 44.62  E-value: 1.70e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2475280252 149 VSIGEGAWIGSGAIILPGSKIGNHVVIGANSVV 181
Cdd:COG1044   109 AKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVI 141
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 88-181 1.98e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 44.36  E-value: 1.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  88 DPVVRIGDRCLIGRGTSIIGHlaIEIGDDVFTGMNVYItdqnhgYENldepigkqlpneqpVSIGEGAWIGSGAIILPGS 167
Cdd:PRK00892  110 DPSAKIGEGVSIGPNAVIGAG--VVIGDGVVIGAGAVI------GDG--------------VKIGADCRLHANVTIYHAV 167

                          90
                  ....*....|....
gi 2475280252 168 KIGNHVVIGANSVV 181
Cdd:PRK00892  168 RIGNRVIIHSGAVI 181
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 63-201 2.02e-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: 44.24  E-value: 2.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  63 IGEDVLIAADVTLSAGMGPGqEMITdpvvRIGDRCLIGRGTSiIGHLAIeIGDDVFTGMNVYITdqnhGYenldepigkq 142
Cdd:COG1043    82 IGDNNTIREFVTIHRGTVQG-GGVT----RIGDDNLLMAYVH-VAHDCV-VGNNVILANNATLA----GH---------- 140

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2475280252 143 lpneqpVSIGEGAWIGSGAIILPGSKIGNHVVIGANSVVTGEIPSYSVAVGSPAKVVRL 201
Cdd:COG1043   141 ------VEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDVPPYVLAAGNPARLRGL 193
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
148-177 2.07e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 40.40  E-value: 2.07e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 2475280252 148 PVSIGEGAWIGSGAIILPGSKIGNHVVIGA 177
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 112-181 2.64e-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: 43.55  E-value: 2.64e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252 112 EIGDDVFTGMNVYItdqnhgyenldepigkqlpnEQPVSIGEGAWIGSGAIILPGSKIGNHVVIGANSVV 181
Cdd:cd03352     3 KIGENVSIGPNAVI--------------------GEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTI 52
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 91-193 4.84e-05

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 43.67  E-value: 4.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  91 VRIGDRC-----LIGRGTSIiGHLAI----EIGDDVFTGMNVyITdqnhgyENLDepiGKqlpNEQPVSIGEGAWIGSGA 161
Cdd:PRK14354  341 VKIGNFVeikksTIGEGTKV-SHLTYigdaEVGENVNIGCGT-IT------VNYD---GK---NKFKTIIGDNAFIGCNS 406

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2475280252 162 IILPGSKIGNHVVIGANSVVTGEIPSYSVAVG 193
Cdd:PRK14354  407 NLVAPVTVGDNAYIAAGSTITKDVPEDALAIA 438
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 91-199 8.34e-05

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 42.82  E-value: 8.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  91 VRIGDRCLIGrGTSIIGHLAIEIGDDVFTGMNVYItdQNHGYENLDEPIGkqlpneqPVSIGEGAWIGSGAIILPGSKIG 170
Cdd:TIGR02353 113 AKIGKGVDIG-SLPPVCTDLLTIGAGTIVRKEVML--LGYRAERGRLHTG-------PVTLGRDAFIGTRSTLDIDTSIG 182

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2475280252 171 NHVVIGANSVVTG--EIPSYSVAVGSPAKVV 199
Cdd:TIGR02353 183 DGAQLGHGSALQGgqSIPDGERWHGSPAQKT 213
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 63-181 9.32e-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: 42.01  E-value: 9.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  63 IGEDVLIAADVTLSAGmgpgqemitdpvVRIGDRCLIGRGTSIighlaieiGDDVftgmnvyitdqnhgyenldepigkq 142
Cdd:cd03352     4 IGENVSIGPNAVIGEG------------VVIGDGVVIGPGVVI--------GDGV------------------------- 38

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2475280252 143 lpneqpvSIGEGAWIGSGAIILPGSKIGNHVVIGANSVV 181
Cdd:cd03352    39 -------VIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 148-201 1.01e-04

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 42.44  E-value: 1.01e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2475280252 148 PVSIGEGAWIGSGAIILPGSKIGNHVVIGANSVVTGEIPSYSVAVGSPAKVVRL 201
Cdd:PRK14357  383 PTFIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQIVKE 436
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 103-186 1.15e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 41.93  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252 103 TSIIgHLAIEIGDDVFTGMNVYITDqnhgyenldepigkqlpneqPVSIGEGAWIGSGAIILPGSKIGNHVVIGANSVVt 182
Cdd:PRK12461    5 TAVI-DPSAKLGSGVEIGPFAVIGA--------------------NVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVV- 62


                  ....
gi 2475280252 183 GEIP 186
Cdd:PRK12461   63 GDEP 66
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 149-197 1.32e-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: 41.24  E-value: 1.32e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2475280252 149 VSIGEGAWIGSGAIILPGSKIGNHVVIGANSVVTGEIPSYSVAVGSPAK 197
Cdd:cd03352   151 TTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQ 199
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 90-199 1.57e-04

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: 40.66  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  90 VVRIGDRCLIGRGTSI----------IGHLAIEIGDDVFTGMNVYITDQNhgyenldepIGKQLPNEQPVSIGEGAWIGS 159
Cdd:cd03359    42 TVSIGRYCILSEGCVIrppfkkfskgVAFFPLHIGDYVFIGENCVVNAAQ---------IGSYVHIGKNCVIGRRCIIKD 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2475280252 160 GAIILPGSkignhvVIGANSVvtgeIPSYSVAVGSPAKVV 199
Cdd:cd03359   113 CVKILDGT------VVPPDTV----IPPYSVVSGRPARFI 142
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 63-181 2.00e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 41.28  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  63 IGEDVLIAADVTLSAG--MGPGqemitdpvVRIGDRCLIGRGTSIighlaieiGDDVFTGMNVYITdqnhgyenldepig 140
Cdd:PRK00892  109 IDPSAKIGEGVSIGPNavIGAG--------VVIGDGVVIGAGAVI--------GDGVKIGADCRLH-------------- 158

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2475280252 141 kqlPNeqpVSIGEGAWIGSGAIILPGSKIG-------------------------NHVVIGANSVV 181
Cdd:PRK00892  159 ---AN---VTIYHAVRIGNRVIIHSGAVIGsdgfgfandrggwvkipqlgrviigDDVEIGANTTI 218
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 63-121 2.03e-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: 41.54  E-value: 2.03e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  63 IGEDVLIAADVTLSAGmgpgqemitdpvVRIGDRCLIGRGTSIIGHlaIEIGDDV-FTGM 121
Cdd:COG1044   243 IGEHTAIAAQVGIAGS------------TKIGDNVVIGGQVGIAGH--LTIGDGViIGAQ 288
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 62-181 2.47e-04

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 41.16  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  62 WIGEDVLIAADVTLSAG--MGPGqemitdpvVRIGDRCLIGRGTSIighlaieiGDDVFTGMNVYItdqnhgYENldepi 139
Cdd:COG1044   104 VIDPSAKIGEGVSIGPFavIGAG--------VVIGDGVVIGPGVVI--------GDGVVIGDDCVL------HPN----- 156

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2475280252 140 gkqlpneqpVSIGEGAWIGSGAIILPGSKIG--------------------------NHVVIGANSVV 181
Cdd:COG1044   157 ---------VTIYERCVIGDRVIIHSGAVIGadgfgfapdedggwvkipqlgrvvigDDVEIGANTTI 215
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 60-126 2.49e-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: 40.87  E-value: 2.49e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2475280252  60 WIWIGEDVLIAADVTLSAG---MG---PGQemiTDPVVrIGDRCLIGRGTSI-IGhlaIEIGDDVFTGMNVYIT 126
Cdd:COG2171   138 WATVGSCAQIGKNVHLSGGagiGGvlePLQ---AAPVI-IEDNCFIGARSGVvEG---VIVGEGAVLGAGVYLT 204
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 61-179 2.90e-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: 41.17  E-value: 2.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  61 IWIGEDVLIAADVTLsagmgpgqemitDP------VVRIGDRCLIGRGTSIIGhlaIEIGDDVfTGMNVYITDqnhgyen 134
Cdd:COG1207   261 TYIDGDVEIGRDVVI------------DPnvilegKTVIGEGVVIGPNCTLKD---STIGDGV-VIKYSVIED------- 317

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2475280252 135 ldepigkqlpneqpVSIGEGAWIG------SGAIILPGSKIGNHV-----VIGANS 179
Cdd:COG1207   318 --------------AVVGAGATVGpfarlrPGTVLGEGVKIGNFVevknsTIGEGS 359
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 151-200 3.05e-04

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 41.00  E-value: 3.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2475280252 151 IGEGAWIGSGAIILPGSKIGNHVVIGANSVVTGEIPSYSVAVGSPAKVVR 200
Cdd:PRK14353  383 IGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALGRARQETK 432
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 149-181 3.51e-04

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: 40.16  E-value: 3.51e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2475280252 149 VSIGEGAWIGSGAIILPGSKIGNHVVIGANSVV 181
Cdd:cd03360    97 AVIGEGCVIMAGAVINPDARIGDNVIINTGAVI 129
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 88-176 3.67e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 40.97  E-value: 3.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  88 DPVVRIGDRCLIGRGTSIIGHlaIEIGDDVFTGMNVYITDQNhgyenldepIGKQLPNEQPV----SIGEGAWIGSGAII 163
Cdd:PRK14354  263 DADVEIGSDTVIEPGVVIKGN--TVIGEDCVIGPGSRIVDST---------IGDGVTITNSVieesKVGDNVTVGPFAHL 331

                          90
                  ....*....|...
gi 2475280252 164 LPGSKIGNHVVIG 176
Cdd:PRK14354  332 RPGSVIGEEVKIG 344
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 61-126 6.02e-04

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: 37.23  E-value: 6.02e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2475280252  61 IWIGEDVLIAADVTLSAGMGPGQEMITdpvvRIGDRCLIGRGTSIIGHlaIEIGDDVFTGMNVYIT 126
Cdd:cd00208    19 VVIGDNVNIGPGAVIGAATGPNEKNPT----IIGDNVEIGANAVIHGG--VKIGDNAVIGAGAVVT 78
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 149-186 6.05e-04

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 39.62  E-value: 6.05e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2475280252 149 VSIGEGAWIGSGAIILPGSKIGNHVVIGANSVVtGEIP 186
Cdd:COG1043    32 VEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASI-GEEP 68
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 151-193 6.51e-04

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 40.09  E-value: 6.51e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2475280252 151 IGEGAWIGSG-AIILPGSkIGNHVVIGANSVVTGEIPSYSVAVG 193
Cdd:PRK14356  401 IGEGAFIGSNtALVAPVT-IGDGALVGAGSVITKDVPDGSLAIA 443
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 91-187 7.59e-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: 7.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  91 VRIGDRCLIGRGTSIIGH--LAIEIGDDVFTGMNVYItdqnHGYENLDEPIGK------QLPNEQPVSIGEGAWIGSGAI 162
Cdd:cd00710    21 VIIGDNVFVGPGASIRADegTPIIIGANVNIQDGVVI----HALEGYSVWIGKnvsiahGAIVHGPAYIGDNCFIGFRSV 96

                          90       100
                  ....*....|....*....|....*.
gi 2475280252 163 ILpGSKIGNHVVIGANSVVTG-EIPS 187
Cdd:cd00710    97 VF-NAKVGDNCVIGHNAVVDGvEIPP 121
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 151-193 9.15e-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: 38.94  E-value: 9.15e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2475280252 151 IGEGAWIGSGAIILPGSKIGNHVVIGANSVVTGEIPSYSVAVG 193
Cdd:cd03353   147 IGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGALAIA 189
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 149-181 1.18e-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: 1.18e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2475280252 149 VSIGEGAWIGSGAIILPGSKIGNHVVIGANSVV 181
Cdd:cd03352     2 AKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVI 34
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 61-176 1.41e-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: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  61 IWIGEDVLIAADVTLSAGMgpgqemITDPVVRIGDRCLIGRGTSIIGhlaIEIGDDVFTGMNVYITDqnhgyenldepig 140
Cdd:cd03353    10 TYIDGDVEIGVDVVIDPGV------ILEGKTVIGEDCVIGPNCVIKD---STIGDGVVIKASSVIEG------------- 67

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2475280252 141 kqlpneqpVSIGEGAWIGSGAIILPGSKIGNHVVIG 176
Cdd:cd03353    68 --------AVIGNGATVGPFAHLRPGTVLGEGVHIG 95
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 63-185 1.57e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 38.58  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  63 IGEDVLIAADVTLSAGmgpgqemitdpvVRIGDRCLIGRGTsIIG------------HLAIE------IGDDVFTGMNVY 124
Cdd:PRK00892  151 IGADCRLHANVTIYHA------------VRIGNRVIIHSGA-VIGsdgfgfandrggWVKIPqlgrviIGDDVEIGANTT 217

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2475280252 125 ItdqnhgyenlDEP------IGK--QLPNEqpVSIGEGAWIGSGAII-----LPGS-KIGNHVVIGANSVVTGEI 185
Cdd:PRK00892  218 I----------DRGalddtvIGEgvKIDNL--VQIAHNVVIGRHTAIaaqvgIAGStKIGRYCMIGGQVGIAGHL 280
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
91-126 3.15e-03

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 34.34  E-value: 3.15e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2475280252  91 VRIGDRCLIGrGTSIIGhlaIEIGDDVFTGMNVYIT 126
Cdd:pfam14602   1 VIIGDNCLIG-ANSGIG---VSLGDNCVVGAGVVIT 32
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
149-186 4.16e-03

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 37.39  E-value: 4.16e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2475280252 149 VSIGEGAWIGSGAIILPGSKIGNHVVIGANSVVtGEIP 186
Cdd:PRK05289   33 VVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASI-GEDP 69
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 79-193 4.37e-03

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: 36.20  E-value: 4.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  79 MGPGQEMITDPVVRIGdrCLIGRGTSIIGHLAIeiGDDVFTGMNVYITdQNHGYENLDEPIGKQlpneqPVSIGEGAWIG 158
Cdd:cd03350    16 IGPGAVLMMPSYVNIG--AYVDEGTMVDSWATV--GSCAQIGKNVHLS-AGAVIGGVLEPLQAT-----PVIIEDDVFIG 85

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2475280252 159 SGAIILPGSKIGNHVVIGANSVVTGEIPSYSVAVG 193
Cdd:cd03350    86 ANCEVVEGVIVGKGAVLAAGVVLTQSTPIYDRETG 120
PLN02296 PLN02296
carbonate dehydratase
 155-200 4.39e-03

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 37.41  E-value: 4.39e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2475280252 155 AWIGSGAIILPGSKIGNHVVIGANSVVT--GEIPSYSVAVGSPAKVVR 200
Cdd:PLN02296  143 AFVGMGATLLDGVVVEKHAMVAAGALVRqnTRIPSGEVWAGNPAKFLR 190
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 145-210 4.71e-03

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 37.60  E-value: 4.71e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2475280252 145 NEQPVSIGEGAWIGSGAIILPGSKIGNHVVIGANSVVTGEIPSYSVAVGSPAKVVRlydgNSWERQ 210
Cdd:PRK14360  387 KKHRTVIGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLAIARSRQVIK----ENWKKK 448
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 137-192 5.82e-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: 5.82e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2475280252 137 EPIGKQlpneqPVSIGEGAWIGSGAIILPGSKIGNHVVIGANSVVT---------------GEIPSYSVAV 192
Cdd:PRK11830  170 EPLQAN-----PVIIEDNCFIGARSEVVEGVIVEEGSVLGMGVFLGqstkiydretgevhyGRVPAGSVVV 235
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
154-181 6.24e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.46  E-value: 6.24e-03
                          10        20
                  ....*....|....*....|....*...
gi 2475280252 154 GAWIGSGAIILPGSKIGNHVVIGANSVV 181
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVII 28
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 103-186 7.13e-03

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


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 36.64  E-value: 7.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252 103 TSIIgHLAIEIGDDVFTGMNVYITDQnhgyenldepigkqlpneqpVSIGEGAWIGSGAIILPGSKIGNHVVIGANSVVt 182
Cdd:cd03351     5 TAIV-DPGAKIGENVEIGPFCVIGPN--------------------VEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASI- 62


                  ....
gi 2475280252 183 GEIP 186
Cdd:cd03351    63 GEAP 66
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 146-181 8.52e-03

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 36.53  E-value: 8.52e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2475280252 146 EQPVSIGEGAWIGSGAIILPGSKIGNHVVIGANSVV 181
Cdd:COG1044   100 HPSAVIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVI 135
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 63-121 8.61e-03

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 36.23  E-value: 8.61e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2475280252  63 IGEDVLIAADVTLSAGmgpgqemitdpvVRIGDRCLIGRGTSIIGHlaIEIGDDV-FTGM 121
Cdd:cd03352   135 IGENCLIAAQVGIAGS------------TTIGDNVIIGGQVGIAGH--LTIGDGVvIGAG 180
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 148-196 9.49e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 36.65  E-value: 9.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2475280252 148 PVSIGEGAWIGSGAIIlPGSKIGNHVVIGANSVVTGEIPSYSVAVGSPA 196
Cdd:PRK14355  286 DTRIGEGCTIEQGVVI-KGCRIGDDVTVKAGSVLEDSVVGDDVAIGPMA 333
 
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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