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Conserved domains on  [gi|490589112|ref|WP_004454132|]
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gamma carbonic anhydrase family protein [Clostridioides difficile]

Protein Classification

gamma carbonic anhydrase family protein( domain architecture ID 11429531)

gamma carbonic anhydrase family protein is a hexapeptide repeat protein similar to carnitine operon protein CaiE and phenylacetic acid degradation protein PaaY, which are involved in amine/polyamine and aromatic compound metabolism, respectively

CATH:  2.160.10.10
EC:  4.2.1.-
Gene Ontology:  GO:0046872
PubMed:  15500694|11747907|11696553|10611359
SCOP:  4002848

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 1-161 2.86e-86

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


:

Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 249.94  E-value: 2.86e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112   1 MIRDYLEDKPLIDESVFVAKSADVIGNVKIGKDSSIWYNAVVRGDEGPITIGENTNIQDCSIVHGD--TETIIGNNVTVG 78
Cdd:COG0663    2 MIYSFDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVDpgYPLTIGDDVTIG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  79 HRSIVHGCKISDNVLIGMGSIILDNAEIGEYTLIGAGTLITSNKKFPPGVLIMGSPGKVVRELTEEDKKYIDESYEWYLE 158
Cdd:COG0663   82 HGAILHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLRESAENYVE 161


                 ...
gi 490589112 159 AAQ 161
Cdd:COG0663  162 LAR 164
 
Name Accession Description Interval E-value
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 1-161 2.86e-86

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 249.94  E-value: 2.86e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112   1 MIRDYLEDKPLIDESVFVAKSADVIGNVKIGKDSSIWYNAVVRGDEGPITIGENTNIQDCSIVHGD--TETIIGNNVTVG 78
Cdd:COG0663    2 MIYSFDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVDpgYPLTIGDDVTIG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  79 HRSIVHGCKISDNVLIGMGSIILDNAEIGEYTLIGAGTLITSNKKFPPGVLIMGSPGKVVRELTEEDKKYIDESYEWYLE 158
Cdd:COG0663   82 HGAILHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLRESAENYVE 161


                 ...
gi 490589112 159 AAQ 161
Cdd:COG0663  162 LAR 164
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 12-161 2.00e-81

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: 237.31  E-value: 2.00e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  12 IDESVFVAKSADVIGNVKIGKDSSIWYNAVVRGDEGPITIGENTNIQDCSIVHGDTE--TIIGNNVTVGHRSIVHGCKIS 89
Cdd:cd04645    2 IDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRGDVNPIRIGERTNIQDGSVLHVDPGypTIIGDNVTVGHGAVLHGCTIG 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490589112  90 DNVLIGMGSIILDNAEIGEYTLIGAGTLITSNKKFPPGVLIMGSPGKVVRELTEEDKKYIDESYEWYLEAAQ 161
Cdd:cd04645   82 DNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGKVIPPGSLVAGSPAKVVRELTDEEIAELRESAEHYVELAK 153
PLN02296 PLN02296
carbonate dehydratase
 7-161 1.29e-55

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 175.70  E-value: 1.29e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112   7 EDKPLIDESVFVAKSADVIGNVKIGKDSSIWYNAVVRGDEGPITIGENTNIQDCSIVH-------GDTE-TIIGNNVTVG 78
Cdd:PLN02296  50 DKAPVVDKDAFVAPSASVIGDVQVGRGSSIWYGCVLRGDVNSISVGSGTNIQDNSLVHvaktnlsGKVLpTIIGDNVTIG 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  79 HRSIVHGCKISDNVLIGMGSIILDNAEIGEYTLIGAGTLITSNKKFPPGVLIMGSPGKVVRELTEEDKKYIDESYEWYLE 158
Cdd:PLN02296 130 HSAVLHGCTVEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNTRIPSGEVWAGNPAKFLRKLTEEEIAFISQSATNYSN 209


                 ...
gi 490589112 159 AAQ 161
Cdd:PLN02296 210 LAQ 212
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 49-118 2.78e-07

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: 47.87  E-value: 2.78e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490589112   49 ITIGENTNIQDCSIVHGDTEtiIGNNVTVGHRSIV-HGCKISDNVLIGMGSIILDNAEIGEYTLIGAGTLI 118
Cdd:TIGR03570 100 ASIGEGTVIMAGAVINPDVR--IGDNVIINTGAIVeHDCVIGDFVHIAPGVTLSGGVVIGEGVFIGAGATI 168
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
85-114 7.10e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.39  E-value: 7.10e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 490589112   85 GCKISDNVLIGMGSIILDNAEIGEYTLIGA 114
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 1-161 2.86e-86

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 249.94  E-value: 2.86e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112   1 MIRDYLEDKPLIDESVFVAKSADVIGNVKIGKDSSIWYNAVVRGDEGPITIGENTNIQDCSIVHGD--TETIIGNNVTVG 78
Cdd:COG0663    2 MIYSFDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVDpgYPLTIGDDVTIG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  79 HRSIVHGCKISDNVLIGMGSIILDNAEIGEYTLIGAGTLITSNKKFPPGVLIMGSPGKVVRELTEEDKKYIDESYEWYLE 158
Cdd:COG0663   82 HGAILHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLRESAENYVE 161


                 ...
gi 490589112 159 AAQ 161
Cdd:COG0663  162 LAR 164
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 12-161 2.00e-81

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: 237.31  E-value: 2.00e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  12 IDESVFVAKSADVIGNVKIGKDSSIWYNAVVRGDEGPITIGENTNIQDCSIVHGDTE--TIIGNNVTVGHRSIVHGCKIS 89
Cdd:cd04645    2 IDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRGDVNPIRIGERTNIQDGSVLHVDPGypTIIGDNVTVGHGAVLHGCTIG 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490589112  90 DNVLIGMGSIILDNAEIGEYTLIGAGTLITSNKKFPPGVLIMGSPGKVVRELTEEDKKYIDESYEWYLEAAQ 161
Cdd:cd04645   82 DNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGKVIPPGSLVAGSPAKVVRELTDEEIAELRESAEHYVELAK 153
PLN02296 PLN02296
carbonate dehydratase
 7-161 1.29e-55

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 175.70  E-value: 1.29e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112   7 EDKPLIDESVFVAKSADVIGNVKIGKDSSIWYNAVVRGDEGPITIGENTNIQDCSIVH-------GDTE-TIIGNNVTVG 78
Cdd:PLN02296  50 DKAPVVDKDAFVAPSASVIGDVQVGRGSSIWYGCVLRGDVNSISVGSGTNIQDNSLVHvaktnlsGKVLpTIIGDNVTIG 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  79 HRSIVHGCKISDNVLIGMGSIILDNAEIGEYTLIGAGTLITSNKKFPPGVLIMGSPGKVVRELTEEDKKYIDESYEWYLE 158
Cdd:PLN02296 130 HSAVLHGCTVEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNTRIPSGEVWAGNPAKFLRKLTEEEIAFISQSATNYSN 209


                 ...
gi 490589112 159 AAQ 161
Cdd:PLN02296 210 LAQ 212
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 10-145 8.30e-47

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: 149.83  E-value: 8.30e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  10 PLIDESVFVAKSADVIGNVKIGKDSSIWYNAVVRGDEGPITIGENTNIQDCSIVHG--DTETIIGNNVTVGHRSIVHGCK 87
Cdd:cd04745    1 PVVDPSSFVHPTAVLIGDVIIGKNCYIGPHASLRGDFGRIVIRDGANVQDNCVIHGfpGQDTVLEENGHIGHGAILHGCT 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490589112  88 ISDNVLIGMGSIILDNAEIGEYTLIGAGTLITSNKKFPPGVLIMGSPGKVVRELTEED 145
Cdd:cd04745   81 IGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAGTVIPPRSLIAGSPAKVIRELSDEE 138
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 10-161 2.15e-44

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: 143.48  E-value: 2.15e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  10 PLIDESVFVAKSADVIGNVKIGKDSSIWYNAVVRGDEGPITIGENTNIQDCSIVHGDT--ETIIGNNVTVGHRSIVHGCK 87
Cdd:cd04650    1 PRISPKAYVHPTSYVIGDVVIGELTSVWHYAVIRGDNDSIYIGKYSNVQENVSIHTDHgyPTEIGDYVTIGHNAVVHGAK 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490589112  88 ISDNVLIGMGSIILDNAEIGEYTLIGAGTLITSNKKFPPGVLIMGSPGKVVRELTEEDKKYIDESYEWYLEAAQ 161
Cdd:cd04650   81 VGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTPGKEIPDYSLVLGVPAKVVRKLTEEEIEWIKKNAEEYVELAE 154
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 10-145 2.17e-34

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 119.14  E-value: 2.17e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  10 PLIDESVFVAKSADVIGNVKIGKDSSIWYNAVVRGDEGPITIGENTNIQDCSIVHG--DTETIIGNNVTVGHRSIVHGCK 87
Cdd:PRK13627  11 PVVHPTAFVHPSAVLIGDVIVGAGVYIGPLASLRGDYGRLIVQAGANLQDGCIMHGycDTDTIVGENGHIGHGAILHGCV 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490589112  88 ISDNVLIGMGSIILDNAEIGEYTLIGAGTLITSNKKFPPGVLIMGSPGKVVRELTEED 145
Cdd:PRK13627  91 IGRDALVGMNSVIMDGAVIGEESIVAAMSFVKAGFQGEKRQLLMGTPARAVRSVSDDE 148
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 8-150 8.64e-31

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: 109.25  E-value: 8.64e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112   8 DKPLIDESVFVAKSADVIGNVKIGKDSSIWYNAVVRGDEG-PITIGENTNIQDCSIVHG--DTETIIGNNVTVGHRSIVH 84
Cdd:cd00710    1 DEPVIDPSAYVHPTAVVIGDVIIGDNVFVGPGASIRADEGtPIIIGANVNIQDGVVIHAleGYSVWIGKNVSIAHGAIVH 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490589112  85 G-CKISDNVLIGMGSIILdNAEIGEYTLIGAGTL-----ITSNKKFPPGVLImgSPGKVVRELTEEDKKYID 150
Cdd:cd00710   81 GpAYIGDNCFIGFRSVVF-NAKVGDNCVIGHNAVvdgveIPPGRYVPAGAVI--TSQTQADALPDVTDSARE 149
PLN02472 PLN02472
uncharacterized protein
 10-149 2.65e-25

uncharacterized protein


Pssm-ID: 215263 [Multi-domain]  Cd Length: 246  Bit Score: 97.34  E-value: 2.65e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  10 PLIDESVFVAKSADVIGNVKIGKDSSIWYNAVVRGDEGPITIGENTNIQDCSIVHGDT--------ETIIGNNVTVGHRS 81
Cdd:PLN02472  60 PKVAVDAYVAPNVVLAGQVTVWDGASVWNGAVLRGDLNKITVGFCSNVQERCVLHAAWnsptglpaETLIDRYVTIGAYS 139

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490589112  82 IVHGCKISDNVLIGMGSIILDNAEIGEYTLIGAGTLITSNKKFPPGVLIMGSPGKVVRELTEEDKKYI 149
Cdd:PLN02472 140 LLRSCTIEPECIIGQHSILMEGSLVETHSILEAGSVLPPGRRIPTGELWAGNPARFVRTLTNEETLEI 207
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
25-146 3.09e-21

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 83.77  E-value: 3.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  25 IGNVKIGKDSSIWYNAVVRGdeGPITIGENTNIQDCSIVHGDTETIIGNNVTVGHRS-----------------IVHGCK 87
Cdd:COG0110    6 LFGARIGDGVVIGPGVRIYG--GNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVtiltgnhpiddpatfplRTGPVT 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490589112  88 ISDNVLIGMGSIILDNAEIGEYTLIGAGTLITsnKKFPPGVLIMGSPGKVVRELTEEDK 146
Cdd:COG0110   84 IGDDVWIGAGATILPGVTIGDGAVVGAGSVVT--KDVPPYAIVAGNPARVIRKRDEEER 140
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 27-138 8.45e-15

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: 66.33  E-value: 8.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  27 NVKIGKDSSIWYNAVVrGDEGPITIGENTNI-QDCSIV---HGDTETIIGNNVTVGHRSIVhgckISDNVLIGMGSIILD 102
Cdd:cd04647    1 NISIGDNVYIGPGCVI-SAGGGITIGDNVLIgPNVTIYdhnHDIDDPERPIEQGVTSAPIV----IGDDVWIGANVVILP 75

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 490589112 103 NAEIGEYTLIGAGTLITsnKKFPPGVLIMGSPGKVV 138
Cdd:cd04647   76 GVTIGDGAVVGAGSVVT--KDVPPNSIVAGNPAKVI 109
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 30-139 1.25e-14

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: 65.99  E-value: 1.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  30 IGKDSSIWYNAVVRGDegpITIGENTNIQD-CSIVHGdteTIIGNNVTVGH----------RSIVH------GCKISDNV 92
Cdd:cd03358    1 IGDNCIIGTNVFIEND---VKIGDNVKIQSnVSIYEG---VTIEDDVFIGPnvvftndlypRSKIYrkwelkGTTVKRGA 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 490589112  93 LIGMGSIILDNAEIGEYTLIGAGTLITsnKKFPPGVLIMGSPGKVVR 139
Cdd:cd03358   75 SIGANATILPGVTIGEYALVGAGAVVT--KDVPPYALVVGNPARIIG 119
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 16-134 3.88e-13

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: 64.04  E-value: 3.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  16 VFVAKSADVIGNVKIGKDSSIWYNAVVrgdeGP-ITIGENTNIQDCSIVHGDTetIIGNNVTVGHRSIVHG-CKISDNVL 93
Cdd:cd03360   85 TLIHPSAVVSPSAVIGEGCVIMAGAVI----NPdARIGDNVIINTGAVIGHDC--VIGDFVHIAPGVVLSGgVTIGEGAF 158

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 490589112  94 IGMGSIILDNAEIGEYTLIGAGTLITSNkkFPPGVLIMGSP 134
Cdd:cd03360  159 IGAGATIIQGVTIGAGAIIGAGAVVTKD--VPDGSVVVGNP 197
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 27-138 7.35e-13

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: 62.82  E-value: 7.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  27 NVKIGKDSSIWYNAVVRgDEGPITIGENTniqdcsivhgdtetIIGNNV---TVGH--------------RSIVhgckIS 89
Cdd:cd03357   62 NIHIGDNFYANFNCTIL-DVAPVTIGDNV--------------LIGPNVqiyTAGHpldpeernrgleyaKPIT----IG 122

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 490589112  90 DNVLIGMGSIILDNAEIGEYTLIGAGTLITsnKKFPPGVLIMGSPGKVV 138
Cdd:cd03357  123 DNVWIGGGVIILPGVTIGDNSVIGAGSVVT--KDIPANVVAAGNPARVI 169
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 18-156 1.33e-12

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: 61.85  E-value: 1.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  18 VAKSADVIG--NVKIGKDSSIWYNAVVRGDEGPITIG------ENTNIQDCSIVHGDTET----IIGNNVTVGHRSIVHG 85
Cdd:cd03359   10 VSRKSVICGsqNIVLNGKTIIQSDVIIRGDLATVSIGrycilsEGCVIRPPFKKFSKGVAffplHIGDYVFIGENCVVNA 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490589112  86 CKISDNVLIGMGSIILDNAEIGEYTLIGAGTLITSNKKFPPGVLIMGSPGKVVRELTEEDKKYI-DESYEWY 156
Cdd:cd03359   90 AQIGSYVHIGKNCVIGRRCIIKDCVKILDGTVVPPDTVIPPYSVVSGRPARFIGELPECTQELMeEETKEYY 161
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 49-140 3.05e-12

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: 61.25  E-value: 3.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  49 ITIGENTNI-QDCSIVHGdtetiignnVTVGHRSIVHG---CKISDNVLIGMGSIILDNAEIGEYTLIGAGTLITsnKKF 124
Cdd:COG1045   86 VVIGETAVIgDNVTIYQG---------VTLGGTGKEKGkrhPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVL--KDV 154

                         90
                 ....*....|....*.
gi 490589112 125 PPGVLIMGSPGKVVRE 140
Cdd:COG1045  155 PPGSTVVGVPARIVKR 170
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 25-140 1.31e-11

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 60.11  E-value: 1.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  25 IGNVKIGKDSSIWYNAVV-RGDEGPITIGENTNIqDcSIVHgdtetiIGNNVTVGHRSIVHGC-------KISDNVLIGM 96
Cdd:cd03352   90 LGGVIIGDDVEIGANTTIdRGALGDTVIGDGTKI-D-NLVQ------IAHNVRIGENCLIAAQvgiagstTIGDNVIIGG 161

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 490589112  97 GSIILDNAEIGEYTLIGAGTLITSNKkfPPGVLIMGSPGKVVRE 140
Cdd:cd03352  162 QVGIAGHLTIGDGVVIGAGSGVTSIV--PPGEYVSGTPAQPHRE 203
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 27-148 2.14e-10

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 56.94  E-value: 2.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  27 NVKIGKDSSIWYNAVVRgDEGPITIGENTniqdcsivhgdtetIIGNNVTV---GHRsiVH------------GCKISDN 91
Cdd:PRK09527  75 NIHIGRNFYANFNLTIV-DDYTVTIGDNV--------------LIAPNVTLsvtGHP--VHhelrkngemysfPITIGNN 137

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490589112  92 VLIGMGSIILDNAEIGEYTLIGAGTLITsnKKFPPGVLIMGSPGKVVRELTEEDKKY 148
Cdd:PRK09527 138 VWIGSHVVINPGVTIGDNSVIGAGSVVT--KDIPPNVVAAGVPCRVIREINDRDKQY 192
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 21-125 8.63e-10

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 56.19  E-value: 8.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  21 SADVIGNVKIGKDSSIWYNAVVRGDegpITIGENTNI-QDCSIvhgdTETIIGNNVTVgHRSIVHGCKISDNVLIG---- 95
Cdd:COG1207  260 TTYIDGDVEIGRDVVIDPNVILEGK---TVIGEGVVIgPNCTL----KDSTIGDGVVI-KYSVIEDAVVGAGATVGpfar 331

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490589112  96 --MGSIILDN----------------------------AEIGEYTLIGAGTlITSN----KKFP 125
Cdd:COG1207  332 lrPGTVLGEGvkignfvevknstigegskvnhlsyigdAEIGEGVNIGAGT-ITCNydgvNKHR 394
PLN02694 PLN02694
serine O-acetyltransferase
 62-138 9.25e-10

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 55.80  E-value: 9.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  62 IVHGDTeTIIGNNVTVGHRSIVHGC---------KISDNVLIGMGSIILDNAEIGEYTLIGAGTLITSNkkFPPGVLIMG 132
Cdd:PLN02694 181 VVIGET-AVIGNNVSILHHVTLGGTgkacgdrhpKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLID--VPPRTTAVG 257


                 ....*.
gi 490589112 133 SPGKVV 138
Cdd:PLN02694 258 NPARLV 263
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 18-154 9.50e-10

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


Pssm-ID: 100052 [Multi-domain]  Cd Length: 164  Bit Score: 54.25  E-value: 9.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  18 VAKSADVIGNVKIGKDSSIWYNAVVRGDEGPITIGENTNIQD-CSIVH----GDTET---IIGNNVTVGHRSIVHGCKIS 89
Cdd:cd04646    8 VCQESEIRGDVTIGPGTVVHPRATIIAEAGPIIIGENNIIEEqVTIVNkkpkDPAEPkpmIIGSNNVFEVGCKCEALKIG 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490589112  90 DNVLIGMGSIILDNAEIGEYTLIGAGTLITSNKKFPPGVLIMGspGKVVRELTEEDKKYIDESYE 154
Cdd:cd04646   88 NNNVFESKSFVGKNVIITDGCIIGAGCKLPSSEILPENTVIYG--ADCLRRTQTDRPKPQTLQLD 150
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 5-118 7.41e-09

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 53.10  E-value: 7.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112   5 YLEDKPLIDESVFVAKSADVIGNVKIGKDSSIWYNAVV---------RGDEGPITIGENTNIQDCSIVH----GDTETII 71
Cdd:PRK12461  25 VIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVgdepqdftyKGEESRLEIGDRNVIREGVTIHrgtkGGGVTRI 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 490589112  72 GN-NVTVGHRSIVHGCKISDNVLIGMGSIILDNAEIGEYTLIGAGTLI 118
Cdd:PRK12461 105 GNdNLLMAYSHVAHDCQIGNNVILVNGALLAGHVTVGDRAIISGNCLV 152
PLN02357 PLN02357
serine acetyltransferase
 62-138 1.54e-08

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 52.58  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  62 IVHGDTeTIIGNNVTVGHRSIVHGC---------KISDNVLIGMGSIILDNAEIGEYTLIGAGTLITsnKKFPPGVLIMG 132
Cdd:PLN02357 247 VVIGET-AVVGNNVSILHNVTLGGTgkqsgdrhpKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVL--KDVPPRTTAVG 323


                 ....*.
gi 490589112 133 SPGKVV 138
Cdd:PLN02357 324 NPARLI 329
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 26-121 2.04e-08

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: 51.27  E-value: 2.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  26 GNVKIGKDSSIWYNAVVRGDegpITIGENTNI-QDCSIvhgdTETIIGNNVTVGHRSIVHGCKISDNVLIG------MGS 98
Cdd:cd03353   14 GDVEIGVDVVIDPGVILEGK---TVIGEDCVIgPNCVI----KDSTIGDGVVIKASSVIEGAVIGNGATVGpfahlrPGT 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490589112  99 IILDN----------------------------AEIGEYTLIGAGTlITSN 121
Cdd:cd03353   87 VLGEGvhignfveikkstigegskanhlsylgdAEIGEGVNIGAGT-ITCN 136
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 24-118 2.15e-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: 51.66  E-value: 2.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  24 VIG-NVKIGKDSSIWYNAVVrgdEGPITIGENTNI----------QDCSIVHGDTETIIGNN------VTVgHRS----- 81
Cdd:cd03351   25 VIGpNVEIGDGTVIGSHVVI---DGPTTIGKNNRIfpfasigeapQDLKYKGEPTRLEIGDNntirefVTI-HRGtaqgg 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490589112  82 ----------------IVHGCKISDNVLIGMGSIILDNAEIGEYTLIGAGTLI 118
Cdd:cd03351  101 gvtrignnnllmayvhVAHDCVIGNNVILANNATLAGHVEIGDYAIIGGLSAV 153
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 28-119 3.64e-08

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: 48.01  E-value: 3.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  28 VKIGKDSSIWYNAVVRGdegPITIGENTNIQDCSIVHGDTETIIGNNVTVGhrsivhgckisDNVLIGMGSIILDNAEIG 107
Cdd:cd00208    1 VFIGEGVKIHPKAVIRG---PVVIGDNVNIGPGAVIGAATGPNEKNPTIIG-----------DNVEIGANAVIHGGVKIG 66

                         90
                 ....*....|..
gi 490589112 108 EYTLIGAGTLIT 119
Cdd:cd00208   67 DNAVIGAGAVVT 78
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
24-137 5.53e-08

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 50.48  E-value: 5.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  24 VIGNVKIGKDSSIWYNAVV---------RGDEGPITIGENTNIQDCSIVH-----GDTETIIGNN------VTVGHRSIV 83
Cdd:PRK05289  47 IDGHTTIGKNNRIFPFASIgedpqdlkyKGEPTRLVIGDNNTIREFVTINrgtvqGGGVTRIGDNnllmayVHVAHDCVV 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490589112  84 --------------HgCKISDNVLIGMGSIILDNAEIGEYTLIGAGTLITsnKKFPPGVLIMGSPGKV 137
Cdd:PRK05289 127 gnhvilannatlagH-VEVGDYAIIGGLTAVHQFVRIGAHAMVGGMSGVS--QDVPPYVLAEGNPARL 191
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 49-134 5.88e-08

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: 48.21  E-value: 5.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  49 ITIGENTNI-QDCSIVHGdtetiignnVTVGHRSIVHGC---KISDNVLIGMGSIILDNAEIGEYTLIGAGTLITSNkkF 124
Cdd:cd03354   23 IVIGETAVIgDNCTIYQG---------VTLGGKGKGGGKrhpTIGDNVVIGAGAKILGNITIGDNVKIGANAVVTKD--V 91

                         90
                 ....*....|
gi 490589112 125 PPGVLIMGSP 134
Cdd:cd03354   92 PANSTVVGVP 101
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 24-138 1.17e-07

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 49.63  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  24 VIG-NVKIGKDSSIWYNAVVrgdEGPITIGENTNI----------QD---------------------CSI----VHGDT 67
Cdd:COG1043   27 VIGpDVEIGDGTVIGSHVVI---EGPTTIGKNNRIfpfasigeepQDlkykgeptrleigdnntirefVTIhrgtVQGGG 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  68 ETIIGNN------VTVGHRSIV--------------HgCKISDNVLIGMGSIILDNAEIGEYTLIGAGTLITsnKKFPPG 127
Cdd:COG1043  104 VTRIGDDnllmayVHVAHDCVVgnnvilannatlagH-VEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVV--KDVPPY 180

                        170
                 ....*....|.
gi 490589112 128 VLIMGSPGKVV 138
Cdd:COG1043  181 VLAAGNPARLR 191
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 25-134 1.60e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 49.37  E-value: 1.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  25 IGNVKIGKDSSIWYNAVV-RGDEGPITIGENTNIqdcsivhgDTETIIGNNVTVGHRSIVHGC-------KISDNVLIGM 96
Cdd:PRK00892 201 LGRVIIGDDVEIGANTTIdRGALDDTVIGEGVKI--------DNLVQIAHNVVIGRHTAIAAQvgiagstKIGRYCMIGG 272

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 490589112  97 GSIILDNAEIGEYTLIGAGTLITSNKKfPPGVLIMGSP 134
Cdd:PRK00892 273 QVGIAGHLEIGDGVTITAMSGVTKSIP-EPGEYSSGIP 309
cysE PRK11132
serine acetyltransferase; Provisional
 49-138 1.77e-07

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 49.31  E-value: 1.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  49 ITIGENTNIQ-DCSIVHGdtetiignnVTVGHRSIVHG---CKISDNVLIGMGSIILDNAEIGEYTLIGAGTLITsnKKF 124
Cdd:PRK11132 162 IVIGETAVIEnDVSILQS---------VTLGGTGKTSGdrhPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVL--QPV 230

                         90
                 ....*....|....
gi 490589112 125 PPGVLIMGSPGKVV 138
Cdd:PRK11132 231 PPHTTAAGVPARIV 244
PLN02739 PLN02739
serine acetyltransferase
 64-145 1.84e-07

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 49.26  E-value: 1.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  64 HGdTETIIGNNVTVGHR-SIVHGC--------------KISDNVLIGMGSIILDNAEIGEYTLIGAGTLITsnKKFPPGV 128
Cdd:PLN02739 222 HG-TGVVIGETAVIGDRvSILHGVtlggtgketgdrhpKIGDGALLGACVTILGNISIGAGAMVAAGSLVL--KDVPSHS 298

                         90
                 ....*....|....*..
gi 490589112 129 LIMGSPGKVVRELTEED 145
Cdd:PLN02739 299 MVAGNPAKLIGFVDEQD 315
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 25-134 2.33e-07

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 48.86  E-value: 2.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  25 IGNVKIGKDSSIWYNAVV-RGDEGPITIGENTNIqDcSIVHgdtetiIGNNVTVGHRSIVHGC-------KISDNVLIGM 96
Cdd:COG1044  198 LGRVVIGDDVEIGANTTIdRGALGDTVIGDGTKI-D-NLVQ------IAHNVRIGEHTAIAAQvgiagstKIGDNVVIGG 269

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 490589112  97 GSIILDNAEIGEYTLIGAGTLITSNkkFPPGVLIMGSP 134
Cdd:COG1044  270 QVGIAGHLTIGDGVIIGAQSGVTKS--IPEGGVYSGSP 305
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 12-101 2.39e-07

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: 46.09  E-value: 2.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  12 IDESVFVAKSADVIGNVKIGKDSSIWYNAVVRGDEGPitigentniqdcsivHGDTETIIGNNVTVGHRS-IVHGCKISD 90
Cdd:cd00208    3 IGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGP---------------NEKNPTIIGDNVEIGANAvIHGGVKIGD 67

                         90
                 ....*....|.
gi 490589112  91 NVLIGMGSIIL 101
Cdd:cd00208   68 NAVIGAGAVVT 78
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 49-118 2.78e-07

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: 47.87  E-value: 2.78e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490589112   49 ITIGENTNIQDCSIVHGDTEtiIGNNVTVGHRSIV-HGCKISDNVLIGMGSIILDNAEIGEYTLIGAGTLI 118
Cdd:TIGR03570 100 ASIGEGTVIMAGAVINPDVR--IGDNVIINTGAIVeHDCVIGDFVHIAPGVTLSGGVVIGEGVFIGAGATI 168
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 28-113 2.80e-07

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 48.97  E-value: 2.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  28 VKIGKDSSIWYNAVVRGDegpitigentniqdcsivhgdteTIIGNNVTVGHRSIVHGCKISDNVLIGMGSiILDNAEIG 107
Cdd:PRK14355 269 VVIGRDTTIYPGVCISGD-----------------------TRIGEGCTIEQGVVIKGCRIGDDVTVKAGS-VLEDSVVG 324


                 ....*.
gi 490589112 108 EYTLIG 113
Cdd:PRK14355 325 DDVAIG 330
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 70-121 1.17e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 47.06  E-value: 1.17e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490589112  70 IIGNNVTVGHRS-IVHGCKISDNVLIGMGSIILDNAEIGEYTLIGAGTLITSN 121
Cdd:PRK00892 114 KIGEGVSIGPNAvIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHA 166
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 9-107 2.30e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 45.90  E-value: 2.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112   9 KPLIDESVFVAKSAdvignvKIGKDSSIWYNAVvrgdegpitIGENTNIQDCSIVHgdTETIIGNNVTVGHRSIVH-GCK 87
Cdd:PRK00892 100 AAGIHPSAVIDPSA------KIGEGVSIGPNAV---------IGAGVVIGDGVVIG--AGAVIGDGVKIGADCRLHaNVT 162

                         90       100
                 ....*....|....*....|
gi 490589112  88 ISDNVLIGMGSIILDNAEIG 107
Cdd:PRK00892 163 IYHAVRIGNRVIIHSGAVIG 182
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 71-115 3.33e-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: 45.39  E-value: 3.33e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 490589112  71 IGNNVTVGHRSIVH-GCKISDNVLIGMGSIILDNAEIGEYTLIGAG 115
Cdd:COG1044  111 IGEGVSIGPFAVIGaGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPN 156
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 9-118 3.56e-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: 45.39  E-value: 3.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112   9 KPLIDESVFVAKSAdvignvKIGKDSSIWYNAVvrgdegpitIGENTNIqdcsivhGDtETIIGNNVTVGHrsivhGCKI 88
Cdd:COG1044   96 APGIHPSAVIDPSA------KIGEGVSIGPFAV---------IGAGVVI-------GD-GVVIGPGVVIGD-----GVVI 147

                         90       100       110
                 ....*....|....*....|....*....|
gi 490589112  89 SDNVLIGMGSIILDNAEIGEYTLIGAGTLI 118
Cdd:COG1044  148 GDDCVLHPNVTIYERCVIGDRVIIHSGAVI 177
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 27-118 6.28e-06

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: 44.32  E-value: 6.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  27 NVKIGKDSSIWYNAVvrgdegpitIGENTNIQDcsivhgdtETIIGNNVTVGHrsivhGCKISDNVLIGMGSIILDNAEI 106
Cdd:cd03352    1 SAKIGENVSIGPNAV---------IGEGVVIGD--------GVVIGPGVVIGD-----GVVIGDDCVIHPNVTIYEGCII 58

                         90
                 ....*....|..
gi 490589112 107 GEYTLIGAGTLI 118
Cdd:cd03352   59 GDRVIIHSGAVI 70
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 70-121 2.56e-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: 2.56e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490589112  70 IIGNNVTVGHRSIVH-GCKISDNVLIGMGSIILDNAEIGEYTLIGAGTLITSN 121
Cdd:cd03352    3 KIGENVSIGPNAVIGeGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEG 55
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 51-121 2.90e-05

eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 40.25  E-value: 2.90e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490589112  51 IGENTNIQDCSIVhgdTETIIGNNVTVGHRSIVHGCKISDNVLIGMG-----SIILDNAEIGEYTLIGAGTLITSN 121
Cdd:cd05787    2 IGRGTSIGEGTTI---KNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGctihhSIVADGAVIGKGCTIPPGSLISFG 74
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 50-140 5.55e-05

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 42.06  E-value: 5.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  50 TIGENTNIQDCSIVhGDTetIIGNNVTVGHRSIV--------HGCKISDNVLIGMGSIILDNAEIGEYTLIGAGTLITSN 121
Cdd:PRK14357 343 TIGENTKAQHLTYL-GDA--TVGKNVNIGAGTITcnydgkkkNPTFIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITED 419

                         90
                 ....*....|....*....
gi 490589112 122 kkFPPGVLIMGSPGKVVRE 140
Cdd:PRK14357 420 --VPPYSLALGRARQIVKE 436
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 51-138 7.43e-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: 42.05  E-value: 7.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112   51 IGENTNIQDCSIVHGDTETIiGNNVTVG----------HRSIVH--GCKISDNVLIGMGSIILDNAEIGEYTLIGAGTLI 118
Cdd:TIGR02353 115 IGKGVDIGSLPPVCTDLLTI-GAGTIVRkevmllgyraERGRLHtgPVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSAL 193

                          90       100
                  ....*....|....*....|
gi 490589112  119 TSNKKFPPGVLIMGSPGKVV 138
Cdd:TIGR02353 194 QGGQSIPDGERWHGSPAQKT 213
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 24-121 2.22e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 40.20  E-value: 2.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  24 VIGNVKIGKDSSIWYNAVVR-----GDEGPI---------TIGENTNIQDCSIVhGDTEtiIGNNVTVGHRSIV------ 83
Cdd:PRK14354 313 VIEESKVGDNVTVGPFAHLRpgsviGEEVKIgnfveikksTIGEGTKVSHLTYI-GDAE--VGENVNIGCGTITvnydgk 389

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 490589112  84 --HGCKISDNVLIGMGSIILDNAEIGEYTLIGAGTLITSN 121
Cdd:PRK14354 390 nkFKTIIGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKD 429
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 28-113 2.51e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 40.20  E-value: 2.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  28 VKIGKDSSIWYNAVVRGDegpITIGENTNI-QDCSIVhgdtETIIGNNVTVGHrSIVHGCKISDNVLIGMGSIILDNAEI 106
Cdd:PRK14354 266 VEIGSDTVIEPGVVIKGN---TVIGEDCVIgPGSRIV----DSTIGDGVTITN-SVIEESKVGDNVTVGPFAHLRPGSVI 337


                 ....*..
gi 490589112 107 GEYTLIG 113
Cdd:PRK14354 338 GEEVKIG 344
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 24-114 4.06e-04

Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 37.22  E-value: 4.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  24 VIGN-VKIGKDSSIwynavvrgdeGPITIGENTNIQDCSIVhgdTETIIGNNVTVGHRSIVHGCKISDNVLIGMGSIILD 102
Cdd:cd03356    1 LIGEsTVIGENAII----------KNSVIGDNVRIGDGVTI---TNSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVN 67

                         90
                 ....*....|..
gi 490589112 103 NAEIGEYTLIGA 114
Cdd:cd03356   68 LCIIGDDVVVED 79
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 51-123 6.31e-04

eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B gamma subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH domain with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 36.79  E-value: 6.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  51 IGENTNIQD-CSIvhgdTETIIGNNVTVGHRSIVHGCKISDNVLIG-----MGSIILDNAEIGE-----YTLIGAGTLIT 119
Cdd:cd04652    2 VGENTQVGEkTSI----KRSVIGANCKIGKRVKITNCVIMDNVTIEdgctlENCIIGNGAVIGEkcklkDCLVGSGYRVE 77


                 ....
gi 490589112 120 SNKK 123
Cdd:cd04652   78 AGTE 81
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 12-113 6.83e-04

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 39.14  E-value: 6.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  12 IDESVFVAKsaDVI--------GNVKIGKDSSIwynavvrgdeGPITIGENTniqdcsivhgdtetIIGNNVTVGHrSIV 83
Cdd:PRK14360 259 ISETVELGP--DVIiepqthlrGNTVIGSGCRI----------GPGSLIENS--------------QIGENVTVLY-SVV 311

                         90       100       110
                 ....*....|....*....|....*....|
gi 490589112  84 HGCKISDNVLIGMGSIILDNAEIGEYTLIG 113
Cdd:PRK14360 312 SDSQIGDGVKIGPYAHLRPEAQIGSNCRIG 341
PRK10502 PRK10502
putative acyl transferase; Provisional
 49-140 6.94e-04

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 38.39  E-value: 6.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  49 ITIGENTNIQDCSIVHGDTETIIGNNVTVGHRS----------------IVHGCKISDNVLIGMGSIILDNAEIGEYTLI 112
Cdd:PRK10502  72 LTIGDYAWIGDDVWLYNLGEITIGAHCVISQKSylctgshdysdphfdlNTAPIVIGEGCWLAADVFVAPGVTIGSGAVV 151

                         90       100
                 ....*....|....*....|....*...
gi 490589112 113 GAGTLITSNkkFPPGVLIMGSPGKVVRE 140
Cdd:PRK10502 152 GARSSVFKS--LPANTICRGNPAVPIRP 177
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
85-114 7.10e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.39  E-value: 7.10e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 490589112   85 GCKISDNVLIGMGSIILDNAEIGEYTLIGA 114
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 50-132 8.09e-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: 38.17  E-value: 8.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  50 TIGENTNIQDCSIVhGDTEtiIGNNVTVGHRSIV--------HGCKISDNVLIGMGSIILDNAEIGEYTLIGAGTLITSN 121
Cdd:cd03353  104 TIGEGSKANHLSYL-GDAE--IGEGVNIGAGTITcnydgvnkHRTVIGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKD 180

                         90
                 ....*....|.
gi 490589112 122 KkfPPGVLIMG 132
Cdd:cd03353  181 V--PPGALAIA 189
LbH_unknown cd05635
Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group ...
 26-123 1.10e-03

Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group are uncharacterized bacterial proteins containing a LbH domain with multiple turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100059 [Multi-domain]  Cd Length: 101  Bit Score: 36.49  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  26 GNVKIGKDSSIWYNAVVRgdeGPITIGENTNIQDCSIVHGdtetiignNVTVGHRSIVHGcKISDNVLIGMGSI----IL 101
Cdd:cd05635   10 GPIYIGKDAVIEPFAVIE---GPVYIGPGSRVKMGARIYG--------NTTIGPTCKIGG-EVEDSIIEGYSNKqhdgFL 77

                         90       100
                 ....*....|....*....|..
gi 490589112 102 DNAEIGEYTLIGAGTlITSNKK 123
Cdd:cd05635   78 GHSYLGSWCNLGAGT-NNSDLK 98
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 51-126 1.30e-03

Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 36.07  E-value: 1.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  51 IGENTNIQDCSIVH----GDtETIIGNNVTVGHRSIVHGCKISDNVLIgMGSIILDNAEIGEYTLIGAGTLITSNKKFPP 126
Cdd:cd03356    2 IGESTVIGENAIIKnsviGD-NVRIGDGVTITNSILMDNVTIGANSVI-VDSIIGDNAVIGENVRVVNLCIIGDDVVVED 79
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 49-123 1.47e-03

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 37.82  E-value: 1.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490589112  49 ITIGENTNIQDCSIVHGDTEtiIGNNVTVGHRSIVHGCKISDNVLIG----MGSIILDNAEIGEYTLIGAGTLITSNKK 123
Cdd:PRK14357 256 VEIGMDTIIYPMTFIEGKTR--IGEDCEIGPMTRIVDCEIGNNVKIIrsecEKSVIEDDVSVGPFSRLREGTVLKKSVK 332
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 51-145 1.81e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 37.54  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  51 IGENTNIQDC-----SIVHGDTE-TIIGNNVTVGHRSIVHGCKISDNVLIGMGSIIlDNAEIGEYTLIGAGTLITSNKKf 124
Cdd:PRK05293 285 IAENAKVKNSlvvegCVVYGTVEhSVLFQGVQVGEGSVVKDSVIMPGAKIGENVVI-ERAIIGENAVIGDGVIIGGGKE- 362

                         90       100
                 ....*....|....*....|.
gi 490589112 125 ppGVLIMGSpGKVVRELTEED 145
Cdd:PRK05293 363 --VITVIGE-NEVIGVGTVIG 380
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
53-118 2.09e-03

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 37.39  E-value: 2.09e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490589112  53 ENTNIQDCSIVHGDTEtiIGNNVTVGhrsivHGCKISDNVLIGMGSIILDNAEIGEYTLIGAGTLI 118
Cdd:PRK05289   1 MMAKIHPTAIVEPGAK--IGENVEIG-----PFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRI 59
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 49-107 2.18e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 37.54  E-value: 2.18e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  49 ITIGENTNIQDCSIVHGdteTIIGNNVTVgHRSIV-HGCKISDNV----------LIGMGSIILDNAEIG 107
Cdd:PRK05293 315 VQVGEGSVVKDSVIMPG---AKIGENVVI-ERAIIgENAVIGDGViigggkevitVIGENEVIGVGTVIG 380
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 56-118 2.86e-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: 37.03  E-value: 2.86e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490589112  56 NIQDCSIVHGDTEtiIGNNVTVGHRSIvhgckISDNVLIGMGSIILDNAEIGEYTLIGAGTLI 118
Cdd:cd03351    1 MIHPTAIVDPGAK--IGENVEIGPFCV-----IGPNVEIGDGTVIGSHVVIDGPTTIGKNNRI 56
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 49-138 3.16e-03

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: 35.27  E-value: 3.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  49 ITIGENTNIQDCSIVHGDTETIIGNNVTVGHRS----------------IVHGCKISDNVLIGMGSIILDNAEIGEYTLI 112
Cdd:cd05825    4 LTIGDNSWIGEGVWIYNLAPVTIGSDACISQGAylctgshdyrspafplITAPIVIGDGAWVAAEAFVGPGVTIGEGAVV 83

                         90       100
                 ....*....|....*....|....*.
gi 490589112 113 GAGTLITsnKKFPPGVLIMGSPGKVV 138
Cdd:cd05825   84 GARSVVV--RDLPAWTVYAGNPAVPV 107
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 50-140 3.28e-03

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 36.83  E-value: 3.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  50 TIGENTNIQDCSIVhGDTEtiIGNNVTVGHRSIV--------HGCKISDNVLIGMGSIILDNAEIGEYTLIGAGTLITsn 121
Cdd:PRK14360 350 QLGEGSKVNHLSYI-GDAT--LGEQVNIGAGTITanydgvkkHRTVIGDRSKTGANSVLVAPITLGEDVTVAAGSTIT-- 424

                         90
                 ....*....|....*....
gi 490589112 122 KKFPPGVLIMGSPGKVVRE 140
Cdd:PRK14360 425 KDVPDNSLAIARSRQVIKE 443
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 30-108 4.75e-03

eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 34.48  E-value: 4.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  30 IGKDSSIWYNAVVRGDegpiTIGENTNIQDCSIVHGD---TETIIGNNVTVGHRSIVHGCKISDNVLIGMGSIILDNAEI 106
Cdd:cd05787    2 IGRGTSIGEGTTIKNS----VIGRNCKIGKNVVIDNSyiwDDVTIEDGCTIHHSIVADGAVIGKGCTIPPGSLISFGVVI 77


                 ..
gi 490589112 107 GE 108
Cdd:cd05787   78 GD 79
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 66-149 5.56e-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: 35.43  E-value: 5.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490589112  66 DTETIIGNNVTVGHRSIV-HGCKISDNVLIG--------MGSIILDNAEIGEYTLIGAGTLITSNKKFPPGVLIMGSPGK 136
Cdd:cd03350   35 DEGTMVDSWATVGSCAQIgKNVHLSAGAVIGgvleplqaTPVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTQSTPI 114

                         90
                 ....*....|...
gi 490589112 137 VVRELTEEDKKYI 149
Cdd:cd03350  115 YDRETGEIYYGRV 127
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 86-118 6.74e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 35.89  E-value: 6.74e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 490589112  86 CKISDNVLIGMGSIILDNAEIGEYTLIGAGTLI 118
Cdd:PRK00892 113 AKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVI 145
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 52-113 9.00e-03

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 35.77  E-value: 9.00e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490589112  52 GENTNIQDCSIvhgDTETIIGNNVTVGHR------SIVHGCKISDNVLIGMGSIILDnAEIGEYTLIG 113
Cdd:PRK09451 264 GTLTHGRDVEI---DTNVIIEGNVTLGNRvkigagCVLKNCVIGDDCEISPYSVVED-ANLGAACTIG 327
 
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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