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Conserved domains on  [gi|589300504|gb|AHK64635|]
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bacterial transferase hexapeptide family protein [Burkholderia pseudomallei MSHR520]

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 ...
 1-170 1.52e-92

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


:

Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 266.51  E-value: 1.52e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504   1 MTIYKLGENAPSIHESVFVADSATIVGKVVLEENASVWFGATIRGDNEPITVGAGSNVQEGAVLHTDPGCPLTIAPNVTV 80
Cdd:COG0663    1 MMIYSFDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVDPGYPLTIGDDVTI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504  81 GHQAMLHGCTIGEGSLIGIQAVILNRAVIGRNCLVGAGAVITEGKAFPDNSLILGAPAKVVRTLSDEDIARMHMNTKSYA 160
Cdd:COG0663   81 GHGAILHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLRESAENYV 160

                        170
                 ....*....|
gi 589300504 161 MRRAYFKEQL 170
Cdd:COG0663  161 ELARRYLAEL 170
 
Name Accession Description Interval E-value
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 1-170 1.52e-92

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 266.51  E-value: 1.52e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504   1 MTIYKLGENAPSIHESVFVADSATIVGKVVLEENASVWFGATIRGDNEPITVGAGSNVQEGAVLHTDPGCPLTIAPNVTV 80
Cdd:COG0663    1 MMIYSFDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVDPGYPLTIGDDVTI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504  81 GHQAMLHGCTIGEGSLIGIQAVILNRAVIGRNCLVGAGAVITEGKAFPDNSLILGAPAKVVRTLSDEDIARMHMNTKSYA 160
Cdd:COG0663   81 GHGAILHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLRESAENYV 160

                        170
                 ....*....|
gi 589300504 161 MRRAYFKEQL 170
Cdd:COG0663  161 ELARRYLAEL 170
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 12-159 7.08e-80

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: 233.84  E-value: 7.08e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504  12 SIHESVFVADSATIVGKVVLEENASVWFGATIRGDNEPITVGAGSNVQEGAVLHTDPGCPLTIAPNVTVGHQAMLHGCTI 91
Cdd:cd04645    1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRGDVNPIRIGERTNIQDGSVLHVDPGYPTIIGDNVTVGHGAVLHGCTI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 589300504  92 GEGSLIGIQAVILNRAVIGRNCLVGAGAVITEGKAFPDNSLILGAPAKVVRTLSDEDIARMHMNTKSY 159
Cdd:cd04645   81 GDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGKVIPPGSLVAGSPAKVVRELTDEEIAELRESAEHY 148
PLN02296 PLN02296
carbonate dehydratase
 2-160 1.60e-41

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 140.26  E-value: 1.60e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504   2 TIYKLGENAPSIHESVFVADSATIVGKVVLEENASVWFGATIRGDNEPITVGAGSNVQEGAVLH---TDPG---CPLTIA 75
Cdd:PLN02296  44 TLMNIFDKAPVVDKDAFVAPSASVIGDVQVGRGSSIWYGCVLRGDVNSISVGSGTNIQDNSLVHvakTNLSgkvLPTIIG 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504  76 PNVTVGHQAMLHGCTIGEGSLIGIQAVILNRAVIGRNCLVGAGAVITEGKAFPDNSLILGAPAKVVRTLSDEDIARMHMN 155
Cdd:PLN02296 124 DNVTIGHSAVLHGCTVEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNTRIPSGEVWAGNPAKFLRKLTEEEIAFISQS 203


                 ....*
gi 589300504 156 TKSYA 160
Cdd:PLN02296 204 ATNYS 208
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 5-138 1.41e-13

sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff.


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 65.59  E-value: 1.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504    5 KLGENAPS-IHESVFVADSATIvgkvvlEENASVWFGATIRGDnepITVGAGSNVQEGAVL--HTDPGCPLTIAPNVTVG 81
Cdd:TIGR03570  81 AKGYRFATlIHPSAIVSPSASI------GEGTVIMAGAVINPD---VRIGDNVIINTGAIVehDCVIGDFVHIAPGVTLS 151

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 589300504   82 HqamlhGCTIGEGSLIGIQAVILNRAVIGRNCLVGAGAVITegKAFPDNSLILGAPA 138
Cdd:TIGR03570 152 G-----GVVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVT--KDIPDGGVVVGVPA 201
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
88-117 5.81e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.78  E-value: 5.81e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 589300504   88 GCTIGEGSLIGIQAVILNRAVIGRNCLVGA 117
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 1-170 1.52e-92

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 266.51  E-value: 1.52e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504   1 MTIYKLGENAPSIHESVFVADSATIVGKVVLEENASVWFGATIRGDNEPITVGAGSNVQEGAVLHTDPGCPLTIAPNVTV 80
Cdd:COG0663    1 MMIYSFDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVDPGYPLTIGDDVTI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504  81 GHQAMLHGCTIGEGSLIGIQAVILNRAVIGRNCLVGAGAVITEGKAFPDNSLILGAPAKVVRTLSDEDIARMHMNTKSYA 160
Cdd:COG0663   81 GHGAILHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLRESAENYV 160

                        170
                 ....*....|
gi 589300504 161 MRRAYFKEQL 170
Cdd:COG0663  161 ELARRYLAEL 170
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 12-159 7.08e-80

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: 233.84  E-value: 7.08e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504  12 SIHESVFVADSATIVGKVVLEENASVWFGATIRGDNEPITVGAGSNVQEGAVLHTDPGCPLTIAPNVTVGHQAMLHGCTI 91
Cdd:cd04645    1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRGDVNPIRIGERTNIQDGSVLHVDPGYPTIIGDNVTVGHGAVLHGCTI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 589300504  92 GEGSLIGIQAVILNRAVIGRNCLVGAGAVITEGKAFPDNSLILGAPAKVVRTLSDEDIARMHMNTKSY 159
Cdd:cd04645   81 GDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGKVIPPGSLVAGSPAKVVRELTDEEIAELRESAEHY 148
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 11-159 1.77e-47

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: 151.57  E-value: 1.77e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504  11 PSIHESVFVADSATIVGKVVLEENASVWFGATIRGDNEPITVGAGSNVQEGAVLHTDPGCPLTIAPNVTVGHQAMLHGCT 90
Cdd:cd04650    1 PRISPKAYVHPTSYVIGDVVIGELTSVWHYAVIRGDNDSIYIGKYSNVQENVSIHTDHGYPTEIGDYVTIGHNAVVHGAK 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 589300504  91 IGEGSLIGIQAVILNRAVIGRNCLVGAGAVITEGKAFPDNSLILGAPAKVVRTLSDEDIARMHMNTKSY 159
Cdd:cd04650   81 VGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTPGKEIPDYSLVLGVPAKVVRKLTEEEIEWIKKNAEEY 149
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 11-159 4.80e-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: 150.60  E-value: 4.80e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504  11 PSIHESVFVADSATIVGKVVLEENASVWFGATIRGDNEPITVGAGSNVQEGAVLHTDPGCPLTIAPNVTVGHQAMLHGCT 90
Cdd:cd04745    1 PVVDPSSFVHPTAVLIGDVIIGKNCYIGPHASLRGDFGRIVIRDGANVQDNCVIHGFPGQDTVLEENGHIGHGAILHGCT 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 589300504  91 IGEGSLIGIQAVILNRAVIGRNCLVGAGAVITEGKAFPDNSLILGAPAKVVRTLSDEDIARMHMNTKSY 159
Cdd:cd04745   81 IGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAGTVIPPRSLIAGSPAKVIRELSDEEVAWKTRGTKEY 149
PLN02296 PLN02296
carbonate dehydratase
 2-160 1.60e-41

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 140.26  E-value: 1.60e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504   2 TIYKLGENAPSIHESVFVADSATIVGKVVLEENASVWFGATIRGDNEPITVGAGSNVQEGAVLH---TDPG---CPLTIA 75
Cdd:PLN02296  44 TLMNIFDKAPVVDKDAFVAPSASVIGDVQVGRGSSIWYGCVLRGDVNSISVGSGTNIQDNSLVHvakTNLSgkvLPTIIG 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504  76 PNVTVGHQAMLHGCTIGEGSLIGIQAVILNRAVIGRNCLVGAGAVITEGKAFPDNSLILGAPAKVVRTLSDEDIARMHMN 155
Cdd:PLN02296 124 DNVTIGHSAVLHGCTVEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNTRIPSGEVWAGNPAKFLRKLTEEEIAFISQS 203


                 ....*
gi 589300504 156 TKSYA 160
Cdd:PLN02296 204 ATNYS 208
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 1-159 8.83e-33

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 115.67  E-value: 8.83e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504   1 MTIYKLGENAPSIHESVFVADSATIVGKVVLEenASVWFG--ATIRGDNEPITVGAGSNVQEGAVLHTDPGCPLTIAPNV 78
Cdd:PRK13627   1 MSYYAFEGLIPVVHPTAFVHPSAVLIGDVIVG--AGVYIGplASLRGDYGRLIVQAGANLQDGCIMHGYCDTDTIVGENG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504  79 TVGHQAMLHGCTIGEGSLIGIQAVILNRAVIGRNCLVGAGAVITEGKAFPDNSLILGAPAKVVRTLSDEDIARMHMNTKS 158
Cdd:PRK13627  79 HIGHGAILHGCVIGRDALVGMNSVIMDGAVIGEESIVAAMSFVKAGFQGEKRQLLMGTPARAVRSVSDDELHWKRLNTKE 158


                 .
gi 589300504 159 Y 159
Cdd:PRK13627 159 Y 159
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 11-133 8.22e-28

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: 101.93  E-value: 8.22e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504  11 PSIHESVFVADSATIVGKVVLEENASVWFGATIRGDN-EPITVGAGSNVQEGAVLHTDPGCPLTIAPNVTVGHQAMLHG- 88
Cdd:cd00710    3 PVIDPSAYVHPTAVVIGDVIIGDNVFVGPGASIRADEgTPIIIGANVNIQDGVVIHALEGYSVWIGKNVSIAHGAIVHGp 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 589300504  89 CTIGEGSLIGIQAVILNrAVIGRNCLVGAGAV-----ITEGKAFPDNSLI 133
Cdd:cd00710   83 AYIGDNCFIGFRSVVFN-AKVGDNCVIGHNAVvdgveIPPGRYVPAGAVI 131
PLN02472 PLN02472
uncharacterized protein
 3-149 2.03e-26

uncharacterized protein


Pssm-ID: 215263 [Multi-domain]  Cd Length: 246  Bit Score: 100.42  E-value: 2.03e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504   3 IYKLGENAPSIHESVFVADSATIVGKVVLEENASVWFGATIRGDNEPITVGAGSNVQEGAVLHTDPGCPLTIAPN----- 77
Cdd:PLN02472  52 IIPLGQWVPKVAVDAYVAPNVVLAGQVTVWDGASVWNGAVLRGDLNKITVGFCSNVQERCVLHAAWNSPTGLPAEtlidr 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 589300504  78 -VTVGHQAMLHGCTIGEGSLIGIQAVILNRAVIGRNCLVGAGAVITEGKAFPDNSLILGAPAKVVRTLSDEDI 149
Cdd:PLN02472 132 yVTIGAYSLLRSCTIEPECIIGQHSILMEGSLVETHSILEAGSVLPPGRRIPTGELWAGNPARFVRTLTNEET 204
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
37-149 6.85e-17

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 72.98  E-value: 6.85e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504  37 VWFGATIRGDNEPITVGAGSNVQEGAVLhtDPGCPLTIAPNVTVGHQAML-----------------HGCTIGEGSLIGI 99
Cdd:COG0110   15 VVIGPGVRIYGGNITIGDNVYIGPGVTI--DDPGGITIGDNVLIGPGVTIltgnhpiddpatfplrtGPVTIGDDVWIGA 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 589300504 100 QAVILNRAVIGRNCLVGAGAVITegKAFPDNSLILGAPAKVVRTLSDEDI 149
Cdd:COG0110   93 GATILPGVTIGDGAVVGAGSVVT--KDVPPYAIVAGNPARVIRKRDEEER 140
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 12-137 1.13e-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: 65.58  E-value: 1.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504  12 SIHESVFVADSATIVGKVVLEENASVWFGATIRGDNepiTVGAGSnvqegavlhtdpgcplTIAPNVTVGHqamlhGCTI 91
Cdd:cd03360   98 VIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDC---VIGDFV----------------HIAPGVVLSG-----GVTI 153

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 589300504  92 GEGSLIGIQAVILNRAVIGRNCLVGAGAVITegKAFPDNSLILGAP 137
Cdd:cd03360  154 GEGAFIGAGATIIQGVTIGAGAIIGAGAVVT--KDVPDGSVVVGNP 197
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 5-138 1.41e-13

sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff.


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 65.59  E-value: 1.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504    5 KLGENAPS-IHESVFVADSATIvgkvvlEENASVWFGATIRGDnepITVGAGSNVQEGAVL--HTDPGCPLTIAPNVTVG 81
Cdd:TIGR03570  81 AKGYRFATlIHPSAIVSPSASI------GEGTVIMAGAVINPD---VRIGDNVIINTGAIVehDCVIGDFVHIAPGVTLS 151

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 589300504   82 HqamlhGCTIGEGSLIGIQAVILNRAVIGRNCLVGAGAVITegKAFPDNSLILGAPA 138
Cdd:TIGR03570 152 G-----GVVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVT--KDIPDGGVVVGVPA 201
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 4-121 2.80e-13

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: 66.19  E-value: 2.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504   4 YKLGENAPSIHESVFVADSATIvgkvvlEENASVwfgatirgdnepitvGAGSNVQEGAVLhtDPGCplTIAPNVTVGHq 83
Cdd:COG1044   90 YPPPAPAPGIHPSAVIDPSAKI------GEGVSI---------------GPFAVIGAGVVI--GDGV--VIGPGVVIGD- 143

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 589300504  84 amlhGCTIGEGSLIGIQAVILNRAVIGRNCLVGAGAVI 121
Cdd:COG1044  144 ----GVVIGDDCVLHPNVTIYERCVIGDRVIIHSGAVI 177
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 50-141 2.36e-11

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: 57.47  E-value: 2.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504  50 ITVGAGSNVQEGAVLhtDPGCPLTIAPNVTVGHQAMLHGC--------------------TIGEGSLIGIQAVILNRAVI 109
Cdd:cd04647    2 ISIGDNVYIGPGCVI--SAGGGITIGDNVLIGPNVTIYDHnhdiddperpieqgvtsapiVIGDDVWIGANVVILPGVTI 79

                         90       100       110
                 ....*....|....*....|....*....|..
gi 589300504 110 GRNCLVGAGAVITegKAFPDNSLILGAPAKVV 141
Cdd:cd04647   80 GDGAVVGAGSVVT--KDVPPNSIVAGNPAKVI 109
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 33-141 7.55e-11

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: 57.43  E-value: 7.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504  33 ENASVWFGATIRgDNEPITVGAgsNVQegavlhtdpgcpltIAPNV---TVGH----QAMLHGC------TIGEGSLIGI 99
Cdd:cd03357   67 DNFYANFNCTIL-DVAPVTIGD--NVL--------------IGPNVqiyTAGHpldpEERNRGLeyakpiTIGDNVWIGG 129

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 589300504 100 QAVILNRAVIGRNCLVGAGAVITegKAFPDNSLILGAPAKVV 141
Cdd:cd03357  130 GVIILPGVTIGDNSVIGAGSVVT--KDIPANVVAAGNPARVI 169
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 21-159 1.35e-10

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: 56.84  E-value: 1.35e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504  21 DSATIVGKVVLEEnasvwfGATIRGDNEPITVGAGSNVQEGAVL--------HTDPGCPLTIAPNVTVGHQAMLHGCTIG 92
Cdd:cd03359   20 QNIVLNGKTIIQS------DVIIRGDLATVSIGRYCILSEGCVIrppfkkfsKGVAFFPLHIGDYVFIGENCVVNAAQIG 93

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 589300504  93 EGSLIGIQAVILNRAVIGRNCLVGAGAVITEGKAFPDNSLILGAPAKVVRTLSdEDIARMHMN-TKSY 159
Cdd:cd03359   94 SYVHIGKNCVIGRRCIIKDCVKILDGTVVPPDTVIPPYSVVSGRPARFIGELP-ECTQELMEEeTKEY 160
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 6-142 2.26e-09

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: 52.50  E-value: 2.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504   6 LGENApSIHESVFVADSATIVGKVVLEENASVWFGATIrGDNepitVGAGSNVqegaVLHTDPgcpltiAPNVTVGHQAM 85
Cdd:cd03358    1 IGDNC-IIGTNVFIENDVKIGDNVKIQSNVSIYEGVTI-EDD----VFIGPNV----VFTNDL------YPRSKIYRKWE 64

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 589300504  86 LHGCTIGEGSLIGIQAVILNRAVIGRNCLVGAGAVITegKAFPDNSLILGAPAKVVR 142
Cdd:cd03358   65 LKGTTVKRGASIGANATILPGVTIGEYALVGAGAVVT--KDVPPYALVVGNPARIIG 119
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 5-148 2.73e-09

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 53.85  E-value: 2.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504   5 KLGENA---PSIHesvFVADSATIVGKvvleeNASVWFGATIRGDnepITVGAGSNVqegavlhtdpgcplTIAPNVT-- 79
Cdd:PRK09527  57 TVGENAwvePPVY---FSYGSNIHIGR-----NFYANFNLTIVDD---YTVTIGDNV--------------LIAPNVTls 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504  80 -----VGHQAMLHG------CTIGEGSLIGIQAVILNRAVIGRNCLVGAGAVITegKAFPDNSLILGAPAKVVRTLSDED 148
Cdd:PRK09527 112 vtghpVHHELRKNGemysfpITIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVT--KDIPPNVVAAGVPCRVIREINDRD 189
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 51-121 3.07e-09

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 53.57  E-value: 3.07e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 589300504  51 TVGAGSNVQEGAVLHtdPGCplTIAPNVTVGHqamlhGCTIGEGSLIGIQAVILNRAVIGRNCLVGAGAVI 121
Cdd:cd03352    9 SIGPNAVIGEGVVIG--DGV--VIGPGVVIGD-----GVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 29-122 3.87e-09

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 50.71  E-value: 3.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504  29 VVLEENASVWFGATIRGdnePITVGAGSNVQEGAVLHTDPGCPLTIAPnvtvghqamlhgcTIGEGSLIGIQAVILNRAV 108
Cdd:cd00208    1 VFIGEGVKIHPKAVIRG---PVVIGDNVNIGPGAVIGAATGPNEKNPT-------------IIGDNVEIGANAVIHGGVK 64

                         90
                 ....*....|....
gi 589300504 109 IGRNCLVGAGAVIT 122
Cdd:cd00208   65 IGDNAVIGAGAVVT 78
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 10-121 5.88e-09

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 53.99  E-value: 5.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504  10 APSIHESVFVADSATIvgkvvlEENASVWFGATIrgdnepitvgaGSNVQEGAvlhtdpGCplTIAPNVTVGHqamlhGC 89
Cdd:PRK00892 100 AAGIHPSAVIDPSAKI------GEGVSIGPNAVI-----------GAGVVIGD------GV--VIGAGAVIGD-----GV 149

                         90       100       110
                 ....*....|....*....|....*....|..
gi 589300504  90 TIGEGSLIGIQAVILNRAVIGRNCLVGAGAVI 121
Cdd:PRK00892 150 KIGADCRLHANVTIYHAVRIGNRVIIHSGAVI 181
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 91-147 1.11e-08

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 52.19  E-value: 1.11e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 589300504  91 IGEGSLIGIQAVILNRAVIGRNCLVGAGAVITegKAFPDNSLILGAPAKVVRTLSDE 147
Cdd:PRK09677 133 IGQRVWIGENVTILPGVSIGNGCIVGANSVVT--KSIPENTVIAGNPAKIIKKYNHE 187
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 31-141 1.80e-08

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: 49.91  E-value: 1.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504  31 LEENASVWFGATIRGDN-EPITVGAGSNVQEGAVL------HTDPGCPLTIAPnvtvghqamlhgCTIGEGSLIGIQAVI 103
Cdd:cd05825    4 LTIGDNSWIGEGVWIYNlAPVTIGSDACISQGAYLctgshdYRSPAFPLITAP------------IVIGDGAWVAAEAFV 71

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 589300504 104 LNRAVIGRNCLVGAGAVITegKAFPDNSLILGAPAKVV 141
Cdd:cd05825   72 GPGVTIGEGAVVGARSVVV--RDLPAWTVYAGNPAVPV 107
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 90-143 2.87e-08

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: 50.47  E-value: 2.87e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 589300504  90 TIGEGSLIGIQAVILNRAVIGRNCLVGAGAVITegKAFPDNSLILGAPAKVVRT 143
Cdd:COG1045  119 TIGDNVVIGAGAKILGPITIGDNAKIGANSVVL--KDVPPGSTVVGVPARIVKR 170
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 47-124 3.45e-08

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 51.68  E-value: 3.45e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 589300504  47 NEPITVGAGSNVQEGAVLHTDPgcplTIAPNVTVGHQAML-HGCTIGEGSLIGIQAVILNRAVIGRNCLVGAGAVITEG 124
Cdd:PRK00892  92 DPPATPSPAAGIHPSAVIDPSA----KIGEGVSIGPNAVIgAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHA 166
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 73-124 5.02e-08

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 51.17  E-value: 5.02e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 589300504  73 TIAPNVTVGHQAMLH-GCTIGEGSLIGIQAVILNRAVIGRNCLVGAGAVITEG 124
Cdd:COG1044  110 KIGEGVSIGPFAVIGaGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYER 162
PLN02739 PLN02739
serine acetyltransferase
 50-148 7.61e-08

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 50.80  E-value: 7.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504  50 ITVGAGSNVQEGAVLhtDPGCPLTIAPNVTVGHQ-AMLHGCT--------------IGEGSLIGIQAVILNRAVIGRNCL 114
Cdd:PLN02739 206 IDIHPAARIGKGILL--DHGTGVVIGETAVIGDRvSILHGVTlggtgketgdrhpkIGDGALLGACVTILGNISIGAGAM 283

                         90       100       110
                 ....*....|....*....|....*....|....
gi 589300504 115 VGAGAVITegKAFPDNSLILGAPAKVVRTLSDED 148
Cdd:PLN02739 284 VAAGSLVL--KDVPSHSMVAGNPAKLIGFVDEQD 315
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 73-124 1.89e-07

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 48.94  E-value: 1.89e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 589300504  73 TIAPNVTVGHQAMLH-GCTIGEGSLIGIQAVILNRAVIGRNCLVGAGAVITEG 124
Cdd:cd03352    3 KIGENVSIGPNAVIGeGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEG 55
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 73-137 5.04e-07

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: 45.89  E-value: 5.04e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 589300504  73 TIAPNVTVGHQAMLHGC---TIGEGSLIGIQAVILNRAVIGRNCLVGAGAVITegKAFPDNSLILGAP 137
Cdd:cd03354   36 TIYQGVTLGGKGKGGGKrhpTIGDNVVIGAGAKILGNITIGDNVKIGANAVVT--KDVPANSTVVGVP 101
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 90-144 9.57e-07

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 46.73  E-value: 9.57e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 589300504  90 TIGEGSLIGIQAVILNRAVIGRNCLVGAGAVITegKAFPDNSLILGAPAKVVRTL 144
Cdd:PRK10092 131 TIGNNVWIGGRAVINPGVTIGDNVVVASGAVVT--KDVPDNVVVGGNPARIIKKL 183
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 45-135 1.24e-05

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 44.33  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504  45 GDNEpitVGAGSNVQEGavlhtdpgcplTIAPNVTVGHQamlHGCTIGEGSLIGIQAVILNRAVIGRNCLVGAGAVITeg 124
Cdd:PRK14356 372 GDAE---IGAGANIGAG-----------TITCNYDGVNK---HRTVIGEGAFIGSNTALVAPVTIGDGALVGAGSVIT-- 432

                         90
                 ....*....|.
gi 589300504 125 KAFPDNSLILG 135
Cdd:PRK14356 433 KDVPDGSLAIA 443
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 67-121 2.27e-05

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 43.08  E-value: 2.27e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 589300504  67 DPGCplTIAPNVTVGHQAMLH-GCTIGEGSLIGIQAVILNRAVIGRNCLVGAGAVI 121
Cdd:COG1043   11 DPGA--KLGENVEIGPFCVIGpDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASI 64
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 12-154 3.46e-05

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: 41.93  E-value: 3.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504  12 SIHESVFVADSATIVGKVVLEENASVWFGATIRGDNEPITVGAGSNVQEGAVLHTDPGCPLTIAPNVTVGHQAMLH-GCT 90
Cdd:cd04646    1 KIAPGAVVCQESEIRGDVTIGPGTVVHPRATIIAEAGPIIIGENNIIEEQVTIVNKKPKDPAEPKPMIIGSNNVFEvGCK 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 589300504  91 -----IGEGSLIGIQAVILNRAVIGRNCLVGAGAVITEGKAFPDNSLILGAPAkVVRTLSDEDIARMHM 154
Cdd:cd04646   81 cealkIGNNNVFESKSFVGKNVIITDGCIIGAGCKLPSSEILPENTVIYGADC-LRRTQTDRPKPQTLQ 148
PRK10502 PRK10502
putative acyl transferase; Provisional
 38-143 1.29e-04

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 40.70  E-value: 1.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504  38 WFGATIrGDNEPI------------TVGAGSNVQEGAVLHTDPgcPLTIAPNVTVGHQAMLhgCT--------------- 90
Cdd:PRK10502  49 LFGAKI-GKGVVIrpsvritypwklTIGDYAWIGDDVWLYNLG--EITIGAHCVISQKSYL--CTgshdysdphfdlnta 123

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 589300504  91 ---IGEGSLIGIQAVILNRAVIGRNCLVGAGAVITegKAFPDNSLILGAPAKVVRT 143
Cdd:PRK10502 124 pivIGEGCWLAADVFVAPGVTIGSGAVVGARSSVF--KSLPANTICRGNPAVPIRP 177
PRK10191 PRK10191
putative acyl transferase; Provisional
 65-140 1.70e-04

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 39.87  E-value: 1.70e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 589300504  65 HTDPGCPLTIAPNVTVGHQAM--LHGCTIGEGSLIGIQAVILNRAVIGRNCLVGAGAVITEgkAFPDNSLILGAPAKV 140
Cdd:PRK10191  67 NVVAGDDFTIRHGVTIGNRGAdnMACPHIGNGVELGANVIILGDITIGNNVTVGAGSVVLD--SVPDNALVVGEKARV 142
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
74-121 5.33e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 39.31  E-value: 5.33e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 589300504  74 IAPNVTVGHQAMLHG-CTIGEGSLIGIQAVILNRAVIGRNCLVGAGAVI 121
Cdd:PRK05289  17 IGENVEIGPFCVIGPnVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASI 65
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
88-117 5.81e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.78  E-value: 5.81e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 589300504   88 GCTIGEGSLIGIQAVILNRAVIGRNCLVGA 117
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 90-152 5.81e-04

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: 38.29  E-value: 5.81e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 589300504  90 TIGEGSLIGIQAVILNRAVIGRNCLVGAGAVITegKAFPDNSLILGAPAKVVRT-LSDEDIARM 152
Cdd:cd03349   75 IIGNDVWIGHGATILPGVTIGDGAVIAAGAVVT--KDVPPYAIVGGNPAKVIRYrFDEETIERL 136
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 5-135 6.10e-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: 38.93  E-value: 6.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504   5 KLGENApSIHESVFVADSATIVGKVVLEENASVWFGATIrgdnepitvGAGSNVQEGAVL-------HTDPGCPLTIA-- 75
Cdd:cd03352   21 VIGDGV-VIGPGVVIGDGVVIGDDCVIHPNVTIYEGCII---------GDRVIIHSGAVIgsdgfgfAPDGGGWVKIPql 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504  76 ------PNVTVG-----HQAML------------------HGCTIGEGSLIGIQAVILNRAVIGRNCLVGAGAVITEGKA 126
Cdd:cd03352   91 ggviigDDVEIGanttiDRGALgdtvigdgtkidnlvqiaHNVRIGENCLIAAQVGIAGSTTIGDNVIIGGQVGIAGHLT 170


                 ....*....
gi 589300504 127 FPDNSLILG 135
Cdd:cd03352  171 IGDGVVIGA 179
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 52-124 6.28e-04

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: 36.79  E-value: 6.28e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 589300504  52 VGAGSNVQEGA-VLHTDPGCPLTIAPNVTVGHQAMLHGCTIGEGSLIGiQAVILNRAVIGRNCLVGAGAVITEG 124
Cdd:cd05787    2 IGRGTSIGEGTtIKNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIH-HSIVADGAVIGKGCTIPPGSLISFG 74
PLN02694 PLN02694
serine O-acetyltransferase
 74-141 6.73e-04

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 38.86  E-value: 6.73e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 589300504  74 IAPNVTVGHQAMLHGC---------TIGEGSLIGIQAVILNRAVIGRNCLVGAGAVITegKAFPDNSLILGAPAKVV 141
Cdd:PLN02694 189 IGNNVSILHHVTLGGTgkacgdrhpKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVL--IDVPPRTTAVGNPARLV 263
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 13-104 7.03e-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: 36.84  E-value: 7.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504  13 IHESVFVADSATIVGKVVLEENASVWFGATIrgdnepitvgagsnvqeGAVLHTDPGCPLTIAPNVTVGHQAMLHG-CTI 91
Cdd:cd00208    3 IGEGVKIHPKAVIRGPVVIGDNVNIGPGAVI-----------------GAATGPNEKNPTIIGDNVEIGANAVIHGgVKI 65

                         90
                 ....*....|...
gi 589300504  92 GEGSLIGIQAVIL 104
Cdd:cd00208   66 GDNAVIGAGAVVT 78
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 74-139 7.97e-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: 38.54  E-value: 7.97e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 589300504  74 IAPNVTVGHQAMLHGC-------TIGEGSLIGIQAVILNRAVIGRNCLVGAGAVITegKAFPDNSLILGAPAK 139
Cdd:cd03352  129 IAHNVRIGENCLIAAQvgiagstTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVT--SIVPPGEYVSGTPAQ 199
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 74-121 8.47e-04

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: 38.57  E-value: 8.47e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 589300504  74 IAPNVTVGHQAMLH-GCTIGEGSLIGIQAVILNRAVIGRNCLVGAGAVI 121
Cdd:cd03351   14 IGENVEIGPFCVIGpNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASI 62
cysE PRK11132
serine acetyltransferase; Provisional
 58-141 9.31e-04

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 38.52  E-value: 9.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504  58 VQEGAVLHTDpgcpLTIAPNVTVGHQAMLHG---CTIGEGSLIGIQAVILNRAVIGRNCLVGAGAVITEgkAFPDNSLIL 134
Cdd:PRK11132 164 IGETAVIEND----VSILQSVTLGGTGKTSGdrhPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQ--PVPPHTTAA 237


                 ....*..
gi 589300504 135 GAPAKVV 141
Cdd:PRK11132 238 GVPARIV 244
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 19-121 1.28e-03

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


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 37.57  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504  19 VADSATIVGKVVLEENASVWFGATIRGdnePITVGAGSNVQEGAVLHtdPGCplTIAPNVTVGHQAMLHGCTIGEGSLIG 98
Cdd:cd05636    8 VEEGVTIKGPVWIGEGAIVRSGAYIEG---PVIIGKGCEIGPNAYIR--GYT--VLGDGCVVGNSVEVKNSIIMDGTKVP 80

                         90       100
                 ....*....|....*....|...
gi 589300504  99 IQAVIlNRAVIGRNCLVGAGAVI 121
Cdd:cd05636   81 HLNYV-GDSVLGENVNLGAGTIT 102
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 62-124 1.47e-03

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 38.07  E-value: 1.47e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 589300504  62 AVLHTDPGCPLTIAPNVTVGHQAmlhgcTIGEGSLIGIQAVILNRAVIGRNCLVGAGAVITEG 124
Cdd:COG1044   87 QLFYPPPAPAPGIHPSAVIDPSA-----KIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDG 144
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 79-141 1.62e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 37.93  E-value: 1.62e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 589300504  79 TVGHQAMLHGCTIGEGSLIgIQAVILNRAVIGRNCLVgAGAVITEGKAFPDNSLILGAPAKVV 141
Cdd:PRK05293 305 TVEHSVLFQGVQVGEGSVV-KDSVIMPGAKIGENVVI-ERAIIGENAVIGDGVIIGGGKEVIT 365
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 74-121 1.70e-03

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: 37.46  E-value: 1.70e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 589300504  74 IAPNVTVGHQAmlhgcTIGEGSLIGIQAVILNRAVIGRNCLVGAGAVI 121
Cdd:cd03360   87 IHPSAVVSPSA-----VIGEGCVIMAGAVINPDARIGDNVIINTGAVI 129
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 55-141 2.44e-03

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 37.81  E-value: 2.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504   55 GSNVQEGAVLHT-DPGCP--LTIAPNVTVGHQAMLHG------------CTIGEGSLIGIQAVILNRAVIGRNCLVGAGA 119
Cdd:TIGR02353 112 GAKIGKGVDIGSlPPVCTdlLTIGAGTIVRKEVMLLGyraergrlhtgpVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGS 191

                          90       100
                  ....*....|....*....|..
gi 589300504  120 VITEGKAFPDNSLILGAPAKVV 141
Cdd:TIGR02353 192 ALQGGQSIPDGERWHGSPAQKT 213
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 52-125 2.44e-03

Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Glucose-1-phosphate adenylyltransferase is also known as ADP-glucose synthase or ADP-glucose pyrophosphorylase. It catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for regulation of storage polysaccharide accumulation in plants and bacteria. The enzyme is a homotetramer, with each subunit containing an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain with at 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The LbH domain is involved in cooperative allosteric regulation and oligomerization.


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 35.90  E-value: 2.44e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 589300504  52 VGAGSNVQEGAVLHT--DPGCplTIAPNVTVGHQAMLHGCTIGEGsligiqaVILNRAVIGRNCLVGAGAVITEGK 125
Cdd:cd04651   15 VSEGCIISGGTVENSvlFRGV--RVGSGSVVEDSVIMPNVGIGRN-------AVIRRAIIDKNVVIPDGVVIGGDP 81
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 91-142 2.66e-03

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 37.44  E-value: 2.66e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 589300504  91 IGEGSLIGIQAVILNRAVIGRNCLVGAGAVITEGkaFPDNSLILGAPAKVVR 142
Cdd:PRK14357 386 IEDGAFIGSNSSLVAPVRIGKGALIGAGSVITED--VPPYSLALGRARQIVK 435
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 87-142 2.77e-03

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 37.21  E-value: 2.77e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 589300504  87 HGCTIGEGSLIGIQAVILNRAVIGRNCLVGAGAVITegKAFPDNSLILGAPAKVVR 142
Cdd:PRK14360 389 HRTVIGDRSKTGANSVLVAPITLGEDVTVAAGSTIT--KDVPDNSLAIARSRQVIK 442
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 89-133 2.91e-03

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 36.62  E-value: 2.91e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 589300504  89 CTIGEGSLIGIQAVILNRAVIGRNCLVGAGAVITEGKAFPDNSLI 133
Cdd:cd03352    2 AKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVI 46
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 40-116 3.17e-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: 36.63  E-value: 3.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504  40 GATIRgdnEPITVGAGSNVQEGAVLHTDPGCPL----TIAPNVTVGHQAMLHGCTIGEGSLIgIQAVILNRAVIGRNCLV 115
Cdd:cd03353    1 GVTLI---DPETTYIDGDVEIGVDVVIDPGVILegktVIGEDCVIGPNCVIKDSTIGDGVVI-KASSVIEGAVIGNGATV 76


                 .
gi 589300504 116 G 116
Cdd:cd03353   77 G 77
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 69-125 4.04e-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: 34.52  E-value: 4.04e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 589300504  69 GCPLTIAPNVTVGHQAMLHGCTIGEGSLIgIQAVILNRAVIGRNCLVGAGAVITEGK 125
Cdd:cd03356   20 GDNVRIGDGVTITNSILMDNVTIGANSVI-VDSIIGDNAVIGENVRVVNLCIIGDDV 75
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 12-115 4.20e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 36.54  E-value: 4.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504  12 SIHESVFVADSATIVGKVVLEENASVWFGATI---------RGDNEPITVGAGSNVQEGAVLH--TDPGCPLTIA----- 75
Cdd:PRK12461  31 EIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVgdepqdftyKGEESRLEIGDRNVIREGVTIHrgTKGGGVTRIGndnll 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 589300504  76 -PNVTVGHQAML-HGCTIGEGSLIGIQAVILNRAVIGRNCLV 115
Cdd:PRK12461 111 mAYSHVAHDCQIgNNVILVNGALLAGHVTVGDRAIISGNCLV 152
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 37-138 4.60e-03

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 36.65  E-value: 4.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504   37 VWFGATIRGDNEPITVGAGSNVQEGAVLHTdpgcpltiapnvtvgH----QAM-LHGCTIGEGSLIGIQAVILNRAVIGR 111
Cdd:TIGR02353 604 VYIDGTDLTERDLVTIGDDSTLNEGSVIQT---------------HlfedRVMkSDTVTIGDGATLGPGAIVLYGVVMGE 668

                          90       100
                  ....*....|....*....|....*..
gi 589300504  112 NCLVGAGAVITEGKAFPDNSLILGAPA 138
Cdd:TIGR02353 669 GSVLGPDSLVMKGEEVPAHTRWRGNPA 695
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 65-121 5.46e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 36.15  E-value: 5.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 589300504  65 HTDPGCplTIAPNVTVGHQAMLH-GCTIGEGSLIGIQAVILNRAVIGRNCLVGAGAVI 121
Cdd:PRK12461   7 VIDPSA--KLGSGVEIGPFAVIGaNVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVV 62
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 52-121 6.10e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 36.34  E-value: 6.10e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504  52 VGAGSNVQEGAVLHTdpgcplTIAPNVTVGHQAMLHGCTIGEGSLIGIQAVIlNRAVIGRNCLVGAGAVI 121
Cdd:PRK00844 318 VSAGSIISGATVRNS------VLSPNVVVESGAEVEDSVLMDGVRIGRGAVV-RRAILDKNVVVPPGATI 380
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 88-141 6.18e-03

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


Pssm-ID: 441774 [Multi-domain]  Cd Length: 268  Bit Score: 36.25  E-value: 6.18e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 589300504  88 GCTIGeGSLIGIQAvilNRAVIGRNCLVGAGAVITEGKAFPDNS-----LILGAPAKVV 141
Cdd:COG2171  156 GAGIG-GVLEPLQA---APVIIEDNCFIGARSGVVEGVIVGEGAvlgagVYLTASTKIY 210
PLN02357 PLN02357
serine acetyltransferase
 58-141 8.88e-03

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 35.63  E-value: 8.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 589300504  58 VQEGAVLhtdpGCPLTIAPNVTVGHQAMLHG---CTIGEGSLIGIQAVILNRAVIGRNCLVGAGAVITegKAFPDNSLIL 134
Cdd:PLN02357 249 IGETAVV----GNNVSILHNVTLGGTGKQSGdrhPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVL--KDVPPRTTAV 322


                 ....*..
gi 589300504 135 GAPAKVV 141
Cdd:PLN02357 323 GNPARLI 329
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 87-122 8.92e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 35.89  E-value: 8.92e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 589300504  87 HGCTIGEGSLIGIQAVILNRAVIGRNCLVGAGAVIT 122
Cdd:PRK00892 242 HNVVIGRHTAIAAQVGIAGSTKIGRYCMIGGQVGIA 277
 
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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