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Conserved domains on  [gi|503750419|ref|WP_013984495|]
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MULTISPECIES: gamma carbonic anhydrase family protein [Stutzerimonas]

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 ...
 1-176 1.78e-94

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


:

Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 271.52  E-value: 1.78e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419   1 MAIRSYQNSTPTLGERVFVDDSAVVIGDVEIGADSSVWPLTVIRGDMHRIRIGARSSIQDGSVLHIThagpynpDGFPLT 80
Cdd:COG0663    1 MMIYSFDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVD-------PGYPLT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  81 IGDEVTVGHKVTLHGCTLGNRILVGMGSIVMDGVVVEDEVIIGAGSLVPPGKTLESGYLYVGSPVKQARPLTDKERSFFS 160
Cdd:COG0663   74 IGDDVTIGHGAILHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLR 153

                        170
                 ....*....|....*.
gi 503750419 161 YTAGNYVKLKDQHLAE 176
Cdd:COG0663  154 ESAENYVELARRYLAE 169
 
Name Accession Description Interval E-value
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 1-176 1.78e-94

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 271.52  E-value: 1.78e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419   1 MAIRSYQNSTPTLGERVFVDDSAVVIGDVEIGADSSVWPLTVIRGDMHRIRIGARSSIQDGSVLHIThagpynpDGFPLT 80
Cdd:COG0663    1 MMIYSFDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVD-------PGYPLT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  81 IGDEVTVGHKVTLHGCTLGNRILVGMGSIVMDGVVVEDEVIIGAGSLVPPGKTLESGYLYVGSPVKQARPLTDKERSFFS 160
Cdd:COG0663   74 IGDDVTIGHGAILHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLR 153

                        170
                 ....*....|....*.
gi 503750419 161 YTAGNYVKLKDQHLAE 176
Cdd:COG0663  154 ESAENYVELARRYLAE 169
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 12-171 1.92e-79

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: 232.69  E-value: 1.92e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  12 TLGERVFVDDSAVVIGDVEIGADSSVWPLTVIRGDMHRIRIGARSSIQDGSVLHITHagpynpdGFPLTIGDEVTVGHKV 91
Cdd:cd04645    1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRGDVNPIRIGERTNIQDGSVLHVDP-------GYPTIIGDNVTVGHGA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  92 TLHGCTLGNRILVGMGSIVMDGVVVEDEVIIGAGSLVPPGKTLESGYLYVGSPVKQARPLTDKERSFFSYTAGNYVKLKD 171
Cdd:cd04645   74 VLHGCTIGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGKVIPPGSLVAGSPAKVVRELTDEEIAELRESAEHYVELAK 153
PLN02296 PLN02296
carbonate dehydratase
 8-176 9.30e-53

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 169.15  E-value: 9.30e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419   8 NSTPTLGERVFVDDSAVVIGDVEIGADSSVWPLTVIRGDMHRIRIGARSSIQDGSVLHITHAgpyNPDG--FPLTIGDEV 85
Cdd:PLN02296  50 DKAPVVDKDAFVAPSASVIGDVQVGRGSSIWYGCVLRGDVNSISVGSGTNIQDNSLVHVAKT---NLSGkvLPTIIGDNV 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  86 TVGHKVTLHGCTLGNRILVGMGSIVMDGVVVEDEVIIGAGSLVPPGKTLESGYLYVGSPVKQARPLTDKERSFFSYTAGN 165
Cdd:PLN02296 127 TIGHSAVLHGCTVEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNTRIPSGEVWAGNPAKFLRKLTEEEIAFISQSATN 206

                        170
                 ....*....|.
gi 503750419 166 YVKLKDQHLAE 176
Cdd:PLN02296 207 YSNLAQVHAAE 217
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 19-144 1.15e-08

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: 52.11  E-value: 1.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419   19 VDDSAVVIGDVEIGADSSVWPLTVIRGDmhrIRIGARSSIQDGSVlhITHagpynpDgfpLTIGDEVTVGHKVTLHG-CT 97
Cdd:TIGR03570  90 IHPSAIVSPSASIGEGTVIMAGAVINPD---VRIGDNVIINTGAI--VEH------D---CVIGDFVHIAPGVTLSGgVV 155

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 503750419   98 LGNRILVGMGSIVMDGVVVEDEVIIGAGSLV----PPGKTlesgylYVGSP 144
Cdd:TIGR03570 156 IGEGVFIGAGATIIQGVTIGAGAIVGAGAVVtkdiPDGGV------VVGVP 200
 
Name Accession Description Interval E-value
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 1-176 1.78e-94

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 271.52  E-value: 1.78e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419   1 MAIRSYQNSTPTLGERVFVDDSAVVIGDVEIGADSSVWPLTVIRGDMHRIRIGARSSIQDGSVLHIThagpynpDGFPLT 80
Cdd:COG0663    1 MMIYSFDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVD-------PGYPLT 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  81 IGDEVTVGHKVTLHGCTLGNRILVGMGSIVMDGVVVEDEVIIGAGSLVPPGKTLESGYLYVGSPVKQARPLTDKERSFFS 160
Cdd:COG0663   74 IGDDVTIGHGAILHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLR 153

                        170
                 ....*....|....*.
gi 503750419 161 YTAGNYVKLKDQHLAE 176
Cdd:COG0663  154 ESAENYVELARRYLAE 169
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 12-171 1.92e-79

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: 232.69  E-value: 1.92e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  12 TLGERVFVDDSAVVIGDVEIGADSSVWPLTVIRGDMHRIRIGARSSIQDGSVLHITHagpynpdGFPLTIGDEVTVGHKV 91
Cdd:cd04645    1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRGDVNPIRIGERTNIQDGSVLHVDP-------GYPTIIGDNVTVGHGA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  92 TLHGCTLGNRILVGMGSIVMDGVVVEDEVIIGAGSLVPPGKTLESGYLYVGSPVKQARPLTDKERSFFSYTAGNYVKLKD 171
Cdd:cd04645   74 VLHGCTIGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGKVIPPGSLVAGSPAKVVRELTDEEIAELRESAEHYVELAK 153
PLN02296 PLN02296
carbonate dehydratase
 8-176 9.30e-53

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 169.15  E-value: 9.30e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419   8 NSTPTLGERVFVDDSAVVIGDVEIGADSSVWPLTVIRGDMHRIRIGARSSIQDGSVLHITHAgpyNPDG--FPLTIGDEV 85
Cdd:PLN02296  50 DKAPVVDKDAFVAPSASVIGDVQVGRGSSIWYGCVLRGDVNSISVGSGTNIQDNSLVHVAKT---NLSGkvLPTIIGDNV 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  86 TVGHKVTLHGCTLGNRILVGMGSIVMDGVVVEDEVIIGAGSLVPPGKTLESGYLYVGSPVKQARPLTDKERSFFSYTAGN 165
Cdd:PLN02296 127 TIGHSAVLHGCTVEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNTRIPSGEVWAGNPAKFLRKLTEEEIAFISQSATN 206

                        170
                 ....*....|.
gi 503750419 166 YVKLKDQHLAE 176
Cdd:PLN02296 207 YSNLAQVHAAE 217
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 11-169 6.05e-43

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: 140.40  E-value: 6.05e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  11 PTLGERVFVDDSAVVIGDVEIGADSSVWPLTVIRGDMHRIRIGARSSIQDGSVLHITHagpynpdGFPLTIGDEVTVGHK 90
Cdd:cd04650    1 PRISPKAYVHPTSYVIGDVVIGELTSVWHYAVIRGDNDSIYIGKYSNVQENVSIHTDH-------GYPTEIGDYVTIGHN 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503750419  91 VTLHGCTLGNRILVGMGSIVMDGVVVEDEVIIGAGSLVPPGKTLESGYLYVGSPVKQARPLTDKERSFFSYTAGNYVKL 169
Cdd:cd04650   74 AVVHGAKVGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTPGKEIPDYSLVLGVPAKVVRKLTEEEIEWIKKNAEEYVEL 152
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 11-155 6.97e-36

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: 122.48  E-value: 6.97e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  11 PTLGERVFVDDSAVVIGDVEIGADSSVWPLTVIRGDMHRIRIGARSSIQDGSVLHithagpynpdGFPL---TIGDEVTV 87
Cdd:cd04745    1 PVVDPSSFVHPTAVLIGDVIIGKNCYIGPHASLRGDFGRIVIRDGANVQDNCVIH----------GFPGqdtVLEENGHI 70

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503750419  88 GHKVTLHGCTLGNRILVGMGSIVMDGVVVEDEVIIGAGSLVPPGKTLESGYLYVGSPVKQARPLTDKE 155
Cdd:cd04745   71 GHGAILHGCTIGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAGTVIPPRSLIAGSPAKVIRELSDEE 138
PLN02472 PLN02472
uncharacterized protein
 11-176 1.82e-30

uncharacterized protein


Pssm-ID: 215263 [Multi-domain]  Cd Length: 246  Bit Score: 111.21  E-value: 1.82e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  11 PTLGERVFVDDSAVVIGDVEIGADSSVWPLTVIRGDMHRIRIGARSSIQDGSVLHithAGPYNPDGFP--LTIGDEVTVG 88
Cdd:PLN02472  60 PKVAVDAYVAPNVVLAGQVTVWDGASVWNGAVLRGDLNKITVGFCSNVQERCVLH---AAWNSPTGLPaeTLIDRYVTIG 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  89 HKVTLHGCTLGNRILVGMGSIVMDGVVVEDEVIIGAGSLVPPGKTLESGYLYVGSPVKQARPLTDKERSFFSYTAGNYVK 168
Cdd:PLN02472 137 AYSLLRSCTIEPECIIGQHSILMEGSLVETHSILEAGSVLPPGRRIPTGELWAGNPARFVRTLTNEETLEIPKLAVAIND 216


                 ....*...
gi 503750419 169 LKDQHLAE 176
Cdd:PLN02472 217 LSQSHFSE 224
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 1-155 6.40e-28

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 103.35  E-value: 6.40e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419   1 MAIRSYQNSTPTLGERVFVDDSAVVIGDVEIGADSSVWPLTVIRGDMHRIRIGARSSIQDGSVLHithaGPYNPDgfpLT 80
Cdd:PRK13627   1 MSYYAFEGLIPVVHPTAFVHPSAVLIGDVIVGAGVYIGPLASLRGDYGRLIVQAGANLQDGCIMH----GYCDTD---TI 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503750419  81 IGDEVTVGHKVTLHGCTLGNRILVGMGSIVMDGVVVEDEVIIGAGSLVPPGKTLESGYLYVGSPVKQARPLTDKE 155
Cdd:PRK13627  74 VGENGHIGHGAILHGCVIGRDALVGMNSVIMDGAVIGEESIVAAMSFVKAGFQGEKRQLLMGTPARAVRSVSDDE 148
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 11-158 2.82e-20

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: 82.67  E-value: 2.82e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  11 PTLGERVFVDDSAVVIGDVEIGADSSVWPLTVIRGD-MHRIRIGARSSIQDGSVLHithagpyNPDGFPLTIGDEVTVGH 89
Cdd:cd00710    3 PVIDPSAYVHPTAVVIGDVIIGDNVFVGPGASIRADeGTPIIIGANVNIQDGVVIH-------ALEGYSVWIGKNVSIAH 75

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503750419  90 KVTLHG-CTLGNRILVGMGSIVMDGVVVEDeVIIGAGSLV-----PPGKTLESGylYVGSPVKQAR---PLTDKERSF 158
Cdd:cd00710   76 GAIVHGpAYIGDNCFIGFRSVVFNAKVGDN-CVIGHNAVVdgveiPPGRYVPAG--AVITSQTQADalpDVTDSAREF 150
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
22-156 3.70e-16

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 71.06  E-value: 3.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  22 SAVVIGDVEIGADSSVWPLTVIRGdmHRIRIGARSSIQDGSVLHITHagpynpdgfPLTIGDEVTVGHKVTL-------- 93
Cdd:COG0110    2 KLLLLFGARIGDGVVIGPGVRIYG--GNITIGDNVYIGPGVTIDDPG---------GITIGDNVLIGPGVTIltgnhpid 70

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503750419  94 ---------HGCTLGNRILVGMGSIVMDGVVVEDEVIIGAGSLVppGKTLESGYLYVGSPVKQARPLTDKER 156
Cdd:COG0110   71 dpatfplrtGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVV--TKDVPPYAIVAGNPARVIRKRDEEER 140
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 42-144 1.20e-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: 1.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  42 VIRGDMHRIRIGARSSIQDGSVLHithaGPYN-----PDGFPLTIGDEVTVGHKVTLHGCTLGNRILVGMGSIVMDGVVV 116
Cdd:cd03359   35 IIRGDLATVSIGRYCILSEGCVIR----PPFKkfskgVAFFPLHIGDYVFIGENCVVNAAQIGSYVHIGKNCVIGRRCII 110

                         90       100
                 ....*....|....*....|....*...
gi 503750419 117 EDEVIIGAGSLVPPGKTLESGYLYVGSP 144
Cdd:cd03359  111 KDCVKILDGTVVPPDTVIPPYSVVSGRP 138
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 17-144 7.01e-10

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: 55.57  E-value: 7.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  17 VFVDDSAVVIGDVEIGADssvwplTVIrgdMHRIRIGARSSIQDGSVL----HITHagpynpDGfplTIGDEVTVGHKVT 92
Cdd:cd03360   85 TLIHPSAVVSPSAVIGEG------CVI---MAGAVINPDARIGDNVIIntgaVIGH------DC---VIGDFVHIAPGVV 146

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 503750419  93 LHG-CTLGNRILVGMGSIVMDGVVVEDEVIIGAGSLV----PPGKTlesgylYVGSP 144
Cdd:cd03360  147 LSGgVTIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVtkdvPDGSV------VVGNP 197
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 49-146 1.85e-09

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: 52.46  E-value: 1.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  49 RIRIGARSSIQDGSVLHithagpynpDGFPLTIGDEVTVGHKVTLHGC--------------------TLGNRILVGMGS 108
Cdd:cd04647    1 NISIGDNVYIGPGCVIS---------AGGGITIGDNVLIGPNVTIYDHnhdiddperpieqgvtsapiVIGDDVWIGANV 71

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 503750419 109 IVMDGVVVEDEVIIGAGSLVPpgKTLESGYLYVGSPVK 146
Cdd:cd04647   72 VILPGVTIGDGAVVGAGSVVT--KDVPPNSIVAGNPAK 107
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 19-144 1.15e-08

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: 52.11  E-value: 1.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419   19 VDDSAVVIGDVEIGADSSVWPLTVIRGDmhrIRIGARSSIQDGSVlhITHagpynpDgfpLTIGDEVTVGHKVTLHG-CT 97
Cdd:TIGR03570  90 IHPSAIVSPSASIGEGTVIMAGAVINPD---VRIGDNVIINTGAI--VEH------D---CVIGDFVHIAPGVTLSGgVV 155

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 503750419   98 LGNRILVGMGSIVMDGVVVEDEVIIGAGSLV----PPGKTlesgylYVGSP 144
Cdd:TIGR03570 156 IGEGVFIGAGATIIQGVTIGAGAIVGAGAVVtkdiPDGGV------VVGVP 200
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 31-149 1.35e-07

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: 47.88  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  31 IGADSSVWPLTVIRGDmhrIRIGARSSIQDGSvlHITHagpynpdgfPLTIGDEVTVGHKVT----------------LH 94
Cdd:cd03358    1 IGDNCIIGTNVFIEND---VKIGDNVKIQSNV--SIYE---------GVTIEDDVFIGPNVVftndlyprskiyrkweLK 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 503750419  95 GCTLGNRILVGMGSIVMDGVVVEDEVIIGAGSLVPpgKTLESGYLYVGSPVKQAR 149
Cdd:cd03358   67 GTTVKRGASIGANATILPGVTIGEYALVGAGAVVT--KDVPPYALVVGNPARIIG 119
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 75-159 1.53e-06

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 46.54  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  75 DGFPLTIGDEVTVGHKVTLH-------------------GCTLGNRILVGMGSIVMDGVVVEDEVIIGAGSLVPpgKTLE 135
Cdd:PRK09527  92 DDYTVTIGDNVLIAPNVTLSvtghpvhhelrkngemysfPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVT--KDIP 169

                         90       100
                 ....*....|....*....|....
gi 503750419 136 SGYLYVGSPVKQARPLTDKERSFF 159
Cdd:PRK09527 170 PNVVAAGVPCRVIREINDRDKQYY 193
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 29-128 2.24e-06

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: 43.39  E-value: 2.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  29 VEIGADSSVWPLTVIRGdmhRIRIGARSSIQDGSVLHithAGPYNPDGFPLTIGDEVTVGHKVTLHGctlgnrilvgmgs 108
Cdd:cd00208    1 VFIGEGVKIHPKAVIRG---PVVIGDNVNIGPGAVIG---AATGPNEKNPTIIGDNVEIGANAVIHG------------- 61

                         90       100
                 ....*....|....*....|
gi 503750419 109 ivmdGVVVEDEVIIGAGSLV 128
Cdd:cd00208   62 ----GVKIGDNAVIGAGAVV 77
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 27-135 2.48e-06

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


Pssm-ID: 100052 [Multi-domain]  Cd Length: 164  Bit Score: 45.39  E-value: 2.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  27 GDVEIGADSSVWPLTVIRGDMHRIRIGARSSIQDGSVlhITHAGPYNPD-GFPLTIGDevtvgHKVTLHGCT-----LGN 100
Cdd:cd04646   16 GDVTIGPGTVVHPRATIIAEAGPIIIGENNIIEEQVT--IVNKKPKDPAePKPMIIGS-----NNVFEVGCKcealkIGN 88

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 503750419 101 RILVGMGSIVMDGVVVEDEVIIGAGSLVPPGKTLE 135
Cdd:cd04646   89 NNVFESKSFVGKNVIITDGCIIGAGCKLPSSEILP 123
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 12-128 3.53e-06

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 45.78  E-value: 3.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  12 TLGERVFVDDSAVVIGDVEIGADSSVWPLTVIRGDMhriRIGARSSIQDGSVL-HITHAGPYNPDGFPLTIGDEVTVGHK 90
Cdd:PRK12461  13 KLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPT---RIGKNNKIHQGAVVgDEPQDFTYKGEESRLEIGDRNVIREG 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503750419  91 VTL-------------------------HGCTLGNRILVGMGSIVMDGVVVEDEVIIGAGSLV 128
Cdd:PRK12461  90 VTIhrgtkgggvtrigndnllmayshvaHDCQIGNNVILVNGALLAGHVTVGDRAIISGNCLV 152
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 18-143 7.84e-06

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 44.82  E-value: 7.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  18 FVDDSAVVIG-DVEIGADSSVWPLTVIRGDMH-----------RI---RIGARSSIQDGSVLHI-----THAGPY---NP 74
Cdd:PRK14354 254 IIDPESTYIDaDVEIGSDTVIEPGVVIKGNTVigedcvigpgsRIvdsTIGDGVTITNSVIEESkvgdnVTVGPFahlRP 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  75 DGfplTIGDEVTVGHKVTLHGCTLGN-----------------RILVGMGSIVM--DGV-----VVEDEVIIGAGS-LVP 129
Cdd:PRK14354 334 GS---VIGEEVKIGNFVEIKKSTIGEgtkvshltyigdaevgeNVNIGCGTITVnyDGKnkfktIIGDNAFIGCNSnLVA 410

                        170
                 ....*....|....
gi 503750419 130 PGKTLESGYLYVGS 143
Cdd:PRK14354 411 PVTVGDNAYIAAGS 424
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 12-111 8.26e-06

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: 42.24  E-value: 8.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  12 TLGERVFVDDSAVVIGdveigadssvwpltvirgdmhRIRIGARSSIQDGSVLhitHAGPYNPDGFPLTIGDEVTVGHKV 91
Cdd:cd00208    2 FIGEGVKIHPKAVIRG---------------------PVVIGDNVNIGPGAVI---GAATGPNEKNPTIIGDNVEIGANA 57

                         90       100
                 ....*....|....*....|.
gi 503750419  92 TLHG-CTLGNRILVGMGSIVM 111
Cdd:cd00208   58 VIHGgVKIGDNAVIGAGAVVT 78
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 49-147 1.12e-05

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: 42.21  E-value: 1.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  49 RIRIGARSSIQDGSVLhithagpYNPDgfPLTIGDEVTVGHKVTLhgCT------------------LGNRILVGMGSIV 110
Cdd:cd05825    3 NLTIGDNSWIGEGVWI-------YNLA--PVTIGSDACISQGAYL--CTgshdyrspafplitapivIGDGAWVAAEAFV 71

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 503750419 111 MDGVVVEDEVIIGAGSLVPpgKTLESGYLYVGSPVKQ 147
Cdd:cd05825   72 GPGVTIGEGAVVGARSVVV--RDLPAWTVYAGNPAVP 106
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 75-151 1.34e-05

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: 43.18  E-value: 1.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  75 DGFPLTIGDEVTVGHKVTL-------------------HGCTLGNRILVGMGSIVMDGVVVEDEVIIGAGSLVPpgKTLE 135
Cdd:cd03357   79 DVAPVTIGDNVLIGPNVQIytaghpldpeernrgleyaKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVT--KDIP 156

                         90
                 ....*....|....*.
gi 503750419 136 SGYLYVGSPvkqARPL 151
Cdd:cd03357  157 ANVVAAGNP---ARVI 169
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
12-128 1.45e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 43.93  E-value: 1.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  12 TLGERVFVDDSAVVIGDVEIGADSSVWPLTVI---------RGDMHRIRIGARSSIQDGSVLHITHAGpynpDGFPLTIG 82
Cdd:PRK05289  34 VIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIgedpqdlkyKGEPTRLVIGDNNTIREFVTINRGTVQ----GGGVTRIG 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 503750419  83 DE------VTVGhkvtlHGCTLGNRILvgMGSIVMDG--VVVEDEVIIGAGSLV 128
Cdd:PRK05289 110 DNnllmayVHVA-----HDCVVGNHVI--LANNATLAghVEVGDYAIIGGLTAV 156
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 81-144 2.43e-05

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: 42.38  E-value: 2.43e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503750419  81 IGDEVTVGHKVTLHGC---------TLGNRILVGMGSIVMDGVVVEDEVIIGAGSL----VPPGKTLesgylyVGSP 144
Cdd:COG1045   94 IGDNVTIYQGVTLGGTgkekgkrhpTIGDNVVIGAGAKILGPITIGDNAKIGANSVvlkdVPPGSTV------VGVP 164
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 18-134 3.78e-05

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 42.81  E-value: 3.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  18 FVDDSAVVIG-DVEIGADSSVWPLTVIRGDMhririgarssiqdgsvlhithagpynpdgfplTIGDEVTVGHKVTLHGC 96
Cdd:PRK14355 257 LIDPETTYIDrGVVIGRDTTIYPGVCISGDT--------------------------------RIGEGCTIEQGVVIKGC 304

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 503750419  97 TLGNRILVGMGSiVMDGVVVEDEVIIGAGSLVPPGKTL 134
Cdd:PRK14355 305 RIGDDVTVKAGS-VLEDSVVGDDVAIGPMAHLRPGTEL 341
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 81-133 4.12e-05

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: 40.50  E-value: 4.12e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503750419  81 IGDEVTVGHKVTL--------HGC-TLGNRILVGMGSIVMDGVVVEDEVIIGAGSLV----PPGKT 133
Cdd:cd03354   31 IGDNCTIYQGVTLggkgkgggKRHpTIGDNVVIGAGAKILGNITIGDNVKIGANAVVtkdvPANST 96
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 9-126 4.70e-05

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 42.70  E-value: 4.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419   9 STPTLGERVFVDDSAVVIGDVEIGADSSVWPLTVirgdmhrirIGARSSIQDGSVLhitHAGpynpdgfpLTIGDEVTVG 88
Cdd:COG1044  107 PSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVV---------IGDGVVIGDDCVL---HPN--------VTIYERCVIG 166

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 503750419  89 HKVTLH-GCTLGNRilvGMGsIVMD------------GVVVEDEVIIGAGS 126
Cdd:COG1044  167 DRVIIHsGAVIGAD---GFG-FAPDedggwvkipqlgRVVIGDDVEIGANT 213
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 12-128 5.24e-05

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


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 42.03  E-value: 5.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  12 TLGERVFVDDSAVVIGDVEIGADSSVWPLTVI---------RGDMHRIRIGARSSIQDGSVLHI-THAGpynpdgfplti 81
Cdd:cd03351   31 EIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIgeapqdlkyKGEPTRLEIGDNNTIREFVTIHRgTAQG----------- 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 503750419  82 GDEVTVGHKVTL-------HGCTLGNRILVGMGSIVMDGVVVEDEVIIGAGSLV 128
Cdd:cd03351  100 GGVTRIGNNNLLmayvhvaHDCVIGNNVILANNATLAGHVEIGDYAIIGGLSAV 153
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 15-129 6.14e-05

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: 42.32  E-value: 6.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  15 ERVFVDdsavviGDVEIGADSSVWPLTVIRGdmhRIRIGARSSIQDGSVLHIThagpynpdgfplTIGDEVTVGHKVtLH 94
Cdd:COG1207  259 ATTYID------GDVEIGRDVVIDPNVILEG---KTVIGEGVVIGPNCTLKDS------------TIGDGVVIKYSV-IE 316

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 503750419  95 GCTLGNRILVG------MGSIVMDGVVVED--EV---IIGAGSLVP 129
Cdd:COG1207  317 DAVVGAGATVGpfarlrPGTVLGEGVKIGNfvEVknsTIGEGSKVN 362
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 4-130 6.84e-05

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: 41.64  E-value: 6.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419   4 RSYQNSTPTLGERVFVDDSAVVIGDVEIGADSSVWPLTVIRGDmhriRIGARSSIQDGSVLH------ITHAGPY----- 72
Cdd:cd03353    9 TTYIDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIKDS----TIGDGVVIKASSVIEgavignGATVGPFahlrp 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  73 -----------------NPdgfplTIGDEVTVGHKVTLHGCTLGNRILVGMGSIVM--DGV-----VVEDEVIIGAGS-L 127
Cdd:cd03353   85 gtvlgegvhignfveikKS-----TIGEGSKANHLSYLGDAEIGEGVNIGAGTITCnyDGVnkhrtVIGDNVFIGSNSqL 159


                 ...
gi 503750419 128 VPP 130
Cdd:cd03353  160 VAP 162
PRK10502 PRK10502
putative acyl transferase; Provisional
 49-150 1.18e-04

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 40.70  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  49 RIRIGARSSIQDGSVLhithagpYNPDgfPLTIGDEVTVGHKVTLhgCT------------------LGNRILVGMGSIV 110
Cdd:PRK10502  71 KLTIGDYAWIGDDVWL-------YNLG--EITIGAHCVISQKSYL--CTgshdysdphfdlntapivIGEGCWLAADVFV 139

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 503750419 111 MDGVVVEDEVIIGAGSLVppGKTLESGYLYVGSPVKQARP 150
Cdd:PRK10502 140 APGVTIGSGAVVGARSSV--FKSLPANTICRGNPAVPIRP 177
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 12-64 1.26e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 41.28  E-value: 1.26e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 503750419  12 TLGERVFVDdSAVVIGD-VEIGADSSVWPLTVIRgdmHRIRIGARSSIQDGSVL 64
Cdd:PRK00892 132 VIGDGVVIG-AGAVIGDgVKIGADCRLHANVTIY---HAVRIGNRVIIHSGAVI 181
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 81-137 1.99e-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: 38.33  E-value: 1.99e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503750419  81 IGDEVTVGHKVTLH------GCTLGNRILVgMGSIVMDGVVVEDEVIIgAGSLVPPGKTLESG 137
Cdd:cd04652    2 VGENTQVGEKTSIKrsvigaNCKIGKRVKI-TNCVIMDNVTIEDGCTL-ENCIIGNGAVIGEK 62
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 12-149 1.99e-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: 40.08  E-value: 1.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  12 TLGERVFVDDSAVVIGDVEIGADSSVWPLTVIRgdmHRIRIGARSSIQDGSVLhithagpyNPDGF------------PL 79
Cdd:cd03352   21 VIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIY---EGCIIGDRVIIHSGAVI--------GSDGFgfapdgggwvkiPQ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  80 T----IGDEVTVGHKVTL-----------------------HGC------------------TLGNRILVGMGSIVMDGV 114
Cdd:cd03352   90 LggviIGDDVEIGANTTIdrgalgdtvigdgtkidnlvqiaHNVrigencliaaqvgiagstTIGDNVIIGGQVGIAGHL 169

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 503750419 115 VVEDEVIIGAGSLVPpgKTLESGYLYVGSPVKQAR 149
Cdd:cd03352  170 TIGDGVVIGAGSGVT--SIVPPGEYVSGTPAQPHR 202
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 80-144 2.15e-04

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: 40.89  E-value: 2.15e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503750419   80 TIGDEVTV--GHKVTLH----------GCTLGNRILVGMGSIVMDGVVVEDEVIIGAGSLVPPGKTLESGYLYVGSP 144
Cdd:TIGR02353 618 TIGDDSTLneGSVIQTHlfedrvmksdTVTIGDGATLGPGAIVLYGVVMGEGSVLGPDSLVMKGEEVPAHTRWRGNP 694
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 18-126 2.26e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 40.51  E-value: 2.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  18 FVDDSAVVIGDVEIGadssvwPLTVIrGDmhRIRIGARSSIQDGSVLhithaGPYnpdgfpLTIGDEVTVGHKVTL-HGC 96
Cdd:PRK00892 108 VIDPSAKIGEGVSIG------PNAVI-GA--GVVIGDGVVIGAGAVI-----GDG------VKIGADCRLHANVTIyHAV 167

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 503750419  97 TLGNRILVGMGSIV-MDG------------------VVVEDEVIIGAGS 126
Cdd:PRK00892 168 RIGNRVIIHSGAVIgSDGfgfandrggwvkipqlgrVIIGDDVEIGANT 216
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 12-126 4.45e-04

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 39.31  E-value: 4.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  12 TLGERVFVDDSAVVIGDVEIGADSSVWPLTVirgdmhrirIGARSSIQDGSVLHiTHAgpynpdgfplTIGDEVTVGHKV 91
Cdd:cd03352    3 KIGENVSIGPNAVIGEGVVIGDGVVIGPGVV---------IGDGVVIGDDCVIH-PNV----------TIYEGCIIGDRV 62

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 503750419  92 TLH-GCTLGNRilvGMGSIVMDG----------VVVEDEVIIGAGS 126
Cdd:cd03352   63 IIHsGAVIGSD---GFGFAPDGGgwvkipqlggVIIGDDVEIGANT 105
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 12-158 7.99e-04

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 38.85  E-value: 7.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  12 TLGERVFVDdSAVVIGD-VEIGADSSVWPLTVIRgdmHRIRIGARSSIQDGSVLhithaGPynpDGF------------- 77
Cdd:COG1044  128 VIGDGVVIG-PGVVIGDgVVIGDDCVLHPNVTIY---ERCVIGDRVIIHSGAVI-----GA---DGFgfapdedggwvki 195

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  78 P----LTIGDEV---------------TV-------------GHKVTL--H-----------GCTLGNRILVGMGSIVMD 112
Cdd:COG1044  196 PqlgrVVIGDDVeiganttidrgalgdTVigdgtkidnlvqiAHNVRIgeHtaiaaqvgiagSTKIGDNVVIGGQVGIAG 275

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 503750419 113 GVVVEDEVIIGAGSLVppGKTLESGYLYVGSPvkqARPLTDKERSF 158
Cdd:COG1044  276 HLTIGDGVIIGAQSGV--TKSIPEGGVYSGSP---AQPHREWLRNA 316
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 19-131 1.09e-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: 38.46  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  19 VDDSAVVIGDVEIGADSSVWPLTVIrgdmhririGARSSIQDGSVLHithAGPYnpdgfpltIGDEVTVGHKVTLHGctl 98
Cdd:COG1044   99 IHPSAVIDPSAKIGEGVSIGPFAVI---------GAGVVIGDGVVIG---PGVV--------IGDGVVIGDDCVLHP--- 155

                         90       100       110
                 ....*....|....*....|....*....|...
gi 503750419  99 gnrilvgmgsivmdGVVVEDEVIIGAGSLVPPG 131
Cdd:COG1044  156 --------------NVTIYERCVIGDRVIIHSG 174
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 19-128 1.24e-03

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 38.08  E-value: 1.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  19 VDDSA-----VVIG-------DVEIGADSSVWPLTVIRGdmhRIRIGARSSIQDGSVL-----HITHAGPynpdgfP--L 79
Cdd:COG1043   10 VDPGAklgenVEIGpfcvigpDVEIGDGTVIGSHVVIEG---PTTIGKNNRIFPFASIgeepqDLKYKGE------PtrL 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503750419  80 TIGDEVTVGHKVTL--------------------------HGCTLGNRILVGMGSIVMDGVVVEDEVIIGAGSLV 128
Cdd:COG1043   81 EIGDNNTIREFVTIhrgtvqgggvtrigddnllmayvhvaHDCVVGNNVILANNATLAGHVEVGDHAIIGGLSAV 155
PLN02357 PLN02357
serine acetyltransferase
 81-155 1.31e-03

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 38.32  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  81 IGDEVTVGHKVTLHGC---------TLGNRILVGMGSIVMDGVVVEDEVIIGAGSL----VPPGKTLesgylyVGSPvkq 147
Cdd:PLN02357 255 VGNNVSILHNVTLGGTgkqsgdrhpKIGDGVLIGAGTCILGNITIGEGAKIGAGSVvlkdVPPRTTA------VGNP--- 325


                 ....*...
gi 503750419 148 ARPLTDKE 155
Cdd:PLN02357 326 ARLIGGKE 333
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 79-146 2.35e-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: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419   79 LTIGDEVTVGHKVTLHG------------CTLGNRILVGMGSIVMDGVVVEDEVIIGAGSLVPPGKTLESGYLYVGSPVK 146
Cdd:TIGR02353 132 LTIGAGTIVRKEVMLLGyraergrlhtgpVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSALQGGQSIPDGERWHGSPAQ 211
PLN02694 PLN02694
serine O-acetyltransferase
 81-156 4.03e-03

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 36.93  E-value: 4.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  81 IGDEVTVGHKVTLHGC---------TLGNRILVGMGSIVMDGVVVEDEVIIGAGSL----VPPGKTLesgylyVGSPvkq 147
Cdd:PLN02694 189 IGNNVSILHHVTLGGTgkacgdrhpKIGDGVLIGAGATILGNVKIGEGAKIGAGSVvlidVPPRTTA------VGNP--- 259


                 ....*....
gi 503750419 148 ARPLTDKER 156
Cdd:PLN02694 260 ARLVGGKEK 268
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 12-122 4.05e-03

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 36.93  E-value: 4.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  12 TLGERVFVDdSAVVIGDVEIGADSSVWPLTVIR----------GDMHRIRIGA---------------RSSIQDGS-VLH 65
Cdd:PRK09451 285 TLGNRVKIG-AGCVLKNCVIGDDCEISPYSVVEdanlgaactiGPFARLRPGAelaegahvgnfvemkKARLGKGSkAGH 363

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503750419  66 ITHAGPY---------------NPDG---FPLTIGDEVTVGHKVTLHG-CTLGNRILVGMGSIVMDGvVVEDEVII 122
Cdd:PRK09451 364 LTYLGDAeigdnvnigagtitcNYDGankFKTIIGDDVFVGSDTQLVApVTVGKGATIGAGTTVTRD-VAENELVI 438
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 28-128 4.27e-03

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 36.23  E-value: 4.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503750419  28 DVEIGADSSVWPLTVIrgdMHRIRIGARSSIQDGSVlhithagpynpdgfpltIGDEVTVGHKVTLHGctlgnrilvgmG 107
Cdd:cd03352    1 SAKIGENVSIGPNAVI---GEGVVIGDGVVIGPGVV-----------------IGDGVVIGDDCVIHP-----------N 49

                         90       100
                 ....*....|....*....|.
gi 503750419 108 SIVMDGVVVEDEVIIGAGSLV 128
Cdd:cd03352   50 VTIYEGCIIGDRVIIHSGAVI 70
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 80-137 9.38e-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: 35.76  E-value: 9.38e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 503750419  80 TIGDEVTVGHkvtlhGCTLGNRILVGMGSIVMDGVVVEDEVIIGAGSLVPPGKTLESG 137
Cdd:COG1044  110 KIGEGVSIGP-----FAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYER 162
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 81-131 9.72e-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: 35.46  E-value: 9.72e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 503750419  81 IGDEVTVGHKVTLH-GCTLGNRILVGMGSIVMDGVVVEDEVIIGAGSLVPPG 131
Cdd:cd03352   16 IGEGVVIGDGVVIGpGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSG 67
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 86-124 9.74e-03

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 35.60  E-value: 9.74e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 503750419  86 TVGHKVTLHGCTLGNRIlVGMGSIVMDGVVVEDEVIIGA 124
Cdd:PLN02241 317 IISHGCFLRECKIEHSV-VGLRSRIGEGVEIEDTVMMGA 354
 
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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