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Conserved domains on  [gi|447029945|ref|WP_001107201|]
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MULTISPECIES: gamma carbonic anhydrase family protein [Acinetobacter]

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

 Zoom to residue level

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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 ...
 4-177 1.63e-87

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


:

Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 253.80  E-value: 1.63e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945   4 NIRPYLDHHPQIDPSCYIDEMSVVVGDVKLAENVSVWPFAVIRGDVNSIQIGKNSNVQDHCMLHVSHkndtkpnGSPLII 83
Cdd:COG0663    2 MIYSFDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVDP-------GYPLTI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  84 GEDVTVGHHVTLHGCTIGNRVLVGINTVILDDVVIEDDVMIGAGSLVPPRKVLKSGYLYVGSPVQQVRPLTEKELAFLPY 163
Cdd:COG0663   75 GDDVTIGHGAILHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLRE 154

                        170
                 ....*....|....
gi 447029945 164 SARHYVKVQNNHKD 177
Cdd:COG0663  155 SAENYVELARRYLA 168
 
Name Accession Description Interval E-value
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 4-177 1.63e-87

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 253.80  E-value: 1.63e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945   4 NIRPYLDHHPQIDPSCYIDEMSVVVGDVKLAENVSVWPFAVIRGDVNSIQIGKNSNVQDHCMLHVSHkndtkpnGSPLII 83
Cdd:COG0663    2 MIYSFDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVDP-------GYPLTI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  84 GEDVTVGHHVTLHGCTIGNRVLVGINTVILDDVVIEDDVMIGAGSLVPPRKVLKSGYLYVGSPVQQVRPLTEKELAFLPY 163
Cdd:COG0663   75 GDDVTIGHGAILHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLRE 154

                        170
                 ....*....|....
gi 447029945 164 SARHYVKVQNNHKD 177
Cdd:COG0663  155 SAENYVELARRYLA 168
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 14-170 5.59e-78

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: 229.22  E-value: 5.59e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  14 QIDPSCYIDEMSVVVGDVKLAENVSVWPFAVIRGDVNSIQIGKNSNVQDHCMLHVSHkndtkpnGSPLIIGEDVTVGHHV 93
Cdd:cd04645    1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRGDVNPIRIGERTNIQDGSVLHVDP-------GYPTIIGDNVTVGHGA 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447029945  94 TLHGCTIGNRVLVGINTVILDDVVIEDDVMIGAGSLVPPRKVLKSGYLYVGSPVQQVRPLTEKELAFLPYSARHYVK 170
Cdd:cd04645   74 VLHGCTIGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGKVIPPGSLVAGSPAKVVRELTDEEIAELRESAEHYVE 150
PLN02296 PLN02296
carbonate dehydratase
 10-175 3.56e-45

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 149.89  E-value: 3.56e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  10 DHHPQIDPSCYIDEMSVVVGDVKLAENVSVWPFAVIRGDVNSIQIGKNSNVQDHCMLHVShKNDTKPNGSPLIIGEDVTV 89
Cdd:PLN02296  50 DKAPVVDKDAFVAPSASVIGDVQVGRGSSIWYGCVLRGDVNSISVGSGTNIQDNSLVHVA-KTNLSGKVLPTIIGDNVTI 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  90 GHHVTLHGCTIGNRVLVGINTVILDDVVIEDDVMIGAGSLVPPRKVLKSGYLYVGSPVQQVRPLTEKELAFLPYSARHYV 169
Cdd:PLN02296 129 GHSAVLHGCTVEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNTRIPSGEVWAGNPAKFLRKLTEEEIAFISQSATNYS 208


                 ....*.
gi 447029945 170 KVQNNH 175
Cdd:PLN02296 209 NLAQVH 214
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 20-146 3.80e-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: 64.44  E-value: 3.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945   20 YIDEMSVVVGDVKLAENVSVWPFAVIRGDVnsiQIGKNSNVQDHCMlhVSHknDTkpngsplIIGEDVTVGHHVTLHG-C 98
Cdd:TIGR03570  89 LIHPSAIVSPSASIGEGTVIMAGAVINPDV---RIGDNVIINTGAI--VEH--DC-------VIGDFVHIAPGVTLSGgV 154

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 447029945   99 TIGNRVLVGINTVILDDVVIEDDVMIGAGSLVppRKVLKSGYLYVGSP 146
Cdd:TIGR03570 155 VIGEGVFIGAGATIIQGVTIGAGAIVGAGAVV--TKDIPDGGVVVGVP 200
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
97-126 3.28e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 36.55  E-value: 3.28e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 447029945   97 GCTIGNRVLVGINTVILDDVVIEDDVMIGA 126
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 4-177 1.63e-87

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 253.80  E-value: 1.63e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945   4 NIRPYLDHHPQIDPSCYIDEMSVVVGDVKLAENVSVWPFAVIRGDVNSIQIGKNSNVQDHCMLHVSHkndtkpnGSPLII 83
Cdd:COG0663    2 MIYSFDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGPIRIGEGSNIQDGVVLHVDP-------GYPLTI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  84 GEDVTVGHHVTLHGCTIGNRVLVGINTVILDDVVIEDDVMIGAGSLVPPRKVLKSGYLYVGSPVQQVRPLTEKELAFLPY 163
Cdd:COG0663   75 GDDVTIGHGAILHGCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLVVGSPAKVVRELTEEEIAFLRE 154

                        170
                 ....*....|....
gi 447029945 164 SARHYVKVQNNHKD 177
Cdd:COG0663  155 SAENYVELARRYLA 168
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 14-170 5.59e-78

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: 229.22  E-value: 5.59e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  14 QIDPSCYIDEMSVVVGDVKLAENVSVWPFAVIRGDVNSIQIGKNSNVQDHCMLHVSHkndtkpnGSPLIIGEDVTVGHHV 93
Cdd:cd04645    1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRGDVNPIRIGERTNIQDGSVLHVDP-------GYPTIIGDNVTVGHGA 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 447029945  94 TLHGCTIGNRVLVGINTVILDDVVIEDDVMIGAGSLVPPRKVLKSGYLYVGSPVQQVRPLTEKELAFLPYSARHYVK 170
Cdd:cd04645   74 VLHGCTIGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGKVIPPGSLVAGSPAKVVRELTDEEIAELRESAEHYVE 150
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 13-170 2.05e-45

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: 146.95  E-value: 2.05e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  13 PQIDPSCYIDEMSVVVGDVKLAENVSVWPFAVIRGDVNSIQIGKNSNVQDHCMLHVSHkndtkpnGSPLIIGEDVTVGHH 92
Cdd:cd04650    1 PRISPKAYVHPTSYVIGDVVIGELTSVWHYAVIRGDNDSIYIGKYSNVQENVSIHTDH-------GYPTEIGDYVTIGHN 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447029945  93 VTLHGCTIGNRVLVGINTVILDDVVIEDDVMIGAGSLVPPRKVLKSGYLYVGSPVQQVRPLTEKELAFLPYSARHYVK 170
Cdd:cd04650   74 AVVHGAKVGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTPGKEIPDYSLVLGVPAKVVRKLTEEEIEWIKKNAEEYVE 151
PLN02296 PLN02296
carbonate dehydratase
 10-175 3.56e-45

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 149.89  E-value: 3.56e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  10 DHHPQIDPSCYIDEMSVVVGDVKLAENVSVWPFAVIRGDVNSIQIGKNSNVQDHCMLHVShKNDTKPNGSPLIIGEDVTV 89
Cdd:PLN02296  50 DKAPVVDKDAFVAPSASVIGDVQVGRGSSIWYGCVLRGDVNSISVGSGTNIQDNSLVHVA-KTNLSGKVLPTIIGDNVTI 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  90 GHHVTLHGCTIGNRVLVGINTVILDDVVIEDDVMIGAGSLVPPRKVLKSGYLYVGSPVQQVRPLTEKELAFLPYSARHYV 169
Cdd:PLN02296 129 GHSAVLHGCTVEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNTRIPSGEVWAGNPAKFLRKLTEEEIAFISQSATNYS 208


                 ....*.
gi 447029945 170 KVQNNH 175
Cdd:PLN02296 209 NLAQVH 214
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 13-168 6.08e-37

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: 125.17  E-value: 6.08e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  13 PQIDPSCYIDEMSVVVGDVKLAENVSVWPFAVIRGDVNSIQIGKNSNVQDHCMLHVShkndtkpNGSPLIIGEDVTVGHH 92
Cdd:cd04745    1 PVVDPSSFVHPTAVLIGDVIIGKNCYIGPHASLRGDFGRIVIRDGANVQDNCVIHGF-------PGQDTVLEENGHIGHG 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447029945  93 VTLHGCTIGNRVLVGINTVILDDVVIEDDVMIGAGSLVPPRKVLKSGYLYVGSPVQQVRPLTEKELAFLPYSARHY 168
Cdd:cd04745   74 AILHGCTIGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAGTVIPPRSLIAGSPAKVIRELSDEEVAWKTRGTKEY 149
PLN02472 PLN02472
uncharacterized protein
 3-172 1.58e-31

uncharacterized protein


Pssm-ID: 215263 [Multi-domain]  Cd Length: 246  Bit Score: 113.90  E-value: 1.58e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945   3 KNIRPYLDHHPQIDPSCYIDEMSVVVGDVKLAENVSVWPFAVIRGDVNSIQIGKNSNVQDHCMLHVSHkndTKPNGSP-- 80
Cdd:PLN02472  50 RQIIPLGQWVPKVAVDAYVAPNVVLAGQVTVWDGASVWNGAVLRGDLNKITVGFCSNVQERCVLHAAW---NSPTGLPae 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  81 LIIGEDVTVGHHVTLHGCTIGNRVLVGINTVILDDVVIEDDVMIGAGSLVPPRKVLKSGYLYVGSPVQQVRPLTEKE--- 157
Cdd:PLN02472 127 TLIDRYVTIGAYSLLRSCTIEPECIIGQHSILMEGSLVETHSILEAGSVLPPGRRIPTGELWAGNPARFVRTLTNEEtle 206

                        170       180       190
                 ....*....|....*....|....*....|.
gi 447029945 158 ---LA-------------FLPYSARhYVKVQ 172
Cdd:PLN02472 207 ipkLAvaindlsqshfseFLPYSTA-YLEVE 236
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 13-168 1.39e-28

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 104.89  E-value: 1.39e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  13 PQIDPSCYIDEMSVVVGDVKLAENVSVWPFAVIRGDVNSIQIGKNSNVQDHCMLHVSHKNDTkpngsplIIGEDVTVGHH 92
Cdd:PRK13627  11 PVVHPTAFVHPSAVLIGDVIVGAGVYIGPLASLRGDYGRLIVQAGANLQDGCIMHGYCDTDT-------IVGENGHIGHG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  93 VTLHGCTIGNRVLVGINTVILDDVVIEDDVMIGAGSLVP------PRKVLksgylyVGSPVQQVRPLTEKELAFLPYSAR 166
Cdd:PRK13627  84 AILHGCVIGRDALVGMNSVIMDGAVIGEESIVAAMSFVKagfqgeKRQLL------MGTPARAVRSVSDDELHWKRLNTK 157


                 ..
gi 447029945 167 HY 168
Cdd:PRK13627 158 EY 159
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 11-139 1.06e-23

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: 91.53  E-value: 1.06e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  11 HHPQIDPSCYIDEMSVVVGDVKLAENVSVWPFAVIRGDV-NSIQIGKNSNVQDHCMLHVShkndtkpNGSPLIIGEDVTV 89
Cdd:cd00710    1 DEPVIDPSAYVHPTAVVIGDVIIGDNVFVGPGASIRADEgTPIIIGANVNIQDGVVIHAL-------EGYSVWIGKNVSI 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447029945  90 GHHVTLHG-CTIGNRVLVGINTVIL-----DDVVIE-----DDVMIGAGSLVPPRKVLKSG 139
Cdd:cd00710   74 AHGAIVHGpAYIGDNCFIGFRSVVFnakvgDNCVIGhnavvDGVEIPPGRYVPAGAVITSQ 134
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
30-157 1.01e-16

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 72.60  E-value: 1.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  30 DVKLAENVSVWPFAVIRGdvNSIQIGKNSNVQDHCMLHVSHKndtkpngspLIIGEDVTVGHHVTL-------------- 95
Cdd:COG0110    8 GARIGDGVVIGPGVRIYG--GNITIGDNVYIGPGVTIDDPGG---------ITIGDNVLIGPGVTIltgnhpiddpatfp 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 447029945  96 ---HGCTIGNRVLVGINTVILDDVVIEDDVMIGAGSLVppRKVLKSGYLYVGSPVQQVRPLTEKE 157
Cdd:COG0110   77 lrtGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVV--TKDVPPYAIVAGNPARVIRKRDEEE 139
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 13-128 1.40e-15

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: 72.74  E-value: 1.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  13 PQIDPSCYIDEmsvvvgDVKLAENVSVWPFAVIRGDVnsiQIGKNSNVQDHCmlhvshkndtkpngsplIIGEDVTVG-- 90
Cdd:COG1044   97 PGIHPSAVIDP------SAKIGEGVSIGPFAVIGAGV---VIGDGVVIGPGV-----------------VIGDGVVIGdd 150

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447029945  91 ----HHVTL-HGCTIGNRVLVGINTVILDD--------------------VVIEDDVMIGAGS 128
Cdd:COG1044  151 cvlhPNVTIyERCVIGDRVIIHSGAVIGADgfgfapdedggwvkipqlgrVVIGDDVEIGANT 213
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 20-146 1.35e-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: 1.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  20 YIDEMSVVVGDVKLAENVSVWPFAVIRGDVnsiQIGKNSNVQDHCmlHVSHknDTKpngspliIGEDVTVGHHVTLHG-C 98
Cdd:cd03360   86 LIHPSAVVSPSAVIGEGCVIMAGAVINPDA---RIGDNVIINTGA--VIGH--DCV-------IGDFVHIAPGVVLSGgV 151

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 447029945  99 TIGNRVLVGINTVILDDVVIEDDVMIGAGSLVppRKVLKSGYLYVGSP 146
Cdd:cd03360  152 TIGEGAFIGAGATIIQGVTIGAGAIIGAGAVV--TKDVPDGSVVVGNP 197
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 43-155 2.04e-13

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: 64.54  E-value: 2.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  43 AVIRGDVNSIQIGKNSNVQDHCMLHVSHK-NDTKPNGSPLIIGEDVTVGHHVTLHGCTIGNRVLVGINTVILDDVVIEDD 121
Cdd:cd03359   34 VIIRGDLATVSIGRYCILSEGCVIRPPFKkFSKGVAFFPLHIGDYVFIGENCVVNAAQIGSYVHIGKNCVIGRRCIIKDC 113

                         90       100       110
                 ....*....|....*....|....*....|....
gi 447029945 122 VMIGAGSLVPPRKVLKSGYLYVGSPVQQVRPLTE 155
Cdd:cd03359  114 VKILDGTVVPPDTVIPPYSVVSGRPARFIGELPE 147
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 13-128 2.99e-13

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 66.32  E-value: 2.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  13 PQIDPSCYIDEmsvvvgDVKLAENVSVWPFAVIRGDVnsiQIGKNSNVQDHCMLhvshkndtkpnGSPLIIGEDVTVGHH 92
Cdd:PRK00892 101 AGIHPSAVIDP------SAKIGEGVSIGPNAVIGAGV---VIGDGVVIGAGAVI-----------GDGVKIGADCRLHAN 160

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 447029945  93 VTL-HGCTIGNRVLVGINTVILDD-------------------VVIEDDVMIGAGS 128
Cdd:PRK00892 161 VTIyHAVRIGNRVIIHSGAVIGSDgfgfandrggwvkipqlgrVIIGDDVEIGANT 216
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 20-146 3.80e-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: 64.44  E-value: 3.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945   20 YIDEMSVVVGDVKLAENVSVWPFAVIRGDVnsiQIGKNSNVQDHCMlhVSHknDTkpngsplIIGEDVTVGHHVTLHG-C 98
Cdd:TIGR03570  89 LIHPSAIVSPSASIGEGTVIMAGAVINPDV---RIGDNVIINTGAI--VEH--DC-------VIGDFVHIAPGVTLSGgV 154

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 447029945   99 TIGNRVLVGINTVILDDVVIEDDVMIGAGSLVppRKVLKSGYLYVGSP 146
Cdd:TIGR03570 155 VIGEGVFIGAGATIIQGVTIGAGAIVGAGAVV--TKDIPDGGVVVGVP 200
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 33-151 5.83e-11

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: 56.74  E-value: 5.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  33 LAENVSVWPFAVIRGDVnsiQIGKNSNVQDHCMLhvshkndtkpnGSPLIIGEDVTVGHHVT----------------LH 96
Cdd:cd03358    1 IGDNCIIGTNVFIENDV---KIGDNVKIQSNVSI-----------YEGVTIEDDVFIGPNVVftndlyprskiyrkweLK 66

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 447029945  97 GCTIGNRVLVGINTVILDDVVIEDDVMIGAGSLVppRKVLKSGYLYVGSPVQQVR 151
Cdd:cd03358   67 GTTVKRGASIGANATILPGVTIGEYALVGAGAVV--TKDVPPYALVVGNPARIIG 119
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 51-146 1.38e-10

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: 55.54  E-value: 1.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  51 SIQIGKNSNVQDHCMLHvshkndtkpNGSPLIIGEDVTVGHHVTLHGC--------------------TIGNRVLVGINT 110
Cdd:cd04647    1 NISIGDNVYIGPGCVIS---------AGGGITIGDNVLIGPNVTIYDHnhdiddperpieqgvtsapiVIGDDVWIGANV 71

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 447029945 111 VILDDVVIEDDVMIGAGSLVppRKVLKSGYLYVGSP 146
Cdd:cd04647   72 VILPGVTIGDGAVVGAGSVV--TKDVPPNSIVAGNP 105
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 13-130 2.57e-09

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: 54.64  E-value: 2.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  13 PQIDPSCYIDEmsvvvgDVKLAENVSVWPFAVIRGDVnsiQIGKNSNVQDHCMLH----------------VSHKN-DTK 75
Cdd:COG1043    2 AMIHPTAIVDP------GAKLGENVEIGPFCVIGPDV---EIGDGTVIGSHVVIEgpttigknnrifpfasIGEEPqDLK 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  76 PNGSP--LIIGEDVTVGHHVTL--------------------------HGCTIGNRVLVGINTVILDDVVIEDDVMIGAG 127
Cdd:COG1043   73 YKGEPtrLEIGDNNTIREFVTIhrgtvqgggvtrigddnllmayvhvaHDCVVGNNVILANNATLAGHVEVGDHAIIGGL 152


                 ...
gi 447029945 128 SLV 130
Cdd:COG1043  153 SAV 155
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 8-130 2.76e-09

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 54.64  E-value: 2.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945   8 YLDHHPQIDPSCYIDEMSVVVGDVKLAENVSVWPFAVI---------RGDVNSIQIGKNSNVQDHCMLHvshkNDTKPNG 78
Cdd:PRK12461  25 VIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVgdepqdftyKGEESRLEIGDRNVIREGVTIH----RGTKGGG 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 447029945  79 SPlIIGED--VTVGHHVTlHGCTIGNRVLVGINTVILDDVVIEDDVMIGAGSLV 130
Cdd:PRK12461 101 VT-RIGNDnlLMAYSHVA-HDCQIGNNVILVNGALLAGHVTVGDRAIISGNCLV 152
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 31-130 3.95e-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: 51.10  E-value: 3.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  31 VKLAENVSVWPFAVIRGDVnsiQIGKNSNVQDHCMLHVSHKNDTKpngSPLIIGEDVTVGHHVTLHGCtignrvlvgint 110
Cdd:cd00208    1 VFIGEGVKIHPKAVIRGPV---VIGDNVNIGPGAVIGAATGPNEK---NPTIIGDNVEIGANAVIHGG------------ 62

                         90       100
                 ....*....|....*....|
gi 447029945 111 vilddVVIEDDVMIGAGSLV 130
Cdd:cd00208   63 -----VKIGDNAVIGAGAVV 77
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 76-130 3.98e-09

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: 51.67  E-value: 3.98e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  76 PNGSPLIIGEDVTVGHHVTL-HGCT--------------IGNRVLVGINTVILDDVVIEDDVMIGAGSLV 130
Cdd:cd03354   18 DHGTGIVIGETAVIGDNCTIyQGVTlggkgkgggkrhptIGDNVVIGAGAKILGNITIGDNVKIGANAVV 87
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 14-130 4.70e-09

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: 53.98  E-value: 4.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  14 QIDPSCYIDEmsvvvgDVKLAENVSVWPFAVIRGDVN-----------SIQ----IGKNSNVQDHCMLhvSHKN-DTKPN 77
Cdd:cd03351    1 MIHPTAIVDP------GAKIGENVEIGPFCVIGPNVEigdgtvigshvVIDgpttIGKNNRIFPFASI--GEAPqDLKYK 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  78 GSP--LIIGEDVTVGHHVTLHG--------------------------CTIGNRVLVGINTVILDDVVIEDDVMIGAGSL 129
Cdd:cd03351   73 GEPtrLEIGDNNTIREFVTIHRgtaqgggvtrignnnllmayvhvahdCVIGNNVILANNATLAGHVEIGDYAIIGGLSA 152


                 .
gi 447029945 130 V 130
Cdd:cd03351  153 V 153
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 15-125 1.49e-08

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: 53.11  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  15 IDP-SCYIDemsvvvGDVKLAENVSVWPFAVIRGDVnsiqigknsnvqdhcmlhvshkndtkpngsplIIGEDVTVGHHV 93
Cdd:COG1207  256 IDPaTTYID------GDVEIGRDVVIDPNVILEGKT--------------------------------VIGEGVVIGPNC 297

                         90       100       110
                 ....*....|....*....|....*....|..
gi 447029945  94 TLHGCTIGNRVLVgINTVIlDDVVIEDDVMIG 125
Cdd:COG1207  298 TLKDSTIGDGVVI-KYSVI-EDAVVGAGATVG 327
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 14-128 1.99e-08

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 51.64  E-value: 1.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  14 QIDPSCYIDEMSVVVGDVKLAENVSVWPFAVIRGDVnsiqigknsnvqdhcmlhvshkndtkpngsplIIGEDVTVGHHV 93
Cdd:cd03352    3 KIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGV--------------------------------VIGDDCVIHPNV 50

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 447029945  94 TL-HGCTIGNRVLVGINTVILDD-------------------VVIEDDVMIGAGS 128
Cdd:cd03352   51 TIyEGCIIGDRVIIHSGAVIGSDgfgfapdgggwvkipqlggVIIGDDVEIGANT 105
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
14-130 3.01e-08

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 51.64  E-value: 3.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  14 QIDPSCYIDEMSVVVGDVKLAENVSVWPFAVIRGDVnsiQIGKNSNVQDHCMlhVSHKN-DTKPNGSP--LIIGEDVTVG 90
Cdd:PRK05289  16 KIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHT---TIGKNNRIFPFAS--IGEDPqDLKYKGEPtrLVIGDNNTIR 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447029945  91 HHVTL--------------------------HGCTIGNRVLVGINTVILDDVVIEDDVMIGAGSLV 130
Cdd:PRK05289  91 EFVTInrgtvqgggvtrigdnnllmayvhvaHDCVVGNHVILANNATLAGHVEVGDYAIIGGLTAV 156
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 14-149 3.28e-08

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: 50.40  E-value: 3.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  14 QIDPSCYIDEMSVVVGDVKLAENVSVWPFAVIRGDVNSIQIGKNSNVQDHCMLhVSHKNDTKPNGSPLIIGEdvtvgHHV 93
Cdd:cd04646    1 KIAPGAVVCQESEIRGDVTIGPGTVVHPRATIIAEAGPIIIGENNIIEEQVTI-VNKKPKDPAEPKPMIIGS-----NNV 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 447029945  94 TLHGCT-----IGNRVLVGINTVILDDVVIEDDVMIGAGSLVPPRKVLKSGYLYVGSPVQQ 149
Cdd:cd04646   75 FEVGCKcealkIGNNNVFESKSFVGKNVIITDGCIIGAGCKLPSSEILPENTVIYGADCLR 135
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 82-130 3.65e-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: 3.65e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 447029945  82 IIGEDVTVGHHVTLHGC---------TIGNRVLVGINTVILDDVVIEDDVMIGAGSLV 130
Cdd:COG1045   93 VIGDNVTIYQGVTLGGTgkekgkrhpTIGDNVVIGAGAKILGPITIGDNAKIGANSVV 150
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 14-152 8.41e-08

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 50.70  E-value: 8.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  14 QIDPSCYIDEMSV---------VVGDVKLAENVSVWPFAVIRGDVN---SIQIG-----KNSNVQDHC-MLHVSHKNDTK 75
Cdd:PRK14360 288 RIGPGSLIENSQIgenvtvlysVVSDSQIGDGVKIGPYAHLRPEAQigsNCRIGnfveiKKSQLGEGSkVNHLSYIGDAT 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  76 pngspliIGEDVTVG--------HHVTLHGCTIGNRVLVGINTVILDDVVIEDDVMIGAGSLVPprKVLKSGYLYVGSPV 147
Cdd:PRK14360 368 -------LGEQVNIGagtitanyDGVKKHRTVIGDRSKTGANSVLVAPITLGEDVTVAAGSTIT--KDVPDNSLAIARSR 438


                 ....*
gi 447029945 148 QQVRP 152
Cdd:PRK14360 439 QVIKE 443
PLN02694 PLN02694
serine O-acetyltransferase
 78-150 5.97e-07

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 48.10  E-value: 5.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  78 GSPLIIGEDVTVGHHVTLHGC---------TIGNRVLVGINTVILDDVVIEDDVMIGAGSL----VPPRKVLksgylyVG 144
Cdd:PLN02694 184 GETAVIGNNVSILHHVTLGGTgkacgdrhpKIGDGVLIGAGATILGNVKIGEGAKIGAGSVvlidVPPRTTA------VG 257


                 ....*.
gi 447029945 145 SPVQQV 150
Cdd:PLN02694 258 NPARLV 263
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 15-113 7.53e-07

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 44.93  E-value: 7.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  15 IDPSCYIDEMSVVVGDVklaenvsvwpfavirgdvnsiQIGKNSNVQDHCMLHVSHKNDTKpngSPLIIGEDVTVGHHVT 94
Cdd:cd00208    3 IGEGVKIHPKAVIRGPV---------------------VIGDNVNIGPGAVIGAATGPNEK---NPTIIGDNVEIGANAV 58

                         90       100
                 ....*....|....*....|
gi 447029945  95 LHG-CTIGNRVLVGINTVIL 113
Cdd:cd00208   59 IHGgVKIGDNAVIGAGAVVT 78
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 15-125 2.41e-06

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: 45.49  E-value: 2.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  15 IDP-SCYIDemsvvvGDVKLAENVSVWPFAVIRGDVnsiqigknsnvqdhcmlhvshkndtkpngsplIIGEDVTVGHHV 93
Cdd:cd03353    5 IDPeTTYID------GDVEIGVDVVIDPGVILEGKT--------------------------------VIGEDCVIGPNC 46

                         90       100       110
                 ....*....|....*....|....*....|..
gi 447029945  94 TLHGCTIGNRVLVGINTVIlDDVVIEDDVMIG 125
Cdd:cd03353   47 VIKDSTIGDGVVIKASSVI-EGAVIGNGATVG 77
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 30-130 3.02e-06

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 45.48  E-value: 3.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  30 DVKLAENVSVWPFAVIRGDVnsiqigknsnvqdhcmlhvshkndtkpngsplIIGEDVTVGHHVTL-HGCTIGNRVLVGI 108
Cdd:cd03352    1 SAKIGENVSIGPNAVIGEGV--------------------------------VIGDGVVIGPGVVIgDGVVIGDDCVIHP 48

                         90       100
                 ....*....|....*....|..
gi 447029945 109 NTVILDDVVIEDDVMIGAGSLV 130
Cdd:cd03352   49 NVTIYEGCIIGDRVIIHSGAVI 70
PLN02357 PLN02357
serine acetyltransferase
 78-133 5.10e-06

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 45.64  E-value: 5.10e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 447029945  78 GSPLIIGEDVTVGHHVTLHGC---------TIGNRVLVGINTVILDDVVIEDDVMIGAGSL----VPPR 133
Cdd:PLN02357 250 GETAVVGNNVSILHNVTLGGTgkqsgdrhpKIGDGVLIGAGTCILGNITIGEGAKIGAGSVvlkdVPPR 318
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 15-145 1.25e-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: 43.56  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  15 IDPSCYIDemsvvvGDVKLAENVSVWPFAVIRGDVnsiqIGKNSNVQDHCMLHVSH-KNDTK--P-----NGSPL----- 81
Cdd:cd03353   24 IDPGVILE------GKTVIGEDCVIGPNCVIKDST----IGDGVVIKASSVIEGAViGNGATvgPfahlrPGTVLgegvh 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  82 ----------IIGEDVTVGHHVTLHGCTIGNRVLVGINTVIL--DDV-----VIEDDVMIGAGS-LVPPRKVLKSGYLYV 143
Cdd:cd03353   94 ignfveikksTIGEGSKANHLSYLGDAEIGEGVNIGAGTITCnyDGVnkhrtVIGDNVFIGSNSqLVAPVTIGDGATIAA 173


                 ..
gi 447029945 144 GS 145
Cdd:cd03353  174 GS 175
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 73-136 1.86e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 43.97  E-value: 1.86e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  73 DTKPNGSPLI-----IGEDVTVGHHVTL-HGCTIGNRVLVGINTVILDDVVIEDDVMIGAGSLVPPRKVL 136
Cdd:PRK00892  94 PATPSPAAGIhpsavIDPSAKIGEGVSIgPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTI 163
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 83-148 1.89e-05

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 43.17  E-value: 1.89e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447029945  83 IGEDVTVGHHVTLHGC-------TIGNRVLVGINTVILDDVVIEDDVMIGAGSLVPprKVLKSGYLYVGSPVQ 148
Cdd:cd03352  129 IAHNVRIGENCLIAAQvgiagstTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVT--SIVPPGEYVSGTPAQ 199
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 82-139 2.15e-05

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 43.17  E-value: 2.15e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 447029945  82 IIGEDVTVGHHVTlhgctIGNRVLVGINTVILDDVVIEDDVMIGAGSLVPPRKVLKSG 139
Cdd:cd03352    3 KIGENVSIGPNAV-----IGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEG 55
PRK10191 PRK10191
putative acyl transferase; Provisional
 77-130 5.77e-05

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 41.41  E-value: 5.77e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447029945  77 NGSPLIIGEDVTVGHHVTL-HGCTIGNR-------------VLVGINTVILDDVVIEDDVMIGAGSLV 130
Cdd:PRK10191  58 HGYAVVINKNVVAGDDFTIrHGVTIGNRgadnmacphigngVELGANVIILGDITIGNNVTVGAGSVV 125
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 99-146 1.03e-04

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: 40.87  E-value: 1.03e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 447029945  99 TIGNRVLVGINTVILDDVVIEDDVMIGAGSLV----PPRKVlksgylYVGSP 146
Cdd:cd03357  120 TIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVtkdiPANVV------AAGNP 165
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 77-146 1.50e-04

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: 39.51  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  77 NGSPLIIGEDVTVGHHVTLhgCT------------------IGNRVLVGINTVILDDVVIEDDVMIGAGSLVppRKVLKS 138
Cdd:cd05825   20 NLAPVTIGSDACISQGAYL--CTgshdyrspafplitapivIGDGAWVAAEAFVGPGVTIGEGAVVGARSVV--VRDLPA 95


                 ....*...
gi 447029945 139 GYLYVGSP 146
Cdd:cd05825   96 WTVYAGNP 103
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 86-126 1.62e-04

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 40.99  E-value: 1.62e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 447029945  86 DVTVGHHVTLHGCTIGNRVlVGINTVILDDVVIEDDVMIGA 126
Cdd:PLN02241 315 DSIISHGCFLRECKIEHSV-VGLRSRIGEGVEIEDTVMMGA 354
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 15-125 1.62e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 40.97  E-value: 1.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  15 IDP-SCYIDEmsvvvgDVKLAENVSVWPFAVIRGDVnsiqigknsnvqdhcmlhvshkndtkpngsplIIGEDVTVGHHV 93
Cdd:PRK14354 255 IDPeSTYIDA------DVEIGSDTVIEPGVVIKGNT--------------------------------VIGEDCVIGPGS 296

                         90       100       110
                 ....*....|....*....|....*....|..
gi 447029945  94 TLHGCTIGNRVLVgINTVILDDvVIEDDVMIG 125
Cdd:PRK14354 297 RIVDSTIGDGVTI-TNSVIEES-KVGDNVTVG 326
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 96-143 1.82e-04

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 41.13  E-value: 1.82e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 447029945  96 HGCTIGNRVLVGINTVILDDVVIEDDVMIGAGSLVppRKVLKSGYLYV 143
Cdd:PRK14359 366 HKTIIGKNVFIGSDTQLVAPVNIEDNVLIAAGSTV--TKDVPKGSLAI 411
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 14-130 2.59e-04

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: 39.49  E-value: 2.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  14 QIDPSCYIDEMSVV------VGDVKLAENVSVWPFAVIRGDV---------NSIQIgKNSNVQDHCmlHVSHKN---DTk 75
Cdd:cd05636   13 TIKGPVWIGEGAIVrsgayiEGPVIIGKGCEIGPNAYIRGYTvlgdgcvvgNSVEV-KNSIIMDGT--KVPHLNyvgDS- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  76 pngsplIIGEDVTVG--------------HHVTLH-----------GCTIGNRVLVGINTVILDDVVIEDDVMIGAGSLV 130
Cdd:cd05636   89 ------VLGENVNLGagtitanlrfddkpVKVRLKgervdtgrrklGAIIGDGVKTGINVSLNPGVKIGPGSWVYPGCVV 162
PLN02739 PLN02739
serine acetyltransferase
 77-157 2.73e-04

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 40.40  E-value: 2.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  77 NGSPLIIGEDVTVGHHVT-LHGCT--------------IGNRVLVGINTVILDDVVIEDDVMIGAGSLVppRKVLKSGYL 141
Cdd:PLN02739 222 HGTGVVIGETAVIGDRVSiLHGVTlggtgketgdrhpkIGDGALLGACVTILGNISIGAGAMVAAGSLV--LKDVPSHSM 299

                         90
                 ....*....|....*.
gi 447029945 142 YVGSPVQQVRPLTEKE 157
Cdd:PLN02739 300 VAGNPAKLIGFVDEQD 315
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
97-126 3.28e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 36.55  E-value: 3.28e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 447029945   97 GCTIGNRVLVGINTVILDDVVIEDDVMIGA 126
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 27-141 4.24e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 39.81  E-value: 4.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  27 VVGDVKLAENVSVWPFAVIRGDVNsiqIGKNSNVQDHcmlhVSHKNDTKPNGSPL----IIGeDVTVGHHVTLhGC---- 98
Cdd:PRK14354 313 VIEESKVGDNVTVGPFAHLRPGSV---IGEEVKIGNF----VEIKKSTIGEGTKVshltYIG-DAEVGENVNI-GCgtit 383

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447029945  99 -----------TIGNRVLVGINTVILDDVVIEDDVMIGAGSL----VPP--------RKVLKSGYL 141
Cdd:PRK14354 384 vnydgknkfktIIGDNAFIGCNSNLVAPVTVGDNAYIAAGSTitkdVPEdalaiaraRQVNKEGYV 449
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 99-157 4.81e-04

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 39.22  E-value: 4.81e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 447029945  99 TIGNRVLVGINTVILDDVVIEDDVMIGAGSLV----PPRKVLksgylyVGSPVQQVRPLTEKE 157
Cdd:PRK09527 133 TIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVtkdiPPNVVA------AGVPCRVIREINDRD 189
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 15-128 5.21e-04

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 39.62  E-value: 5.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  15 IDPSCYIDemsvvvGDVKLAENVSVWPFAVIRgdvNSiQIGKNSNVQdHCMLHVSH-KNDTK--------PnGSPL---- 81
Cdd:COG1207  275 IDPNVILE------GKTVIGEGVVIGPNCTLK---DS-TIGDGVVIK-YSVIEDAVvGAGATvgpfarlrP-GTVLgegv 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  82 -----------IIGE-----------DVTVGHHVTLhGC---------------TIGNRVLVGINTVILDDVVIEDDVMI 124
Cdd:COG1207  343 kignfvevknsTIGEgskvnhlsyigDAEIGEGVNI-GAgtitcnydgvnkhrtVIGDGAFIGSNTNLVAPVTIGDGATI 421


                 ....
gi 447029945 125 GAGS 128
Cdd:COG1207  422 GAGS 425
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 83-130 6.86e-04

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


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 38.13  E-value: 6.86e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 447029945  83 IGEDVTVGHHVTLHGC-TIGNRVLVGINTVI--------LDDVVIEDDVMIGAGSLV 130
Cdd:cd03350   34 VDEGTMVDSWATVGSCaQIGKNVHLSAGAVIggvleplqATPVIIEDDVFIGANCEV 90
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 52-116 8.15e-04

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: 37.03  E-value: 8.15e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  52 IQIGKNSNVQDHCMLH----VSHKNDTKPNGSPlIIGEDVTVGHHVT-LHGCTIGNRVLVGINTVILDDV 116
Cdd:cd03354   23 IVIGETAVIGDNCTIYqgvtLGGKGKGGGKRHP-TIGDNVVIGAGAKiLGNITIGDNVKIGANAVVTKDV 91
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 52-137 1.16e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 38.57  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  52 IQIGKNSNVQDHCMLhvshkndtkpnGSPLIIGEDVTVGHHVTLHGCTIGNRVLVGINTViLDDVVIEDDVMIGAGSLVP 131
Cdd:PRK14355 269 VVIGRDTTIYPGVCI-----------SGDTRIGEGCTIEQGVVIKGCRIGDDVTVKAGSV-LEDSVVGDDVAIGPMAHLR 336


                 ....*.
gi 447029945 132 PRKVLK 137
Cdd:PRK14355 337 PGTELS 342
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 47-151 1.58e-03

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 37.55  E-value: 1.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  47 GDVNSIQIGKNSNVQDHCMLhVSHKNDTKPNGSPLIIGEDVTVGHHVTLHGCTIGNRVLVGINTVILDDVVIEDDVMIGA 126
Cdd:PRK09677  81 ACIESITIGRDTLIASKVFI-TDHNHGSFKHSDDFSSPNLPPDMRTLESSAVVIGQRVWIGENVTILPGVSIGNGCIVGA 159

                         90       100
                 ....*....|....*....|....*
gi 447029945 127 GSLVppRKVLKSGYLYVGSPVQQVR 151
Cdd:PRK09677 160 NSVV--TKSIPENTVIAGNPAKIIK 182
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 14-130 2.05e-03

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 38.08  E-value: 2.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  14 QIDPSCYIDEMSVVvGDVKLAENVSVWPFAVIRG--------------DVNSIQIGKNSNVQdhcmlHVSHKNDTKpngs 79
Cdd:PRK09451 302 VIGDDCEISPYSVV-EDANLGAACTIGPFARLRPgaelaegahvgnfvEMKKARLGKGSKAG-----HLTYLGDAE---- 371

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 447029945  80 pliIGEDVTVGHHVTL--------HGCTIGNRVLVGINTVILDDVVIEDDVMIGAGSLV 130
Cdd:PRK09451 372 ---IGDNVNIGAGTITcnydgankFKTIIGDDVFVGSDTQLVAPVTVGKGATIGAGTTV 427
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 19-140 2.14e-03

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 37.82  E-value: 2.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  19 CYI-DEMSVVVGDVKLA---ENVSVWPFAVIR-GDV--NSIQIG-----------KNSNVQdhcmlHVSHKNDTkpngsp 80
Cdd:PRK14357 291 CEIgNNVKIIRSECEKSvieDDVSVGPFSRLReGTVlkKSVKIGnfveikkstigENTKAQ-----HLTYLGDA------ 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  81 lIIGEDVTVG--------HHVTLHGCTIGNRVLVGINTVILDDVVIEDDVMIGAGSL----VPP--------RKVLKSGY 140
Cdd:PRK14357 360 -TVGKNVNIGagtitcnyDGKKKNPTFIEDGAFIGSNSSLVAPVRIGKGALIGAGSVitedVPPyslalgraRQIVKEGW 438
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 81-150 2.36e-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: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945   81 LIIGEDVTVGHHVTLHG------------CTIGNRVLVGINTVILDDVVIEDDVMIGAGSLVPPRKVLKSGYLYVGSPVQ 148
Cdd:TIGR02353 132 LTIGAGTIVRKEVMLLGyraergrlhtgpVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSALQGGQSIPDGERWHGSPAQ 211


                  ..
gi 447029945  149 QV 150
Cdd:TIGR02353 212 KT 213
PRK10502 PRK10502
putative acyl transferase; Provisional
 51-157 5.42e-03

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 36.08  E-value: 5.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  51 SIQIGKNSNVQDHCMLHVSHKNDTKP----NGSPLIIGEdvtvghhvtlhGCTIGNRVLVGintvilDDVVIEDDVMIGA 126
Cdd:PRK10502  91 EITIGAHCVISQKSYLCTGSHDYSDPhfdlNTAPIVIGE-----------GCWLAADVFVA------PGVTIGSGAVVGA 153

                         90       100       110
                 ....*....|....*....|....*....|.
gi 447029945 127 GSLVppRKVLKSGYLYVGSPVQQVRPLTEKE 157
Cdd:PRK10502 154 RSSV--FKSLPANTICRGNPAVPIRPRVETE 182
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 82-139 7.37e-03

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


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 34.09  E-value: 7.37e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447029945  82 IIGEDVTVGHHVTLHGCTIGNRVLVGINTV-----ILDDVVIEDD-----------VMIGAGSLVPPRKVLKSG 139
Cdd:cd05787    1 VIGRGTSIGEGTTIKNSVIGRNCKIGKNVVidnsyIWDDVTIEDGctihhsivadgAVIGKGCTIPPGSLISFG 74
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 14-154 7.56e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 36.26  E-value: 7.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447029945  14 QIDPSCYIdEMSVVVGDVKLAENVSVWPFAVIRGDV--NSIQIGKNSNVQDHCML--HVSHKN--DTKPngspLIIGEDV 87
Cdd:PRK14355 288 RIGEGCTI-EQGVVIKGCRIGDDVTVKAGSVLEDSVvgDDVAIGPMAHLRPGTELsaHVKIGNfvETKK----IVMGEGS 362

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447029945  88 TVGHHVTLHGCTIGNRVLVGINTVI--LDDV-----VIEDDVmigagslvpprkvlksgylYVGSPVQQVRPLT 154
Cdd:PRK14355 363 KASHLTYLGDATIGRNVNIGCGTITcnYDGVkkhrtVIEDDV-------------------FVGSDVQFVAPVT 417
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 82-139 8.91e-03

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: 33.71  E-value: 8.91e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 447029945  82 IIGEDVTVGHHVTLH------GCTIGNRVLVgINTVILDDVVIEDDVMIgAGSLVPPRKVLKSG 139
Cdd:cd04652    1 LVGENTQVGEKTSIKrsvigaNCKIGKRVKI-TNCVIMDNVTIEDGCTL-ENCIIGNGAVIGEK 62
 
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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