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Conserved domains on  [gi|1175185373|ref|WP_081733286|]
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DapH/DapD/GlmU-related protein [Paenarthrobacter nicotinovorans]

Protein Classification

WbbJ family protein( domain architecture ID 11414744)

WbbJ family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
36-189 9.94e-46

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


:

Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 157.73  E-value: 9.94e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  36 IQRTGATIGEGAFLSPKASIDPDTLCIGERSFIAAHAYVTGtitmgndctvnaftvvRGNITMGDGVRIGAHTSILGFNH 115
Cdd:COG0110     4 LLLFGARIGDGVVIGPGVRIYGGNITIGDNVYIGPGVTIDD----------------PGGITIGDNVLIGPGVTILTGNH 67

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1175185373 116 SMDPAEpvfRQPLTSKGIRIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVTKDVPDWSIVGGNPARRIRDRRDP 189
Cdd:COG0110    68 PIDDPA---TFPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEE 138
 
Name Accession Description Interval E-value
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
36-189 9.94e-46

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 157.73  E-value: 9.94e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  36 IQRTGATIGEGAFLSPKASIDPDTLCIGERSFIAAHAYVTGtitmgndctvnaftvvRGNITMGDGVRIGAHTSILGFNH 115
Cdd:COG0110     4 LLLFGARIGDGVVIGPGVRIYGGNITIGDNVYIGPGVTIDD----------------PGGITIGDNVLIGPGVTILTGNH 67

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1175185373 116 SMDPAEpvfRQPLTSKGIRIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVTKDVPDWSIVGGNPARRIRDRRDP 189
Cdd:COG0110    68 PIDDPA---TFPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEE 138
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 78-183 1.65e-43

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: 150.68  E-value: 1.65e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  78 ITMGNDCTVNAFTVV--RGNITMGDGVRIGAHTSILGFNHSMDPAEPVFRQPLTSKGIRIGDDVWIGSNVVVLDGVRVGS 155
Cdd:cd04647     2 ISIGDNVYIGPGCVIsaGGGITIGDNVLIGPNVTIYDHNHDIDDPERPIEQGVTSAPIVIGDDVWIGANVVILPGVTIGD 81

                          90       100
                  ....*....|....*....|....*...
gi 1175185373 156 HAVLAAGAVVTKDVPDWSIVGGNPARRI 183
Cdd:cd04647    82 GAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 50-180 4.18e-22

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: 94.48  E-value: 4.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  50 SPKASIDPDTLcIGERSFIAAHAYVTGTITMGNDCTVNAFTVVRGNITMGDGVRIGAHTSILGfnhsmdpaepvfrqplt 129
Cdd:TIGR03570  91 HPSAIVSPSAS-IGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSG----------------- 152

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1175185373 130 skGIRIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVTKDVPDWSIVGGNPA 180
Cdd:TIGR03570 153 --GVVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
PRK10502 PRK10502
putative acyl transferase; Provisional
 40-186 1.08e-20

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 89.62  E-value: 1.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  40 GATIGEGAFLSPKASID-PDTLCIGERSFIaahayvtgtitmGNDctVNAFTVvrGNITMGDGVRIGAHTSILGFNHsmD 118
Cdd:PRK10502   51 GAKIGKGVVIRPSVRITyPWKLTIGDYAWI------------GDD--VWLYNL--GEITIGAHCVISQKSYLCTGSH--D 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1175185373 119 PAEPVFRqpLTSKGIRIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVTKDVPDWSIVGGNPARRIRDR 186
Cdd:PRK10502  113 YSDPHFD--LNTAPIVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIRPR 178
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
132-161 2.93e-06

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 43.86  E-value: 2.93e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 1175185373 132 GIRIGDDVWIGSNVVVLDGVRVGSHAVLAA 161
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
36-189 9.94e-46

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 157.73  E-value: 9.94e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  36 IQRTGATIGEGAFLSPKASIDPDTLCIGERSFIAAHAYVTGtitmgndctvnaftvvRGNITMGDGVRIGAHTSILGFNH 115
Cdd:COG0110     4 LLLFGARIGDGVVIGPGVRIYGGNITIGDNVYIGPGVTIDD----------------PGGITIGDNVLIGPGVTILTGNH 67

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1175185373 116 SMDPAEpvfRQPLTSKGIRIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVTKDVPDWSIVGGNPARRIRDRRDP 189
Cdd:COG0110    68 PIDDPA---TFPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEE 138
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 78-183 1.65e-43

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: 150.68  E-value: 1.65e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  78 ITMGNDCTVNAFTVV--RGNITMGDGVRIGAHTSILGFNHSMDPAEPVFRQPLTSKGIRIGDDVWIGSNVVVLDGVRVGS 155
Cdd:cd04647     2 ISIGDNVYIGPGCVIsaGGGITIGDNVLIGPNVTIYDHNHDIDDPERPIEQGVTSAPIVIGDDVWIGANVVILPGVTIGD 81

                          90       100
                  ....*....|....*....|....*...
gi 1175185373 156 HAVLAAGAVVTKDVPDWSIVGGNPARRI 183
Cdd:cd04647    82 GAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 78-183 2.09e-31

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: 119.83  E-value: 2.09e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  78 ITMGNDCTVNA-FTVVRGN-ITMGDGVRIGAHTSILGFNHSMDPAEpvfRQ--PLTSKGIRIGDDVWIGSNVVVLDGVRV 153
Cdd:cd03357    63 IHIGDNFYANFnCTILDVApVTIGDNVLIGPNVQIYTAGHPLDPEE---RNrgLEYAKPITIGDNVWIGGGVIILPGVTI 139

                          90       100       110
                  ....*....|....*....|....*....|
gi 1175185373 154 GSHAVLAAGAVVTKDVPDWSIVGGNPARRI 183
Cdd:cd03357   140 GDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 93-189 6.55e-28

Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of a large number of microbial enzymes that catalyze the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. Members of this class of enzymes include Enterococcus faecium streptogramin A acetyltransferase and Pseudomonas aeruginosa chloramphenicol acetyltransferase. They contain repeated copies of a six-residue hexapeptide repeat sequence motif (X-[STAV]-X-[LIV]-[GAED]-X) and adopt a left-handed parallel beta helix (LbH) structure. The active enzyme is a trimer with CoA and substrate binding sites at the interface of two separate LbH subunits. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients.


Pssm-ID: 100040 [Multi-domain]  Cd Length: 145  Bit Score: 109.17  E-value: 6.55e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  93 RGNITMGDGVRIGAHTSIL-GFNHSMD-------------PAEPVFRQPLTSKG-IRIGDDVWIGSNVVVLDGVRVGSHA 157
Cdd:cd03349    19 GDKLSIGKFCSIAPGVKIGlGGNHPTDwvstypfyifggeWEDDAKFDDWPSKGdVIIGNDVWIGHGATILPGVTIGDGA 98

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1175185373 158 VLAAGAVVTKDVPDWSIVGGNPARRIRDRRDP 189
Cdd:cd03349    99 VIAAGAVVTKDVPPYAIVGGNPAKVIRYRFDE 130
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 62-184 4.11e-25

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: 100.27  E-value: 4.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  62 IGERSFIAAHAYVTGTITMGNDCTVNAFTVVRGNITMGDGVRIGAHTSIlgfnhSMDPAEPVFRQPLTS-KGIRIGDDVW 140
Cdd:cd03358     1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVF-----TNDLYPRSKIYRKWElKGTTVKRGAS 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1175185373 141 IGSNVVVLDGVRVGSHAVLAAGAVVTKDVPDWSIVGGNPARRIR 184
Cdd:cd03358    76 IGANATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 50-179 3.05e-24

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: 100.25  E-value: 3.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  50 SPKASIDPDTlCIGERSFIAAHAYVTGTITMGNDCTVNAFTVVRGNITMGDGVRIGAHTSILGfnhsmdpaepvfrqplt 129
Cdd:cd03360    88 HPSAVVSPSA-VIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSG----------------- 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1175185373 130 skGIRIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVTKDVPDWSIVGGNP 179
Cdd:cd03360   150 --GVTIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 62-188 2.16e-22

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 94.32  E-value: 2.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  62 IGERSFIAAHAYVTGTITMGNDCTVNAFTVVRG-----------NI--------TMGDGVRIGAHTSIlGFN---Hsmdp 119
Cdd:COG0663    13 IHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGdvgpirigegsNIqdgvvlhvDPGYPLTIGDDVTI-GHGailH---- 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1175185373 120 aepvfrqpltskGIRIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVT--KDVPDWSIVGGNPARRIRDRRD 188
Cdd:COG0663    88 ------------GCTIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTegKVVPPGSLVVGSPAKVVRELTE 146
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 50-180 4.18e-22

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: 94.48  E-value: 4.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  50 SPKASIDPDTLcIGERSFIAAHAYVTGTITMGNDCTVNAFTVVRGNITMGDGVRIGAHTSILGfnhsmdpaepvfrqplt 129
Cdd:TIGR03570  91 HPSAIVSPSAS-IGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSG----------------- 152

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1175185373 130 skGIRIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVTKDVPDWSIVGGNPA 180
Cdd:TIGR03570 153 --GVVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
PRK10502 PRK10502
putative acyl transferase; Provisional
 40-186 1.08e-20

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 89.62  E-value: 1.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  40 GATIGEGAFLSPKASID-PDTLCIGERSFIaahayvtgtitmGNDctVNAFTVvrGNITMGDGVRIGAHTSILGFNHsmD 118
Cdd:PRK10502   51 GAKIGKGVVIRPSVRITyPWKLTIGDYAWI------------GDD--VWLYNL--GEITIGAHCVISQKSYLCTGSH--D 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1175185373 119 PAEPVFRqpLTSKGIRIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVTKDVPDWSIVGGNPARRIRDR 186
Cdd:PRK10502  113 YSDPHFD--LNTAPIVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIRPR 178
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 62-185 4.08e-20

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: 87.08  E-value: 4.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  62 IGERSFIAAHAYVTGTITMGNDCTVNAFTVVRG---NITMGDGVRIGAHTSIlgfnHSmDPAEPVFRQPLTS-------K 131
Cdd:cd04645     2 IDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRGdvnPIRIGERTNIQDGSVL----HV-DPGYPTIIGDNVTvghgavlH 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1175185373 132 GIRIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVT--KDVPDWSIVGGNPARRIRD 185
Cdd:cd04645    77 GCTIGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPpgKVIPPGSLVAGSPAKVVRE 132
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 96-183 1.35e-19

wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar proteins. WcaF is part of the gene cluster responsible for the biosynthesis of the extracellular polysaccharide colanic acid. The wcaF protein is predicted to contain a left-handed parallel beta-helix (LbH) domain encoded by imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Many are trimeric in their active forms.


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 84.19  E-value: 1.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  96 ITMGDGVRIGAHTSILGFNHSMDpaEPVFrqPLTSKGIRIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVTKDVPDWSIV 175
Cdd:cd05825    24 VTIGSDACISQGAYLCTGSHDYR--SPAF--PLITAPIVIGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVY 99


                  ....*...
gi 1175185373 176 GGNPARRI 183
Cdd:cd05825   100 AGNPAVPV 107
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 72-186 1.91e-19

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 86.47  E-value: 1.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  72 AYVTGTITMGNDCTVNAFTVVRG--NITMGDGVRIGAHTSILGFNHS--------MDPAEPVFRQPLTSKGIRIGDDVWI 141
Cdd:PRK09677   60 AFGRGKLFFGDNVQVNDYVHIACieSITIGRDTLIASKVFITDHNHGsfkhsddfSSPNLPPDMRTLESSAVVIGQRVWI 139

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1175185373 142 GSNVVVLDGVRVGSHAVLAAGAVVTKDVPDWSIVGGNPARRIRDR 186
Cdd:PRK09677  140 GENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKKY 184
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 7-188 4.13e-18

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 83.13  E-value: 4.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373   7 LNYDYSpwtfwtsasHSeREAQHGYHRDFIQRTGATIGEGAFLSPkasidPDTLCIGERSFIAAHAYVTGTITMGNDCTV 86
Cdd:PRK09527   32 LMYEFN---------HS-HPSEVEKRESLIKEMFATVGENAWVEP-----PVYFSYGSNIHIGRNFYANFNLTIVDDYTV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  87 naftvvrgniTMGDGVRIGAHT--SILG--FNHSMDPAEPVFRQPLTskgirIGDDVWIGSNVVVLDGVRVGSHAVLAAG 162
Cdd:PRK09527   97 ----------TIGDNVLIAPNVtlSVTGhpVHHELRKNGEMYSFPIT-----IGNNVWIGSHVVINPGVTIGDNSVIGAG 161

                         170       180
                  ....*....|....*....|....*.
gi 1175185373 163 AVVTKDVPDWSIVGGNPARRIRDRRD 188
Cdd:PRK09527  162 SVVTKDIPPNVVAAGVPCRVIREIND 187
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 53-184 8.09e-18

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 81.40  E-value: 8.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  53 ASIDPDTLC-IGERSFIAAHAYVTGTITMGNDCTVNaftvVRGNITMGDGVRIGAHTsilgfnHSMDPAEPVFRQPLtSK 131
Cdd:PRK10092   60 AYIEPTFRCdYGYNIFLGNNFYANFDCVMLDVCPIR----IGDNCMLAPGVHIYTAT------HPLDPVARNSGAEL-GK 128

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1175185373 132 GIRIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVTKDVPDWSIVGGNPARRIR 184
Cdd:PRK10092  129 PVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIK 181
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 40-187 2.70e-16

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: 77.83  E-value: 2.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  40 GATIGEGAFLSPKASIDPDTLcIGERSFIAAHAYVTGTITMGNDCTVNAFTVV-------------------RGNITMGD 100
Cdd:cd03352    19 GVVIGDGVVIGPGVVIGDGVV-IGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIgsdgfgfapdgggwvkipqLGGVIIGD 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373 101 GVRIGAHTSI---------------------LGFN-----HSMdpaepvfrqpLTSK-GI----RIGDDVWIGSNVVVLD 149
Cdd:cd03352    98 DVEIGANTTIdrgalgdtvigdgtkidnlvqIAHNvrigeNCL----------IAAQvGIagstTIGDNVIIGGQVGIAG 167

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1175185373 150 GVRVGSHAVLAAGAVVTKDVPDWSIVGGNPARRIRDRR 187
Cdd:cd03352   168 HLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQPHREWL 205
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 54-179 8.32e-16

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: 73.24  E-value: 8.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  54 SIDPDTlCIGERSFIAaHAyvTGTItmgndctVNAFTVVRGNITMGDGVRIGAHTSILGFNHsmdpaepvfrqpltskgI 133
Cdd:cd03354     4 DIHPGA-KIGPGLFID-HG--TGIV-------IGETAVIGDNCTIYQGVTLGGKGKGGGKRH-----------------P 55

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1175185373 134 RIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVTKDVPDWSIVGGNP 179
Cdd:cd03354    56 TIGDNVVIGAGAKILGNITIGDNVKIGANAVVTKDVPANSTVVGVP 101
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 40-181 2.29e-15

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: 75.93  E-value: 2.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  40 GATIGEGAFLSPKASIDPDTLcIGERSFIAAHAYVTGTITMGNDCTVNAF------------------------TVVRGN 95
Cdd:cd03351    11 GAKIGENVEIGPFCVIGPNVE-IGDGTVIGSHVVIDGPTTIGKNNRIFPFasigeapqdlkykgeptrleigdnNTIREF 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  96 ITM------GDGV-RIG-----------AHTSILGfNHSmdpaepVFRQPLTSKG-IRIGDDVWIGSNVVVLDGVRVGSH 156
Cdd:cd03351    90 VTIhrgtaqGGGVtRIGnnnllmayvhvAHDCVIG-NNV------ILANNATLAGhVEIGDYAIIGGLSAVHQFCRIGRH 162

                         170       180
                  ....*....|....*....|....*
gi 1175185373 157 AVLAAGAVVTKDVPDWSIVGGNPAR 181
Cdd:cd03351   163 AMVGGGSGVVQDVPPYVIAAGNRAR 187
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 61-189 5.45e-15

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


Pssm-ID: 440667 [Multi-domain]  Cd Length: 174  Bit Score: 73.19  E-value: 5.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  61 CIGERSFIAaHAyvTGTI-----TMGNDCTVNAftvvrgnitmgdGVRIGAHTSilgfnhsmdpaEPVFRQPltskgiRI 135
Cdd:COG1045    73 TIGRGFFID-HG--TGVVigetaVIGDNVTIYQ------------GVTLGGTGK-----------EKGKRHP------TI 120

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1175185373 136 GDDVWIGSNVVVLDGVRVGSHAVLAAGAVVTKDVPDWSIVGGNPARRIRDRRDP 189
Cdd:COG1045   121 GDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVKRKGSK 174
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 78-166 2.01e-14

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: 68.43  E-value: 2.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  78 ITMGNDCTVNAFTVVRGNITMGDGVRIGAHTSILGFnhsmdpaepvfRQPLTSKGIRIGDDVWIGSNVVVLDGVRVGSHA 157
Cdd:cd00208     1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAA-----------TGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNA 69


                  ....*....
gi 1175185373 158 VLAAGAVVT 166
Cdd:cd00208    70 VIGAGAVVT 78
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 40-181 3.92e-14

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: 72.36  E-value: 3.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  40 GATIGEGAFLSPKASIDPDTlCIGERSFIAAHAYVTGTITMGNDCTVNAF------------------------TVVRGN 95
Cdd:COG1043    13 GAKLGENVEIGPFCVIGPDV-EIGDGTVIGSHVVIEGPTTIGKNNRIFPFasigeepqdlkykgeptrleigdnNTIREF 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  96 ITM------GDGV-RIG-----------AHTSILGFN-----------HsmdpaepvfrqpltskgIRIGDDVWIGSNVV 146
Cdd:COG1043    92 VTIhrgtvqGGGVtRIGddnllmayvhvAHDCVVGNNvilannatlagH-----------------VEVGDHAIIGGLSA 154

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1175185373 147 VLDGVRVGSHAVLAAGAVVTKDVPDWSIVGGNPAR 181
Cdd:COG1043   155 VHQFVRIGAHAMVGGGSGVVKDVPPYVLAAGNPAR 189
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 62-188 3.32e-13

Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in iron acquisition. It binds iron when it is complexed with pyochelin. It adopts the left-handed parallel beta-helix (LbH) structure, and contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Acyltransferase activity has not been observed in this group.


Pssm-ID: 100055 [Multi-domain]  Cd Length: 154  Bit Score: 67.60  E-value: 3.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  62 IGERSFIAAHAYVTGTITMGNDCTVNAFTVVRGNItmgDGVRIGAHTSILGfNHSM--DPAEPVFRQPLTS-------KG 132
Cdd:cd04650     3 ISPKAYVHPTSYVIGDVVIGELTSVWHYAVIRGDN---DSIYIGKYSNVQE-NVSIhtDHGYPTEIGDYVTighnavvHG 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1175185373 133 IRIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVT--KDVPDWSIVGGNPARRIRDRRD 188
Cdd:cd04650    79 AKVGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTpgKEIPDYSLVLGVPAKVVRKLTE 136
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 40-180 4.53e-13

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 69.28  E-value: 4.53e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  40 GATIGEGAFLSPKASIDpDTLCIGERSFIAAHAYVTGTITMGNDCTVNAFTVV---------RGNIT---MGDG------ 101
Cdd:PRK12461   11 SAKLGSGVEIGPFAVIG-ANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVgdepqdftyKGEESrleIGDRnvireg 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373 102 ------------VRIG-----------AHTSILGfNHSMdpaepVFRQPLTSKGIRIGDDVWIGSNVVVLDGVRVGSHAV 158
Cdd:PRK12461   90 vtihrgtkgggvTRIGndnllmayshvAHDCQIG-NNVI-----LVNGALLAGHVTVGDRAIISGNCLVHQFCRIGALAM 163

                         170       180
                  ....*....|....*....|..
gi 1175185373 159 LAAGAVVTKDVPDWSIVGGNPA 180
Cdd:PRK12461  164 MAGGSRISKDVPPYCMMAGHPT 185
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
40-181 1.26e-12

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 68.20  E-value: 1.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  40 GATIGEGAFLSPKASIDPDTLcIGERSFIAAHAYVTGTITMGNDCTVNAFTVV------------------------RGN 95
Cdd:PRK05289   14 GAKIGENVEIGPFCVIGPNVV-IGDGTVIGSHVVIDGHTTIGKNNRIFPFASIgedpqdlkykgeptrlvigdnntiREF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  96 ITM------GDGV-RIG-----------AHTSILGfNHSmdpaepVFRQPLTSKG-IRIGDDVWIGSNVVVLDGVRVGSH 156
Cdd:PRK05289   93 VTInrgtvqGGGVtRIGdnnllmayvhvAHDCVVG-NHV------ILANNATLAGhVEVGDYAIIGGLTAVHQFVRIGAH 165

                         170       180
                  ....*....|....*....|....*
gi 1175185373 157 AVLAAGAVVTKDVPDWSIVGGNPAR 181
Cdd:PRK05289  166 AMVGGMSGVSQDVPPYVLAEGNPAR 190
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 40-185 1.32e-12

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: 69.28  E-value: 1.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  40 GATIGEGAFLSPKASIDPDTlCIGERSFIAAHAYVTGTITMGNDCTVNAFTVV--------------------RGNITMG 99
Cdd:COG1044   126 GVVIGDGVVIGPGVVIGDGV-VIGDDCVLHPNVTIYERCVIGDRVIIHSGAVIgadgfgfapdedggwvkipqLGRVVIG 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373 100 DGVRIGAHTSI---------------------LGFN-----HSMdpaepvfrqpLTSK-GI----RIGDDVWIGSNVVVL 148
Cdd:COG1044   205 DDVEIGANTTIdrgalgdtvigdgtkidnlvqIAHNvrigeHTA----------IAAQvGIagstKIGDNVVIGGQVGIA 274

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1175185373 149 DGVRVGSHAVLAAGAVVTKDVPDWSIVGGNPARRIRD 185
Cdd:COG1044   275 GHLTIGDGVIIGAQSGVTKSIPEGGVYSGSPAQPHRE 311
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 68-165 1.77e-12

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 68.63  E-value: 1.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  68 IAAHAYVTGTITMGNDCTVNAFTVVRGNITMGDGVRIGAHTSIlgfnhsmdpaepvfrqpltSKGIRIGDDVWIGSNVVV 147
Cdd:PRK00892  103 IHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVI-------------------GDGVKIGADCRLHANVTI 163

                          90
                  ....*....|....*...
gi 1175185373 148 LDGVRVGSHAVLAAGAVV 165
Cdd:PRK00892  164 YHAVRIGNRVIIHSGAVI 181
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 68-165 2.27e-12

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: 68.51  E-value: 2.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  68 IAAHAYVTGTITMGNDCTVNAFTVVRGNITMGDGVRIGAHTSIlgfnhsmdpaepvfrqpltSKGIRIGDDVWIGSNVVV 147
Cdd:COG1044    99 IHPSAVIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVI-------------------GDGVVIGDDCVLHPNVTI 159

                          90
                  ....*....|....*...
gi 1175185373 148 LDGVRVGSHAVLAAGAVV 165
Cdd:COG1044   160 YERCVIGDRVIIHSGAVI 177
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 40-170 5.07e-12

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: 63.55  E-value: 5.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  40 GATIGEGAFLSPKASIDPDtlcigerSFIAAHAYVtGTITMgndctVNAFTVVRGNITMGDGVRIGAHTSILGFnhsmdp 119
Cdd:cd03350     7 GAIIRDGAFIGPGAVLMMP-------SYVNIGAYV-DEGTM-----VDSWATVGSCAQIGKNVHLSAGAVIGGV------ 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1175185373 120 AEPVFRQPLTskgirIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVTKDVP 170
Cdd:cd03350    68 LEPLQATPVI-----IEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTQSTP 113
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 43-166 7.89e-11

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: 60.68  E-value: 7.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  43 IGEGAFLSPKASIDPDTLcIGERSFIAAHAYVTGTITMGNDCTVNAFTVVRGNITMgDGVRIGAHT----SILGFN---- 114
Cdd:cd05636    20 IGEGAIVRSGAYIEGPVI-IGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSIIM-DGTKVPHLNyvgdSVLGENvnlg 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1175185373 115 ---------HSMDPAEPVFRQPLTSKGIR-----IGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVT 166
Cdd:cd05636    98 agtitanlrFDDKPVKVRLKGERVDTGRRklgaiIGDGVKTGINVSLNPGVKIGPGSWVYPGCVVR 163
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 40-181 9.59e-11

acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes LpxA, an enzyme for the biosynthesis of lipid A, a component oflipopolysaccharide (LPS) in the outer membrane outer leaflet of most Gram-negative bacteria. Some differences are found between lipid A of different species, but this protein represents the first step (from UDP-N-acetyl-D-glucosamine) and appears to be conserved in function. Proteins from this family contain many copies of the bacterial transferase hexapeptide repeat (pfam00132). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 62.28  E-value: 9.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  40 GATIGEGAFLSPKASIDPDTLcIGERSFIAAHAYVTGTITMGNDCTVNAFTV------------------------VRGN 95
Cdd:TIGR01852  10 GAEIGENVEIGPFCIVGPGVK-IGDGVELKSHVVILGHTTIGEGTRIFPGAViggvpqdlkykgektrliigdnntIREF 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  96 ITM------GDGV-RIGAHTSILGFNHSmdpAEP-------VFRQPLTSKG-IRIGDDVWIGSNVVVLDGVRVGSHAVLA 160
Cdd:TIGR01852  89 VTInrgtasGGGVtRIGNNNLLMAYSHI---AHDcvvgnhvILANNATLAGhVEVGDYAIIGGLVAVHQFVRIGRYAMIG 165

                         170       180
                  ....*....|....*....|.
gi 1175185373 161 AGAVVTKDVPDWSIVGGNPAR 181
Cdd:TIGR01852 166 GLSAVSKDVPPYCLAEGNRAR 186
PLN02739 PLN02739
serine acetyltransferase
 96-189 9.99e-11

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 63.52  E-value: 9.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  96 ITMGDGVRIGAHTSIL-GFNHSMDPAEPVFRQPltskgiRIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVTKDVPDWSI 174
Cdd:PLN02739  226 VVIGETAVIGDRVSILhGVTLGGTGKETGDRHP------KIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSM 299

                          90
                  ....*....|....*..
gi 1175185373 175 VGGNPARRIR--DRRDP 189
Cdd:PLN02739  300 VAGNPAKLIGfvDEQDP 316
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 40-185 1.83e-10

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 62.46  E-value: 1.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  40 GATIGEGAFLSPKASIDPDTlCIGERSFIAAHAYVTGTITMGNDCTVNAFTVV-------------------RGNITMGD 100
Cdd:PRK00892  130 GVVIGDGVVIGAGAVIGDGV-KIGADCRLHANVTIYHAVRIGNRVIIHSGAVIgsdgfgfandrggwvkipqLGRVIIGD 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373 101 GVRIGAHTSI---------------------LGFN-----HSMDPAepvfrqpltSKGI----RIGDDVWIGSNVVVLDG 150
Cdd:PRK00892  209 DVEIGANTTIdrgalddtvigegvkidnlvqIAHNvvigrHTAIAA---------QVGIagstKIGRYCMIGGQVGIAGH 279

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1175185373 151 VRVGSHAVLAAGAVVTKDVPDW-SIVGGNPARRIRD 185
Cdd:PRK00892  280 LEIGDGVTITAMSGVTKSIPEPgEYSSGIPAQPNKE 315
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 42-171 1.83e-10

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: 60.51  E-value: 1.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  42 TIGEGAFLSPKASIDPDTlcIGERSFIAAHAYVTGTItMGNDCTVNAFTVVRGNITMGDGVRIGAH----TSILG----F 113
Cdd:cd03353    35 VIGEDCVIGPNCVIKDST--IGDGVVIKASSVIEGAV-IGNGATVGPFAHLRPGTVLGEGVHIGNFveikKSTIGegskA 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373 114 NHsmdpaepvfrqpLTSKG--------------I------------RIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVTK 167
Cdd:cd03353   112 NH------------LSYLGdaeigegvnigagtItcnydgvnkhrtVIGDNVFIGSNSQLVAPVTIGDGATIAAGSTITK 179


                  ....
gi 1175185373 168 DVPD 171
Cdd:cd03353   180 DVPP 183
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 41-111 1.90e-10

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 57.26  E-value: 1.90e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1175185373  41 ATIGEGAFLSPKASIDpDTLCIGERSFIAAHAYVTGT--------ITMGNDCTVNAFTVVRGNITMGDGVRIGAHTSIL 111
Cdd:cd00208     1 VFIGEGVKIHPKAVIR-GPVVIGDNVNIGPGAVIGAAtgpneknpTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 41-177 4.75e-10

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 61.31  E-value: 4.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  41 ATIGEGAFLSPKASIDPDTlCIGERSFIAAHAYVTGTITMGNDCTVNAFTVVRGNITMGDGVRIGAHTSI--LGFNHSMD 118
Cdd:PRK00892  113 AKIGEGVSIGPNAVIGAGV-VIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVIgsDGFGFAND 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373 119 PAEPVfrqpltsK-----GIRIGDDVWIGSNV---------------VVLD-------GVRVGSHAVLAAGAVV---TKd 168
Cdd:PRK00892  192 RGGWV-------KipqlgRVIIGDDVEIGANTtidrgalddtvigegVKIDnlvqiahNVVIGRHTAIAAQVGIagsTK- 263


                  ....*....
gi 1175185373 169 VPDWSIVGG 177
Cdd:PRK00892  264 IGRYCMIGG 272
PLN02296 PLN02296
carbonate dehydratase
 43-188 1.67e-09

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 58.98  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  43 IGEGAFLSPKASIDPDTLcIGERSFIAAHAYVTG---TITMGNDCTVNAFTVV---RGNI-------TMGDGVRIGaHTS 109
Cdd:PLN02296   55 VDKDAFVAPSASVIGDVQ-VGRGSSIWYGCVLRGdvnSISVGSGTNIQDNSLVhvaKTNLsgkvlptIIGDNVTIG-HSA 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373 110 ILgfnHsmdpaepvfrqpltskGIRIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVTKD--VPDWSIVGGNPARRIRDRR 187
Cdd:PLN02296  133 VL---H----------------GCTVEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNtrIPSGEVWAGNPAKFLRKLT 193


                  .
gi 1175185373 188 D 188
Cdd:PLN02296  194 E 194
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 43-184 3.59e-09

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: 55.84  E-value: 3.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  43 IGEGAFLSPKASIDPDTLcIGERSFIAAHAYVTG---TITMGNDCTVNAFTVVRG----NITMGDGVRIGaHTSILgfnH 115
Cdd:cd04745     3 VDPSSFVHPTAVLIGDVI-IGKNCYIGPHASLRGdfgRIVIRDGANVQDNCVIHGfpgqDTVLEENGHIG-HGAIL---H 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1175185373 116 smdpaepvfrqpltskGIRIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVTK--DVPDWSIVGGNPARRIR 184
Cdd:cd04745    78 ----------------GCTIGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAgtVIPPRSLIAGSPAKVIR 132
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 40-186 2.05e-08

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 56.79  E-value: 2.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  40 GATIGEGAFLSPKASIDPDTLcIGERSFIaahayvtgtitmGNDCTVNAFTVVRG----NIT-MGDGVrIGAHTSI---- 110
Cdd:PRK14353  303 GAHVGEGAEVGPYARLRPGAE-LGEGAKV------------GNFVEVKNAKLGEGakvnHLTyIGDAT-IGAGANIgagt 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373 111 -----LGFNHsmdpaepvFRqpltskgIRIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVTKDVPDWSIVGGNP------ 179
Cdd:PRK14353  369 itcnyDGFNK--------HR-------TEIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALGRArqetkp 433


                  ....*....
gi 1175185373 180 --ARRIRDR 186
Cdd:PRK14353  434 gwAKKLRER 442
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 40-171 3.65e-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: 55.80  E-value: 3.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  40 GAT-IGEGAflspkaSIDPDtlCIGERSFIAAHAYVTGTI----TMGNDCTVNAFTVVRGNITMGDGVRIGAHT----SI 110
Cdd:COG1207   283 GKTvIGEGV------VIGPN--CTLKDSTIGDGVVIKYSViedaVVGAGATVGPFARLRPGTVLGEGVKIGNFVevknST 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373 111 LG----FNHsmdpaepvfrqpLTSKG--------------I------------RIGDDVWIGSNVVVLDGVRVGSHAVLA 160
Cdd:COG1207   355 IGegskVNH------------LSYIGdaeigegvnigagtItcnydgvnkhrtVIGDGAFIGSNTNLVAPVTIGDGATIG 422

                         170
                  ....*....|.
gi 1175185373 161 AGAVVTKDVPD 171
Cdd:COG1207   423 AGSTITKDVPA 433
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 97-169 4.63e-08

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 55.02  E-value: 4.63e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1175185373  97 TMGDGVRIGAHTSIlgfnhsmdpaepvfrqpltSKGIRIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVTKDV 169
Cdd:COG1044   110 KIGEGVSIGPFAVI-------------------GAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERC 163
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 40-167 7.93e-08

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


Pssm-ID: 441774 [Multi-domain]  Cd Length: 268  Bit Score: 53.97  E-value: 7.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  40 GATIGEGAFLSPKASIDPdtlcigerSFIAAHAYVTGTiTMgndctvnaftvVRGNIT------MGDGVRIGAHTSILGf 113
Cdd:COG2171   103 GARVRLGAYLAPGVVLMP--------SFVNIGAYVDEG-TM-----------VDTWATvgscaqIGKNVHLSGGAGIGG- 161

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1175185373 114 nhSMDP--AEPVfrqpltskgiRIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVTK 167
Cdd:COG2171   162 --VLEPlqAAPV----------IIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLTA 205
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 75-200 9.88e-08

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: 51.83  E-value: 9.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  75 TGTITMGNDCTVNAFTVVRGNITMgdgVRIGAHtSILGFNHSMDPAEPVFRQPLTSKGIRIGDDVWIGSNVVVlDGVRVG 154
Cdd:cd03359    19 SQNIVLNGKTIIQSDVIIRGDLAT---VSIGRY-CILSEGCVIRPPFKKFSKGVAFFPLHIGDYVFIGENCVV-NAAQIG 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1175185373 155 SHAVLAAGAV-----VTKD---------------VPDWSIVGGNPARrirdrrdpvaaPTADLPET 200
Cdd:cd03359    94 SYVHIGKNCVigrrcIIKDcvkildgtvvppdtvIPPYSVVSGRPAR-----------FIGELPEC 148
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 94-183 1.14e-07

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 54.38  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  94 GNITMGDGVRIGAHTsiLGFNHSMDPAEPVFrqpltskgirIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVTKDVPDWS 173
Cdd:PRK14357  357 GDATVGKNVNIGAGT--ITCNYDGKKKNPTF----------IEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYS 424

                          90
                  ....*....|
gi 1175185373 174 IVGGNpARRI 183
Cdd:PRK14357  425 LALGR-ARQI 433
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 42-174 5.23e-07

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 52.14  E-value: 5.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  42 TIGEGAFLSPKASIdpdtlcigERSFIAAHAYVTGTI----TMGNDCTVNAFTVVRGNITMGDGVRIG------------ 105
Cdd:PRK14354  285 VIGEDCVIGPGSRI--------VDSTIGDGVTITNSVieesKVGDNVTVGPFAHLRPGSVIGEEVKIGnfveikkstige 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373 106 ----AHTSILGfnhsmDpAEpvfrqplTSKGI-------------------RIGDDVWIGSNVVVLDGVRVGSHAVLAAG 162
Cdd:PRK14354  357 gtkvSHLTYIG-----D-AE-------VGENVnigcgtitvnydgknkfktIIGDNAFIGCNSNLVAPVTVGDNAYIAAG 423

                         170
                  ....*....|..
gi 1175185373 163 AVVTKDVPDWSI 174
Cdd:PRK14354  424 STITKDVPEDAL 435
PRK10191 PRK10191
putative acyl transferase; Provisional
 77-181 5.81e-07

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 49.12  E-value: 5.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  77 TITMGNDCTVNAFTVVRGNITMGDGVRIGAhtsiLGFNhsmDPAEPVfrqpltskgirIGDDVWIGSNVVVLDGVRVGSH 156
Cdd:PRK10191   55 TIHHGYAVVINKNVVAGDDFTIRHGVTIGN----RGAD---NMACPH-----------IGNGVELGANVIILGDITIGNN 116

                          90       100
                  ....*....|....*....|....*
gi 1175185373 157 AVLAAGAVVTKDVPDWSIVGGNPAR 181
Cdd:PRK10191  117 VTVGAGSVVLDSVPDNALVVGEKAR 141
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 40-171 1.53e-06

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 50.88  E-value: 1.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  40 GATIGEGAFLSPKASIDPDTlCIGERSFIAAHAYVTGTiTMGNDCTVNAFTVVrGNITMGDGVRIGAHTSILGFN----H 115
Cdd:PRK14356  321 GAEVGDGCSVGPYARLRPGA-VLEEGARVGNFVEMKKA-VLGKGAKANHLTYL-GDAEIGAGANIGAGTITCNYDgvnkH 397

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1175185373 116 SMDpaepvfrqpltskgirIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVTKDVPD 171
Cdd:PRK14356  398 RTV----------------IGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPD 437
PLN02357 PLN02357
serine acetyltransferase
 134-190 2.11e-06

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 50.27  E-value: 2.11e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1175185373 134 RIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVTKDVPDWSIVGGNPARRIRDRRDPV 190
Cdd:PLN02357  280 KIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLIGGKENPI 336
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
132-161 2.93e-06

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 43.86  E-value: 2.93e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 1175185373 132 GIRIGDDVWIGSNVVVLDGVRVGSHAVLAA 161
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 35-185 4.08e-06

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 49.54  E-value: 4.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  35 FIQRTGATIGEGAFLSPKASIDPDTL----------C-IGERSFI----------AAHAYVTGTiTMGNDCTVNAFTVVR 93
Cdd:PRK14360  251 FIDPASCTISETVELGPDVIIEPQTHlrgntvigsgCrIGPGSLIensqigenvtVLYSVVSDS-QIGDGVKIGPYAHLR 329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  94 GNITMGDGVRIG----------------AHTSILGfnhsmDPA--EPV-------------FRQPLTskgiRIGDDVWIG 142
Cdd:PRK14360  330 PEAQIGSNCRIGnfveikksqlgegskvNHLSYIG-----DATlgEQVnigagtitanydgVKKHRT----VIGDRSKTG 400

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1175185373 143 SNVVVLDGVRVGSHAVLAAGAVVTKDVPDWSIVGGNPARRIRD 185
Cdd:PRK14360  401 ANSVLVAPITLGEDVTVAAGSTITKDVPDNSLAIARSRQVIKE 443
PLN02694 PLN02694
serine O-acetyltransferase
 134-189 4.47e-06

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 48.87  E-value: 4.47e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1175185373 134 RIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVTKDVPDWSIVGGNPARRIRDRRDP 189
Cdd:PLN02694  214 KIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLVGGKEKP 269
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 40-190 6.31e-06

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 48.87  E-value: 6.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  40 GATIGEGAFLSPKASIDPDtlcigerSFIAAHAYVTGTITM-----GNDCTVNAFTVVrGNITMGDGVRIGAHTSILGFn 114
Cdd:PRK09451  317 DANLGAACTIGPFARLRPG-------AELAEGAHVGNFVEMkkarlGKGSKAGHLTYL-GDAEIGDNVNIGAGTITCNY- 387

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1175185373 115 hsmDPAEpvfrqplTSKGIrIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVTKDVPDWSIVGGN-PARRIRDRRDPV 190
Cdd:PRK09451  388 ---DGAN-------KFKTI-IGDDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDVAENELVISRvPQRHIQGWQRPV 453
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 40-170 6.33e-06

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 48.97  E-value: 6.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  40 GATIGEGAFLSPKASIDPDTLcigersfIAAHAYV-----TGTITMGNDCTVNAFTVVrGNITMGDGVRIGAHTSILGFN 114
Cdd:PRK14355  320 DSVVGDDVAIGPMAHLRPGTE-------LSAHVKIgnfveTKKIVMGEGSKASHLTYL-GDATIGRNVNIGCGTITCNYD 391

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1175185373 115 hsmdpaepvfrqpltskGIR-----IGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVTKDVP 170
Cdd:PRK14355  392 -----------------GVKkhrtvIEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVP 435
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 39-195 6.67e-06

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 48.78  E-value: 6.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  39 TGATIGEGAFLSPKASIDPDTLcIGERSFIAAhaYV-TGTITMGNDCTVNAFTVVrGNITMGDGVRIGAHTSILGF---- 113
Cdd:PRK14352  321 SESEIGAGATVGPFTYLRPGTV-LGEEGKLGA--FVeTKNATIGRGTKVPHLTYV-GDADIGEHSNIGASSVFVNYdgvn 396

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373 114 -NHSMdpaepvfrqpltskgirIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVTKDVPDWSI-VGGNPARRI-----RDR 186
Cdd:PRK14352  397 kHRTT-----------------IGSHVRTGSDTMFVAPVTVGDGAYTGAGTVIREDVPPGALaVSEGPQRNIegwvqRKR 459


                  ....*....
gi 1175185373 187 RDPVAAPTA 195
Cdd:PRK14352  460 PGTPAAEAA 468
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
133-167 8.36e-06

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 42.81  E-value: 8.36e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1175185373 133 IRIGDDVWIGSNVVVldGVRVGSHAVLAAGAVVTK 167
Cdd:pfam14602   1 VIIGDNCLIGANSGI--GVSLGDNCVVGAGVVITA 33
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 97-169 9.91e-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: 46.63  E-value: 9.91e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1175185373  97 TMGDGVRIGAHTSIlgfnhsmdpaepvfrqpltSKGIRIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVTKDV 169
Cdd:cd03352     3 KIGENVSIGPNAVI-------------------GEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGC 56
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 40-170 4.24e-05

2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 45.57  E-value: 4.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  40 GATIGEGAFLSPKASIDPdtlcigerSFIAAHAYVtGTITMgndctVNAFTVVRGNITMGDGVRIGAHTSILGFnhsMDP 119
Cdd:PRK11830  109 GAVVRRGAYIAPNVVLMP--------SYVNIGAYV-DEGTM-----VDTWATVGSCAQIGKNVHLSGGVGIGGV---LEP 171

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1175185373 120 --AEPVFrqpltskgirIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVTKDVP 170
Cdd:PRK11830  172 lqANPVI----------IEDNCFIGARSEVVEGVIVEEGSVLGMGVFLGQSTK 214
PLN02472 PLN02472
uncharacterized protein
 66-184 1.76e-04

uncharacterized protein


Pssm-ID: 215263 [Multi-domain]  Cd Length: 246  Bit Score: 43.41  E-value: 1.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  66 SFIAAHAYVTGTITMGNDCTVNAFTVVRGN---ITMGDGVRIG-------AHTSILGFnhsmdPAEPVFRQPLTS----- 130
Cdd:PLN02472   66 AYVAPNVVLAGQVTVWDGASVWNGAVLRGDlnkITVGFCSNVQercvlhaAWNSPTGL-----PAETLIDRYVTIgaysl 140

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1175185373 131 -KGIRIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVT--KDVPDWSIVGGNPARRIR 184
Cdd:PLN02472  141 lRSCTIEPECIIGQHSILMEGSLVETHSILEAGSVLPpgRRIPTGELWAGNPARFVR 197
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 42-167 2.17e-04

Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three distinct groups of carbonic anhydrases - alpha, beta and gamma - which show no significant sequence identity or structural similarity. Gamma CAs are homotrimeric enzymes, with each subunit containing a left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 42.23  E-value: 2.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  42 TIGEGAFLSPKASI---DPDTLCIGERSFI----AAHAYVTGTITMGNDCTVNAFTVVRGNITMGDGVRIgahtsilGFN 114
Cdd:cd00710    22 IIGDNVFVGPGASIradEGTPIIIGANVNIqdgvVIHALEGYSVWIGKNVSIAHGAIVHGPAYIGDNCFI-------GFR 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1175185373 115 HSmdpaepVFRQpltskgiRIGDDVWIGSNVVVlDGVRVGSHAVLAAGAVVTK 167
Cdd:cd00710    95 SV------VFNA-------KVGDNCVIGHNAVV-DGVEIPPGRYVPAGAVITS 133
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 40-180 4.07e-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: 43.20  E-value: 4.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  40 GATIGEGAFLspkasidpDTLCIGERSFIaahayvtgtiTMGNDCTVNAFTVVRgnitmgdgvrigahtsilgfNHSMDp 119
Cdd:TIGR02353 597 GVKIGRGVYI--------DGTDLTERDLV----------TIGDDSTLNEGSVIQ--------------------THLFE- 637

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1175185373 120 aEPVFRqpltSKGIRIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVTK--DVPDWSIVGGNPA 180
Cdd:TIGR02353 638 -DRVMK----SDTVTIGDGATLGPGAIVLYGVVMGEGSVLGPDSLVMKgeEVPAHTRWRGNPA 695
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
78-106 1.04e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 36.55  E-value: 1.04e-03
                          10        20
                  ....*....|....*....|....*....
gi 1175185373  78 ITMGNDCTVNAFTVVRGNITMGDGVRIGA 106
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 91-193 1.08e-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: 42.05  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  91 VVRGNITMGDGVRIGAHTSILGfnHSMDpaepvfRQPLTSKGIRIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVTKD-- 168
Cdd:TIGR02353 127 VCTDLLTIGAGTIVRKEVMLLG--YRAE------RGRLHTGPVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSALQGGqs 198

                          90       100
                  ....*....|....*....|....*..
gi 1175185373 169 VPDWSIVGGNPARRIR--DRRDPVAAP 193
Cdd:TIGR02353 199 IPDGERWHGSPAQKTGadYRKVQPARP 225
cysE PRK11132
serine acetyltransferase; Provisional
 133-203 1.85e-03

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 40.45  E-value: 1.85e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1175185373 133 IRIGddVWIGSNVVVLDGVRVGSHAVLAAGAVVTKDVPDWSIVGGNPARrirdrrdPVAAPTADLPETDAD 203
Cdd:PRK11132  196 IREG--VMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPAR-------IVGKPESDKPSMDMD 257
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 97-186 4.06e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 39.24  E-value: 4.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  97 TMGDGVRIGAHTSIlgfnhsmdpaepvfrqpltSKGIRIGDDVWIGSNVVVLDGVRVGSHAVLAAGAVVTKDVPDWSIVG 176
Cdd:PRK12461   13 KLGSGVEIGPFAVI-------------------GANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGDEPQDFTYKG 73

                          90
                  ....*....|
gi 1175185373 177 GNPARRIRDR 186
Cdd:PRK12461   74 EESRLEIGDR 83
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 81-176 6.54e-03

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


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 35.68  E-value: 6.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  81 GNDCTVNAFTVVrGNITMGDGVRIGAHTSIlgfNHSMdpaepvfrqpltskgirIGDDVWIGSNVVVLDGVrVGSHAVLA 160
Cdd:cd03356     3 GESTVIGENAII-KNSVIGDNVRIGDGVTI---TNSI-----------------LMDNVTIGANSVIVDSI-IGDNAVIG 60

                          90
                  ....*....|....*.
gi 1175185373 161 AGAvvtkDVPDWSIVG 176
Cdd:cd03356    61 ENV----RVVNLCIIG 72
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 79-169 9.16e-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: 37.77  E-value: 9.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  79 TMGNDCTVNAFTVVrgnitmGDGVRIGAHTsilgfnhsmdpaepvfrqpltskgiRIGDDVWIGSNVVVLDGVRVGSHAV 158
Cdd:cd03352     3 KIGENVSIGPNAVI------GEGVVIGDGV-------------------------VIGPGVVIGDGVVIGDDCVIHPNVT 51

                          90
                  ....*....|.
gi 1175185373 159 LAAGAVVTKDV 169
Cdd:cd03352    52 IYEGCIIGDRV 62
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 86-165 9.47e-03

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: 37.22  E-value: 9.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1175185373  86 VNAFTVVRGNITMGDGVRIGAHTSILGfnhsmDPAEPvfrqpltskgIRIGDDVWIGSNVVV--LDG--VRVGSHAVLAA 161
Cdd:cd00710    11 VHPTAVVIGDVIIGDNVFVGPGASIRA-----DEGTP----------IIIGANVNIQDGVVIhaLEGysVWIGKNVSIAH 75


                  ....
gi 1175185373 162 GAVV 165
Cdd:cd00710    76 GAIV 79
 
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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