NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1085007614|gb|OGS16908|]
View 

hypothetical protein A2251_05245 [Elusimicrobia bacterium RIFOXYA2_FULL_47_53]

Protein Classification

CatB-related O-acetyltransferase( domain architecture ID 10129626)

CatB-related O-acetyltransferase may catalyze the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin A

CATH:  2.160.10.10
EC:  2.3.1.-
Gene Ontology:  GO:0046677|GO:0016746

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 49-190 6.32e-65

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: 197.38  E-value: 6.32e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  49 STIGDHTYIQKNSTVIL---AKIGKYCSIAGGVRIGLG-KHAIDSVSTHPAFYSASQPLAKtysktNKFSYFDE---TTI 121
Cdd:cd03349     2 ISVGDYSYGSGPDCDVGgdkLSIGKFCSIAPGVKIGLGgNHPTDWVSTYPFYIFGGEWEDD-----AKFDDWPSkgdVII 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085007614 122 GHDVWIGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYAVAAGVPAKVIKLRFSENIIKELLALKWWDFP 190
Cdd:cd03349    77 GNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRYRFDEETIERLLALKWWDWP 145
 
Name Accession Description Interval E-value
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 49-190 6.32e-65

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: 197.38  E-value: 6.32e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  49 STIGDHTYIQKNSTVIL---AKIGKYCSIAGGVRIGLG-KHAIDSVSTHPAFYSASQPLAKtysktNKFSYFDE---TTI 121
Cdd:cd03349     2 ISVGDYSYGSGPDCDVGgdkLSIGKFCSIAPGVKIGLGgNHPTDWVSTYPFYIFGGEWEDD-----AKFDDWPSkgdVII 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085007614 122 GHDVWIGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYAVAAGVPAKVIKLRFSENIIKELLALKWWDFP 190
Cdd:cd03349    77 GNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRYRFDEETIERLLALKWWDWP 145
phn_thr-fam TIGR03308
phosphonate metabolism protein, transferase hexapeptide repeat family; This family of proteins ...
 31-201 2.59e-53

phosphonate metabolism protein, transferase hexapeptide repeat family; This family of proteins contains copies of the Bacterial transferase hexapeptide repeat family (pfam00132) and is only found in operons encoding the phosphonate C-P lyase system (GenProp0232). Many C-P lyase operons, however, lack a homolog of this protein.


Pssm-ID: 132351 [Multi-domain]  Cd Length: 204  Bit Score: 169.95  E-value: 2.59e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  31 NSKLGKYNVIFQNTRIISSTIGDHTYIQKNSTVILAKIGKYCSIAGGVRIGLGKHAIDSVSTHPAFYSASqplaktyskt 110
Cdd:TIGR03308  19 ESKLGRYTEIGERTRLREVALGDYSYVMRDCDIIYTTIGKFCSIAAMVRINATNHPMERPTLHHFTYRAA---------- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614 111 nkfSYFDET---------------TIGHDVWIGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYAVAAGVPAKVIKLRFSE 175
Cdd:TIGR03308  89 ---MYFDDAsddadffawrrakrvTIGHDVWIGHGAVILPGVTIGNGAVIAAGAVVTKDVAPYTIVAGVPAKLIRRRFPP 165

                         170       180
                  ....*....|....*....|....*.
gi 1085007614 176 NIIKELLALKWWDFPEDFLEKNYEFF 201
Cdd:TIGR03308 166 EIAARIEALAWWDWDHETLREALPDF 191
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
31-177 7.85e-42

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 138.47  E-value: 7.85e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  31 NSKLGKYNVIFQNTRIISS--TIGDHTYIQKNSTVILA---KIGKYCSIAGGVRIGLGKHAIDSVSTHPAfysasqplak 105
Cdd:COG0110     8 GARIGDGVVIGPGVRIYGGniTIGDNVYIGPGVTIDDPggiTIGDNVLIGPGVTILTGNHPIDDPATFPL---------- 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1085007614 106 tysktnkfsYFDETTIGHDVWIGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYAVAAGVPAKVIKLRFSENI 177
Cdd:COG0110    78 ---------RTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEEER 140
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 68-170 9.18e-19

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 80.24  E-value: 9.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  68 IGKYCSIAGGVRIglgkhaidsvsthpafYSASQPLAKTySKTNKFSYFDETTIGHDVWIGENAMIKDGIKIGNGAIIAA 147
Cdd:PRK10092   96 IGDNCMLAPGVHI----------------YTATHPLDPV-ARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVAS 158

                          90       100
                  ....*....|....*....|...
gi 1085007614 148 GAIVTKDVPDYAVAAGVPAKVIK 170
Cdd:PRK10092  159 GAVVTKDVPDNVVVGGNPARIIK 181
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
119-147 5.27e-06

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 41.94  E-value: 5.27e-06
                          10        20
                  ....*....|....*....|....*....
gi 1085007614 119 TTIGHDVWIGENAMIKDGIKIGNGAIIAA 147
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 49-190 6.32e-65

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: 197.38  E-value: 6.32e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  49 STIGDHTYIQKNSTVIL---AKIGKYCSIAGGVRIGLG-KHAIDSVSTHPAFYSASQPLAKtysktNKFSYFDE---TTI 121
Cdd:cd03349     2 ISVGDYSYGSGPDCDVGgdkLSIGKFCSIAPGVKIGLGgNHPTDWVSTYPFYIFGGEWEDD-----AKFDDWPSkgdVII 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085007614 122 GHDVWIGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYAVAAGVPAKVIKLRFSENIIKELLALKWWDFP 190
Cdd:cd03349    77 GNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRYRFDEETIERLLALKWWDWP 145
phn_thr-fam TIGR03308
phosphonate metabolism protein, transferase hexapeptide repeat family; This family of proteins ...
 31-201 2.59e-53

phosphonate metabolism protein, transferase hexapeptide repeat family; This family of proteins contains copies of the Bacterial transferase hexapeptide repeat family (pfam00132) and is only found in operons encoding the phosphonate C-P lyase system (GenProp0232). Many C-P lyase operons, however, lack a homolog of this protein.


Pssm-ID: 132351 [Multi-domain]  Cd Length: 204  Bit Score: 169.95  E-value: 2.59e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  31 NSKLGKYNVIFQNTRIISSTIGDHTYIQKNSTVILAKIGKYCSIAGGVRIGLGKHAIDSVSTHPAFYSASqplaktyskt 110
Cdd:TIGR03308  19 ESKLGRYTEIGERTRLREVALGDYSYVMRDCDIIYTTIGKFCSIAAMVRINATNHPMERPTLHHFTYRAA---------- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614 111 nkfSYFDET---------------TIGHDVWIGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYAVAAGVPAKVIKLRFSE 175
Cdd:TIGR03308  89 ---MYFDDAsddadffawrrakrvTIGHDVWIGHGAVILPGVTIGNGAVIAAGAVVTKDVAPYTIVAGVPAKLIRRRFPP 165

                         170       180
                  ....*....|....*....|....*.
gi 1085007614 176 NIIKELLALKWWDFPEDFLEKNYEFF 201
Cdd:TIGR03308 166 EIAARIEALAWWDWDHETLREALPDF 191
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
31-177 7.85e-42

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 138.47  E-value: 7.85e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  31 NSKLGKYNVIFQNTRIISS--TIGDHTYIQKNSTVILA---KIGKYCSIAGGVRIGLGKHAIDSVSTHPAfysasqplak 105
Cdd:COG0110     8 GARIGDGVVIGPGVRIYGGniTIGDNVYIGPGVTIDDPggiTIGDNVLIGPGVTILTGNHPIDDPATFPL---------- 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1085007614 106 tysktnkfsYFDETTIGHDVWIGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYAVAAGVPAKVIKLRFSENI 177
Cdd:COG0110    78 ---------RTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEEER 140
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 50-169 1.07e-31

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: 111.39  E-value: 1.07e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  50 TIGDHTYIQKNSTVI---LAKIGKYCSIAGGVRIGLGKHAIDSVSTHPAFYSASQPlaktysktnkfsyfdeTTIGHDVW 126
Cdd:cd04647     3 SIGDNVYIGPGCVISaggGITIGDNVLIGPNVTIYDHNHDIDDPERPIEQGVTSAP----------------IVIGDDVW 66

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1085007614 127 IGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYAVAAGVPAKVI 169
Cdd:cd04647    67 IGANVVILPGVTIGDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 50-169 2.33e-24

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: 94.41  E-value: 2.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  50 TIGDHTYIQKNSTVI---LAKIGKYCSIAGGVRIglgkhaidsvsthpafYSASQPL-------AKTYSKtnkfsyfdET 119
Cdd:cd03357    64 HIGDNFYANFNCTILdvaPVTIGDNVLIGPNVQI----------------YTAGHPLdpeernrGLEYAK--------PI 119

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1085007614 120 TIGHDVWIGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYAVAAGVPAKVI 169
Cdd:cd03357   120 TIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 26-165 5.85e-21

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: 86.00  E-value: 5.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  26 ADVDDNSKLGKYNVIFQNTRI-ISSTIGDHTYIqkNSTVILA---KIGKYCSIAGGVRIGlGkhaidsvsthpafysasq 101
Cdd:cd03360    91 AVVSPSAVIGEGCVIMAGAVInPDARIGDNVII--NTGAVIGhdcVIGDFVHIAPGVVLS-G------------------ 149

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1085007614 102 plaktysktnkfsyfdETTIGHDVWIGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYAVAAGVP 165
Cdd:cd03360   150 ----------------GVTIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 26-166 5.95e-21

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: 86.39  E-value: 5.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  26 ADVDDNSKLGKYNVIFQNTRI-ISSTIGDHTYIQKNSTVIL-AKIGKYCSIAGGVRIGLGkhaidsvsthpafysasqpl 103
Cdd:TIGR03570  94 AIVSPSASIGEGTVIMAGAVInPDVRIGDNVIINTGAIVEHdCVIGDFVHIAPGVTLSGG-------------------- 153

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1085007614 104 aktysktnkfsyfdeTTIGHDVWIGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYAVAAGVPA 166
Cdd:TIGR03570 154 ---------------VVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 51-170 8.17e-21

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: 83.70  E-value: 8.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  51 IGDHTYIQKNstvilAKIGKYCSIAGGVRIGLGKHAIDSVSTHP--AFYSASQPLAKTYSKTNkfsyFDETTIGHDVWIG 128
Cdd:cd03358     7 IGTNVFIEND-----VKIGDNVKIQSNVSIYEGVTIEDDVFIGPnvVFTNDLYPRSKIYRKWE----LKGTTVKRGASIG 77

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1085007614 129 ENAMIKDGIKIGNGAIIAAGAIVTKDVPDYAVAAGVPAKVIK 170
Cdd:cd03358    78 ANATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 66-170 9.50e-21

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: 85.13  E-value: 9.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  66 AKIGKYCSIAGGVRIG-LGKHAIDSvstHPafysasqplaktysktnkfsyfdetTIGHDVWIGENAMIKDGIKIGNGAI 144
Cdd:COG1045    92 AVIGDNVTIYQGVTLGgTGKEKGKR---HP-------------------------TIGDNVVIGAGAKILGPITIGDNAK 143

                          90       100
                  ....*....|....*....|....*.
gi 1085007614 145 IAAGAIVTKDVPDYAVAAGVPAKVIK 170
Cdd:COG1045   144 IGANSVVLKDVPPGSTVVGVPARIVK 169
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 68-170 9.18e-19

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 80.24  E-value: 9.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  68 IGKYCSIAGGVRIglgkhaidsvsthpafYSASQPLAKTySKTNKFSYFDETTIGHDVWIGENAMIKDGIKIGNGAIIAA 147
Cdd:PRK10092   96 IGDNCMLAPGVHI----------------YTATHPLDPV-ARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVAS 158

                          90       100
                  ....*....|....*....|...
gi 1085007614 148 GAIVTKDVPDYAVAAGVPAKVIK 170
Cdd:PRK10092  159 GAVVTKDVPDNVVVGGNPARIIK 181
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 51-170 2.26e-17

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 76.97  E-value: 2.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  51 IGDHTYIQKNSTVI---LAKIGKYCSIAGGVRIglgkhaidSVSTHPAFYSASQplaktysKTNKFSYfdETTIGHDVWI 127
Cdd:PRK09527   78 IGRNFYANFNLTIVddyTVTIGDNVLIAPNVTL--------SVTGHPVHHELRK-------NGEMYSF--PITIGNNVWI 140

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1085007614 128 GENAMIKDGIKIGNGAIIAAGAIVTKDVPDYAVAAGVPAKVIK 170
Cdd:PRK09527  141 GSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIR 183
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 48-165 1.49e-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: 72.09  E-value: 1.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  48 SSTIGDHTYIQKNSTVIL---AKIGKYCSIAGGVRIGLGKHaiDSVSTHPafysasqplaktysktnkfsyfdetTIGHD 124
Cdd:cd03354     8 GAKIGPGLFIDHGTGIVIgetAVIGDNCTIYQGVTLGGKGK--GGGKRHP-------------------------TIGDN 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1085007614 125 VWIGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYAVAAGVP 165
Cdd:cd03354    61 VVIGAGAKILGNITIGDNVKIGANAVVTKDVPANSTVVGVP 101
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 121-175 2.22e-16

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 74.14  E-value: 2.22e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1085007614 121 IGHDVWIGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYAVAAGVPAKVIKLRFSE 175
Cdd:PRK09677  133 IGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKKYNHE 187
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 5-170 1.93e-15

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: 73.91  E-value: 1.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614   5 RDTVKFVNlkrkcpsCHFyKGadvddNSKLGKYNVIFQNTRIISSTIGDHTYIqKNSTVILAKIGKYCSI---------- 74
Cdd:COG1207   271 RDVVIDPN-------VIL-EG-----KTVIGEGVVIGPNCTLKDSTIGDGVVI-KYSVIEDAVVGAGATVgpfarlrpgt 336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  75 --AGGVRIG---------LGKHaidsvsthpafysasqplaktySKTNKFSY--------------------FD-----E 118
Cdd:COG1207   337 vlGEGVKIGnfvevknstIGEG----------------------SKVNHLSYigdaeigegvnigagtitcnYDgvnkhR 394

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1085007614 119 TTIGHDVWIGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYAVAAGVPAKVIK 170
Cdd:COG1207   395 TVIGDGAFIGSNTNLVAPVTIGDGATIGAGSTITKDVPAGALAIARARQRNI 446
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 50-170 5.04e-14

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 66.97  E-value: 5.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  50 TIGDHTYIQKNSTV-ILAK----IGKYCSIAGGVRIglgkHAIdsvsthpafysasqplaktysktnkfsyfdetTIGHD 124
Cdd:COG0663    51 RIGEGSNIQDGVVLhVDPGypltIGDDVTIGHGAIL----HGC--------------------------------TIGDN 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1085007614 125 VWIGENAMIKDGIKIGNGAIIAAGAIVT--KDVPDYAVAAGVPAKVIK 170
Cdd:COG0663    95 VLIGMGAIVLDGAVIGDGSIVGAGALVTegKVVPPGSLVVGSPAKVVR 142
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 50-170 5.84e-14

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: 66.67  E-value: 5.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  50 TIGDHTYIQKNSTVILAK-----IGKYCSIAGGVRIglgkHAidsvsthpafysasqplaktysktnkfsyfdeTTIGHD 124
Cdd:cd04645    40 RIGERTNIQDGSVLHVDPgyptiIGDNVTVGHGAVL----HG--------------------------------CTIGDN 83

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1085007614 125 VWIGENAMIKDGIKIGNGAIIAAGAIVT--KDVPDYAVAAGVPAKVIK 170
Cdd:cd04645    84 CLIGMGAIILDGAVIGKGSIVAAGSLVPpgKVIPPGSLVAGSPAKVVR 131
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 50-169 1.51e-13

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: 64.16  E-value: 1.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  50 TIGDHTYIQKNS---TVILAKIGKYCSIAGGVRIGLGKHAIDSvsthPAFYSASQPLaktysktnkfsyfdetTIGHDVW 126
Cdd:cd05825     5 TIGDNSWIGEGVwiyNLAPVTIGSDACISQGAYLCTGSHDYRS----PAFPLITAPI----------------VIGDGAW 64

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1085007614 127 IGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYAVAAGVPAKVI 169
Cdd:cd05825    65 VAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 31-161 2.22e-13

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 67.93  E-value: 2.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  31 NSKLGKYNVIFQNTRIISSTIGDHTYIQkNSTVILAKIGKYCS------------IAGGVRIG---------LGKHaidS 89
Cdd:PRK14354  283 NTVIGEDCVIGPGSRIVDSTIGDGVTIT-NSVIEESKVGDNVTvgpfahlrpgsvIGEEVKIGnfveikkstIGEG---T 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  90 VSTHPAFYSASQPLAKT----------YSKTNKFsyfdETTIGHDVWIGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYA 159
Cdd:PRK14354  359 KVSHLTYIGDAEVGENVnigcgtitvnYDGKNKF----KTIIGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDA 434


                  ..
gi 1085007614 160 VA 161
Cdd:PRK14354  435 LA 436
PRK10502 PRK10502
putative acyl transferase; Provisional
 50-173 7.91e-13

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 64.20  E-value: 7.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  50 TIGDHTYIQKNS---TVILAKIGKYCSIAGGVRIGLGKHAIDSvsthPAFYSASQPLaktysktnkfsyfdetTIGHDVW 126
Cdd:PRK10502   73 TIGDYAWIGDDVwlyNLGEITIGAHCVISQKSYLCTGSHDYSD----PHFDLNTAPI----------------VIGEGCW 132

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1085007614 127 IGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYAVAAGVPAKVIKLRF 173
Cdd:PRK10502  133 LAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIRPRV 179
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 120-167 4.89e-12

serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 61.54  E-value: 4.89e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1085007614 120 TIGHDVWIGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYAVAAGVPAK 167
Cdd:TIGR01172 115 TIGEGVMIGAGAKVLGNIEVGENAKIGANSVVLKDVPPGATVVGVPAR 162
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 119-167 6.36e-12

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: 62.04  E-value: 6.36e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1085007614 119 TTIGHDVWIGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYAVAAGVPAK 167
Cdd:cd03352   151 TTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQ 199
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 18-161 2.99e-11

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: 60.13  E-value: 2.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  18 PSCHFyKGadvddNSKLGKYNVIFQNTRIISSTIGDHTYIQKNSTVILAKIGKYCSI------------AGGVRIG---- 81
Cdd:cd03353    26 PGVIL-EG-----KTVIGEDCVIGPNCVIKDSTIGDGVVIKASSVIEGAVIGNGATVgpfahlrpgtvlGEGVHIGnfve 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  82 -----LGKHaidsvsthpafysasqplaktySKTNKFSYFDETTIGHDV-------------------WIGENAMIkdG- 136
Cdd:cd03353   100 ikkstIGEG----------------------SKANHLSYLGDAEIGEGVnigagtitcnydgvnkhrtVIGDNVFI--Gs 155

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1085007614 137 -------IKIGNGAIIAAGAIVTKDVPDYAVA 161
Cdd:cd03353   156 nsqlvapVTIGDGATIAAGSTITKDVPPGALA 187
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 49-152 2.36e-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: 54.95  E-value: 2.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  49 STIGDHTYIQKNSTVIL-AKIGKYCSIAGGVRIGLGKHAIDSVSTHpafysasqplaktysktnkfsyfdettIGHDVWI 127
Cdd:cd00208     1 VFIGEGVKIHPKAVIRGpVVIGDNVNIGPGAVIGAATGPNEKNPTI---------------------------IGDNVEI 53

                          90       100
                  ....*....|....*....|....*
gi 1085007614 128 GENAMIKDGIKIGNGAIIAAGAIVT 152
Cdd:cd00208    54 GANAVIHGGVKIGDNAVIGAGAVVT 78
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 51-177 2.79e-10

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: 56.81  E-value: 2.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  51 IGDHTYIQKNSTVI-------LAKIGKYCSIAG---GVRIGLGKHAIDSVSTHPafysasqplaktySKTNKFSYFDETT 120
Cdd:cd04650     3 ISPKAYVHPTSYVIgdvvigeLTSVWHYAVIRGdndSIYIGKYSNVQENVSIHT-------------DHGYPTEIGDYVT 69

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614 121 IGHD-----------VWIGENAMIKDGIKIGNGAIIAAGAIVT--KDVPDYAVAAGVPAKVIKLRFSENI 177
Cdd:cd04650    70 IGHNavvhgakvgnyVIVGMGAILLNGAKIGDHVIIGAGAVVTpgKEIPDYSLVLGVPAKVVRKLTEEEI 139
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 118-170 2.83e-10

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 59.11  E-value: 2.83e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1085007614 118 ETTIGHDVWIGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYAVAAGVPAKVIK 170
Cdd:PRK14353  380 RTEIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALGRARQETK 432
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 28-181 3.26e-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: 55.13  E-value: 3.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  28 VDDNSKLGKYNVIFQN----------------TRIIsstIGDHTYIQKNSTVILA--------KIGKYCSIAGGVRIG-- 81
Cdd:cd03351    44 IDGPTTIGKNNRIFPFasigeapqdlkykgepTRLE---IGDNNTIREFVTIHRGtaqgggvtRIGNNNLLMAYVHVAhd 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  82 --LGKHAIdsvsthpaFYSASQpLAktysktnkfsyfDETTIGHDVWIGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYA 159
Cdd:cd03351   121 cvIGNNVI--------LANNAT-LA------------GHVEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYV 179

                         170       180       190
                  ....*....|....*....|....*....|
gi 1085007614 160 VAAGVPAK-----VIKLR---FSENIIKEL 181
Cdd:cd03351   180 IAAGNRARlrglnLVGLKrrgFSREEIRAL 209
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 119-167 8.83e-09

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: 54.25  E-value: 8.83e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1085007614 119 TTIGHDVWIGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYAVAAGVPAK 167
Cdd:COG1044   259 TKIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSGSPAQ 307
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 32-171 8.88e-09

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: 8.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  32 SKLGKYNVIFQNTRIISSTIGDHTYIQKnSTVILAKIGKYCSIAGGVRIGLGKHAIDSVSTHpAFYSASQPLAKTYSKTN 111
Cdd:PRK14357  274 TRIGEDCEIGPMTRIVDCEIGNNVKIIR-SECEKSVIEDDVSVGPFSRLREGTVLKKSVKIG-NFVEIKKSTIGENTKAQ 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614 112 KFSYFDETTIGHDVWIGENAM-------------IKDG------------IKIGNGAIIAAGAIVTKDVPDYAVAAGVPA 166
Cdd:PRK14357  352 HLTYLGDATVGKNVNIGAGTItcnydgkkknptfIEDGafigsnsslvapVRIGKGALIGAGSVITEDVPPYSLALGRAR 431


                  ....*
gi 1085007614 167 KVIKL 171
Cdd:PRK14357  432 QIVKE 436
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 25-166 9.63e-09

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: 52.00  E-value: 9.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  25 GADVDDNSKLGKYNVIFQNTRI-ISSTIGDHTYIQKNSTV-ILAKIGKYCSIAGGVRIGlgkhaidsvsthpafySASQP 102
Cdd:cd03350     7 GAIIRDGAFIGPGAVLMMPSYVnIGAYVDEGTMVDSWATVgSCAQIGKNVHLSAGAVIG----------------GVLEP 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614 103 LAKTysktnkfsyfdETTIGHDVWIGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYAVAAG------VPA 166
Cdd:cd03350    71 LQAT-----------PVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTQSTPIYDRETGeiyygrVPP 129
cysE PRK11132
serine acetyltransferase; Provisional
 125-169 1.71e-08

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 53.16  E-value: 1.71e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1085007614 125 VWIGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYAVAAGVPAKVI 169
Cdd:PRK11132  200 VMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIV 244
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 30-170 3.77e-08

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 52.62  E-value: 3.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  30 DNSKLGKyNVIFQNTRIISSTIGDHT------YIQKNstvilAKIGKYCSIAGGVRIG---LGKHaidsvsthpafysas 100
Cdd:PRK14360  296 ENSQIGE-NVTVLYSVVSDSQIGDGVkigpyaHLRPE-----AQIGSNCRIGNFVEIKksqLGEG--------------- 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614 101 qplaktySKTNKFSYFDETTIGHDVWIG-------------ENAMIKDG------------IKIGNGAIIAAGAIVTKDV 155
Cdd:PRK14360  355 -------SKVNHLSYIGDATLGEQVNIGagtitanydgvkkHRTVIGDRsktgansvlvapITLGEDVTVAAGSTITKDV 427

                         170
                  ....*....|....*
gi 1085007614 156 PDYAVAAGVPAKVIK 170
Cdd:PRK14360  428 PDNSLAIARSRQVIK 442
PLN02739 PLN02739
serine acetyltransferase
 48-171 4.02e-08

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 52.35  E-value: 4.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  48 SSTIGDHTYIQKNSTVIL---AKIGKYCSIAGGVRIG-LGKHAIDSvstHPafysasqplaktysktnkfsyfdetTIGH 123
Cdd:PLN02739  211 AARIGKGILLDHGTGVVIgetAVIGDRVSILHGVTLGgTGKETGDR---HP-------------------------KIGD 262

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1085007614 124 DVWIGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYAVAAGVPAKVIKL 171
Cdd:PLN02739  263 GALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGF 310
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 28-181 1.41e-07

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 50.40  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  28 VDDNSKLGKYNVIFQN----------------TRIIsstIGDHTYIQKNSTVILA--------KIGKYCSIAGGVRIG-- 81
Cdd:COG1043    46 IEGPTTIGKNNRIFPFasigeepqdlkykgepTRLE---IGDNNTIREFVTIHRGtvqgggvtRIGDDNLLMAYVHVAhd 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  82 --LGKHAIdsvsthpaFYSASQpLAktysktnkfsyfDETTIGHDVWIGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYA 159
Cdd:COG1043   123 cvVGNNVI--------LANNAT-LA------------GHVEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDVPPYV 181

                         170       180       190
                  ....*....|....*....|....*....|
gi 1085007614 160 VAAGVPAKV-----IKLR---FSENIIKEL 181
Cdd:COG1043   182 LAAGNPARLrglnlVGLKrrgFSREQIRAL 211
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 25-157 3.44e-07

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 50.03  E-value: 3.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  25 GADVDDNSKLGKYnVIFQNTRI-ISSTIGDHTYIQKnstvilAKIGKYCSIAGGVriglgkhaidsvsthpafysasqpL 103
Cdd:PRK09451  335 GAELAEGAHVGNF-VEMKKARLgKGSKAGHLTYLGD------AEIGDNVNIGAGT------------------------I 383

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1085007614 104 AKTYSKTNKFsyfdETTIGHDVWIGENAMIKDGIKIGNGAIIAAGAIVTKDVPD 157
Cdd:PRK09451  384 TCNYDGANKF----KTIIGDDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDVAE 433
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 50-170 4.58e-07

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: 47.75  E-value: 4.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  50 TIGDHTYIQKNSTVIlakiGKYcsiaGGVRIGLGKHAIDSVSTH--PAFYSasqpLAKTYSKTNKFSYFDETTIGHDVWI 127
Cdd:cd04745    20 IIGKNCYIGPHASLR----GDF----GRIVIRDGANVQDNCVIHgfPGQDT----VLEENGHIGHGAILHGCTIGRNALV 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1085007614 128 GENAMIKDGIKIGNGAIIAAGAIVTK--DVPDYAVAAGVPAKVIK 170
Cdd:cd04745    88 GMNAVVMDGAVIGEESIVGAMAFVKAgtVIPPRSLIAGSPAKVIR 132
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 33-180 5.84e-07

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: 47.59  E-value: 5.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  33 KLGKYNVIFQNTRIISS-------------TIGDHTYIQKNSTVILAKIGKYcsiaggvriglgkhaidsvsthpafysa 99
Cdd:cd03359    44 SIGRYCILSEGCVIRPPfkkfskgvaffplHIGDYVFIGENCVVNAAQIGSY---------------------------- 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614 100 sqplaktysktnkfsyfdeTTIGHDVWIGENAMIKDGIKIGNGAIIAAGAIvtkdVPDYAVAAGVPAKVIKL--RFSENI 177
Cdd:cd03359    96 -------------------VHIGKNCVIGRRCIIKDCVKILDGTVVPPDTV----IPPYSVVSGRPARFIGElpECTQEL 152


                  ...
gi 1085007614 178 IKE 180
Cdd:cd03359   153 MEE 155
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 31-161 6.06e-07

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 48.95  E-value: 6.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  31 NSKLGKYNVIFQNTRIISSTIGDHTYIQKNSTVILAKIGKYCSIA------------GGVRIG---------LGKHAids 89
Cdd:PRK14356  287 ASRIARGAVIHSHCWLRDAVVSSGATIHSFSHLEGAEVGDGCSVGpyarlrpgavleEGARVGnfvemkkavLGKGA--- 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  90 VSTHPAFYSASQPLAKT----------YSKTNKfsyfDETTIGHDVWIGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYA 159
Cdd:PRK14356  364 KANHLTYLGDAEIGAGAnigagtitcnYDGVNK----HRTVIGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGS 439


                  ..
gi 1085007614 160 VA 161
Cdd:PRK14356  440 LA 441
PLN02357 PLN02357
serine acetyltransferase
 121-169 1.05e-06

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 48.34  E-value: 1.05e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1085007614 121 IGHDVWIGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYAVAAGVPAKVI 169
Cdd:PLN02357  281 IGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLI 329
PLN02694 PLN02694
serine O-acetyltransferase
 121-169 1.07e-06

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 48.10  E-value: 1.07e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1085007614 121 IGHDVWIGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYAVAAGVPAKVI 169
Cdd:PLN02694  215 IGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLV 263
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 67-170 1.78e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 47.44  E-value: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  67 KIGKYCSIAGGVRIglgkhaidsvsthpafySASqplaktysktnkfsyfdeTTIGHDVWIGENAMIKDGIKIGNGAIIA 146
Cdd:PRK00892  245 VIGRHTAIAAQVGI-----------------AGS------------------TKIGRYCMIGGQVGIAGHLEIGDGVTIT 289

                          90       100
                  ....*....|....*....|....*
gi 1085007614 147 AGAIVTKDVPDY-AVAAGVPAKVIK 170
Cdd:PRK00892  290 AMSGVTKSIPEPgEYSSGIPAQPNK 314
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 26-151 4.76e-06

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 46.16  E-value: 4.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  26 ADVDDNSKLGKyNVifqntriissTIGDHTYIQKNstvilAKIGKYCSIAGGVRIGlgkhaidsvsthpafysasqplak 105
Cdd:COG1044   103 AVIDPSAKIGE-GV----------SIGPFAVIGAG-----VVIGDGVVIGPGVVIG------------------------ 142

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1085007614 106 tysktnkfsyfDETTIGHDVWIGENAMIKDGIKIGNGAIIAAGAIV 151
Cdd:COG1044   143 -----------DGVVIGDDCVLHPNVTIYERCVIGDRVIIHSGAVI 177
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
119-147 5.27e-06

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 41.94  E-value: 5.27e-06
                          10        20
                  ....*....|....*....|....*....
gi 1085007614 119 TTIGHDVWIGENAMIKDGIKIGNGAIIAA 147
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 120-155 1.13e-05

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 45.01  E-value: 1.13e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1085007614 120 TIGHDVWIGENAMIKDGIKIGNGAIIAAGAIVTKDV 155
Cdd:COG1044   110 KIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGV 145
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 48-151 1.37e-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: 44.32  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  48 SSTIGDHTYIQKNstvilAKIGKYCSIAGGVRIGlgkhaidsvsthpafysasqplaktysktnkfsyfDETTIGHDVWI 127
Cdd:cd03352     7 NVSIGPNAVIGEG-----VVIGDGVVIGPGVVIG-----------------------------------DGVVIGDDCVI 46

                          90       100
                  ....*....|....*....|....
gi 1085007614 128 GENAMIKDGIKIGNGAIIAAGAIV 151
Cdd:cd03352    47 HPNVTIYEGCIIGDRVIIHSGAVI 70
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 23-161 1.59e-05

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 44.73  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  23 YKGADVDDNSKLGKYNVIFQNTRIISSTIGDHTYIQKNSTVILAKIGKYCSI------------AGGVRIGlgkhaiDSV 90
Cdd:PRK14355  278 YPGVCISGDTRIGEGCTIEQGVVIKGCRIGDDVTVKAGSVLEDSVVGDDVAIgpmahlrpgtelSAHVKIG------NFV 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  91 STHPAFYSASqplaktySKTNKFSYFDETTIGHDVWIG-------------ENAMIKDGI------------KIGNGAII 145
Cdd:PRK14355  352 ETKKIVMGEG-------SKASHLTYLGDATIGRNVNIGcgtitcnydgvkkHRTVIEDDVfvgsdvqfvapvTVGRNSLI 424

                         170
                  ....*....|....*.
gi 1085007614 146 AAGAIVTKDVPDYAVA 161
Cdd:PRK14355  425 AAGTTVTKDVPPDSLA 440
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 25-161 2.12e-05

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 44.54  E-value: 2.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  25 GADVDDNSKLGKYnVIFQNtriisSTIGDHTYIQKNSTVILAKIGKYCSIAGGvriglgkhaidSVSTHpafysasqpla 104
Cdd:PRK14352  340 GTVLGEEGKLGAF-VETKN-----ATIGRGTKVPHLTYVGDADIGEHSNIGAS-----------SVFVN----------- 391

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1085007614 105 ktYSKTNKfsyfDETTIGHDVWIGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYAVA 161
Cdd:PRK14352  392 --YDGVNK----HRTTIGSHVRTGSDTMFVAPVTVGDGAYTGAGTVIREDVPPGALA 442
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 120-155 5.30e-05

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 42.40  E-value: 5.30e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1085007614 120 TIGHDVWIGENAMIKDGIKIGNGAIIAAGAIVTKDV 155
Cdd:cd03352     3 KIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGV 38
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 28-161 8.26e-05

bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 42.66  E-value: 8.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  28 VDDNSKLGKYNVIfqntriISSTIGDHTYIQKNSTVILAKIGK------YCSIAGGVRIGLGKHAIDSVST--------- 92
Cdd:PRK14358  291 VADGVTIGAYSVV------TDSVLHEGAVIKPHSVLEGAEVGAgsdvgpFARLRPGTVLGEGVHIGNFVETknarldagv 364

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1085007614  93 ---HPAFYSASQPLAKTYSKTNKF-SYFD-----ETTIGHDVWIGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYAVA 161
Cdd:PRK14358  365 kagHLAYLGDVTIGAETNVGAGTIvANFDgvnkhQSKVGAGVFIGSNTTLIAPRVVGDAAFIAAGSAVHDDVPEGAMA 442
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
28-181 8.98e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 42.01  E-value: 8.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  28 VDDNSKLGKYNVIFQN----------------TRIIsstIGDHTYIQKNSTVILA--------KIGKYCSIAGGVRIG-- 81
Cdd:PRK05289   47 IDGHTTIGKNNRIFPFasigedpqdlkykgepTRLV---IGDNNTIREFVTINRGtvqgggvtRIGDNNLLMAYVHVAhd 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  82 --LGKHAIdsvsthpaFYSASQpLAktysktnkfsyfdettiGHdVWIGENAMIkdG--------IKIGNGAIIAAGAIV 151
Cdd:PRK05289  124 cvVGNHVI--------LANNAT-LA-----------------GH-VEVGDYAII--GgltavhqfVRIGAHAMVGGMSGV 174

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1085007614 152 TKDVPDYAVAAGVPAK-----VIKLR---FSENIIKEL 181
Cdd:PRK05289  175 SQDVPPYVLAEGNPARlrglnLVGLKrrgFSREEIHAL 212
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 18-181 1.42e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 41.55  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  18 PSCHFYKGADVDDNSKLGKYNVIFQNtriisSTIGDHTYIQKNSTVI-LAKIGKYCSIAGG------------------V 78
Cdd:PRK12461    4 PTAVIDPSAKLGSGVEIGPFAVIGAN-----VEIGDGTWIGPHAVILgPTRIGKNNKIHQGavvgdepqdftykgeesrL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  79 RIGLGKHAIDSVSTHpafySASQPLAKTYSKTNKFsYFDETTIGHDVWIGENAMIKDG---------------------- 136
Cdd:PRK12461   79 EIGDRNVIREGVTIH----RGTKGGGVTRIGNDNL-LMAYSHVAHDCQIGNNVILVNGallaghvtvgdraiisgnclvh 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1085007614 137 --IKIGNGAIIAAGAIVTKDVPDYAVAAGVPAKV-----IKLR---FSENIIKEL 181
Cdd:PRK12461  154 qfCRIGALAMMAGGSRISKDVPPYCMMAGHPTNVhglnaVGLRrrgFSSRAIRAL 208
PLN02296 PLN02296
carbonate dehydratase
 117-167 2.06e-04

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 41.26  E-value: 2.06e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1085007614 117 DETTIGH-----------DVWIGENAMIKDGIKIGNGAIIAAGAIVTKD--VPDYAVAAGVPAK 167
Cdd:PLN02296  124 DNVTIGHsavlhgctvedEAFVGMGATLLDGVVVEKHAMVAAGALVRQNtrIPSGEVWAGNPAK 187
PRK10191 PRK10191
putative acyl transferase; Provisional
 121-168 2.11e-04

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 40.26  E-value: 2.11e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1085007614 121 IGHDVWIGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYAVAAGVPAKV 168
Cdd:PRK10191   95 IGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKARV 142
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 31-170 2.29e-04

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 41.51  E-value: 2.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  31 NSKLGKYNVIfQNTRIISSTIGDHTYIQKNSTVILAKIGKYC----SIAGGVRIG----LGKHAIDSVSTHPAfysasQP 102
Cdd:PRK14359  282 NSHIKAHSVI-EESIIENSDVGPLAHIRPKSEIKNTHIGNFVetknAKLNGVKAGhlsyLGDCEIDEGTNIGA-----GT 355

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1085007614 103 LAKTYSKTNKFsyfdETTIGHDVWIGENAMIKDGIKIGNGAIIAAGAIVTKDVPDYAVA-AGVPAKVIK 170
Cdd:PRK14359  356 ITCNYDGKKKH----KTIIGKNVFIGSDTQLVAPVNIEDNVLIAAGSTVTKDVPKGSLAiSRAPQKNIK 420
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 120-155 2.85e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 40.89  E-value: 2.85e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1085007614 120 TIGHDVWIGENAMIKDGIKIGNGAIIAAGAIVTKDV 155
Cdd:PRK00892  114 KIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGV 149
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 25-151 5.73e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 40.12  E-value: 5.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1085007614  25 GADVDDNSKLGKynvifqntriiSSTIGDHTYIQKNstvilAKIGKYCSIAGGVRIGlgkhaidsvsthpafysasqpla 104
Cdd:PRK00892  106 SAVIDPSAKIGE-----------GVSIGPNAVIGAG-----VVIGDGVVIGAGAVIG----------------------- 146

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1085007614 105 ktysktnkfsyfDETTIGHDVWIGENAMIKDGIKIGNGAIIAAGAIV 151
Cdd:PRK00892  147 ------------DGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVI 181
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
119-153 8.56e-04

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 35.88  E-value: 8.56e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1085007614 119 TTIGHDVWIGENAMIkdGIKIGNGAIIAAGAIVTK 153
Cdd:pfam14602   1 VIIGDNCLIGANSGI--GVSLGDNCVVGAGVVITA 33
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH