NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1680958597|ref|WP_139111830|]
View 

LbetaH domain-containing protein, partial [Acinetobacter pittii]

Protein Classification

LbetaH domain-containing protein( domain architecture ID 10082836)

LbetaH (Left-handed parallel beta-Helix) domain-containing protein similar to Escherichia coli uncharacterized acetyltransferase YdcK

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 51-123 1.32e-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: 53.41  E-value: 1.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1680958597  51 VEIGENCFISPLAHIfaepGRKIIIGDNSFIAADCTLHG--------PLEIGNEVAINHHCILDGgrtGIKLHDQVRIAA 122
Cdd:cd00208     1 VFIGEGVKIHPKAVI----RGPVVIGDNVNIGPGAVIGAatgpneknPTIIGDNVEIGANAVIHG---GVKIGDNAVIGA 73


                  .
gi 1680958597 123 Y 123
Cdd:cd00208    74 G 74
 
Name Accession Description Interval E-value
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 51-123 1.32e-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: 53.41  E-value: 1.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1680958597  51 VEIGENCFISPLAHIfaepGRKIIIGDNSFIAADCTLHG--------PLEIGNEVAINHHCILDGgrtGIKLHDQVRIAA 122
Cdd:cd00208     1 VFIGEGVKIHPKAVI----RGPVVIGDNVNIGPGAVIGAatgpneknPTIIGDNVEIGANAVIHG---GVKIGDNAVIGA 73


                  .
gi 1680958597 123 Y 123
Cdd:cd00208    74 G 74
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
51-105 1.76e-10

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 54.49  E-value: 1.76e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1680958597  51 VEIGENCFISPLAHIFaepGRKIIIGDNSFIAADCTL--HGPLEIGNEVAINHHCIL 105
Cdd:COG0110     9 ARIGDGVVIGPGVRIY---GGNITIGDNVYIGPGVTIddPGGITIGDNVLIGPGVTI 62
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 51-107 1.81e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 45.13  E-value: 1.81e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1680958597  51 VEIGENCFISPLAHIfaepGRKIIIGDNSFIAADCTLHGPLEIGNEVAINHHCIL--DG 107
Cdd:PRK00892  131 VVIGDGVVIGAGAVI----GDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVIgsDG 185
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
51-83 3.90e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.39  E-value: 3.90e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1680958597  51 VEIGENCFISPLAHIfaepGRKIIIGDNSFIAA 83
Cdd:pfam00132   2 TVIGDNVLIGPNAVI----GGGVIIGDNVIIGA 30
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 49-107 2.09e-03

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: 35.93  E-value: 2.09e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1680958597  49 ETVEIGENCFISPLAHI--FAEPGRKII------------IGDNSFIAADCTLHGPLEIGNEVAIN-HHCILDG 107
Cdd:TIGR03570  98 PSASIGEGTVIMAGAVInpDVRIGDNVIintgaivehdcvIGDFVHIAPGVTLSGGVVIGEGVFIGaGATIIQG 171
 
Name Accession Description Interval E-value
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 51-123 1.32e-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: 53.41  E-value: 1.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1680958597  51 VEIGENCFISPLAHIfaepGRKIIIGDNSFIAADCTLHG--------PLEIGNEVAINHHCILDGgrtGIKLHDQVRIAA 122
Cdd:cd00208     1 VFIGEGVKIHPKAVI----RGPVVIGDNVNIGPGAVIGAatgpneknPTIIGDNVEIGANAVIHG---GVKIGDNAVIGA 73


                  .
gi 1680958597 123 Y 123
Cdd:cd00208    74 G 74
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
51-105 1.76e-10

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 54.49  E-value: 1.76e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1680958597  51 VEIGENCFISPLAHIFaepGRKIIIGDNSFIAADCTL--HGPLEIGNEVAINHHCIL 105
Cdd:COG0110     9 ARIGDGVVIGPGVRIY---GGNITIGDNVYIGPGVTIddPGGITIGDNVLIGPGVTI 62
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 51-107 7.95e-09

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 50.80  E-value: 7.95e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1680958597  51 VEIGENCFISPLAHIFAEPGRkIIIGDNSFIAADCTLHG----PLEIGNEVAINHHCILDG 107
Cdd:COG0663    29 VTIGEDVSVWPGAVLRGDVGP-IRIGEGSNIQDGVVLHVdpgyPLTIGDDVTIGHGAILHG 88
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 51-107 2.16e-08

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: 49.55  E-value: 2.16e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1680958597  51 VEIGENCFISPLAHIFAEPGRKIIIGDNSFIAADCTLHG----PLEIGNEVAINHHCILDG 107
Cdd:cd00710    21 VIIGDNVFVGPGASIRADEGTPIIIGANVNIQDGVVIHAlegySVWIGKNVSIAHGAIVHG 81
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
41-99 1.33e-07

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 46.79  E-value: 1.33e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1680958597  41 YQAYLMDMETVEIGENCFISPLAHI------------FAEPGRKIIIGDNSFIAADCTLHGPLEIGNEVAI 99
Cdd:COG0110    38 PGVTIDDPGGITIGDNVLIGPGVTIltgnhpiddpatFPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVV 108
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 51-111 1.35e-07

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: 47.02  E-value: 1.35e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1680958597  51 VEIGENCFISPLAHIFAEPGRkIIIGDNSFIAADCTLH----GPLEIGNEVAINHHCILDGGRTG 111
Cdd:cd04645    18 VTLGEGSSVWFGAVLRGDVNP-IRIGERTNIQDGSVLHvdpgYPTIIGDNVTVGHGAVLHGCTIG 81
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 51-107 2.67e-07

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: 45.53  E-value: 2.67e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1680958597  51 VEIGENCFISPLAHIFAepGRKIIIGDNSFIAADCTLH-------------------GPLEIGNEVAINHHC-ILDG 107
Cdd:cd04647     2 ISIGDNVYIGPGCVISA--GGGITIGDNVLIGPNVTIYdhnhdiddperpieqgvtsAPIVIGDDVWIGANVvILPG 76
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 49-108 3.83e-07

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 44.55  E-value: 3.83e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1680958597  49 ETVEIGENCFISPLAHIFAEPG----RKIIIGDNSFIAADCTLHGPLEIGnevainHHCILDGG 108
Cdd:cd00208    17 GPVVIGDNVNIGPGAVIGAATGpnekNPTIIGDNVEIGANAVIHGGVKIG------DNAVIGAG 74
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
73-123 1.49e-06

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 44.09  E-value: 1.49e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1680958597  73 IIIGDNSFIAADCTLHGP-LEIGNEVAINHHCILDgGRTGIKLHDQVRIAAY 123
Cdd:COG0110     9 ARIGDGVVIGPGVRIYGGnITIGDNVYIGPGVTID-DPGGITIGDNVLIGPG 59
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 51-107 1.81e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 45.13  E-value: 1.81e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1680958597  51 VEIGENCFISPLAHIfaepGRKIIIGDNSFIAADCTLHGPLEIGNEVAINHHCIL--DG 107
Cdd:PRK00892  131 VVIGDGVVIGAGAVI----GDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVIgsDG 185
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 41-99 5.78e-06

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: 42.06  E-value: 5.78e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1680958597  41 YQAYLMDMETVEIGENCFISPLAHIFA---------------EPGRKIIIGDNSFIAADCTLHGPLEIGNEVAI 99
Cdd:cd04647    12 PGCVISAGGGITIGDNVLIGPNVTIYDhnhdiddperpieqgVTSAPIVIGDDVWIGANVVILPGVTIGDGAVV 85
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 49-99 7.85e-06

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: 41.27  E-value: 7.85e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1680958597  49 ETVEIGENCFISPLAHI----FAEPGRKIIIGDNSFIAADCTLHGPLEIGNEVAI 99
Cdd:cd03354    27 ETAVIGDNCTIYQGVTLggkgKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVKI 81
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 72-108 9.26e-06

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: 41.29  E-value: 9.26e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1680958597  72 KIIIGDNSFIAADCTL--HGPLEIGNEVAINHHC-ILDGG 108
Cdd:cd04647     1 NISIGDNVYIGPGCVIsaGGGITIGDNVLIGPNVtIYDHN 40
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 49-107 1.26e-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: 1.26e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1680958597  49 ETVEIGENCFISPLAHIfaepGRKIIIGDNSFIAADCTLHGPLEIGNEVAINHHCIL--DG 107
Cdd:cd03352    18 EGVVIGDGVVIGPGVVI----GDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIgsDG 74
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 47-107 1.73e-05

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: 41.63  E-value: 1.73e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1680958597  47 DMETVEIGENCFISPLAHIFAEPGRKIIIGDNSFIAADCTLHGpLEIGNEVAINHHC-ILDG 107
Cdd:cd04645    35 DVNPIRIGERTNIQDGSVLHVDPGYPTIIGDNVTVGHGAVLHG-CTIGDNCLIGMGAiILDG 95
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 51-111 2.32e-05

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: 41.20  E-value: 2.32e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1680958597  51 VEIGENCFISPLAHIFAEPGRkIIIGDNSFIAADCTLHG-PLE---IGNEVAINHHCILDGGRTG 111
Cdd:cd04745    19 VIIGKNCYIGPHASLRGDFGR-IVIRDGANVQDNCVIHGfPGQdtvLEENGHIGHGAILHGCTIG 82
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 49-122 3.25e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 41.66  E-value: 3.25e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1680958597  49 ETVeIGENCFISPLAHIfaepGRKIIIGDNSFIAADCTLHGPLEIGNevainhHCILdGGRTGIKLH----DQVRIAA 122
Cdd:PRK00892  225 DTV-IGEGVKIDNLVQI----AHNVVIGRHTAIAAQVGIAGSTKIGR------YCMI-GGQVGIAGHleigDGVTITA 290
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 50-108 3.39e-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: 41.24  E-value: 3.39e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1680958597  50 TVEIGENCFISPLAHIfaEPGRKI----------IIGDNSFIAADCTLHGPLEIGNEVAINHHCILDGG 108
Cdd:cd03352     1 SAKIGENVSIGPNAVI--GEGVVIgdgvvigpgvVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSG 67
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 49-105 4.88e-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: 41.16  E-value: 4.88e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1680958597  49 ETVEIGENCFISPLAHIfaEPGRKI----------IIGDNSFIAADCTLHgpleiGNeVAINHHCIL 105
Cdd:COG1044   107 PSAKIGEGVSIGPFAVI--GAGVVIgdgvvigpgvVIGDGVVIGDDCVLH-----PN-VTIYERCVI 165
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
49-105 1.03e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 40.08  E-value: 1.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1680958597  49 ETVEIGENCFISPLAHIfaepGRKIIIGDNSFIAADCTLHGPLEIGNEVAINHHCIL 105
Cdd:PRK05289   13 PGAKIGENVEIGPFCVI----GPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASI 65
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 49-122 1.34e-04

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 39.31  E-value: 1.34e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1680958597  49 ETVeIGENCFISPLAHIfaepGRKIIIGDNSFIAADCTLHGPLEIGNevainhHCILdGGRTGIKLH----DQVRIAA 122
Cdd:cd03352   114 DTV-IGDGTKIDNLVQI----AHNVRIGENCLIAAQVGIAGSTTIGD------NVII-GGQVGIAGHltigDGVVIGA 179
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 24-94 1.98e-04

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


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 37.97  E-value: 1.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1680958597  24 WTLKPKNRAWAEEwqkeyQAYLMDMETVEIGENCFISPLAHI-----------FAEPGRKIIIGDNSFIAADCTLHGPLE 92
Cdd:cd05825     2 WNLTIGDNSWIGE-----GVWIYNLAPVTIGSDACISQGAYLctgshdyrspaFPLITAPIVIGDGAWVAAEAFVGPGVT 76


                  ..
gi 1680958597  93 IG 94
Cdd:cd05825    77 IG 78
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 53-105 2.46e-04

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: 37.87  E-value: 2.46e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1680958597  53 IGENCFISPLAHIfaepGRKIIIGDNSFIAADCTLHGPLEIGNEVAINHHCIL 105
Cdd:cd03358     1 IGDNCIIGTNVFI----ENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVF 49
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 49-122 3.27e-04

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 38.46  E-value: 3.27e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1680958597  49 ETVeIGENCFISPLAHIfaepGRKIIIGDNSFIAADCTLHGPLEIGNevainhHCILdGGRTGI----KLHDQVRIAA 122
Cdd:COG1044   222 DTV-IGDGTKIDNLVQI----AHNVRIGEHTAIAAQVGIAGSTKIGD------NVVI-GGQVGIaghlTIGDGVIIGA 287
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 53-99 3.80e-04

Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively at the C6 position of the nonreducing end glucosyl moiety. GAT specifically acetylates galactopyranosides. Furthermore, MAT shows higher affinity toward artificial substrates containing an alkyl or hydrophobic chain as well as a glucosyl unit. Active MAT and GAT are homotrimers, with each subunit consisting of an N-terminal alpha-helical region and a C-terminal left-handed parallel alpha-helix (LbH) subdomain with 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100047 [Multi-domain]  Cd Length: 169  Bit Score: 37.79  E-value: 3.80e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1680958597  53 IGENCFISPlaHIFAEPGRKIIIGDNSFIAADCTL--HGPLEIGNEVAI 99
Cdd:cd03357    45 VGENVYIEP--PFHCDYGYNIHIGDNFYANFNCTIldVAPVTIGDNVLI 91
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 51-99 3.84e-04

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: 38.23  E-value: 3.84e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1680958597  51 VEIGENCFISPLAHIfaePGRkIIIGDNSFIAADCTLHGPLEIGNEVAI 99
Cdd:cd03360   133 CVIGDFVHIAPGVVL---SGG-VTIGEGAFIGAGATIIQGVTIGAGAII 177
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
51-83 3.90e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.39  E-value: 3.90e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1680958597  51 VEIGENCFISPLAHIfaepGRKIIIGDNSFIAA 83
Cdd:pfam00132   2 TVIGDNVLIGPNAVI----GGGVIIGDNVIIGA 30
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 49-122 5.36e-04

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 37.85  E-value: 5.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1680958597  49 ETVEIGENCFISPLAHI--FAEPGRKII------------IGDNSFIAADCTLHGPLEIGNEVAIN-HHCILDggrtGIK 113
Cdd:cd03360    95 PSAVIGEGCVIMAGAVInpDARIGDNVIintgavighdcvIGDFVHIAPGVVLSGGVTIGEGAFIGaGATIIQ----GVT 170


                  ....*....
gi 1680958597 114 LHDQVRIAA 122
Cdd:cd03360   171 IGAGAIIGA 179
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 49-105 5.45e-04

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 37.77  E-value: 5.45e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1680958597  49 ETVEIGENCFISPLAHIfaepGRKIIIGDNSFIAADCTLHGPLEIGNEVAINHHCIL 105
Cdd:cd03352     6 ENVSIGPNAVIGEGVVI----GDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCII 58
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 52-105 1.25e-03

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 36.92  E-value: 1.25e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1680958597  52 EIGENCFISPLAHIfaepGRKIIIGDNSFIAADCTLHGPLEIGNEVAINHHCIL 105
Cdd:COG1043    15 KLGENVEIGPFCVI----GPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASI 64
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 51-105 1.36e-03

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: 36.64  E-value: 1.36e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1680958597  51 VEIGENCFISPLAHIfaepGRKIIIGDNSFIAADCTLHGPLEIGNEVAINHHCIL 105
Cdd:cd03351    12 AKIGENVEIGPFCVI----GPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASI 62
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 49-107 2.09e-03

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: 35.93  E-value: 2.09e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1680958597  49 ETVEIGENCFISPLAHI--FAEPGRKII------------IGDNSFIAADCTLHGPLEIGNEVAIN-HHCILDG 107
Cdd:TIGR03570  98 PSASIGEGTVIMAGAVInpDVRIGDNVIintgaivehdcvIGDFVHIAPGVTLSGGVVIGEGVFIGaGATIIQG 171
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 51-81 2.31e-03

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


Pssm-ID: 100052 [Multi-domain]  Cd Length: 164  Bit Score: 35.76  E-value: 2.31e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1680958597  51 VEIGENCFISPLAHIFAEPGrKIIIGDNSFI 81
Cdd:cd04646    18 VTIGPGTVVHPRATIIAEAG-PIIIGENNII 47
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 51-111 3.05e-03

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: 35.24  E-value: 3.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1680958597  51 VEIGENCFISPLAHIFAEpGRKIIIGDNSFIAADCTLHG----PLEIGNEVAINHHCILDGGRTG 111
Cdd:cd04650    19 VVIGELTSVWHYAVIRGD-NDSIYIGKYSNVQENVSIHTdhgyPTEIGDYVTIGHNAVVHGAKVG 82
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 45-99 3.20e-03

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 35.56  E-value: 3.20e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1680958597  45 LMDMETVEIGENCFISPLAHIF--------------AEPGRKIIIGDNSFIAADCTLHGPLEIGNEVAI 99
Cdd:PRK10092   88 MLDVCPIRIGDNCMLAPGVHIYtathpldpvarnsgAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVV 156
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 72-99 4.71e-03

N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix (LbH) acetyltransferase domain: GlmU is also known as UDP-N-acetylglucosamine pyrophosphorylase. It is a bifunctional bacterial enzyme that catalyzes two consecutive steps in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), an important precursor in bacterial cell wall formation. The two enzymatic activities, uridyltransferase and acetyltransferase, are carried out by two independent domains. The C-terminal LbH domain possesses the acetyltransferase activity. It catalyzes the CoA-dependent acetylation of GlcN-1-phosphate to GlcNAc-1-phosphate. The LbH domain contains 10 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X. The acetyltransferase active site is located at the interface between two subunits of the active LbH trimer.


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 35.09  E-value: 4.71e-03
                          10        20
                  ....*....|....*....|....*...
gi 1680958597  72 KIIIGDNSFIAADCTLHGPLEIGNEVAI 99
Cdd:cd03353   144 RTVIGDNVFIGSNSQLVAPVTIGDGATI 171
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 49-100 7.36e-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: 32.98  E-value: 7.36e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1680958597  49 ETVEIGENCFISP---LAHIFAEPGRKI---IIGDNSFIAADCTLHGPLeIGNEVAIN 100
Cdd:cd03356     4 ESTVIGENAIIKNsviGDNVRIGDGVTItnsILMDNVTIGANSVIVDSI-IGDNAVIG 60
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 58-123 9.30e-03

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 34.38  E-value: 9.30e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1680958597  58 FISPLAHIfaepGRKIIIGDNSFIAADCTLHGPLEIGNEVAINHHCILDggrtgiklHDqVRIAAY 123
Cdd:cd03360    86 LIHPSAVV----SPSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIG--------HD-CVIGDF 138
 
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