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Conserved domains on  [gi|495007623|ref|WP_007733635|]
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acyltransferase [Cronobacter dublinensis]

Protein Classification

acyltransferase( domain architecture ID 10129729)

acyltransferase belonging to the transferase hexapeptide repeat family, catalyzes the transfer of an acyl group from an acyl-CoA to a substrate; similar to Helicobacter pullorum N-acetyltransferase

CATH:  2.160.10.10
EC:  2.3.1.-
Gene Ontology:  GO:0016746|GO:0120225
PubMed:  15500694

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 35-153 6.32e-43

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: 138.02  E-value: 6.32e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  35 LGDGVFIGPFVEIQRYTRIGRGTRVQSHTFICESVTIGEDCFIGHGVMFANDMFRDGKPDPNSDhWVRITIGDNVSIGSG 114
Cdd:cd03358    1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKIYRKWE-LKGTTVKRGASIGAN 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 495007623 115 ATILAE-SICSGAVIGAGSVVTKPITEKGVYAGNPARLLR 153
Cdd:cd03358   80 ATILPGvTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
 
Name Accession Description Interval E-value
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 35-153 6.32e-43

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: 138.02  E-value: 6.32e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  35 LGDGVFIGPFVEIQRYTRIGRGTRVQSHTFICESVTIGEDCFIGHGVMFANDMFRDGKPDPNSDhWVRITIGDNVSIGSG 114
Cdd:cd03358    1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKIYRKWE-LKGTTVKRGASIGAN 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 495007623 115 ATILAE-SICSGAVIGAGSVVTKPITEKGVYAGNPARLLR 153
Cdd:cd03358   80 ATILPGvTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
30-155 9.00e-32

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 110.35  E-value: 9.00e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  30 LYECELGDGVFIGPFVEIQRYT-RIGRGTRVQSHTFI--CESVTIGEDCFIGHGVMFANDMFRDGKPDPNSDHWVRITIG 106
Cdd:COG0110    6 LFGARIGDGVVIGPGVRIYGGNiTIGDNVYIGPGVTIddPGGITIGDNVLIGPGVTILTGNHPIDDPATFPLRTGPVTIG 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 495007623 107 DNVSIGSGATILAE-SICSGAVIGAGSVVTKPITEKGVYAGNPARLLRRL 155
Cdd:COG0110   86 DDVWIGAGATILPGvTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKR 135
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 32-149 1.33e-20

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: 83.31  E-value: 1.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623   32 ECELGDGVFIGPFVEIQRYTRIGRGTRVQShtficeSVTIGEDCFIGHGVMFAndmfrdgkpdPNSDHWVRITIGDNVSI 111
Cdd:TIGR03570  99 SASIGEGTVIMAGAVINPDVRIGDNVIINT------GAIVEHDCVIGDFVHIA----------PGVTLSGGVVIGEGVFI 162

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 495007623  112 GSGATILAE-SICSGAVIGAGSVVTKPITEKGVYAGNPA 149
Cdd:TIGR03570 163 GAGATIIQGvTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 32-136 1.08e-14

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 69.86  E-value: 1.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  32 ECELGDGVFIGPFVEIQRYTrIGRGTRVqSH-TFICESvTIGEDCFIGHGVMFANdmfRDGKpdpnsdHWVRITIGDNVS 110
Cdd:PRK14354 334 GSVIGEEVKIGNFVEIKKST-IGEGTKV-SHlTYIGDA-EVGENVNIGCGTITVN---YDGK------NKFKTIIGDNAF 401

                         90       100
                 ....*....|....*....|....*..
gi 495007623 111 IGSGATILAE-SICSGAVIGAGSVVTK 136
Cdd:PRK14354 402 IGCNSNLVAPvTVGDNAYIAAGSTITK 428
 
Name Accession Description Interval E-value
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 35-153 6.32e-43

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: 138.02  E-value: 6.32e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  35 LGDGVFIGPFVEIQRYTRIGRGTRVQSHTFICESVTIGEDCFIGHGVMFANDMFRDGKPDPNSDhWVRITIGDNVSIGSG 114
Cdd:cd03358    1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKIYRKWE-LKGTTVKRGASIGAN 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 495007623 115 ATILAE-SICSGAVIGAGSVVTKPITEKGVYAGNPARLLR 153
Cdd:cd03358   80 ATILPGvTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
30-155 9.00e-32

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 110.35  E-value: 9.00e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  30 LYECELGDGVFIGPFVEIQRYT-RIGRGTRVQSHTFI--CESVTIGEDCFIGHGVMFANDMFRDGKPDPNSDHWVRITIG 106
Cdd:COG0110    6 LFGARIGDGVVIGPGVRIYGGNiTIGDNVYIGPGVTIddPGGITIGDNVLIGPGVTILTGNHPIDDPATFPLRTGPVTIG 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 495007623 107 DNVSIGSGATILAE-SICSGAVIGAGSVVTKPITEKGVYAGNPARLLRRL 155
Cdd:COG0110   86 DDVWIGAGATILPGvTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKR 135
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 45-152 3.15e-23

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: 87.51  E-value: 3.15e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  45 VEIQRYTRIGRGTRVQSHtficESVTIGEDCFIGHGVMFANDMFRDGKPDPNSDHWVR---ITIGDNVSIGSGATILAE- 120
Cdd:cd04647    2 ISIGDNVYIGPGCVISAG----GGITIGDNVLIGPNVTIYDHNHDIDDPERPIEQGVTsapIVIGDDVWIGANVVILPGv 77

                         90       100       110
                 ....*....|....*....|....*....|..
gi 495007623 121 SICSGAVIGAGSVVTKPITEKGVYAGNPARLL 152
Cdd:cd04647   78 TIGDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 32-149 1.33e-20

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: 83.31  E-value: 1.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623   32 ECELGDGVFIGPFVEIQRYTRIGRGTRVQShtficeSVTIGEDCFIGHGVMFAndmfrdgkpdPNSDHWVRITIGDNVSI 111
Cdd:TIGR03570  99 SASIGEGTVIMAGAVINPDVRIGDNVIINT------GAIVEHDCVIGDFVHIA----------PGVTLSGGVVIGEGVFI 162

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 495007623  112 GSGATILAE-SICSGAVIGAGSVVTKPITEKGVYAGNPA 149
Cdd:TIGR03570 163 GAGATIIQGvTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 32-148 2.31e-19

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: 80.22  E-value: 2.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  32 ECELGDGVFIGPFVEIQRYTRIGRGTRVQSHTficesvTIGEDCFIGHGVMFAndmfrdgkpdPNsdhwVRI----TIGD 107
Cdd:cd03360   96 SAVIGEGCVIMAGAVINPDARIGDNVIINTGA------VIGHDCVIGDFVHIA----------PG----VVLsggvTIGE 155

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 495007623 108 NVSIGSGATILAE-SICSGAVIGAGSVVTKPITEKGVYAGNP 148
Cdd:cd03360  156 GAFIGAGATIIQGvTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 35-152 1.31e-18

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: 77.46  E-value: 1.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  35 LGDGVFIGP--FVEiqrYtriGRGTRVQSHTFI--------CESVTIGEDCFIGHGVMFA-----------NDMFRDGKP 93
Cdd:cd03357   45 VGENVYIEPpfHCD---Y---GYNIHIGDNFYAnfnctildVAPVTIGDNVLIGPNVQIYtaghpldpeerNRGLEYAKP 118

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  94 dpnsdhwvrITIGDNVSIGSGATILAE-SICSGAVIGAGSVVTKPITEKGVYAGNPARLL 152
Cdd:cd03357  119 ---------ITIGDNVWIGGGVIILPGvTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 34-155 1.68e-18

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: 80.06  E-value: 1.68e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  34 ELGDGVFIGPFVEIQRYTRIGRGTRVQSHTFICESVTIGEDCFIGHGVM-------------------------FANDmf 88
Cdd:COG1044  110 KIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTiyercvigdrviihsgavigadgfgFAPD-- 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  89 RDGkpdpnsdHWVRI------TIGDNVSIGSGATI---------------------------------------LAES-- 121
Cdd:COG1044  188 EDG-------GWVKIpqlgrvVIGDDVEIGANTTIdrgalgdtvigdgtkidnlvqiahnvrigehtaiaaqvgIAGStk 260

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495007623 122 ------------------ICSGAVIGAGSVVTKPITEKGVYAGNPAR----------LLRRL 155
Cdd:COG1044  261 igdnvviggqvgiaghltIGDGVIIGAQSGVTKSIPEGGVYSGSPAQphrewlrnaaALRRL 322
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 33-155 1.56e-17

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 74.68  E-value: 1.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  33 CELGDGVFIGPFVEIqR----YTRIGRGTRVQS----HTFICESVTIGEDCFIGHGVMfandmfrdgkpdpnsdhwvrI- 103
Cdd:COG0663   29 VTIGEDVSVWPGAVL-RgdvgPIRIGEGSNIQDgvvlHVDPGYPLTIGDDVTIGHGAI--------------------Lh 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 495007623 104 --TIGDNVSIGSGATILAES-ICSGAVIGAGSVVT--KPITEKGVYAGNPARLLRRL 155
Cdd:COG0663   88 gcTIGDNVLIGMGAIVLDGAvIGDGSIVGAGALVTegKVVPPGSLVVGSPAKVVREL 144
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 45-148 1.57e-17

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: 72.86  E-value: 1.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  45 VEIQRYTRIGRGTRVQSHTFIC--ESVTIGEDCFIGHGVMFANDMFRDGKPDPnsdhwvriTIGDNVSIGSGATILAE-S 121
Cdd:cd03354    3 IDIHPGAKIGPGLFIDHGTGIVigETAVIGDNCTIYQGVTLGGKGKGGGKRHP--------TIGDNVVIGAGAKILGNiT 74

                         90       100
                 ....*....|....*....|....*..
gi 495007623 122 ICSGAVIGAGSVVTKPITEKGVYAGNP 148
Cdd:cd03354   75 IGDNVKIGANAVVTKDVPANSTVVGVP 101
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 44-153 3.54e-17

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: 72.96  E-value: 3.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  44 FVEIQRYTRIGRGTRVQSHTFicesVTIGEDCFIGHGV---MFAN------------DMFRDGKPDPNSDHWV---RITI 105
Cdd:cd03349    1 NISVGDYSYGSGPDCDVGGDK----LSIGKFCSIAPGVkigLGGNhptdwvstypfyIFGGEWEDDAKFDDWPskgDVII 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 495007623 106 GDNVSIGSGATILAE-SICSGAVIGAGSVVTKPITEKGVYAGNPARLLR 153
Cdd:cd03349   77 GNDVWIGHGATILPGvTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIR 125
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 32-141 2.99e-16

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: 71.68  E-value: 2.99e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  32 ECELGDGVFIGPFVEIQRyTRIGRGTRVQSHTFICESvTIGEDCFIGHGVMFANdmfRDGKpdpnSDHwvRITIGDNVSI 111
Cdd:cd03353   85 GTVLGEGVHIGNFVEIKK-STIGEGSKANHLSYLGDA-EIGEGVNIGAGTITCN---YDGV----NKH--RTVIGDNVFI 153

                         90       100       110
                 ....*....|....*....|....*....|.
gi 495007623 112 GSGATILAE-SICSGAVIGAGSVVTKPITEK 141
Cdd:cd03353  154 GSNSQLVAPvTIGDGATIAAGSTITKDVPPG 184
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 45-154 3.65e-16

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: 71.27  E-value: 3.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  45 VEIQRYTRIGRGTRVQsHTF---ICESVTIGEDCFIGHGVMFANDMFRDGKPDPnsdhwvriTIGDNVSIGSGATIL-AE 120
Cdd:COG1045   66 IDIHPGATIGRGFFID-HGTgvvIGETAVIGDNVTIYQGVTLGGTGKEKGKRHP--------TIGDNVVIGAGAKILgPI 136

                         90       100       110
                 ....*....|....*....|....*....|....
gi 495007623 121 SICSGAVIGAGSVVTKPITEKGVYAGNPARLLRR 154
Cdd:COG1045  137 TIGDNAKIGANSVVLKDVPPGSTVVGVPARIVKR 170
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 34-155 2.77e-15

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: 68.21  E-value: 2.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  34 ELGDGVFIGPFVEI---QRYTRIGRGTRVQS----HTFICESVTIGEDCFIGHGVMfandmfrdgkpdpnsdhwvrI--- 103
Cdd:cd04645   19 TLGEGSSVWFGAVLrgdVNPIRIGERTNIQDgsvlHVDPGYPTIIGDNVTVGHGAV--------------------Lhgc 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 495007623 104 TIGDNVSIGSGATILAES-ICSGAVIGAGSVVT--KPITEKGVYAGNPARLLRRL 155
Cdd:cd04645   79 TIGDNCLIGMGAIILDGAvIGKGSIVAAGSLVPpgKVIPPGSLVAGSPAKVVREL 133
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 15-154 9.08e-15

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: 68.20  E-value: 9.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  15 DVVVGRDVMIYhpANLY---ECELGDGVFIGPFVEIQRYTRIGRGTRVQSHTFICESVTIGEDCFIGHGVMFANDMFRDG 91
Cdd:cd03352    1 SAKIGENVSIG--PNAVigeGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIGSDGFGFA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  92 kpdPNSDHWVRI------TIGDNVSIGSGATI---------------------------------------LAES----- 121
Cdd:cd03352   79 ---PDGGGWVKIpqlggvIIGDDVEIGANTTIdrgalgdtvigdgtkidnlvqiahnvrigencliaaqvgIAGSttigd 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 495007623 122 ---------------ICSGAVIGAGSVVTKPITEKGVYAGNPARLLRR 154
Cdd:cd03352  156 nviiggqvgiaghltIGDGVVIGAGSGVTSIVPPGEYVSGTPAQPHRE 203
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 32-136 1.08e-14

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 69.86  E-value: 1.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  32 ECELGDGVFIGPFVEIQRYTrIGRGTRVqSH-TFICESvTIGEDCFIGHGVMFANdmfRDGKpdpnsdHWVRITIGDNVS 110
Cdd:PRK14354 334 GSVIGEEVKIGNFVEIKKST-IGEGTKV-SHlTYIGDA-EVGENVNIGCGTITVN---YDGK------NKFKTIIGDNAF 401

                         90       100
                 ....*....|....*....|....*..
gi 495007623 111 IGSGATILAE-SICSGAVIGAGSVVTK 136
Cdd:PRK14354 402 IGCNSNLVAPvTVGDNAYIAAGSTITK 428
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 32-136 1.64e-14

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: 69.28  E-value: 1.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  32 ECELGDGVFIGPFVEIQRyTRIGRGTRVQSHTFICESvTIGEDCFIGHGVMFANdmfRDGKpdpnSDHwvRITIGDNVSI 111
Cdd:COG1207  335 GTVLGEGVKIGNFVEVKN-STIGEGSKVNHLSYIGDA-EIGEGVNIGAGTITCN---YDGV----NKH--RTVIGDGAFI 403

                         90       100
                 ....*....|....*....|....*.
gi 495007623 112 GSGATILAE-SICSGAVIGAGSVVTK 136
Cdd:COG1207  404 GSNTNLVAPvTIGDGATIGAGSTITK 429
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 33-153 2.39e-14

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 68.63  E-value: 2.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  33 CELGDGVFIGPFVEIQRYTRIGRGTRVQSHTFICESVTIGEDCFIG------HGVM-------------------FANDm 87
Cdd:PRK00892 113 AKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHanvtiyHAVRignrviihsgavigsdgfgFAND- 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  88 frDGKpdpnsdhWVRI------TIGDNVSIGSGATI---------------------------------------LAES- 121
Cdd:PRK00892 192 --RGG-------WVKIpqlgrvIIGDDVEIGANTTIdrgalddtvigegvkidnlvqiahnvvigrhtaiaaqvgIAGSt 262

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 495007623 122 -------------------ICSGAVIGAGSVVTKPITEKGVY-AGNPARLLR 153
Cdd:PRK00892 263 kigrycmiggqvgiaghleIGDGVTITAMSGVTKSIPEPGEYsSGIPAQPNK 314
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 34-140 6.45e-12

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 61.97  E-value: 6.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  34 ELGDGVFIGPFVEIQRyTRIGRGTRVQSHTFICESvTIGEDCFIGHGVMFANdmfRDGKpdpNSdhwVRITIGDNVSIGS 113
Cdd:PRK09451 337 ELAEGAHVGNFVEMKK-ARLGKGSKAGHLTYLGDA-EIGDNVNIGAGTITCN---YDGA---NK---FKTIIGDDVFVGS 405

                         90       100
                 ....*....|....*....|....*...
gi 495007623 114 GATILAE-SICSGAVIGAGSVVTKPITE 140
Cdd:PRK09451 406 DTQLVAPvTVGKGATIGAGTTVTRDVAE 433
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 27-152 1.61e-11

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: 57.62  E-value: 1.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  27 PANLyecELGDGVFIGPFVEIqrYTRigrgtrvqshtficESVTIGEDCFIGHGVM-------FANDMFR-DGKPdpnsd 98
Cdd:cd05825    1 PWNL---TIGDNSWIGEGVWI--YNL--------------APVTIGSDACISQGAYlctgshdYRSPAFPlITAP----- 56

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 495007623  99 hwvrITIGDNVSIGSGATIL-AESICSGAVIGAGSVVTKPITEKGVYAGNPARLL 152
Cdd:cd05825   57 ----IVIGDGAWVAAEAFVGpGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
PLN02694 PLN02694
serine O-acetyltransferase
 45-152 1.76e-11

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 60.43  E-value: 1.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  45 VEIQRYTRIGRGTRVQSHTficeSVTIGEDCFIGHGVMFANDMFRDGKPDPNSDHWVRItiGDNVSIGSGATILAE-SIC 123
Cdd:PLN02694 161 VDIHPAAKIGKGILFDHAT----GVVIGETAVIGNNVSILHHVTLGGTGKACGDRHPKI--GDGVLIGAGATILGNvKIG 234

                         90       100
                 ....*....|....*....|....*....
gi 495007623 124 SGAVIGAGSVVTKPITEKGVYAGNPARLL 152
Cdd:PLN02694 235 EGAKIGAGSVVLIDVPPRTTAVGNPARLV 263
PLN02739 PLN02739
serine acetyltransferase
 45-153 2.69e-11

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 60.05  E-value: 2.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  45 VEIQRYTRIGRGTRVQSHT--FICESVTIGEDCFIGHGVMFANDMFRDGKPDPNsdhwvritIGDNVSIGSGATILAE-S 121
Cdd:PLN02739 206 IDIHPAARIGKGILLDHGTgvVIGETAVIGDRVSILHGVTLGGTGKETGDRHPK--------IGDGALLGACVTILGNiS 277

                         90       100       110
                 ....*....|....*....|....*....|..
gi 495007623 122 ICSGAVIGAGSVVTKPITEKGVYAGNPARLLR 153
Cdd:PLN02739 278 IGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIG 309
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 34-153 8.57e-11

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 57.19  E-value: 8.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  34 ELGDGVFIGPFVEIQ--RYTRIGRGTRVQSHTFICESvtigedcfiGHGVMFANDMFRDGK--PDPNSDHWVRITIGDNV 109
Cdd:PRK09677  67 FFGDNVQVNDYVHIAciESITIGRDTLIASKVFITDH---------NHGSFKHSDDFSSPNlpPDMRTLESSAVVIGQRV 137

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 495007623 110 SIGSGATIL-AESICSGAVIGAGSVVTKPITEKGVYAGNPARLLR 153
Cdd:PRK09677 138 WIGENVTILpGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIK 182
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-140 1.44e-10

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 58.24  E-value: 1.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623   3 GNTPKMREARVSDVVVGRDVMIYHPANLYE-CELGDGVFIGPFVEIQRyTRIGRGTRVQSHTFICESvTIGEDCFIGHGV 81
Cdd:PRK14357 294 GNNVKIIRSECEKSVIEDDVSVGPFSRLREgTVLKKSVKIGNFVEIKK-STIGENTKAQHLTYLGDA-TVGKNVNIGAGT 371

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  82 MFANdmfRDGKPDPNSdhwvriTIGDNVSIGSGATILAE-SICSGAVIGAGSVVTKPITE 140
Cdd:PRK14357 372 ITCN---YDGKKKNPT------FIEDGAFIGSNSSLVAPvRIGKGALIGAGSVITEDVPP 422
PLN02357 PLN02357
serine acetyltransferase
 45-152 1.75e-10

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 57.97  E-value: 1.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  45 VEIQRYTRIGRGTRVQSHT--FICESVTIGEDCFIGHGVMFANDMFRDGKPDPNsdhwvritIGDNVSIGSGATILAE-S 121
Cdd:PLN02357 227 VDIHPGAKIGQGILLDHATgvVIGETAVVGNNVSILHNVTLGGTGKQSGDRHPK--------IGDGVLIGAGTCILGNiT 298

                         90       100       110
                 ....*....|....*....|....*....|.
gi 495007623 122 ICSGAVIGAGSVVTKPITEKGVYAGNPARLL 152
Cdd:PLN02357 299 IGEGAKIGAGSVVLKDVPPRTTAVGNPARLI 329
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 34-138 1.80e-10

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 57.95  E-value: 1.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  34 ELGDGVFIGPFVEIQRyTRIGRGTRVQSHTFICESvTIGEDCFIGHGVMFAN-DMFrdgkpdpnsdHWVRITIGDNVSIG 112
Cdd:PRK14353 323 ELGEGAKVGNFVEVKN-AKLGEGAKVNHLTYIGDA-TIGAGANIGAGTITCNyDGF----------NKHRTEIGAGAFIG 390

                         90       100
                 ....*....|....*....|....*..
gi 495007623 113 SGATILAE-SICSGAVIGAGSVVTKPI 138
Cdd:PRK14353 391 SNSALVAPvTIGDGAYIASGSVITEDV 417
PRK10502 PRK10502
putative acyl transferase; Provisional
 36-153 4.28e-10

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 55.34  E-value: 4.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  36 GDGVFIGP--------FVEIQRYTRIGRGTRVQShtfiCESVTIGEDCFIGHGVMFANdmfrdGKPDPNSDHW---VR-I 103
Cdd:PRK10502  55 GKGVVIRPsvritypwKLTIGDYAWIGDDVWLYN----LGEITIGAHCVISQKSYLCT-----GSHDYSDPHFdlnTApI 125

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495007623 104 TIGDNVSIGSGATI-LAESICSGAVIGAGSVVTKPITEKGVYAGNPARLLR 153
Cdd:PRK10502 126 VIGEGCWLAADVFVaPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIR 176
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 12-141 4.83e-10

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 56.66  E-value: 4.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  12 RVSDVVVGRDVMIYHPANLYECELGDGVFIGP------------------FVEIQRyTRIGRGTRVQSHTFICESVtIGE 73
Cdd:PRK14356 301 WLRDAVVSSGATIHSFSHLEGAEVGDGCSVGPyarlrpgavleegarvgnFVEMKK-AVLGKGAKANHLTYLGDAE-IGA 378

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495007623  74 DCFIGHGVMFANdmfRDGKpdpnsdHWVRITIGDNVSIGSGATILAE-SICSGAVIGAGSVVTKPITEK 141
Cdd:PRK14356 379 GANIGAGTITCN---YDGV------NKHRTVIGEGAFIGSNTALVAPvTIGDGALVGAGSVITKDVPDG 438
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 34-136 2.22e-09

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 54.56  E-value: 2.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  34 ELGDGVFIGPFVEIQRYTrIGRGTRVQSHTFICESvTIGEDCFIGHGVMFANdmfRDGKpdpnSDHwvRITIGDNVSIGS 113
Cdd:PRK14352 342 VLGEEGKLGAFVETKNAT-IGRGTKVPHLTYVGDA-DIGEHSNIGASSVFVN---YDGV----NKH--RTTIGSHVRTGS 410

                         90       100
                 ....*....|....*....|....
gi 495007623 114 GATILAE-SICSGAVIGAGSVVTK 136
Cdd:PRK14352 411 DTMFVAPvTVGDGAYTGAGTVIRE 434
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 13-138 3.10e-09

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 54.16  E-value: 3.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  13 VSDVVVGRDVMIYHpANLYECELGDGVFIGP------------------FVEIQRyTRIGRGTRVQSHTFICESvTIGED 74
Cdd:PRK14360 295 IENSQIGENVTVLY-SVVSDSQIGDGVKIGPyahlrpeaqigsncrignFVEIKK-SQLGEGSKVNHLSYIGDA-TLGEQ 371

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495007623  75 CFIGHGVMFANdmfRDGKpdpnSDHwvRITIGDNVSIGSGATILAE-SICSGAVIGAGSVVTKPI 138
Cdd:PRK14360 372 VNIGAGTITAN---YDGV----KKH--RTVIGDRSKTGANSVLVAPiTLGEDVTVAAGSTITKDV 427
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 68-155 7.96e-09

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 52.31  E-value: 7.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  68 SVTIGEDCFI---------GHGVMFANDMFRDGKPDPnsdhwvrITIGDNVSIGSGATI-LAESICSGAVIGAGSVVTKP 137
Cdd:PRK09527  95 TVTIGDNVLIapnvtlsvtGHPVHHELRKNGEMYSFP-------ITIGNNVWIGSHVVInPGVTIGDNSVIGAGSVVTKD 167

                         90
                 ....*....|....*...
gi 495007623 138 ITEKGVYAGNPARLLRRL 155
Cdd:PRK09527 168 IPPNVVAAGVPCRVIREI 185
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 65-155 1.07e-08

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 51.74  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  65 ICEsVTIGEDCFIGHGVMF-----------ANDMFRDGKPdpnsdhwvrITIGDNVSIGSGATI-LAESICSGAVIGAGS 132
Cdd:PRK10092  91 VCP-IRIGDNCMLAPGVHIytathpldpvaRNSGAELGKP---------VTIGNNVWIGGRAVInPGVTIGDNVVVASGA 160

                         90       100
                 ....*....|....*....|...
gi 495007623 133 VVTKPITEKGVYAGNPARLLRRL 155
Cdd:PRK10092 161 VVTKDVPDNVVVGGNPARIIKKL 183
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
34-117 3.72e-08

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 50.87  E-value: 3.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  34 ELGDGVFIGPFVEIQRYTRIGRGTRVQSHTFICESVTIGEDCFIGHGVMFAN---DMFRDGKPdpnsdhwVRITIGDNVS 110
Cdd:PRK05289  16 KIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIGEdpqDLKYKGEP-------TRLVIGDNNT 88


                 ....*..
gi 495007623 111 IGSGATI 117
Cdd:PRK05289  89 IREFVTI 95
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 32-154 3.91e-08

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: 50.51  E-value: 3.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  32 ECELGDGVFIGPFVEIQRYTRIGRG-TRVQSHTFICESVTIGEDCFIGHGVMFANdmfrdgkpdpNSD---HwvrITIGD 107
Cdd:cd03351   77 RLEIGDNNTIREFVTIHRGTAQGGGvTRIGNNNLLMAYVHVAHDCVIGNNVILAN----------NATlagH---VEIGD 143

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 495007623 108 NVSIGSGATILAES-ICSGAVIGAGSVVTKPITEKGVYAGNPARL-------LRR 154
Cdd:cd03351  144 YAIIGGLSAVHQFCrIGRHAMVGGGSGVVQDVPPYVIAAGNRARLrglnlvgLKR 198
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 34-117 4.05e-08

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: 4.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  34 ELGDGVFIGPFVEIQRYTRIGRGTRVQSHTFICESVTIGEDCFIGHGVMFAND----MFRDGKPdpnsdhwvRITIGDNV 109
Cdd:COG1043   15 KLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASIGEEpqdlKYKGEPT--------RLEIGDNN 86


                 ....*...
gi 495007623 110 SIGSGATI 117
Cdd:COG1043   87 TIREFVTI 94
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 32-154 5.02e-08

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: 5.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  32 ECELGDGVFIGPFVEIQRYTRIGRG-TRVQSHTFICESVTIGEDCFIGHGVMFANdmfrdgkpdpNSD---HwvrITIGD 107
Cdd:COG1043   79 RLEIGDNNTIREFVTIHRGTVQGGGvTRIGDDNLLMAYVHVAHDCVVGNNVILAN----------NATlagH---VEVGD 145

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 495007623 108 NVSIGsGATILAE--SICSGAVIGAGSVVTKPITEKGVYAGNPARL-------LRR 154
Cdd:COG1043  146 HAIIG-GLSAVHQfvRIGAHAMVGGGSGVVKDVPPYVLAAGNPARLrglnlvgLKR 200
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 34-117 5.51e-08

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: 50.12  E-value: 5.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  34 ELGDGVFIGPFVEIQRYTRIGRGTRVQSHTFICESVTIGEDCFIGHGVMFAND----MFRDGKpdpnsdhwVRITIGDNV 109
Cdd:cd03351   13 KIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIGEApqdlKYKGEP--------TRLEIGDNN 84


                 ....*...
gi 495007623 110 SIGSGATI 117
Cdd:cd03351   85 TIREFVTI 92
cysE PRK11132
serine acetyltransferase; Provisional
 45-154 2.31e-07

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 48.54  E-value: 2.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  45 VEIQRYTRIGRGTRVQSHTFIcesvTIGEDCFIGHGVMFANDMFRDGKPDPNSDHWVRITIGdnVSIGSGATILAE-SIC 123
Cdd:PRK11132 142 VDIHPAAKIGRGIMLDHATGI----VIGETAVIENDVSILQSVTLGGTGKTSGDRHPKIREG--VMIGAGAKILGNiEVG 215

                         90       100       110
                 ....*....|....*....|....*....|.
gi 495007623 124 SGAVIGAGSVVTKPITEKGVYAGNPARLLRR 154
Cdd:PRK11132 216 RGAKIGAGSVVLQPVPPHTTAAGVPARIVGK 246
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 13-140 1.34e-06

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 46.51  E-value: 1.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  13 VSDVVVGRDVMIYHPANLYECELGDGVFIGPFVEIQRYTRIGRGTRV----------------QSHTFICESVTIGEDCF 76
Cdd:PRK14358 303 VTDSVLHEGAVIKPHSVLEGAEVGAGSDVGPFARLRPGTVLGEGVHIgnfvetknarldagvkAGHLAYLGDVTIGAETN 382

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495007623  77 IGHGVMFANdmfRDGKPDPNSdhwvriTIGDNVSIGSGATILAESIC-SGAVIGAGSVVTKPITE 140
Cdd:PRK14358 383 VGAGTIVAN---FDGVNKHQS------KVGAGVFIGSNTTLIAPRVVgDAAFIAAGSAVHDDVPE 438
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 53-134 1.44e-06

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


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 43.72  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  53 IGRGTRVQSHTFICESVtIGEDCFIGHGVMFANDMfrdgkpdpnsdhwvritIGDNVSIGSGATILAESICSGAVIGAGS 132
Cdd:cd05787    2 IGRGTSIGEGTTIKNSV-IGRNCKIGKNVVIDNSY-----------------IWDDVTIEDGCTIHHSIVADGAVIGKGC 63


                 ..
gi 495007623 133 VV 134
Cdd:cd05787   64 TI 65
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 52-135 1.46e-06

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 43.78  E-value: 1.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  52 RIGRGTRVQSHTFICESVTIGEDCFIGHGVMFANDMFRDGKPDPnsdhwvriTIGDNVSIGSGATILAES-ICSGAVIGA 130
Cdd:cd00208    2 FIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGPNEKNPT--------IIGDNVEIGANAVIHGGVkIGDNAVIGA 73


                 ....*
gi 495007623 131 GSVVT 135
Cdd:cd00208   74 GAVVT 78
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 39-134 2.57e-06

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 45.10  E-value: 2.57e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  39 VFIGPFVEIqrytriGRGTRVQSHTFICESVTIGEDCFIGHGVMFandmfrdgkpdpnsdhwvritigDNVSIGSGATIL 118
Cdd:cd03353   10 TYIDGDVEI------GVDVVIDPGVILEGKTVIGEDCVIGPNCVI-----------------------KDSTIGDGVVIK 60

                         90
                 ....*....|....*.
gi 495007623 119 AESICSGAVIGAGSVV 134
Cdd:cd03353   61 ASSVIEGAVIGNGATV 76
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
32-154 3.18e-06

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 45.09  E-value: 3.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  32 ECELGDGVFIGPFVEIQRYTRIGRG-TRVQSHTFICESVTIGEDCFIGHGVMFANdmfrdgkpdpNSD---HwvrITIGD 107
Cdd:PRK05289  80 RLVIGDNNTIREFVTINRGTVQGGGvTRIGDNNLLMAYVHVAHDCVVGNHVILAN----------NATlagH---VEVGD 146

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 495007623 108 NVSIGSGATILA-ESICSGAVIGAGSVVTKPITEKGVYAGNPARL-------LRR 154
Cdd:PRK05289 147 YAIIGGLTAVHQfVRIGAHAMVGGMSGVSQDVPPYVLAEGNPARLrglnlvgLKR 201
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 26-117 3.54e-06

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


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 44.94  E-value: 3.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623   26 HPANLYE--CELGDGVFIGPFVEIQRYTRIGRGTRVQSHTFICESVTIGEDCFIGHGVMFANdmfrdgkpDPNSDHW--- 100
Cdd:TIGR01852   2 HPTAIIEpgAEIGENVEIGPFCIVGPGVKIGDGVELKSHVVILGHTTIGEGTRIFPGAVIGG--------VPQDLKYkge 73

                          90
                  ....*....|....*...
gi 495007623  101 -VRITIGDNVSIGSGATI 117
Cdd:TIGR01852  74 kTRLIIGDNNTIREFVTI 91
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 34-117 4.18e-06

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 45.01  E-value: 4.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  34 ELGDGVFIGPFVEIQRYTRIGRGTRVQSHTFICESVTIGEDCFIGHGVMFAN---DMFRDGKPDpnsdhwvRITIGDNVS 110
Cdd:PRK12461  13 KLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGDepqDFTYKGEES-------RLEIGDRNV 85


                 ....*..
gi 495007623 111 IGSGATI 117
Cdd:PRK12461  86 IREGVTI 92
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 35-135 5.22e-06

Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix (LbH) domain: Proteins in this family show simlarity to glucose-1-phosphate adenylyltransferases in that they contain N-terminal catalytic domains that resemble a dinucleotide-binding Rossmann fold and C-terminal LbH fold domains. Members in this family are predicted to be glucose-1-phosphate thymidylyltransferases, which are involved in the dTDP-L-rhamnose biosynthetic pathway. Glucose-1-phosphate thymidylyltransferase catalyzes the synthesis of deoxy-thymidine di-phosphate (dTDP)-L-rhamnose, an important component of the cell wall of many microorganisms. The C-terminal LbH domain contains multiple turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 43.73  E-value: 5.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  35 LGDGVFIGPFVEIQRyTRIGRGTRVQSHTFICESVtIGEDCFIGHGVMFANDMFrDGKPDPNSDHWVRIT---------I 105
Cdd:cd05636   56 LGDGCVVGNSVEVKN-SIIMDGTKVPHLNYVGDSV-LGENVNLGAGTITANLRF-DDKPVKVRLKGERVDtgrrklgaiI 132

                         90       100       110
                 ....*....|....*....|....*....|.
gi 495007623 106 GDNVSIGSGATILAES-ICSGAVIGAGSVVT 135
Cdd:cd05636  133 GDGVKTGINVSLNPGVkIGPGSWVYPGCVVR 163
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 13-139 6.70e-06

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 44.53  E-value: 6.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  13 VSDVVVGRDVMIYHPANLY-ECELGDGVFIGPFVEIQRyTRIGRGTRVQSHTFICESvTIGEDCFIGHGVMFANdmfRDG 91
Cdd:PRK14360 311 VSDSQIGDGVKIGPYAHLRpEAQIGSNCRIGNFVEIKK-SQLGEGSKVNHLSYIGDA-TLGEQVNIGAGTITAN---YDG 385

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 495007623  92 KpdpnSDHwvRITIGDNVSIGsgatilaesicsgavigAGSVVTKPIT 139
Cdd:PRK14360 386 V----KKH--RTVIGDRSKTG-----------------ANSVLVAPIT 410
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 11-138 7.29e-06

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 44.35  E-value: 7.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  11 ARVSDVVVGRDVMIYHPANLYECELGDGVFIGP------------------FVEIQRyTRIGRGTRVQSHTFICESvTIG 72
Cdd:PRK14355 299 VVIKGCRIGDDVTVKAGSVLEDSVVGDDVAIGPmahlrpgtelsahvkignFVETKK-IVMGEGSKASHLTYLGDA-TIG 376

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495007623  73 EDCFIGHGVMFANdmfRDGKpdpnsdHWVRITIGDNVSIGSGATILAE-SICSGAVIGAGSVVTKPI 138
Cdd:PRK14355 377 RNVNIGCGTITCN---YDGV------KKHRTVIEDDVFVGSDVQFVAPvTVGRNSLIAAGTTVTKDV 434
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 63-151 1.19e-05

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 43.18  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  63 TFICESVTIGEDCFIGHGVMFANdmfrdgkpdpnsdhwvRITIGDNVSIGSGATILAESICSGAVIGAGSVVTKPITEKG 142
Cdd:cd03353   10 TYIDGDVEIGVDVVIDPGVILEG----------------KTVIGEDCVIGPNCVIKDSTIGDGVVIKASSVIEGAVIGNG 73


                 ....*....
gi 495007623 143 VYAGNPARL 151
Cdd:cd03353   74 ATVGPFAHL 82
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 51-149 1.25e-05

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 43.97  E-value: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623   51 TRIGRGTRVQSHTFICES-VTIGEDCFIGHGVMFANdmfrdgkpdpnsdHWV--------RITIGDNVSIGSGATILAE- 120
Cdd:TIGR02353 113 AKIGKGVDIGSLPPVCTDlLTIGAGTIVRKEVMLLG-------------YRAergrlhtgPVTLGRDAFIGTRSTLDIDt 179

                          90       100       110
                  ....*....|....*....|....*....|.
gi 495007623  121 SICSGAVIGAGSVVT--KPITEKGVYAGNPA 149
Cdd:TIGR02353 180 SIGDGAQLGHGSALQggQSIPDGERWHGSPA 210
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 37-135 1.49e-05

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: 42.37  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  37 DGVFIGP--------FVEIQRYtrIGRGTRVQSHTFICESVTIGEDCFIGHGVMFANDMfrdgkpdpNSDHWVRITIGDN 108
Cdd:cd03350   12 DGAFIGPgavlmmpsYVNIGAY--VDEGTMVDSWATVGSCAQIGKNVHLSAGAVIGGVL--------EPLQATPVIIEDD 81

                         90       100
                 ....*....|....*....|....*...
gi 495007623 109 VSIGSGATILAESIC-SGAVIGAGSVVT 135
Cdd:cd03350   82 VFIGANCEVVEGVIVgKGAVLAAGVVLT 109
PLN02296 PLN02296
carbonate dehydratase
 104-155 2.98e-05

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 42.42  E-value: 2.98e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495007623 104 TIGDNVSIGS-----------------GATILAESIC-SGAVIGAGSVVTK----PITEkgVYAGNPARLLRRL 155
Cdd:PLN02296 121 IIGDNVTIGHsavlhgctvedeafvgmGATLLDGVVVeKHAMVAAGALVRQntriPSGE--VWAGNPAKFLRKL 192
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 52-149 3.16e-05

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 42.82  E-value: 3.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623   52 RIGRGTRVQShTFICES--VTIGEDCFIGHGVMFANDMFRDG--KPDpnsdhwvRITIGDNVSIGSGATILAES-ICSGA 126
Cdd:TIGR02353 599 KIGRGVYIDG-TDLTERdlVTIGDDSTLNEGSVIQTHLFEDRvmKSD-------TVTIGDGATLGPGAIVLYGVvMGEGS 670

                          90       100
                  ....*....|....*....|....*
gi 495007623  127 VIGAGSVVTK--PITEKGVYAGNPA 149
Cdd:TIGR02353 671 VLGPDSLVMKgeEVPAHTRWRGNPA 695
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 64-134 4.75e-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: 41.93  E-value: 4.75e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495007623  64 FICESVTIGEDCFIGHGVmfandmfrdgkpdpnsdhwvriTIGDNVSIGSGATILAesicsGAVIGAGSVV 134
Cdd:COG1044  104 VIDPSAKIGEGVSIGPFA----------------------VIGAGVVIGDGVVIGP-----GVVIGDGVVI 147
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 64-135 5.22e-05

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: 39.53  E-value: 5.22e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495007623  64 FICESVTIGEDCFIGHGVMFANDMFRDGkpdpnsdhwVRIT---IGDNVSIGSGATILAESICSGAVIGAGSVVT 135
Cdd:cd03356    1 LIGESTVIGENAIIKNSVIGDNVRIGDG---------VTITnsiLMDNVTIGANSVIVDSIIGDNAVIGENVRVV 66
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 64-134 8.72e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 41.28  E-value: 8.72e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495007623  64 FICESVTIGEDCFIGHGVmfandmfrdgkpdpnsdhwvriTIGDNVSIGSGATILAesicsGAVIGAGSVV 134
Cdd:PRK00892 108 VIDPSAKIGEGVSIGPNA----------------------VIGAGVVIGDGVVIGA-----GAVIGDGVKI 151
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 37-129 1.02e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 40.97  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  37 DGVFIGPFVEIQRYTRIGRGTRVQSHTFICESVTIG-----EDCFIGHGVMFANDMFRDGKpdpnsdhwvritIGDNVSI 111
Cdd:PRK14354 258 ESTYIDADVEIGSDTVIEPGVVIKGNTVIGEDCVIGpgsriVDSTIGDGVTITNSVIEESK------------VGDNVTV 325

                         90
                 ....*....|....*....
gi 495007623 112 GSGATILAES-ICSGAVIG 129
Cdd:PRK14354 326 GPFAHLRPGSvIGEEVKIG 344
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 35-155 1.37e-04

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: 39.66  E-value: 1.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  35 LGDGVFIGP-------FVEIqrytRIGRGTRVQS----HTFICESVTIGEDCFIGHGVMFandmfrdgkpdpnsdHWVRI 103
Cdd:cd04745   21 IGKNCYIGPhaslrgdFGRI----VIRDGANVQDncviHGFPGQDTVLEENGHIGHGAIL---------------HGCTI 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495007623 104 ----TIGDNVSIGSGATILAESIC-------SGAVIGAGSVVtkpitekgvyAGNPARLLRRL 155
Cdd:cd04745   82 grnaLVGMNAVVMDGAVIGEESIVgamafvkAGTVIPPRSLI----------AGSPAKVIREL 134
PRK10191 PRK10191
putative acyl transferase; Provisional
 46-151 1.44e-04

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 39.87  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  46 EIQRYTRIGRgtRVQSH----TFICESVTIGEDCFIGHGVMFANDmfrdGKPDPNSDHwvritIGDNVSIGSGATILAE- 120
Cdd:PRK10191  43 EIQAAATIGR--RFTIHhgyaVVINKNVVAGDDFTIRHGVTIGNR----GADNMACPH-----IGNGVELGANVIILGDi 111

                         90       100       110
                 ....*....|....*....|....*....|.
gi 495007623 121 SICSGAVIGAGSVVTKPITEKGVYAGNPARL 151
Cdd:PRK10191 112 TIGNNVTVGAGSVVLDSVPDNALVVGEKARV 142
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 41-145 1.50e-04

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 40.74  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  41 IGPFVEIQRYTRigRGTRVQSHTFI--CEsvtIGEDCFIGHGVMFANdmfRDGKpdpnSDHwvRITIGDNVSIGSGATIL 118
Cdd:PRK14359 318 IGNFVETKNAKL--NGVKAGHLSYLgdCE---IDEGTNIGAGTITCN---YDGK----KKH--KTIIGKNVFIGSDTQLV 383

                         90       100
                 ....*....|....*....|....*...
gi 495007623 119 AE-SICSGAVIGAGSVVTKPItEKGVYA 145
Cdd:PRK14359 384 APvNIEDNVLIAAGSTVTKDV-PKGSLA 410
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 35-134 2.57e-04

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


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 39.15  E-value: 2.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  35 LGDGVFIGPFVEIQ----RYTRIGRGTRVQS----HTFICESVTIGEDCFIGHGVMFANDMfrdgkpdpnsdhwvriTIG 106
Cdd:cd00710   23 IGDNVFVGPGASIRadegTPIIIGANVNIQDgvviHALEGYSVWIGKNVSIAHGAIVHGPA----------------YIG 86

                         90       100
                 ....*....|....*....|....*...
gi 495007623 107 DNVSIGSGATILAESICSGAVIGAGSVV 134
Cdd:cd00710   87 DNCFIGFRSVVFNAKVGDNCVIGHNAVV 114
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 32-129 3.02e-04

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 39.91  E-value: 3.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  32 ECELGDGVFIGPFVEIQRYTRIGRGTRVQSHTFIcESVTIGEDCFIGHGVMFandmfrdgkpdpNSdhwvriTIGDNVSI 111
Cdd:PRK14360 262 TVELGPDVIIEPQTHLRGNTVIGSGCRIGPGSLI-ENSQIGENVTVLYSVVS------------DS------QIGDGVKI 322

                         90
                 ....*....|....*....
gi 495007623 112 GSGATILAES-ICSGAVIG 129
Cdd:PRK14360 323 GPYAHLRPEAqIGSNCRIG 341
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 52-155 5.76e-04

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: 37.93  E-value: 5.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  52 RIGRGTRVQSHTFICESVTIGEDCFIGHGVMFA--NDMFRDGKPDP-------NSDHWVRITIGDNVSIGSGATI----- 117
Cdd:cd04650    2 RISPKAYVHPTSYVIGDVVIGELTSVWHYAVIRgdNDSIYIGKYSNvqenvsiHTDHGYPTEIGDYVTIGHNAVVhgakv 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 495007623 118 -------LAESICSGA------VIGAGSVVT--KPITEKGVYAGNPARLLRRL 155
Cdd:cd04650   82 gnyvivgMGAILLNGAkigdhvIIGAGAVVTpgKEIPDYSLVLGVPAKVVRKL 134
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 32-119 7.44e-04

Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix (LbH) domain: Proteins in this family show simlarity to glucose-1-phosphate adenylyltransferases in that they contain N-terminal catalytic domains that resemble a dinucleotide-binding Rossmann fold and C-terminal LbH fold domains. Members in this family are predicted to be glucose-1-phosphate thymidylyltransferases, which are involved in the dTDP-L-rhamnose biosynthetic pathway. Glucose-1-phosphate thymidylyltransferase catalyzes the synthesis of deoxy-thymidine di-phosphate (dTDP)-L-rhamnose, an important component of the cell wall of many microorganisms. The C-terminal LbH domain contains multiple turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 37.95  E-value: 7.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  32 ECELGDGVFIGPFVEIQRYTRIGRGTRVQSHTFICESVTIGEDCFIGHGVMFANDMFRDGKPDPNSDHWVRITIGDNVSI 111
Cdd:cd05636   17 PVWIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSIIMDGTKVPHLNYVGDSVLGENVNL 96


                 ....*...
gi 495007623 112 GSGaTILA 119
Cdd:cd05636   97 GAG-TITA 103
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 53-135 9.03e-04

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


Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 36.40  E-value: 9.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  53 IGRGTRVQSHTFICESVtIGEDCFIGHGVMFANdmfrdgkpdpnsdhwvrITIGDNVSIGSGATILAESICSGAVIGAGS 132
Cdd:cd04652    2 VGENTQVGEKTSIKRSV-IGANCKIGKRVKITN-----------------CVIMDNVTIEDGCTLENCIIGNGAVIGEKC 63


                 ...
gi 495007623 133 VVT 135
Cdd:cd04652   64 KLK 66
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 38-136 3.55e-03

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


Pssm-ID: 441774 [Multi-domain]  Cd Length: 268  Bit Score: 36.25  E-value: 3.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  38 GVFIGP-------FVEIQRYTriGRGTRVQSHTFICESVTIGEDCFIGHGV--MfandmfrdGKPDPNSDhwVRITIGDN 108
Cdd:COG2171  109 GAYLAPgvvlmpsFVNIGAYV--DEGTMVDTWATVGSCAQIGKNVHLSGGAgiG--------GVLEPLQA--APVIIEDN 176

                         90       100       110
                 ....*....|....*....|....*....|
gi 495007623 109 VSIGSGAtILAE--SICSGAVIGAGSVVTK 136
Cdd:COG2171  177 CFIGARS-GVVEgvIVGEGAVLGAGVYLTA 205
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 52-134 6.02e-03

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 36.07  E-value: 6.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495007623  52 RIGRGTRVQSHTFICESVTIGEDCFIGhgvmfandmfrdgkPDpnsdhwvriTIGDNVSIGSGATILaESICSGAVIGAG 131
Cdd:PRK14352 273 TIGRDVVIHPGTQLLGRTTIGEDAVVG--------------PD---------TTLTDVTVGEGASVV-RTHGSESEIGAG 328


                 ...
gi 495007623 132 SVV 134
Cdd:PRK14352 329 ATV 331
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 68-136 9.95e-03

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: 34.50  E-value: 9.95e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495007623  68 SVTIGEDCFIGHGVMF--ANDMFRDGKpdpnsdHWVRITIGDNVSIGSGATILAESICSGAVIGAGSVVTK 136
Cdd:cd03359   42 TVSIGRYCILSEGCVIrpPFKKFSKGV------AFFPLHIGDYVFIGENCVVNAAQIGSYVHIGKNCVIGR 106
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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