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Conserved domains on  [gi|1290347225|gb|PJY73868|]
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putative acetyltransferase [Bacteroides fragilis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 191-365 1.61e-71

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: 225.38  E-value: 1.61e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 191 LDAEVLVMINRTKGYLSVLNDIK-TAENEKKEILSKMLGNIGNHSSVGQNFTCQCGKHIFIGEQTIINKNCTMMDENQIH 269
Cdd:cd03357     5 SDPELVAERARARRLLHEYNQTPpSDAEERRELLKELFGSVGENVYIEPPFHCDYGYNIHIGDNFYANFNCTILDVAPVT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 270 IGDRVLVAPNVQFYTATHPINFDERfvenwneDSGELFfrtkALPITVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTK 349
Cdd:cd03357    85 IGDNVLIGPNVQIYTAGHPLDPEER-------NRGLEY----AKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTK 153

                         170
                  ....*....|....*.
gi 1290347225 350 SIPENCLAAGNPCKVI 365
Cdd:cd03357   154 DIPANVVAAGNPARVI 169
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 401-525 1.61e-18

Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


:

Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 81.55  E-value: 1.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 401 YTQEEVEDWASCgDSVEHLKELL--SHNHFIGAFDEaGRMVGFSSMNKDGYLHSMFVHKDWQGKGVATQLLSEVERIAKQ 478
Cdd:pfam13673   5 YSEEGIETFYEF-ISPEALRERIdqGEYFFFVAFEG-GQIVGVIALRDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEK 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1290347225 479 --LEVAEITSEVSLTARPFFEKKGYEIVKIQKYRANkLELTNfvMRKLL 525
Cdd:pfam13673  83 dgIKLSELTVNASPYAVPFYEKLGFRATGPEQEFNG-IRFVP--MEKEL 128
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 45-156 1.03e-14

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


:

Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 70.24  E-value: 1.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225  45 IETPSKEVINAPELKLYIENFGTKKDDFCLVADCAGKVIGAVWVRIMNDY---GHIDnqtpslSISLYKEYRNKGIGSHL 121
Cdd:pfam00583   7 LLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEppvGEIE------GLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1290347225 122 MNEMLASLKDKGYNRVSLSVQKAN-YAVNMYLKLGF 156
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADNlAAIALYEKLGF 116
 
Name Accession Description Interval E-value
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 191-365 1.61e-71

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: 225.38  E-value: 1.61e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 191 LDAEVLVMINRTKGYLSVLNDIK-TAENEKKEILSKMLGNIGNHSSVGQNFTCQCGKHIFIGEQTIINKNCTMMDENQIH 269
Cdd:cd03357     5 SDPELVAERARARRLLHEYNQTPpSDAEERRELLKELFGSVGENVYIEPPFHCDYGYNIHIGDNFYANFNCTILDVAPVT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 270 IGDRVLVAPNVQFYTATHPINFDERfvenwneDSGELFfrtkALPITVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTK 349
Cdd:cd03357    85 IGDNVLIGPNVQIYTAGHPLDPEER-------NRGLEY----AKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTK 153

                         170
                  ....*....|....*.
gi 1290347225 350 SIPENCLAAGNPCKVI 365
Cdd:cd03357   154 DIPANVVAAGNPARVI 169
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
225-371 9.29e-52

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 172.75  E-value: 9.29e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 225 KMLGNIGNHSSVGQNFTCqCGKHIFIGEQTIINKNCTMMDENQIHIGDRVLVAPNVQFYTATHPINFDERFvenwnedsg 304
Cdd:COG0110     6 LFGARIGDGVVIGPGVRI-YGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPATF--------- 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1290347225 305 elffRTKALPITVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTKSIPENCLAAGNPCKVIRWLSPQ 371
Cdd:COG0110    76 ----PLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEE 138
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 215-368 1.34e-38

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 139.18  E-value: 1.34e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 215 AENEKKEILSKMLGNIGNhSSVGQNFTCQCGKHIFIGEQTIINKNCTMMDENQIHIGDRVLVAPNVQFYTATHPINFDER 294
Cdd:PRK10092   42 EHTLRQQILADLFGQVTE-AYIEPTFRCDYGYNIFLGNNFYANFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPLDPVAR 120

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1290347225 295 fvenwneDSGELFfrtkALPITVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTKSIPENCLAAGNPCKVIRWL 368
Cdd:PRK10092  121 -------NSGAEL----GKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIKKL 183
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 250-361 1.14e-19

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: 87.16  E-value: 1.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 250 IGEQTIINKNCTMmdENQIHIGDRVLVAPNVqfytathpinfderFVenwnedSGElffrtkalpITVEDNAWIGGGSII 329
Cdd:TIGR03570 120 IGDNVIINTGAIV--EHDCVIGDFVHIAPGV--------------TL------SGG---------VVIGEGVFIGAGATI 168

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1290347225 330 LAGVTIGKGSVIGAGSVVTKSIPENCLAAGNP 361
Cdd:TIGR03570 169 IQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVP 200
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 401-525 1.61e-18

Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 81.55  E-value: 1.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 401 YTQEEVEDWASCgDSVEHLKELL--SHNHFIGAFDEaGRMVGFSSMNKDGYLHSMFVHKDWQGKGVATQLLSEVERIAKQ 478
Cdd:pfam13673   5 YSEEGIETFYEF-ISPEALRERIdqGEYFFFVAFEG-GQIVGVIALRDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEK 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1290347225 479 --LEVAEITSEVSLTARPFFEKKGYEIVKIQKYRANkLELTNfvMRKLL 525
Cdd:pfam13673  83 dgIKLSELTVNASPYAVPFYEKLGFRATGPEQEFNG-IRFVP--MEKEL 128
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
376-525 1.75e-18

L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 82.73  E-value: 1.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 376 PLEEKDIPEMQELFRSTVLNVNIR-HYTQEEVEDWAscgdsvEHLKELLSHNHFIGAFDEAGRMVGFSSM----NKDGY- 449
Cdd:COG1247     6 PATPEDAPAIAAIYNEAIAEGTATfETEPPSEEERE------AWFAAILAPGRPVLVAEEDGEVVGFASLgpfrPRPAYr 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 450 ---LHSMFVHKDWQGKGVATQLLSEVERIAKQLEVAEITSEVSLT---ARPFFEKKGYEIVKIQKYRANKLE--LTNFVM 521
Cdd:COG1247    80 gtaEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADneaSIALYEKLGFEEVGTLPEVGFKFGrwLDLVLM 159


                  ....
gi 1290347225 522 RKLL 525
Cdd:COG1247   160 QKRL 163
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 45-156 1.03e-14

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 70.24  E-value: 1.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225  45 IETPSKEVINAPELKLYIENFGTKKDDFCLVADCAGKVIGAVWVRIMNDY---GHIDnqtpslSISLYKEYRNKGIGSHL 121
Cdd:pfam00583   7 LLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEppvGEIE------GLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1290347225 122 MNEMLASLKDKGYNRVSLSVQKAN-YAVNMYLKLGF 156
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADNlAAIALYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
17-159 3.96e-14

L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 70.02  E-value: 3.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225  17 NYKIRPLRQEETFLLREFLYEAIfiPKGIETPSKEVINAPELKLYIENFgTKKDDFCLVADCAGKVIGAVWV---RIMND 93
Cdd:COG1247     1 EMTIRPATPEDAPAIAAIYNEAI--AEGTATFETEPPSEEEREAWFAAI-LAPGRPVLVAEEDGEVVGFASLgpfRPRPA 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1290347225  94 YGHidnqTPSLSISLYKEYRNKGIGSHLMNEMLASLKDKGYNRVSLSVQKANY-AVNMYLKLGFKII 159
Cdd:COG1247    78 YRG----TAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEaSIALYEKLGFEEV 140
PRK09831 PRK09831
GNAT family N-acetyltransferase;
381-523 3.87e-12

GNAT family N-acetyltransferase;


Pssm-ID: 182099  Cd Length: 147  Bit Score: 64.21  E-value: 3.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 381 DIPEMQELFRSTVLNVNIRHYTQEEVEDWASCGDSveHLKELLSHNHFIGAFDEAgRMVGFSSMnKDGYLHSMFVHKDWQ 460
Cdd:PRK09831   10 DFQQLCAIFIRAVTMTASQHYSPQQIAAWAQIDES--RWKEKLAKSQVRVAVINA-QPVGFITC-IEHYIDMLFVDPEYT 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1290347225 461 GKGVATQLLsevERIAKQleVAEITSEVSLTARPFFEKKGYEIVKIQKYRANKLELTNFVMRK 523
Cdd:PRK09831   86 RRGVASALL---KPLIKS--ESELTVDASITAKPFFERYGFQTVKQQRVECRGEWFINFYMRY 143
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 73-140 1.33e-09

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 54.20  E-value: 1.33e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1290347225  73 CLVADCAGKVIGAVWVRI---MNDYGHIDNqtpslsISLYKEYRNKGIGSHLMNEMLASLKDKGYNRVSLS 140
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPdgsGGDTAYIGD------LAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 428-485 3.11e-09

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 53.05  E-value: 3.11e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1290347225 428 FIGAFDEaGRMVGFSSMNKD------GYLHSMFVHKDWQGKGVATQLLSEVERIAKQLEVAEIT 485
Cdd:cd04301     1 FLVAEDD-GEIVGFASLSPDgsggdtAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 61-161 4.63e-09

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 54.64  E-value: 4.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225  61 YIENFGTKKDDFcLVADCAGKVIGAVWVRIMNDYGHIdnqtpsLSISLYKEYRNKGIGSHLMNEMLASLKDKGYNRVSLS 140
Cdd:TIGR01575  22 FAEELANYHLCY-LLARIGGKVVGYAGVQIVLDEAHI------LNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLE 94

                          90       100
                  ....*....|....*....|..
gi 1290347225 141 VQKAN-YAVNMYLKLGFKIIKE 161
Cdd:TIGR01575  95 VRVSNiAAQALYKKLGFNEIAI 116
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
315-349 6.45e-06

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 42.81  E-value: 6.45e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1290347225 315 ITVEDNAWIGGGSIIlaGVTIGKGSVIGAGSVVTK 349
Cdd:pfam14602   1 VIIGDNCLIGANSGI--GVSLGDNCVVGAGVVITA 33
PRK03624 PRK03624
putative acetyltransferase; Provisional
 54-156 3.81e-04

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 40.68  E-value: 3.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225  54 NAPELKlyIENFGTKKDDFCLVADCAGKVIGAVwvriMNDY-GHidnqTPSL-SISLYKEYRNKGIGSHLMNEMLASLKD 131
Cdd:PRK03624   30 NDPEMD--IERKLNHDPSLFLVAEVGGEVVGTV----MGGYdGH----RGWAyYLAVHPDFRGRGIGRALVARLEKKLIA 99

                          90       100
                  ....*....|....*....|....*.
gi 1290347225 132 KGYNRVSLSVQKANYAV-NMYLKLGF 156
Cdd:PRK03624  100 RGCPKINLQVREDNDAVlGFYEALGY 125
 
Name Accession Description Interval E-value
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 191-365 1.61e-71

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: 225.38  E-value: 1.61e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 191 LDAEVLVMINRTKGYLSVLNDIK-TAENEKKEILSKMLGNIGNHSSVGQNFTCQCGKHIFIGEQTIINKNCTMMDENQIH 269
Cdd:cd03357     5 SDPELVAERARARRLLHEYNQTPpSDAEERRELLKELFGSVGENVYIEPPFHCDYGYNIHIGDNFYANFNCTILDVAPVT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 270 IGDRVLVAPNVQFYTATHPINFDERfvenwneDSGELFfrtkALPITVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTK 349
Cdd:cd03357    85 IGDNVLIGPNVQIYTAGHPLDPEER-------NRGLEY----AKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTK 153

                         170
                  ....*....|....*.
gi 1290347225 350 SIPENCLAAGNPCKVI 365
Cdd:cd03357   154 DIPANVVAAGNPARVI 169
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
225-371 9.29e-52

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 172.75  E-value: 9.29e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 225 KMLGNIGNHSSVGQNFTCqCGKHIFIGEQTIINKNCTMMDENQIHIGDRVLVAPNVQFYTATHPINFDERFvenwnedsg 304
Cdd:COG0110     6 LFGARIGDGVVIGPGVRI-YGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPATF--------- 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1290347225 305 elffRTKALPITVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTKSIPENCLAAGNPCKVIRWLSPQ 371
Cdd:COG0110    76 ----PLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEE 138
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 247-365 1.95e-45

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: 154.92  E-value: 1.95e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 247 HIFIGEQTIINKNCTMMDENQIHIGDRVLVAPNVQFYTATHPINFDERFVENWNedsgelffrtKALPITVEDNAWIGGG 326
Cdd:cd04647     1 NISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDHNHDIDDPERPIEQGV----------TSAPIVIGDDVWIGAN 70

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1290347225 327 SIILAGVTIGKGSVIGAGSVVTKSIPENCLAAGNPCKVI 365
Cdd:cd04647    71 VVILPGVTIGDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 215-368 1.34e-38

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 139.18  E-value: 1.34e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 215 AENEKKEILSKMLGNIGNhSSVGQNFTCQCGKHIFIGEQTIINKNCTMMDENQIHIGDRVLVAPNVQFYTATHPINFDER 294
Cdd:PRK10092   42 EHTLRQQILADLFGQVTE-AYIEPTFRCDYGYNIFLGNNFYANFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPLDPVAR 120

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1290347225 295 fvenwneDSGELFfrtkALPITVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTKSIPENCLAAGNPCKVIRWL 368
Cdd:PRK10092  121 -------NSGAEL----GKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIKKL 183
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 214-366 8.57e-37

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 135.13  E-value: 8.57e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 214 TAENEKKEILSKMLGNIGNHSSVGQNFTCQCGKHIFIGEQTIINKNCTMMDENQIHIGDRVLVAPNVQFYTATHPINFDE 293
Cdd:PRK09527   42 SEVEKRESLIKEMFATVGENAWVEPPVYFSYGSNIHIGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGHPVHHEL 121

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1290347225 294 RFvenwnedSGELFfrtkALPITVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTKSIPENCLAAGNPCKVIR 366
Cdd:PRK09527  122 RK-------NGEMY----SFPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIR 183
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 247-367 2.30e-28

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


Pssm-ID: 100040 [Multi-domain]  Cd Length: 145  Bit Score: 109.94  E-value: 2.30e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 247 HIFIGEQTIINKNCTMMDENQIHIGDRVLVAPNVQFYT-ATHPIN-----FDERFVENWNEDSGELFFRTKAlPITVEDN 320
Cdd:cd03349     1 NISVGDYSYGSGPDCDVGGDKLSIGKFCSIAPGVKIGLgGNHPTDwvstyPFYIFGGEWEDDAKFDDWPSKG-DVIIGND 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1290347225 321 AWIGGGSIILAGVTIGKGSVIGAGSVVTKSIPENCLAAGNPCKVIRW 367
Cdd:cd03349    80 VWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRY 126
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 236-366 8.14e-26

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: 101.81  E-value: 8.14e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 236 VGQNftCQCGKHIFIGEQTIINKNCTMMDENQIH----IGDRVLVAPNVQFYTATHPINFDERFVEnwnedsgelffrtk 311
Cdd:cd03358     1 IGDN--CIIGTNVFIENDVKIGDNVKIQSNVSIYegvtIEDDVFIGPNVVFTNDLYPRSKIYRKWE-------------- 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1290347225 312 ALPITVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTKSIPENCLAAGNPCKVIR 366
Cdd:cd03358    65 LKGTTVKRGASIGANATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 230-373 4.60e-21

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: 89.78  E-value: 4.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 230 IGNHSSVGQNftcqC-----GKHIFIGEQTIINKNCTMM--DENQIHIGDRVLVAPNVQFYTAThpinfderfvenwned 302
Cdd:cd04645    20 LGEGSSVWFG----AvlrgdVNPIRIGERTNIQDGSVLHvdPGYPTIIGDNVTVGHGAVLHGCT---------------- 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1290347225 303 sgelffrtkalpitVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVT--KSIPENCLAAGNPCKVIRWLSPQYR 373
Cdd:cd04645    80 --------------IGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPpgKVIPPGSLVAGSPAKVVRELTDEEI 138
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 230-365 1.52e-20

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: 86.51  E-value: 1.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 230 IGNHSSVGQNFTCQCgkhifigeqtiinknctmMDEnqIHIGDRVLVAPNVQFYTATHpinfderfveNWNEDSgelfFR 309
Cdd:cd05825     6 IGDNSWIGEGVWIYN------------------LAP--VTIGSDACISQGAYLCTGSH----------DYRSPA----FP 51

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1290347225 310 TKALPITVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTKSIPENCLAAGNPCKVI 365
Cdd:cd05825    52 LITAPIVIGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 250-361 1.14e-19

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: 87.16  E-value: 1.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 250 IGEQTIINKNCTMmdENQIHIGDRVLVAPNVqfytathpinfderFVenwnedSGElffrtkalpITVEDNAWIGGGSII 329
Cdd:TIGR03570 120 IGDNVIINTGAIV--EHDCVIGDFVHIAPGV--------------TL------SGG---------VVIGEGVFIGAGATI 168

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1290347225 330 LAGVTIGKGSVIGAGSVVTKSIPENCLAAGNP 361
Cdd:TIGR03570 169 IQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVP 200
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 242-366 2.16e-19

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


Pssm-ID: 440667 [Multi-domain]  Cd Length: 174  Bit Score: 85.52  E-value: 2.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 242 CQCGKHIF--------IGEQTIINKNCTMMdenQ--------IHIGDRvlvapnvqfytatHPinfderfvenwnedsge 305
Cdd:COG1045    72 ATIGRGFFidhgtgvvIGETAVIGDNVTIY---QgvtlggtgKEKGKR-------------HP----------------- 118

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1290347225 306 lffrtkalpiTVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTKSIPENCLAAGNPCKVIR 366
Cdd:COG1045   119 ----------TIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVK 169
PRK10502 PRK10502
putative acyl transferase; Provisional
 245-366 1.31e-18

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 83.46  E-value: 1.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 245 GKHIFIGEQTIINkNCTmmdenQIHIGDRVLVAPNVQFYTATHpinfderfveNWNEDSgelfFRTKALPITVEDNAWIG 324
Cdd:PRK10502   75 GDYAWIGDDVWLY-NLG-----EITIGAHCVISQKSYLCTGSH----------DYSDPH----FDLNTAPIVIGEGCWLA 134

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1290347225 325 GGSIILAGVTIGKGSVIGAGSVVTKSIPENCLAAGNPCKVIR 366
Cdd:PRK10502  135 ADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIR 176
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 230-403 1.32e-18

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 83.15  E-value: 1.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 230 IGNHSSVGqnFTCQC---GKHIFIGEQTIINKNCTM-MDENQ-IHIGDRVLVAPNVQFYTAThpinfderfvenwnedsg 304
Cdd:COG0663    31 IGEDVSVW--PGAVLrgdVGPIRIGEGSNIQDGVVLhVDPGYpLTIGDDVTIGHGAILHGCT------------------ 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 305 elffrtkalpitVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVT--KSIPENCLAAGNPCKVIRwlspqyrllPLEEKDI 382
Cdd:COG0663    91 ------------IGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTegKVVPPGSLVVGSPAKVVR---------ELTEEEI 149

                         170       180
                  ....*....|....*....|.
gi 1290347225 383 PEMQElfrstvlnvNIRHYTQ 403
Cdd:COG0663   150 AFLRE---------SAENYVE 161
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 401-525 1.61e-18

Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 81.55  E-value: 1.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 401 YTQEEVEDWASCgDSVEHLKELL--SHNHFIGAFDEaGRMVGFSSMNKDGYLHSMFVHKDWQGKGVATQLLSEVERIAKQ 478
Cdd:pfam13673   5 YSEEGIETFYEF-ISPEALRERIdqGEYFFFVAFEG-GQIVGVIALRDRGHISLLFVDPDYQGQGIGKALLEAVEDYAEK 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1290347225 479 --LEVAEITSEVSLTARPFFEKKGYEIVKIQKYRANkLELTNfvMRKLL 525
Cdd:pfam13673  83 dgIKLSELTVNASPYAVPFYEKLGFRATGPEQEFNG-IRFVP--MEKEL 128
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 242-361 1.73e-18

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: 80.56  E-value: 1.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 242 CQCGKHIFIGEQT--IINKNCtmmdenqiHIGDRVLVAPNVQFytathpinfderfvenwnedsGELFFRTKALPITVED 319
Cdd:cd03354     9 AKIGPGLFIDHGTgiVIGETA--------VIGDNCTIYQGVTL---------------------GGKGKGGGKRHPTIGD 59

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1290347225 320 NAWIGGGSIILAGVTIGKGSVIGAGSVVTKSIPENCLAAGNP 361
Cdd:cd03354    60 NVVIGAGAKILGNITIGDNVKIGANAVVTKDVPANSTVVGVP 101
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
376-525 1.75e-18

L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 82.73  E-value: 1.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 376 PLEEKDIPEMQELFRSTVLNVNIR-HYTQEEVEDWAscgdsvEHLKELLSHNHFIGAFDEAGRMVGFSSM----NKDGY- 449
Cdd:COG1247     6 PATPEDAPAIAAIYNEAIAEGTATfETEPPSEEERE------AWFAAILAPGRPVLVAEEDGEVVGFASLgpfrPRPAYr 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 450 ---LHSMFVHKDWQGKGVATQLLSEVERIAKQLEVAEITSEVSLT---ARPFFEKKGYEIVKIQKYRANKLE--LTNFVM 521
Cdd:COG1247    80 gtaEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADneaSIALYEKLGFEEVGTLPEVGFKFGrwLDLVLM 159


                  ....
gi 1290347225 522 RKLL 525
Cdd:COG1247   160 QKRL 163
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 217-361 6.05e-18

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: 82.15  E-value: 6.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 217 NEKKEILSKMLGNIGN------HSSVGQNFTCQCGKHIFIGEQTIIN------KNCTMMDENQI----HIGDRVLVAPNV 280
Cdd:cd03360    66 NKLRRKLAEKLLAAGYrfatliHPSAVVSPSAVIGEGCVIMAGAVINpdarigDNVIINTGAVIghdcVIGDFVHIAPGV 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 281 QFytathpinfderfvenwnedSGElffrtkalpITVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTKSIPENCLAAGN 360
Cdd:cd03360   146 VL--------------------SGG---------VTIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGN 196


                  .
gi 1290347225 361 P 361
Cdd:cd03360   197 P 197
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 376-525 1.24e-17

N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440859 [Multi-domain]  Cd Length: 132  Bit Score: 79.27  E-value: 1.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 376 PLEEKDIPEMQELFRSTVLNVNIRHYTqeevedwascgdsvehlkellshnhfigAFDEAGRMVGFSSM----NKDGYLH 451
Cdd:COG1246     5 PATPDDVPAILELIRPYALEEEIGEFW----------------------------VAEEDGEIVGCAALhpldEDLAELR 56

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1290347225 452 SMFVHKDWQGKGVATQLLSEVERIAKQLEVAEITSEVSLTARPFFEKKGYEIVKIQKYRANKLELTNFV-MRKLL 525
Cdd:COG1246    57 SLAVHPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTSAAIHFYEKLGFEEIDKEDLPYAKVWQRDSVvMEKDL 131
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 233-366 1.42e-16

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 77.99  E-value: 1.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 233 HSSVGQNFTCQCG--------KHIFIGEQTIINKNCTMMDENQIHIGDRVLVAPNVQFYTATHPinfdeRFVENWNEDSG 304
Cdd:PRK09677   43 SINFGEGFTSGVGlrldafgrGKLFFGDNVQVNDYVHIACIESITIGRDTLIASKVFITDHNHG-----SFKHSDDFSSP 117

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1290347225 305 EL--FFRT-KALPITVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTKSIPENCLAAGNPCKVIR 366
Cdd:PRK09677  118 NLppDMRTlESSAVVIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIK 182
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 45-156 1.03e-14

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 70.24  E-value: 1.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225  45 IETPSKEVINAPELKLYIENFGTKKDDFCLVADCAGKVIGAVWVRIMNDY---GHIDnqtpslSISLYKEYRNKGIGSHL 121
Cdd:pfam00583   7 LLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEEDGELVGFASLSIIDDEppvGEIE------GLAVAPEYRGKGIGTAL 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1290347225 122 MNEMLASLKDKGYNRVSLSVQKAN-YAVNMYLKLGF 156
Cdd:pfam00583  81 LQALLEWARERGCERIFLEVAADNlAAIALYEKLGF 116
MnaT COG1247
L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];
17-159 3.96e-14

L-amino acid N-acyltransferase MnaT [Amino acid transport and metabolism];


Pssm-ID: 440860 [Multi-domain]  Cd Length: 163  Bit Score: 70.02  E-value: 3.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225  17 NYKIRPLRQEETFLLREFLYEAIfiPKGIETPSKEVINAPELKLYIENFgTKKDDFCLVADCAGKVIGAVWV---RIMND 93
Cdd:COG1247     1 EMTIRPATPEDAPAIAAIYNEAI--AEGTATFETEPPSEEEREAWFAAI-LAPGRPVLVAEEDGEVVGFASLgpfRPRPA 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1290347225  94 YGHidnqTPSLSISLYKEYRNKGIGSHLMNEMLASLKDKGYNRVSLSVQKANY-AVNMYLKLGFKII 159
Cdd:COG1247    78 YRG----TAEESIYVDPDARGRGIGRALLEALIERARARGYRRLVAVVLADNEaSIALYEKLGFEEV 140
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 85-173 9.67e-14

Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 66.99  E-value: 9.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225  85 AVWVRIMNDYGHIDNqtpslsISLYKEYRNKGIGSHLMNEMLASLKDKGYNRVSLSVQKANY-AVNMYLKLGFKIIKETL 163
Cdd:COG0456     4 LLGLVDGGDEAEIED------LAVDPEYRGRGIGRALLEAALERARERGARRLRLEVREDNEaAIALYEKLGFEEVGERP 77

                          90
                  ....*....|....*
gi 1290347225 164 E-----EFLMVNELN 173
Cdd:COG0456    78 NyygddALVMEKELA 92
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
376-525 1.21e-13

Predicted N-acetyltransferase YhbS [General function prediction only];


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 68.19  E-value: 1.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 376 PLEEKDIPEMQELFRSTvlnvnirhYTQEEVEDwascgdSVEHLKELLSHNHFIGAFDEaGRMVGFSSMNKD-------- 447
Cdd:COG3153     3 PATPEDAEAIAALLRAA--------FGPGREAE------LVDRLREDPAAGLSLVAEDD-GEIVGHVALSPVdidgegpa 67

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1290347225 448 GYLHSMFVHKDWQGKGVATQLLSEVERIAKQLEVAEITSEVSLTARPFFEKKGYEIVKIQKYRANKLEltnFVMRKLL 525
Cdd:COG3153    68 LLLGPLAVDPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLPFYERFGFRPAGELGLTLGPDE---VFLAKEL 142
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 57-159 2.03e-13

N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only];


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 67.39  E-value: 2.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225  57 ELKLYIENF-GTKKDDFCLVADCAGKVIGAVWVRIMND-YGHIDNqtpslsisLY--KEYRNKGIGSHLMNEMLASLKDK 132
Cdd:COG0454    19 ALDAELKAMeGSLAGAEFIAVDDKGEPIGFAGLRRLDDkVLELKR--------LYvlPEYRGKGIGKALLEALLEWARER 90

                          90       100
                  ....*....|....*....|....*...
gi 1290347225 133 GYNRVSLSVQKANY-AVNMYLKLGFKII 159
Cdd:COG0454    91 GCTALELDTLDGNPaAIRFYERLGFKEI 118
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 248-348 3.29e-13

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: 64.96  E-value: 3.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 248 IFIGEQTIINKNCTMMDEnqIHIGDRVLVAPNVQFYTATHPinfderfvenwnedsgelffrTKALPITVEDNAWIGGGS 327
Cdd:cd00208     1 VFIGEGVKIHPKAVIRGP--VVIGDNVNIGPGAVIGAATGP---------------------NEKNPTIIGDNVEIGANA 57

                          90       100
                  ....*....|....*....|.
gi 1290347225 328 IILAGVTIGKGSVIGAGSVVT 348
Cdd:cd00208    58 VIHGGVKIGDNAVIGAGAVVT 78
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 424-503 3.48e-13

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 65.17  E-value: 3.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 424 SHNHFIGAFDEaGRMVGFSSMNKDGY-----LHSMFVHKDWQGKGVATQLLSEVERIAKQLEVAEITSEVSLTARPFFEK 498
Cdd:pfam13508   1 PGGRFFVAEDD-GKIVGFAALLPLDDegalaELRLAVHPEYRGQGIGRALLEAAEAAAKEGGIKLLELETTNRAAAFYEK 79


                  ....*
gi 1290347225 499 KGYEI 503
Cdd:pfam13508  80 LGFEE 84
Acetyltransf_7 pfam13508
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 69-158 4.19e-13

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 463905 [Multi-domain]  Cd Length: 84  Bit Score: 64.78  E-value: 4.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225  69 KDDFCLVADCAGKVIGAVWVRIMNDYGHIdnqtpsLSISLY--KEYRNKGIGSHLMNEMLASLKDKGYNRVSLSVQkaNY 146
Cdd:pfam13508   1 PGGRFFVAEDDGKIVGFAALLPLDDEGAL------AELRLAvhPEYRGQGIGRALLEAAEAAAKEGGIKLLELETT--NR 72

                          90
                  ....*....|..
gi 1290347225 147 AVNMYLKLGFKI 158
Cdd:pfam13508  73 AAAFYEKLGFEE 84
RimI COG0456
Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal ...
 438-525 7.26e-13

Ribosomal protein S18 acetylase RimI and related acetyltransferases [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440224 [Multi-domain]  Cd Length: 92  Bit Score: 64.29  E-value: 7.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 438 MVGFSSMNKDGYLHSMFVHKDWQGKGVATQLLSEVERIAKQLEVAEITSEV---SLTARPFFEKKGYEIVKIqkyRANKL 514
Cdd:COG0456     4 LLGLVDGGDEAEIEDLAVDPEYRGRGIGRALLEAALERARERGARRLRLEVredNEAAIALYEKLGFEEVGE---RPNYY 80

                          90
                  ....*....|.
gi 1290347225 515 ELTNFVMRKLL 525
Cdd:COG0456    81 GDDALVMEKEL 91
PRK09831 PRK09831
GNAT family N-acetyltransferase;
381-523 3.87e-12

GNAT family N-acetyltransferase;


Pssm-ID: 182099  Cd Length: 147  Bit Score: 64.21  E-value: 3.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 381 DIPEMQELFRSTVLNVNIRHYTQEEVEDWASCGDSveHLKELLSHNHFIGAFDEAgRMVGFSSMnKDGYLHSMFVHKDWQ 460
Cdd:PRK09831   10 DFQQLCAIFIRAVTMTASQHYSPQQIAAWAQIDES--RWKEKLAKSQVRVAVINA-QPVGFITC-IEHYIDMLFVDPEYT 85

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1290347225 461 GKGVATQLLsevERIAKQleVAEITSEVSLTARPFFEKKGYEIVKIQKYRANKLELTNFVMRK 523
Cdd:PRK09831   86 RRGVASALL---KPLIKS--ESELTVDASITAKPFFERYGFQTVKQQRVECRGEWFINFYMRY 143
yhbS COG3153
Predicted N-acetyltransferase YhbS [General function prediction only];
20-172 6.75e-12

Predicted N-acetyltransferase YhbS [General function prediction only];


Pssm-ID: 442387 [Multi-domain]  Cd Length: 142  Bit Score: 63.18  E-value: 6.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225  20 IRPLRQEETFLLREFLYEAiFIPKGIETPSKEVINAPElklyienfgtkkDDFCLVADCAGKVIGAVWVRIMndygHIDN 99
Cdd:COG3153     1 IRPATPEDAEAIAALLRAA-FGPGREAELVDRLREDPA------------AGLSLVAEDDGEIVGHVALSPV----DIDG 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 100 QTPSLSIS-LY--KEYRNKGIGSHLMNEMLASLKDKGYNRVSLSVQKANYAvnMYLKLGFKIIKETL-----EEFLMVNE 171
Cdd:COG3153    64 EGPALLLGpLAvdPEYRGQGIGRALMRAALEAARERGARAVVLLGDPSLLP--FYERFGFRPAGELGltlgpDEVFLAKE 141


                  .
gi 1290347225 172 L 172
Cdd:COG3153   142 L 142
PhnO COG0454
N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, ...
 427-504 8.43e-12

N-acetyltransferase, GNAT superfamily (includes histone acetyltransferase HPA2) [Transcription, General function prediction only];


Pssm-ID: 440222 [Multi-domain]  Cd Length: 136  Bit Score: 62.76  E-value: 8.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 427 HFIGAfDEAGRMVGFSSMN----KDGYLHSMFVHKDWQGKGVATQLLSEVERIAKQLEVAEITSEVSL---TARPFFEKK 499
Cdd:COG0454    35 EFIAV-DDKGEPIGFAGLRrlddKVLELKRLYVLPEYRGKGIGKALLEALLEWARERGCTALELDTLDgnpAAIRFYERL 113


                  ....*
gi 1290347225 500 GYEIV 504
Cdd:COG0454   114 GFKEI 118
ArgA COG1246
N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and ...
 69-162 1.32e-11

N-acetylglutamate synthase or related acetyltransferase, GNAT family [Amino acid transport and metabolism]; N-acetylglutamate synthase or related acetyltransferase, GNAT family is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 440859 [Multi-domain]  Cd Length: 132  Bit Score: 61.93  E-value: 1.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225  69 KDDFCLVADCAGKVIGAVWVRIM-NDYGHIDnqtpslsiSLY--KEYRNKGIGSHLMNEMLASLKDKGYNRVSLSVQKAn 145
Cdd:COG1246    26 EIGEFWVAEEDGEIVGCAALHPLdEDLAELR--------SLAvhPDYRGRGIGRRLLEALLAEARELGLKRLFLLTTSA- 96

                          90
                  ....*....|....*..
gi 1290347225 146 yAVNMYLKLGFKIIKET 162
Cdd:COG1246    97 -AIHFYEKLGFEEIDKE 112
Acetyltransf_1 pfam00583
Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase ...
 399-501 1.66e-11

Acetyltransferase (GNAT) family; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 395465 [Multi-domain]  Cd Length: 116  Bit Score: 61.38  E-value: 1.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 399 RHYTQEEVEDWASCGDSVEHLKELLSHNHFIGAFDEaGRMVGFSSMNKD------GYLHSMFVHKDWQGKGVATQLLSEV 472
Cdd:pfam00583   6 ELLSEEFPEPWPDEPLDLLEDWDEDASEGFFVAEED-GELVGFASLSIIddeppvGEIEGLAVAPEYRGKGIGTALLQAL 84

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1290347225 473 ERIAKQLEVAEITSEVSLT---ARPFFEKKGY 501
Cdd:pfam00583  85 LEWARERGCERIFLEVAADnlaAIALYEKLGF 116
Acetyltransf_10 pfam13673
Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase ...
 42-165 2.03e-11

Acetyltransferase (GNAT) domain; This family contains proteins with N-acetyltransferase functions such as Elp3-related proteins.


Pssm-ID: 463953 [Multi-domain]  Cd Length: 128  Bit Score: 61.52  E-value: 2.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225  42 PKGIETPsKEVINAPELKLYIenfgTKKDDFCLVADCAGKVIGAVWVRimnDYGHIDNqtpslsisLY--KEYRNKGIGS 119
Cdd:pfam13673   7 EEGIETF-YEFISPEALRERI----DQGEYFFFVAFEGGQIVGVIALR---DRGHISL--------LFvdPDYQGQGIGK 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1290347225 120 HLMNEMLASLKDKGYNRVSLSVQKANYAVNMYLKLGFKIIKETLEE 165
Cdd:pfam13673  71 ALLEAVEDYAEKDGIKLSELTVNASPYAVPFYEKLGFRATGPEQEF 116
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 308-357 4.67e-11

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 62.05  E-value: 4.67e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1290347225 308 FRTkalpiTVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTKSIPENCLA 357
Cdd:cd03353   143 HRT-----VIGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGALA 187
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
110-173 8.45e-11

Predicted N-acyltransferase, GNAT family [General function prediction only];


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 59.81  E-value: 8.45e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1290347225 110 KEYRNKGIGSHLMNEMLASLKDKGYNRVSLSVQKanYAVNMYLKLGFKIIKETLEE-----FLMVNELN 173
Cdd:COG2153    68 PEYRGQGLGRALMEAAIEEARERGARRIVLSAQA--HAVGFYEKLGFVPVGEEFLEagiphIDMRKPLS 134
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 312-352 4.37e-10

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: 57.78  E-value: 4.37e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1290347225 312 ALPITVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTKSIP 352
Cdd:cd03350    73 ATPVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTQSTP 113
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 308-357 4.57e-10

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: 61.58  E-value: 4.57e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1290347225 308 FRTkalpiTVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTKSIPENCLA 357
Cdd:COG1207   393 HRT-----VIGDGAFIGSNTNLVAPVTIGDGATIGAGSTITKDVPAGALA 437
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 73-140 1.33e-09

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 54.20  E-value: 1.33e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1290347225  73 CLVADCAGKVIGAVWVRI---MNDYGHIDNqtpslsISLYKEYRNKGIGSHLMNEMLASLKDKGYNRVSLS 140
Cdd:cd04301     1 FLVAEDDGEIVGFASLSPdgsGGDTAYIGD------LAVLPEYRGKGIGSALLEAAEEEARERGAKRLRLE 65
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 428-485 3.11e-09

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 53.05  E-value: 3.11e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1290347225 428 FIGAFDEaGRMVGFSSMNKD------GYLHSMFVHKDWQGKGVATQLLSEVERIAKQLEVAEIT 485
Cdd:cd04301     1 FLVAEDD-GEIVGFASLSPDgsggdtAYIGDLAVLPEYRGKGIGSALLEAAEEEARERGAKRLR 63
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 312-352 3.12e-09

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: 57.82  E-value: 3.12e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1290347225 312 ALPITVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTKSIP 352
Cdd:COG2171   168 AAPVIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLTASTK 208
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 251-364 3.78e-09

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 57.34  E-value: 3.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 251 GEQTIINKNCTMMDENQI----HIGDRVLVAPNVQFytATHpinfderfvenwnedsgelffrtkalpITVEDNAWIGGG 326
Cdd:COG1043   102 GGVTRIGDDNLLMAYVHVahdcVVGNNVILANNATL--AGH---------------------------VEVGDHAIIGGL 152

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1290347225 327 SIILAGVTIGKGSVIGAGSVVTKSIPENCLAAGNPCKV 364
Cdd:COG1043   153 SAVHQFVRIGAHAMVGGGSGVVKDVPPYVLAAGNPARL 190
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 248-369 3.96e-09

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: 55.65  E-value: 3.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 248 IFIGEQTIINKNCTMMDEN--QIHIGDRVLVAPNVQFYTAThpinfderfvenwnedsgelffrtkalpitVEDNAWIGG 325
Cdd:cd04650    40 IYIGKYSNVQENVSIHTDHgyPTEIGDYVTIGHNAVVHGAK------------------------------VGNYVIVGM 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1290347225 326 GSIILAGVTIGKGSVIGAGSVVT--KSIPENCLAAGNPCKVIRWLS 369
Cdd:cd04650    90 GAILLNGAKIGDHVIIGAGAVVTpgKEIPDYSLVLGVPAKVVRKLT 135
rimI TIGR01575
ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related ...
 61-161 4.63e-09

ribosomal-protein-alanine acetyltransferase; Members of this model belong to the GCN5-related N-acetyltransferase (GNAT) superfamily. This model covers prokarotes and the archaea. The seed contains a characterized accession for Gram negative E. coli. An untraceable characterized accession (PIR|S66013) for Gram positive B. subtilis scores well (205.0) in the full alignment. Characterized members are lacking in the archaea. Noise cutoff (72.4) was set to exclude M. loti paralog of rimI. Trusted cutoff (80.0) was set at next highest scoring member in the mini-database. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273701 [Multi-domain]  Cd Length: 131  Bit Score: 54.64  E-value: 4.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225  61 YIENFGTKKDDFcLVADCAGKVIGAVWVRIMNDYGHIdnqtpsLSISLYKEYRNKGIGSHLMNEMLASLKDKGYNRVSLS 140
Cdd:TIGR01575  22 FAEELANYHLCY-LLARIGGKVVGYAGVQIVLDEAHI------LNIAVKPEYQGQGIGRALLRELIDEAKGRGVNEIFLE 94

                          90       100
                  ....*....|....*....|..
gi 1290347225 141 VQKAN-YAVNMYLKLGFKIIKE 161
Cdd:TIGR01575  95 VRVSNiAAQALYKKLGFNEIAI 116
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 312-352 5.59e-09

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


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 57.12  E-value: 5.59e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1290347225 312 ALPITVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTKSIP 352
Cdd:PRK11830  174 ANPVIIEDNCFIGARSEVVEGVIVEEGSVLGMGVFLGQSTK 214
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 316-368 7.98e-09

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: 55.88  E-value: 7.98e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1290347225 316 TVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTKSIPENCLAAGNPCKVIR-WL 368
Cdd:cd03352   152 TIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQPHReWL 205
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
83-161 3.02e-08

Predicted acetyltransferase, GNAT family [General function prediction only];


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 51.06  E-value: 3.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225  83 IGAVWVRimndyghidnqtpslsislyKEYRNKGIGSHLMNEMLASLKDKGYNRVSLSVQKANY-AVNMYLKLGFKIIKE 161
Cdd:COG3393    18 ISGVYTH--------------------PEYRGRGLASALVAALAREALARGARTPFLYVDADNPaARRLYERLGFRPVGE 77
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 314-366 3.13e-08

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 55.92  E-value: 3.13e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1290347225 314 PITVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTKSIPENCLAAGNPCKVIR 366
Cdd:PRK14357  383 PTFIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQIVK 435
PLN02296 PLN02296
carbonate dehydratase
 316-369 4.58e-08

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 54.36  E-value: 4.58e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1290347225 316 TVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTKS--IPENCLAAGNPCKVIRWLS 369
Cdd:PLN02296  138 TVEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNtrIPSGEVWAGNPAKFLRKLT 193
ElaA COG2153
Predicted N-acyltransferase, GNAT family [General function prediction only];
453-504 4.78e-08

Predicted N-acyltransferase, GNAT family [General function prediction only];


Pssm-ID: 441756 [Multi-domain]  Cd Length: 134  Bit Score: 51.72  E-value: 4.78e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1290347225 453 MFVHKDWQGKGVATQLLSEVERIAKQLEVAEITSEVSLTARPFFEKKGYEIV 504
Cdd:COG2153    64 VAVLPEYRGQGLGRALMEAAIEEARERGARRIVLSAQAHAVGFYEKLGFVPV 115
PLN02357 PLN02357
serine acetyltransferase
 319-365 6.83e-08

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 54.50  E-value: 6.83e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1290347225 319 DNAWIGGGSIILAGVTIGKGSVIGAGSVVTKSIPENCLAAGNPCKVI 365
Cdd:PLN02357  283 DGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLI 329
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 251-364 7.23e-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: 53.59  E-value: 7.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 251 GEQTIINKNCTMMDENQI----HIGDRVLVAPNVQFytATHpinfderfvenwnedsgelffrtkalpITVEDNAWIGGG 326
Cdd:cd03351   100 GGVTRIGNNNLLMAYVHVahdcVIGNNVILANNATL--AGH---------------------------VEIGDYAIIGGL 150

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1290347225 327 SIILAGVTIGKGSVIGAGSVVTKSIPENCLAAGNPCKV 364
Cdd:cd03351   151 SAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARL 188
PRK07757 PRK07757
N-acetyltransferase;
380-505 8.93e-08

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 51.35  E-value: 8.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 380 KDIPEMQELfrstvlnvnIRHYTQEEVEDWASCGDSVEHLKEllshnhFIGAFDEaGRMVGFSSmnkdgyLH-------- 451
Cdd:PRK07757   10 SDVKAIHAL---------INVYAKKGLMLPRSLDELYENIRD------FYVAEEE-GEIVGCCA------LHilwedlae 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1290347225 452 --SMFVHKDWQGKGVATQLLSEVERIAKQLEVAEItseVSLTARP-FFEKKGYEIVK 505
Cdd:PRK07757   68 irSLAVSEDYRGQGIGRMLVEACLEEARELGVKRV---FALTYQPeFFEKLGFREVD 121
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 316-357 1.01e-07

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 54.45  E-value: 1.01e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1290347225 316 TVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTKSIPENCLA 357
Cdd:PRK14354  395 IIGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDALA 436
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 316-366 1.21e-07

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 54.10  E-value: 1.21e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1290347225 316 TVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTKSIPENCLAAGNPCKVIR 366
Cdd:PRK14353  382 EIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALGRARQETK 432
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 316-371 1.27e-07

paaY-like: This group is composed by uncharacterized proteins with similarity to the protein product of the E. coli paaY gene, which is part of the paa gene cluster responsible for phenylacetic acid degradation. Proteins in this group are expected to adopt the left-handed parallel beta-helix (LbH) structure. They contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Similarity to gamma carbonic anhydrase and Ferripyochelin Binding Protein (FBP) may suggest metal binding capacity.


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 51.21  E-value: 1.27e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1290347225 316 TVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTKS--IPENCLAAGNPCKVIRWLSPQ 371
Cdd:cd04745    80 TIGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAGtvIPPRSLIAGSPAKVIRELSDE 137
cysE PRK11132
serine acetyltransferase; Provisional
 323-365 2.19e-07

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 52.39  E-value: 2.19e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1290347225 323 IGGGSIILAGVTIGKGSVIGAGSVVTKSIPENCLAAGNPCKVI 365
Cdd:PRK11132  202 IGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIV 244
PLN02739 PLN02739
serine acetyltransferase
 317-390 2.47e-07

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 52.73  E-value: 2.47e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1290347225 317 VEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTKSIPENCLAAGNPCKVIRWLSPQYRLLPLEEKdipEMQELFR 390
Cdd:PLN02739  260 IGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFVDEQDPSLTMEYD---ATREFFQ 330
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 319-357 3.02e-07

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 52.80  E-value: 3.02e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1290347225 319 DNAWIGGGSIILAGVTIGKGSVIGAGSVVTKSIPENCLA 357
Cdd:PRK14356  403 EGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSLA 441
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
251-364 4.33e-07

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 51.25  E-value: 4.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 251 GEQTIINKNCTMMDENQI----HIGDRVLVAPNVQFytATHpinfderfvenwnedsgelffrtkalpITVEDNAWIGGG 326
Cdd:PRK05289  103 GGVTRIGDNNLLMAYVHVahdcVVGNHVILANNATL--AGH---------------------------VEVGDYAIIGGL 153

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1290347225 327 SIILAGVTIGKGSVIGAGSVVTKSIPENCLAAGNPCKV 364
Cdd:PRK05289  154 TAVHQFVRIGAHAMVGGMSGVSQDVPPYVLAEGNPARL 191
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 20-170 5.56e-07

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 49.61  E-value: 5.56e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225  20 IRPLRQEETFLLREFLYE---AIFIPKGIETPSkevinapELKLYIENFGTKKDD-----FCLVADCAGKVIGAVWVRIM 91
Cdd:COG1670    10 LRPLRPEDAEALAELLNDpevARYLPGPPYSLE-------EARAWLERLLADWADggalpFAIEDKEDGELIGVVGLYDI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225  92 NDyghiDNQTPSLSISLYKEYRNKGIGSHLMNEMLA-SLKDKGYNRVSLSVQKANYA-VNMYLKLGFKIIKeTLEEFLMV 169
Cdd:COG1670    83 DR----ANRSAEIGYWLAPAYWGKGYATEALRALLDyAFEELGLHRVEAEVDPDNTAsIRVLEKLGFRLEG-TLRDALVI 157


                  .
gi 1290347225 170 N 170
Cdd:COG1670   158 D 158
PLN02694 PLN02694
serine O-acetyltransferase
 317-365 1.62e-06

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 50.03  E-value: 1.62e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1290347225 317 VEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTKSIPENCLAAGNPCKVI 365
Cdd:PLN02694  215 IGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLV 263
RimL COG1670
Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, ...
 369-508 3.30e-06

Protein N-acetyltransferase, RimJ/RimL family [Translation, ribosomal structure and biogenesis, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 441276 [Multi-domain]  Cd Length: 173  Bit Score: 47.30  E-value: 3.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 369 SPQYRLLPLEEKDIPEMQELFRS--TVLNVNIRHYTQEEVEDWAscgDSVEHLKELLSHNHFIGAFDEAGRMVGFSS-MN 445
Cdd:COG1670     5 TERLRLRPLRPEDAEALAELLNDpeVARYLPGPPYSLEEARAWL---ERLLADWADGGALPFAIEDKEDGELIGVVGlYD 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1290347225 446 KDGYLHS----MFVHKDWQGKGVATQLLSEVERIA-KQLEVAEITSEVSLT---ARPFFEKKGYEIVKIQK 508
Cdd:COG1670    82 IDRANRSaeigYWLAPAYWGKGYATEALRALLDYAfEELGLHRVEAEVDPDntaSIRVLEKLGFRLEGTLR 152
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
315-349 6.45e-06

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 42.81  E-value: 6.45e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1290347225 315 ITVEDNAWIGGGSIIlaGVTIGKGSVIGAGSVVTK 349
Cdd:pfam14602   1 VIIGDNCLIGANSGI--GVSLGDNCVVGAGVVITA 33
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
314-343 1.05e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 42.32  E-value: 1.05e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1290347225 314 PITVEDNAWIGGGSIILAGVTIGKGSVIGA 343
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
PLN02472 PLN02472
uncharacterized protein
 316-424 1.35e-05

uncharacterized protein


Pssm-ID: 215263 [Multi-domain]  Cd Length: 246  Bit Score: 46.49  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 316 TVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVT--KSIPENCLAAGNPCKVIRWLSPQyrllplEEKDIPEmqelfrstv 393
Cdd:PLN02472  145 TIEPECIIGQHSILMEGSLVETHSILEAGSVLPpgRRIPTGELWAGNPARFVRTLTNE------ETLEIPK--------- 209

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1290347225 394 LNVNIRHYTQEEVEDWASCGDS---VEHLKELLS 424
Cdd:PLN02472  210 LAVAINDLSQSHFSEFLPYSTAyleVEKLKKSLG 243
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 319-366 2.73e-05

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 46.46  E-value: 2.73e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1290347225 319 DNAWIGGGSIILAGVTIGKGSVIGAGSVVTKSIPENCLAAGNPCKVIR 366
Cdd:PRK14360  395 DRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLAIARSRQVIK 442
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 316-354 4.06e-05

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 45.78  E-value: 4.06e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1290347225 316 TVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTKSIPEN 354
Cdd:COG1044   260 KIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEG 298
COG3393 COG3393
Predicted acetyltransferase, GNAT family [General function prediction only];
438-504 4.35e-05

Predicted acetyltransferase, GNAT family [General function prediction only];


Pssm-ID: 442620 [Multi-domain]  Cd Length: 86  Bit Score: 42.20  E-value: 4.35e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1290347225 438 MVGFSSMNKD-GYLHSMFVHKDWQGKGVATQLLSEVERIAKQLEVAEITSEVSL---TARPFFEKKGYEIV 504
Cdd:COG3393     5 MAGVRAESPGvAEISGVYTHPEYRGRGLASALVAALAREALARGARTPFLYVDAdnpAARRLYERLGFRPV 75
PRK10191 PRK10191
putative acyl transferase; Provisional
 312-364 4.62e-05

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 43.73  E-value: 4.62e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1290347225 312 ALPItVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTKSIPENCLAAGNPCKV 364
Cdd:PRK10191   91 ACPH-IGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKARV 142
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 230-348 5.59e-05

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: 5.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 230 IGNHSSVGQN-----FTCqCGKHIFIGEQTIInKNCTMMDENQI----HIGDRVL----------VAPNVQFYTATHPIN 290
Cdd:cd05636    38 IGKGCEIGPNayirgYTV-LGDGCVVGNSVEV-KNSIIMDGTKVphlnYVGDSVLgenvnlgagtITANLRFDDKPVKVR 115

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1290347225 291 FDERFVenwneDSGelffRTKaLPITVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVT 348
Cdd:cd05636   116 LKGERV-----DTG----RRK-LGAIIGDGVKTGINVSLNPGVKIGPGSWVYPGCVVR 163
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 319-356 7.44e-05

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 45.40  E-value: 7.44e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1290347225 319 DNAWIGGGSIILAGVTIGKGSVIGAGSVVTKSIPENCL 356
Cdd:PRK09451  399 DDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDVAENEL 436
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 315-361 7.52e-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: 45.51  E-value: 7.52e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1290347225 315 ITVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTK--SIPENCLAAGNP 361
Cdd:TIGR02353 646 VTIGDGATLGPGAIVLYGVVMGEGSVLGPDSLVMKgeEVPAHTRWRGNP 694
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 317-356 1.27e-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: 44.24  E-value: 1.27e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1290347225 317 VEDNAWIGGGSIILAGVTIGKGSVIGAGSV----VTksIPENCL 356
Cdd:COG1044   123 IGAGVVIGDGVVIGPGVVIGDGVVIGDDCVlhpnVT--IYERCV 164
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 317-357 2.04e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 43.96  E-value: 2.04e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1290347225 317 VEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTKSIPENCLA 357
Cdd:PRK14355  400 IEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPPDSLA 440
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 316-347 2.83e-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: 43.08  E-value: 2.83e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1290347225 316 TVEDNAWIGGGSIILAGVTIGKGSVIGAGSVV 347
Cdd:COG1044   110 KIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVI 141
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 245-364 3.51e-04

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 43.20  E-value: 3.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 245 GKHIFIGEQTIInknCTMMdenqIHIGDRVLVApnvqfytathpinfDERFVENWNEDSGELffRTKalPITVEDNAWIG 324
Cdd:TIGR02353 116 GKGVDIGSLPPV---CTDL----LTIGAGTIVR--------------KEVMLLGYRAERGRL--HTG--PVTLGRDAFIG 170

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1290347225 325 GGSIILAGVTIGKGSVIGAGSVVT--KSIPENCLAAGNP-CKV 364
Cdd:TIGR02353 171 TRSTLDIDTSIGDGAQLGHGSALQggQSIPDGERWHGSPaQKT 213
PRK03624 PRK03624
putative acetyltransferase; Provisional
 54-156 3.81e-04

putative acetyltransferase; Provisional


Pssm-ID: 235142 [Multi-domain]  Cd Length: 140  Bit Score: 40.68  E-value: 3.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225  54 NAPELKlyIENFGTKKDDFCLVADCAGKVIGAVwvriMNDY-GHidnqTPSL-SISLYKEYRNKGIGSHLMNEMLASLKD 131
Cdd:PRK03624   30 NDPEMD--IERKLNHDPSLFLVAEVGGEVVGTV----MGGYdGH----RGWAyYLAVHPDFRGRGIGRALVARLEKKLIA 99

                          90       100
                  ....*....|....*....|....*.
gi 1290347225 132 KGYNRVSLSVQKANYAV-NMYLKLGF 156
Cdd:PRK03624  100 RGCPKINLQVREDNDAVlGFYEALGY 125
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 316-354 4.27e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 42.43  E-value: 4.27e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1290347225 316 TVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTKSIPEN 354
Cdd:PRK00892  263 KIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEP 301
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 316-347 6.69e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 42.05  E-value: 6.69e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1290347225 316 TVEDNAWIGGGSIILAGVTIGKGSVIGAGSVV 347
Cdd:PRK00892  126 VIGAGVVIGDGVVIGAGAVIGDGVKIGADCRL 157
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 316-359 7.98e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 41.66  E-value: 7.98e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1290347225 316 TVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTK--SIPENC-LAAG 359
Cdd:PRK00892  114 KIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDgvKIGADCrLHAN 160
PRK07922 PRK07922
amino-acid N-acetyltransferase;
428-502 1.17e-03

amino-acid N-acetyltransferase;


Pssm-ID: 236132 [Multi-domain]  Cd Length: 169  Bit Score: 39.90  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 428 FIGAFDEAGRMVGFssmnkdGYLHSMF----------VHKDWQGKGVATQLLSEVERIAKQLEVAEI---TSEVsltarP 494
Cdd:PRK07922   47 FWVAEHLDGEVVGC------GALHVMWedlaeirtvaVDPAARGRGVGHAIVERLLDVARELGLSRVfvlTFEV-----E 115


                  ....*...
gi 1290347225 495 FFEKKGYE 502
Cdd:PRK07922  116 FFARHGFV 123
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 317-347 1.32e-03

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 40.08  E-value: 1.32e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1290347225 317 VEDNAWIGGGSIILAGVTIGKGSVIGAGSVV 347
Cdd:cd03352    16 IGEGVVIGDGVVIGPGVVIGDGVVIGDDCVI 46
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 316-356 2.23e-03

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 39.31  E-value: 2.23e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1290347225 316 TVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTK--SIPENCL 356
Cdd:cd03352     3 KIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDgvVIGDDCV 45
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 316-347 2.30e-03

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: 40.39  E-value: 2.30e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1290347225 316 TVEDNAWIGGGSIILAGVTIGKGSVIGAGSVV 347
Cdd:COG1044   128 VIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTI 159
FR47 pfam08445
FR47-like protein; The members of this family are similar to the C-terminal region of the D. ...
 429-502 2.38e-03

FR47-like protein; The members of this family are similar to the C-terminal region of the D. melanogaster hypothetical protein FR47. This protein has been found to consist of two N-acyltransferase-like domains swapped with the C-terminal strands.


Pssm-ID: 117022 [Multi-domain]  Cd Length: 86  Bit Score: 37.31  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 429 IGAFDEA-GRMVGFSSMNKDGYLHSMFVHKDWQGKGVATQLlseVERIAKQLEVAEITSEVSL-----TARPFFEKKGYE 502
Cdd:pfam08445   2 LGIYRGDtGELAAWCLRLPGGELGALQTLPEHRRRGLGSRL---VAALARGIAERGITPFAVVvagntPSRRLYEKLGFR 78
PRK07757 PRK07757
N-acetyltransferase;
75-163 2.46e-03

N-acetyltransferase;


Pssm-ID: 236088 [Multi-domain]  Cd Length: 152  Bit Score: 38.64  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225  75 VADCAGKVIGAVWVRIM-NDYGHIDnqtpSLSISlyKEYRNKGIGSHLMNEMLASLKDKGYNRV-SLSvqkanYAVNMYL 152
Cdd:PRK07757   45 VAEEEGEIVGCCALHILwEDLAEIR----SLAVS--EDYRGQGIGRMLVEACLEEARELGVKRVfALT-----YQPEFFE 113

                          90
                  ....*....|..
gi 1290347225 153 KLGFKII-KETL 163
Cdd:PRK07757  114 KLGFREVdKEAL 125
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 20-158 2.85e-03

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 37.94  E-value: 2.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225  20 IRPLRQEEtflLREF--LYEAIFipkgietpskEVINAPELKLYIENfgTKKDDFCLVADCAGKVIGAV---WVRiMNDY 94
Cdd:pfam13527   1 IRPLTEDE---FDEVlrLLEYAF----------QDEDSPELREYFRP--LLEEGRVLGAFDDGELVSTLalyPFE-LNVP 64

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1290347225  95 GHIdnqTPSL---SISLYKEYRNKGIGSHLMNEMLASLKDKGYNRVSLSVqkanYAVNMYLKLGFKI 158
Cdd:pfam13527  65 GKT---LPAAgitGVATYPEYRGRGVMSRLLRRSLEEMRERGVPLSFLYP----SSYPIYRRFGYEI 124
Acetyltransf_9 pfam13527
Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.
 398-503 2.96e-03

Acetyltransferase (GNAT) domain; This domain catalyzes N-acetyltransferase reactions.


Pssm-ID: 404421 [Multi-domain]  Cd Length: 124  Bit Score: 37.94  E-value: 2.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1290347225 398 IRHYTQEEVEDWAS----------CGDSVEHLKELLSHNHFIGAFDEaGRMVGFSSMN-----------KDGYLHSMFVH 456
Cdd:pfam13527   1 IRPLTEDEFDEVLRlleyafqdedSPELREYFRPLLEEGRVLGAFDD-GELVSTLALYpfelnvpgktlPAAGITGVATY 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1290347225 457 KDWQGKGVATQLLSEVERIAKQLEVAeitseVSL---TARPFFEKKGYEI 503
Cdd:pfam13527  80 PEYRGRGVMSRLLRRSLEEMRERGVP-----LSFlypSSYPIYRRFGYEI 124
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 316-365 5.33e-03

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 39.54  E-value: 5.33e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1290347225 316 TVEDNAWIGGGSIILAGVTIGKGSVIGAGSVVTKSIPENCLA-AGNPCKVI 365
Cdd:PRK14352  401 TIGSHVRTGSDTMFVAPVTVGDGAYTGAGTVIREDVPPGALAvSEGPQRNI 451
Mac pfam12464
Maltose acetyltransferase; This domain family is found in bacteria, archaea and eukaryotes, ...
 175-231 6.18e-03

Maltose acetyltransferase; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 50 amino acids in length. The family is found in association with pfam00132. Mac uses acetyl-CoA as acetyl donor to acetylated cytoplasmic maltose.


Pssm-ID: 463596 [Multi-domain]  Cd Length: 52  Bit Score: 34.77  E-value: 6.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1290347225 175 KMsnyqhfLSGEYCNYLDAEVLVMINRTKGYLSVLNDIKTAENEKK-EILSKMLGNIG 231
Cdd:pfam12464   1 KM------LAGELYDASDPELVAERLRARRLLRRYNNTPPEDAEEReELLKELFGSVG 52
 
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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