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Conserved domains on  [gi|499337259|ref|WP_011026968|]
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MULTISPECIES: sugar O-acetyltransferase [Streptomyces]

Protein Classification

sugar O-acetyltransferase( domain architecture ID 10129706)

sugar O-acetyltransferase similar to maltose O-acetyltransferase and galactoside O-acetyltransferase, which catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates

CATH:  2.160.10.10
EC:  2.3.1.-
Gene Ontology:  GO:0016407
PubMed:  11747907

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 ...
 4-171 3.46e-58

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: 179.54  E-value: 3.46e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499337259   4 HTPEFArhAERIvEVTDATSRLNVLPFSDSAGRSELLSVVFGGPlPESVTIYPPFFTEYGLNTTFGENVFVNQGCTFMDK 83
Cdd:cd03357    5 SDPELV--AERA-RARRLLHEYNQTPPSDAEERRELLKELFGSV-GENVYIEPPFHCDYGYNIHIGDNFYANFNCTILDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499337259  84 GGIRIGNRVMIAPKASLVTGGHPLPLAERRAHLSFA-PIVVEDDVWIGTAAVITQGVTIGAGAVVAAGAVVTRDVPAGTV 162
Cdd:cd03357   81 APVTIGDNVLIGPNVQIYTAGHPLDPEERNRGLEYAkPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVV 160


                 ....*....
gi 499337259 163 VAGVPARVI 171
Cdd:cd03357  161 AAGNPARVI 169
 
Name Accession Description Interval E-value
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 4-171 3.46e-58

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: 179.54  E-value: 3.46e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499337259   4 HTPEFArhAERIvEVTDATSRLNVLPFSDSAGRSELLSVVFGGPlPESVTIYPPFFTEYGLNTTFGENVFVNQGCTFMDK 83
Cdd:cd03357    5 SDPELV--AERA-RARRLLHEYNQTPPSDAEERRELLKELFGSV-GENVYIEPPFHCDYGYNIHIGDNFYANFNCTILDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499337259  84 GGIRIGNRVMIAPKASLVTGGHPLPLAERRAHLSFA-PIVVEDDVWIGTAAVITQGVTIGAGAVVAAGAVVTRDVPAGTV 162
Cdd:cd03357   81 APVTIGDNVLIGPNVQIYTAGHPLDPEERNRGLEYAkPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVV 160


                 ....*....
gi 499337259 163 VAGVPARVI 171
Cdd:cd03357  161 AAGNPARVI 169
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
44-174 8.63e-34

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 116.51  E-value: 8.63e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499337259  44 FGGPLPESVTIYPPFFTeYGLNTTFGENVFVNQGCTFMDKGGIRIGNRVMIAPKASLVTGGHPLPLAERRaHLSFAPIVV 123
Cdd:COG0110    7 FGARIGDGVVIGPGVRI-YGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPATF-PLRTGPVTI 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499337259 124 EDDVWIGTAAVITQGVTIGAGAVVAAGAVVTRDVPAGTVVAGVPARVIKQI 174
Cdd:COG0110   85 GDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKR 135
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 36-174 4.19e-29

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 105.67  E-value: 4.19e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499337259  36 RSELLSVVFGGPlpESVTIYPPFFTEYGLNTTFGENVFVNQGCTFMDKGGIRIGNRVMIAPKASLVTGGHPLPLAERRAH 115
Cdd:PRK10092  46 RQQILADLFGQV--TEAYIEPTFRCDYGYNIFLGNNFYANFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPLDPVARNSG 123

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499337259 116 LSFA-PIVVEDDVWIGTAAVITQGVTIGAGAVVAAGAVVTRDVPAGTVVAGVPARVIKQI 174
Cdd:PRK10092 124 AELGkPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIKKL 183
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 65-168 9.61e-09

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: 52.50  E-value: 9.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499337259   65 NTTFGENVFVNQGCTfmdkggI----RIGNRVMIAPKASLvtGGHplplaerrahlsfapIVVEDDVWIGTAAVITQGVT 140
Cdd:TIGR03570 117 DVRIGDNVIINTGAI------VehdcVIGDFVHIAPGVTL--SGG---------------VVIGEGVFIGAGATIIQGVT 173

                          90       100
                  ....*....|....*....|....*...
gi 499337259  141 IGAGAVVAAGAVVTRDVPAGTVVAGVPA 168
Cdd:TIGR03570 174 IGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
 
Name Accession Description Interval E-value
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 4-171 3.46e-58

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: 179.54  E-value: 3.46e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499337259   4 HTPEFArhAERIvEVTDATSRLNVLPFSDSAGRSELLSVVFGGPlPESVTIYPPFFTEYGLNTTFGENVFVNQGCTFMDK 83
Cdd:cd03357    5 SDPELV--AERA-RARRLLHEYNQTPPSDAEERRELLKELFGSV-GENVYIEPPFHCDYGYNIHIGDNFYANFNCTILDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499337259  84 GGIRIGNRVMIAPKASLVTGGHPLPLAERRAHLSFA-PIVVEDDVWIGTAAVITQGVTIGAGAVVAAGAVVTRDVPAGTV 162
Cdd:cd03357   81 APVTIGDNVLIGPNVQIYTAGHPLDPEERNRGLEYAkPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVV 160


                 ....*....
gi 499337259 163 VAGVPARVI 171
Cdd:cd03357  161 AAGNPARVI 169
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
44-174 8.63e-34

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 116.51  E-value: 8.63e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499337259  44 FGGPLPESVTIYPPFFTeYGLNTTFGENVFVNQGCTFMDKGGIRIGNRVMIAPKASLVTGGHPLPLAERRaHLSFAPIVV 123
Cdd:COG0110    7 FGARIGDGVVIGPGVRI-YGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPATF-PLRTGPVTI 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499337259 124 EDDVWIGTAAVITQGVTIGAGAVVAAGAVVTRDVPAGTVVAGVPARVIKQI 174
Cdd:COG0110   85 GDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKR 135
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 65-171 5.41e-31

Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 108.31  E-value: 5.41e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499337259  65 NTTFGENVFVNQGCTFMDKGGIRIGNRVMIAPKASLVTGGHPLPLAERRA--HLSFAPIVVEDDVWIGTAAVITQGVTIG 142
Cdd:cd04647    1 NISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDHNHDIDDPERPIeqGVTSAPIVIGDDVWIGANVVILPGVTIG 80

                         90       100
                 ....*....|....*....|....*....
gi 499337259 143 AGAVVAAGAVVTRDVPAGTVVAGVPARVI 171
Cdd:cd04647   81 DGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 36-174 4.19e-29

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 105.67  E-value: 4.19e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499337259  36 RSELLSVVFGGPlpESVTIYPPFFTEYGLNTTFGENVFVNQGCTFMDKGGIRIGNRVMIAPKASLVTGGHPLPLAERRAH 115
Cdd:PRK10092  46 RQQILADLFGQV--TEAYIEPTFRCDYGYNIFLGNNFYANFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPLDPVARNSG 123

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499337259 116 LSFA-PIVVEDDVWIGTAAVITQGVTIGAGAVVAAGAVVTRDVPAGTVVAGVPARVIKQI 174
Cdd:PRK10092 124 AELGkPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIKKL 183
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 31-174 1.02e-27

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 102.77  E-value: 1.02e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499337259  31 SDSAGRSELLSVVFGgPLPESVTIYPPFFTEYGLNTTFGENVFVNQGCTFMDKGGIRIGNRVMIAPKASLVTGGHPLPLA 110
Cdd:PRK09527  42 SEVEKRESLIKEMFA-TVGENAWVEPPVYFSYGSNIHIGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGHPVHHE 120

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499337259 111 ERRAHLSFA-PIVVEDDVWIGTAAVITQGVTIGAGAVVAAGAVVTRDVPAGTVVAGVPARVIKQI 174
Cdd:PRK09527 121 LRKNGEMYSfPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIREI 185
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 65-173 3.01e-15

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: 68.72  E-value: 3.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499337259  65 NTTFGENVFVNQGCTFMDKGGIRIGNRVMIAPKASLVTGG-HPL----------------PLAERRAHLSFAPIVVEDDV 127
Cdd:cd03349    1 NISVGDYSYGSGPDCDVGGDKLSIGKFCSIAPGVKIGLGGnHPTdwvstypfyifggeweDDAKFDDWPSKGDVIIGNDV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 499337259 128 WIGTAAVITQGVTIGAGAVVAAGAVVTRDVPAGTVVAGVPARVIKQ 173
Cdd:cd03349   81 WIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRY 126
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 65-171 8.11e-15

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: 66.48  E-value: 8.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499337259  65 NTTFGENVFVNQGCTFMDKGGIRIGNRVMIAPKASLVTGGHplplAERRAHLSF--APIVVEDDVWIGTAAVITQGVTIG 142
Cdd:cd05825    3 NLTIGDNSWIGEGVWIYNLAPVTIGSDACISQGAYLCTGSH----DYRSPAFPLitAPIVIGDGAWVAAEAFVGPGVTIG 78

                         90       100
                 ....*....|....*....|....*....
gi 499337259 143 AGAVVAAGAVVTRDVPAGTVVAGVPARVI 171
Cdd:cd05825   79 EGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
PRK10502 PRK10502
putative acyl transferase; Provisional
 44-173 8.91e-13

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 63.04  E-value: 8.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499337259  44 FGGPLPESVTIYPPFFTEYGLNTTFGENVFVNQGCTFMDKGGIRIGNRVMIAPKASLVTGGHPLplaeRRAH--LSFAPI 121
Cdd:PRK10502  50 FGAKIGKGVVIRPSVRITYPWKLTIGDYAWIGDDVWLYNLGEITIGAHCVISQKSYLCTGSHDY----SDPHfdLNTAPI 125

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499337259 122 VVEDDVWIGTAAVITQGVTIGAGAVVAAGAVVTRDVPAGTVVAGVPARVIKQ 173
Cdd:PRK10502 126 VIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIRP 177
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 63-172 2.60e-11

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: 57.51  E-value: 2.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499337259  63 GLNTTFGENVFVNQGCTFMDK----------GGIRIGNRVMIAPkaSLVTGGHPLPLAERRAHLSFAPIVVEDDVWIGTA 132
Cdd:cd03358    2 GDNCIIGTNVFIENDVKIGDNvkiqsnvsiyEGVTIEDDVFIGP--NVVFTNDLYPRSKIYRKWELKGTTVKRGASIGAN 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 499337259 133 AVITQGVTIGAGAVVAAGAVVTRDVPAGTVVAGVPARVIK 172
Cdd:cd03358   80 ATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 65-168 9.61e-09

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: 52.50  E-value: 9.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499337259   65 NTTFGENVFVNQGCTfmdkggI----RIGNRVMIAPKASLvtGGHplplaerrahlsfapIVVEDDVWIGTAAVITQGVT 140
Cdd:TIGR03570 117 DVRIGDNVIINTGAI------VehdcVIGDFVHIAPGVTL--SGG---------------VVIGEGVFIGAGATIIQGVT 173

                          90       100
                  ....*....|....*....|....*...
gi 499337259  141 IGAGAVVAAGAVVTRDVPAGTVVAGVPA 168
Cdd:TIGR03570 174 IGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 68-172 3.76e-08

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 50.64  E-value: 3.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499337259  68 FGENVFVNQGCTFMDKGGIRIGNRVMIAPKASLVTGGH------------PLPLAERRahLSFAPIVVEDDVWIGTAAVI 135
Cdd:PRK09677  68 FGDNVQVNDYVHIACIESITIGRDTLIASKVFITDHNHgsfkhsddfsspNLPPDMRT--LESSAVVIGQRVWIGENVTI 145

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 499337259 136 TQGVTIGAGAVVAAGAVVTRDVPAGTVVAGVPARVIK 172
Cdd:PRK09677 146 LPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIK 182
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 69-175 5.24e-07

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: 47.00  E-value: 5.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499337259  69 GENVFVNQGCTF------MDKGGIRIGNRVMIAPKASlVTGghplplaerrahlsfaPIVVEDDVWIGTAAVITqgvtig 142
Cdd:COG1045   95 GDNVTIYQGVTLggtgkeKGKRHPTIGDNVVIGAGAK-ILG----------------PITIGDNAKIGANSVVL------ 151

                         90       100       110
                 ....*....|....*....|....*....|...
gi 499337259 143 agavvaagavvtRDVPAGTVVAGVPARVIKQIG 175
Cdd:COG1045  152 ------------KDVPPGSTVVGVPARIVKRKG 172
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 65-167 5.95e-07

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: 47.48  E-value: 5.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499337259  65 NTTFGENVFVNQGCTfmdkggI----RIGNRVMIAPKASLvtGGHplplaerrahlsfapIVVEDDVWIGTAAVITQGVT 140
Cdd:cd03360  114 DARIGDNVIINTGAV------IghdcVIGDFVHIAPGVVL--SGG---------------VTIGEGAFIGAGATIIQGVT 170

                         90       100
                 ....*....|....*....|....*..
gi 499337259 141 IGAGAVVAAGAVVTRDVPAGTVVAGVP 167
Cdd:cd03360  171 IGAGAIIGAGAVVTKDVPDGSVVVGNP 197
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 69-167 4.70e-05

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: 40.50  E-value: 4.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499337259  69 GENVFVNQGCTFMDKGGIR------IGNRVMIAPKASLVtgghplplaerrahlsfAPIVVEDDVWIGTAAVITqgvtig 142
Cdd:cd03354   32 GDNCTIYQGVTLGGKGKGGgkrhptIGDNVVIGAGAKIL-----------------GNITIGDNVKIGANAVVT------ 88

                         90       100
                 ....*....|....*....|....*
gi 499337259 143 agavvaagavvtRDVPAGTVVAGVP 167
Cdd:cd03354   89 ------------KDVPANSTVVGVP 101
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 69-141 3.91e-04

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: 37.61  E-value: 3.91e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 499337259  69 GENVFVNQGCTFmdKGGIRIGNRVMIAPKASLVTGGHPLplaerrahlSFAPIVVEDDVWIGTAAVITQGVTI 141
Cdd:cd00208    4 GEGVKIHPKAVI--RGPVVIGDNVNIGPGAVIGAATGPN---------EKNPTIIGDNVEIGANAVIHGGVKI 65
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 60-170 2.73e-03

UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this family catalyze the transfer of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to UDP-GlcNAc. It is the first enzyme in the lipid A biosynthetic pathway and is also referred to as LpxA. Lipid A is essential for the growth of Escherichia coli and related bacteria. It is also essential for maintaining the integrity of the outer membrane. UDP-GlcNAc acyltransferase is a homotrimer of left-handed parallel beta helix (LbH) subunits. Each subunit contains an N-terminal LbH region with 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal alpha-helical region.


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 37.03  E-value: 2.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499337259  60 TEYGLNTTFGENVFVNQG-------------CTFMDKGGI----RIGNRVMIAPKASLvtGGHplplaerrahlsfapIV 122
Cdd:cd03351   78 LEIGDNNTIREFVTIHRGtaqgggvtrignnNLLMAYVHVahdcVIGNNVILANNATL--AGH---------------VE 140

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 499337259 123 VEDDVWIGTAAVITQGVTIGAGAVVAAGAVVTRDVPAGTVVAGVPARV 170
Cdd:cd03351  141 IGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARL 188
 
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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