NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1317777326|gb|AUI19099|]
View 

Serine acetyltransferase [Enterococcus faecium]

Protein Classification

LbetaH domain-containing protein( domain architecture ID 372)

LbetaH (left-handed parallel beta-helix) domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
LbetaH super family cl00160
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 90-181 9.34e-27

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.


The actual alignment was detected with superfamily member cd03354:

Pssm-ID: 469633 [Multi-domain]  Cd Length: 101  Bit Score: 97.90  E-value: 9.34e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317777326  90 NVFDEGVRFYHTQGIVINGNAIIGKNCYLYGNNCIGNDGID--PKCPVIGNNVRVCVGAKIIGNVKIANNVVVAAGAIVI 167
Cdd:cd03354     9 AKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGggKRHPTIGDNVVIGAGAKILGNITIGDNVKIGANAVVT 88

                          90
                  ....*....|....
gi 1317777326 168 KDcLENGAILAGVP 181
Cdd:cd03354    89 KD-VPANSTVVGVP 101
 
Name Accession Description Interval E-value
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 90-181 9.34e-27

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: 97.90  E-value: 9.34e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317777326  90 NVFDEGVRFYHTQGIVINGNAIIGKNCYLYGNNCIGNDGID--PKCPVIGNNVRVCVGAKIIGNVKIANNVVVAAGAIVI 167
Cdd:cd03354     9 AKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGggKRHPTIGDNVVIGAGAKILGNITIGDNVKIGANAVVT 88

                          90
                  ....*....|....
gi 1317777326 168 KDcLENGAILAGVP 181
Cdd:cd03354    89 KD-VPANSTVVGVP 101
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 50-186 1.03e-24

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: 94.76  E-value: 1.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317777326  50 RITSYYYSKRKKNIIYAIMYIVScrrmnslgRKCGIE------CGENVFdegvrFYHTQGIVINGNAIIGKNCYLYGNNC 123
Cdd:COG1045    39 RLAHWLWKRGLPLLARLLSERAR--------FLTGIDihpgatIGRGFF-----IDHGTGVVIGETAVIGDNVTIYQGVT 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1317777326 124 IG--NDGIDPKCPVIGNNVRVCVGAKIIGNVKIANNVVVAAGAIVIKDcLENGAILAGVPAKIIG 186
Cdd:COG1045   106 LGgtGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKD-VPPGSTVVGVPARIVK 169
PRK10191 PRK10191
putative acyl transferase; Provisional
 95-184 5.85e-11

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 57.98  E-value: 5.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317777326  95 GVRF--YHTQGIVINGNAIIGKNCYLYGNNCIGNDGID-PKCPVIGNNVRVCVGAKIIGNVKIANNVVVAAGAIVIkDCL 171
Cdd:PRK10191   51 GRRFtiHHGYAVVINKNVVAGDDFTIRHGVTIGNRGADnMACPHIGNGVELGANVIILGDITIGNNVTVGAGSVVL-DSV 129

                          90
                  ....*....|...
gi 1317777326 172 ENGAILAGVPAKI 184
Cdd:PRK10191  130 PDNALVVGEKARV 142
 
Name Accession Description Interval E-value
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 90-181 9.34e-27

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: 97.90  E-value: 9.34e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317777326  90 NVFDEGVRFYHTQGIVINGNAIIGKNCYLYGNNCIGNDGID--PKCPVIGNNVRVCVGAKIIGNVKIANNVVVAAGAIVI 167
Cdd:cd03354     9 AKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGggKRHPTIGDNVVIGAGAKILGNITIGDNVKIGANAVVT 88

                          90
                  ....*....|....
gi 1317777326 168 KDcLENGAILAGVP 181
Cdd:cd03354    89 KD-VPANSTVVGVP 101
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 50-186 1.03e-24

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: 94.76  E-value: 1.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317777326  50 RITSYYYSKRKKNIIYAIMYIVScrrmnslgRKCGIE------CGENVFdegvrFYHTQGIVINGNAIIGKNCYLYGNNC 123
Cdd:COG1045    39 RLAHWLWKRGLPLLARLLSERAR--------FLTGIDihpgatIGRGFF-----IDHGTGVVIGETAVIGDNVTIYQGVT 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1317777326 124 IG--NDGIDPKCPVIGNNVRVCVGAKIIGNVKIANNVVVAAGAIVIKDcLENGAILAGVPAKIIG 186
Cdd:COG1045   106 LGgtGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKD-VPPGSTVVGVPARIVK 169
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
83-189 1.04e-17

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 75.68  E-value: 1.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317777326  83 CGIECGENVF-DEGVRFYHTQGIVINGNAIIGKNCYLYGNN----CIGNDGIDPKCPVIGNNVRVCVGAKIIGNVKIANN 157
Cdd:COG0110    26 GNITIGDNVYiGPGVTIDDPGGITIGDNVLIGPGVTILTGNhpidDPATFPLRTGPVTIGDDVWIGAGATILPGVTIGDG 105

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1317777326 158 VVVAAGAIVIKDcLENGAILAGVPAKIIGYVN 189
Cdd:COG0110   106 AVVGAGSVVTKD-VPPYAIVAGNPARVIRKRD 136
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 84-185 6.33e-17

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: 72.49  E-value: 6.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317777326  84 GIECGENVF-DEGVRFYHTQGIVINGNAIIGKNCYLYGNN---CIGNDGIDPKCP----VIGNNVRVCVGAKIIGNVKIA 155
Cdd:cd04647     1 NISIGDNVYiGPGCVISAGGGITIGDNVLIGPNVTIYDHNhdiDDPERPIEQGVTsapiVIGDDVWIGANVVILPGVTIG 80

                          90       100       110
                  ....*....|....*....|....*....|
gi 1317777326 156 NNVVVAAGAIVIKDCLENgAILAGVPAKII 185
Cdd:cd04647    81 DGAVVGAGSVVTKDVPPN-SIVAGNPAKVI 109
PRK10191 PRK10191
putative acyl transferase; Provisional
 95-184 5.85e-11

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 57.98  E-value: 5.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317777326  95 GVRF--YHTQGIVINGNAIIGKNCYLYGNNCIGNDGID-PKCPVIGNNVRVCVGAKIIGNVKIANNVVVAAGAIVIkDCL 171
Cdd:PRK10191   51 GRRFtiHHGYAVVINKNVVAGDDFTIRHGVTIGNRGADnMACPHIGNGVELGANVIILGDITIGNNVTVGAGSVVL-DSV 129

                          90
                  ....*....|...
gi 1317777326 172 ENGAILAGVPAKI 184
Cdd:PRK10191  130 PDNALVVGEKARV 142
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 105-181 6.73e-11

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: 58.65  E-value: 6.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317777326 105 VINGNAIIGKNCYLYGNNCIGNDG-------IDPKCPV-----IGNNVRVCVGAKIIGNVKIANNVVVAAGAIVIKDcLE 172
Cdd:cd03360   110 VINPDARIGDNVIINTGAVIGHDCvigdfvhIAPGVVLsggvtIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKD-VP 188


                  ....*....
gi 1317777326 173 NGAILAGVP 181
Cdd:cd03360   189 DGSVVVGNP 197
PLN02739 PLN02739
serine acetyltransferase
 94-189 2.21e-10

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 58.51  E-value: 2.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317777326  94 EGVRFYHTQGIVINGNAIIGKNCYLYGNNCIGNDGIDP--KCPVIGNNVRVCVGAKIIGNVKIANNVVVAAGAIVIKDcL 171
Cdd:PLN02739  216 KGILLDHGTGVVIGETAVIGDRVSILHGVTLGGTGKETgdRHPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKD-V 294

                          90
                  ....*....|....*...
gi 1317777326 172 ENGAILAGVPAKIIGYVN 189
Cdd:PLN02739  295 PSHSMVAGNPAKLIGFVD 312
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 102-186 5.67e-10

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: 54.43  E-value: 5.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317777326 102 QGIVINGNAIIGKNC------YLYGNNCIGND-----------------GIDPKC----PVIGNNVRVCVGAKIIGNVKI 154
Cdd:cd03358     9 TNVFIENDVKIGDNVkiqsnvSIYEGVTIEDDvfigpnvvftndlyprsKIYRKWelkgTTVKRGASIGANATILPGVTI 88

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1317777326 155 ANNVVVAAGAIVIKDcLENGAILAGVPAKIIG 186
Cdd:cd03358    89 GEYALVGAGAVVTKD-VPPYALVVGNPARIIG 119
PLN02694 PLN02694
serine O-acetyltransferase
 94-186 6.32e-10

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 56.96  E-value: 6.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317777326  94 EGVRFYHTQGIVINGNAIIGKNCYLYGNNCIGNDG--IDPKCPVIGNNVRVCVGAKIIGNVKIANNVVVAAGAIVIKDcL 171
Cdd:PLN02694  171 KGILFDHATGVVIGETAVIGNNVSILHHVTLGGTGkaCGDRHPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLID-V 249

                          90
                  ....*....|....*
gi 1317777326 172 ENGAILAGVPAKIIG 186
Cdd:PLN02694  250 PPRTTAVGNPARLVG 264
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 119-187 1.10e-09

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: 54.47  E-value: 1.10e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317777326 119 YGNNCIGNDGIDPKCPV-IGNNVRVCVGAKIIGNVKIANNVVVAAGAIVIKDClENGAILAGVPAKIIGY 187
Cdd:cd03349    58 EWEDDAKFDDWPSKGDViIGNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDV-PPYAIVGGNPAKVIRY 126
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 83-185 2.39e-09

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: 53.97  E-value: 2.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317777326  83 CGIECGENVF--------DEGvrfyhtqGIVINGNAIIGKNCYLYGNNCigndGIDPK---------CPV-IGNNVRVCV 144
Cdd:cd03357    61 YNIHIGDNFYanfnctilDVA-------PVTIGDNVLIGPNVQIYTAGH----PLDPEernrgleyaKPItIGDNVWIGG 129

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1317777326 145 GAKIIGNVKIANNVVVAAGAIVIKDcLENGAILAGVPAKII 185
Cdd:cd03357   130 GVIILPGVTIGDNSVIGAGSVVTKD-IPANVVAAGNPARVI 169
PLN02357 PLN02357
serine acetyltransferase
 94-186 1.37e-08

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 53.35  E-value: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317777326  94 EGVRFYHTQGIVINGNAIIGKNCYLYGNNCIGNDG--IDPKCPVIGNNVRVCVGAKIIGNVKIANNVVVAAGAIVIKDcL 171
Cdd:PLN02357  237 QGILLDHATGVVIGETAVVGNNVSILHNVTLGGTGkqSGDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKD-V 315

                          90
                  ....*....|....*
gi 1317777326 172 ENGAILAGVPAKIIG 186
Cdd:PLN02357  316 PPRTTAVGNPARLIG 330
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 94-185 6.18e-08

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: 48.76  E-value: 6.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317777326  94 EGVRFYHTQGIVINGNAIIGKNCYLygnnCIGN-DGIDPKCP------VIGNNVRVCVGAKIIGNVKIANNVVVAAGAIV 166
Cdd:cd05825    14 EGVWIYNLAPVTIGSDACISQGAYL----CTGShDYRSPAFPlitapiVIGDGAWVAAEAFVGPGVTIGEGAVVGARSVV 89

                          90
                  ....*....|....*....
gi 1317777326 167 IKDcLENGAILAGVPAKII 185
Cdd:cd05825    90 VRD-LPAWTVYAGNPAVPV 107
cysE PRK11132
serine acetyltransferase; Provisional
 95-186 1.04e-06

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 47.77  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317777326  95 GVRFYHTQGIVINGNAIIGKNCYLYGNNCIGNDGID--PKCPVIGNNVRVCVGAKIIGNVKIANNVVVAAGAIVIKDCLE 172
Cdd:PRK11132  153 GIMLDHATGIVIGETAVIENDVSILQSVTLGGTGKTsgDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPP 232

                          90
                  ....*....|....
gi 1317777326 173 NgAILAGVPAKIIG 186
Cdd:PRK11132  233 H-TTAAGVPARIVG 245
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 126-185 2.47e-06

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 45.96  E-value: 2.47e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1317777326 126 NDGIDPKCPV-IGNNVRVCVGAKIIGNVKIANNVVVAAGAIVIKDCLENgAILAGVPAKII 185
Cdd:PRK10092  121 NSGAELGKPVtIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDN-VVVGGNPARII 180
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 109-183 2.60e-06

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: 45.86  E-value: 2.60e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1317777326 109 NAIIGKNCYLYGNNCIGNdgidpkCPVIGNNVRVCVGAKIIGNVKIANNVVVAAGAIVIKDcLENGAILAGVPAK 183
Cdd:cd03352   132 NVRIGENCLIAAQVGIAG------STTIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSI-VPPGEYVSGTPAQ 199
PRK10502 PRK10502
putative acyl transferase; Provisional
 94-185 5.18e-06

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 44.94  E-value: 5.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317777326  94 EGVRFYHTQGIVINGNAIIGKNCYLygnnCIGNDgiDPKCP---------VIGNNVRVCVGAKIIGNVKIANNVVVAAGA 164
Cdd:PRK10502   82 DDVWLYNLGEITIGAHCVISQKSYL----CTGSH--DYSDPhfdlntapiVIGEGCWLAADVFVAPGVTIGSGAVVGARS 155

                          90       100
                  ....*....|....*....|.
gi 1317777326 165 IVIKDcLENGAILAGVPAKII 185
Cdd:PRK10502  156 SVFKS-LPANTICRGNPAVPI 175
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 103-166 6.49e-06

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 42.62  E-value: 6.49e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1317777326 103 GIVINGNAIIGKNCYLYGNNCIGNDGID--PKCPVIGNNVRVCVGAKIIGNVKIANNVVVAAGAIV 166
Cdd:cd00208    12 KAVIRGPVVIGDNVNIGPGAVIGAATGPneKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVV 77
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 100-185 1.48e-05

Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 43.17  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317777326 100 HTQGIVINGNAIIGKNCYLYGnncigndgidpkCpVIGNNVRVCVGAKIIGNVKIANNVVVAAGAIVIKDC-LENGAILA 178
Cdd:cd04645    57 PGYPTIIGDNVTVGHGAVLHG------------C-TIGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGKvIPPGSLVA 123


                  ....*..
gi 1317777326 179 GVPAKII 185
Cdd:cd04645   124 GSPAKVV 130
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 105-186 2.29e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 43.97  E-value: 2.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317777326 105 VINGNAIIGKNCYLYGNNCIGNDGidpkcpVIGNNVRVCVGAKIIGNVKIANNVVVAAGAIVIKDCL--ENGAILAGVpa 182
Cdd:PRK00892  108 VIDPSAKIGEGVSIGPNAVIGAGV------VIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRigNRVIIHSGA-- 179


                  ....
gi 1317777326 183 kIIG 186
Cdd:PRK00892  180 -VIG 182
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 128-189 5.33e-05

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 42.17  E-value: 5.33e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317777326 128 GIDPKCPVIGNNVRVCVGAKIIGNVKIANNVVVAAGAIVIKDcLENGAILAGVPAKIIGYVN 189
Cdd:PRK09677  125 TLESSAVVIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKS-IPENTVIAGNPAKIIKKYN 185
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 112-183 7.69e-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: 42.31  E-value: 7.69e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1317777326 112 IGKNCYLyGNNCI--GNDGIDPKCpVIGNNVRVCVGAKIIGNVKIANNVVVAAGAIVIKDcLENGAILAGVPAK 183
Cdd:COG1044   237 IAHNVRI-GEHTAiaAQVGIAGST-KIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKS-IPEGGVYSGSPAQ 307
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 108-185 8.86e-05

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 42.32  E-value: 8.86e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1317777326 108 GNAIIGKNCYLYGNNCIGN-DGIDPKCPVIGNNVRVCVGAKIIGNVKIANNVVVAAGAIVIKDCLENGAILAGVPAKII 185
Cdd:PRK09451  368 GDAEIGDNVNIGAGTITCNyDGANKFKTIIGDDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDVAENELVISRVPQRHI 446
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 109-183 4.81e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 39.74  E-value: 4.81e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1317777326 109 NAIIGKNCYLYGnnCIGNDGidpkCPVIGNNVRVCVGAKIIGNVKIANNVVVAAGAIVIKDCLENGAILAGVPAK 183
Cdd:PRK00892  243 NVVIGRHTAIAA--QVGIAG----STKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEPGEYSSGIPAQ 311
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 136-185 6.65e-04

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 38.85  E-value: 6.65e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1317777326 136 IGNNVRVCVGAKIIGNVKIANNVVVAAGAIVI--KDcLENGAILAGVPAKII 185
Cdd:COG0663    91 IGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTegKV-VPPGSLVVGSPAKVV 141
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 105-186 1.39e-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: 38.46  E-value: 1.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317777326 105 VINGNAIIGKNCYLYGNNCIGNDGidpkcpVIGNNVRVCVGAKIIGNVKIANNVVVAAGAIVIKDCL--ENGAILAGVpa 182
Cdd:COG1044   104 VIDPSAKIGEGVSIGPFAVIGAGV------VIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVigDRVIIHSGA-- 175


                  ....
gi 1317777326 183 kIIG 186
Cdd:COG1044   176 -VIG 178
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 105-166 1.86e-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: 37.77  E-value: 1.86e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317777326 105 VINGNAIIGKNCYLYGNNCIGNDGidpkcpVIGNNVRVCVGAKIIGNVKIANNVVVAAGAIV 166
Cdd:cd03352    15 VIGEGVVIGDGVVIGPGVVIGDGV------VIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 109-170 3.12e-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: 37.00  E-value: 3.12e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1317777326 109 NAIIGKNCYLYGNNCIGNDgidpkcPVIGNNVRVCVGAKIIGNVKIANNVVVAAGAIVIKDC 170
Cdd:cd03352     1 SAKIGENVSIGPNAVIGEG------VVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGC 56
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 136-185 4.24e-03

Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in iron acquisition. It binds iron when it is complexed with pyochelin. It adopts the left-handed parallel beta-helix (LbH) structure, and contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Acyltransferase activity has not been observed in this group.


Pssm-ID: 100055 [Multi-domain]  Cd Length: 154  Bit Score: 36.39  E-value: 4.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1317777326 136 IGNNVRVCVGAKIIGNVKIANNVVVAAGAIVIKDC-LENGAILAGVPAKII 185
Cdd:cd04650    81 VGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTPGKeIPDYSLVLGVPAKVV 131
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 103-166 6.93e-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: 35.85  E-value: 6.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1317777326 103 GIVINGNAIIGKNCYLYGNNCIGNDgidpkCpVIGNNVRVCVGAKI-------------------IGNVKIANNVVVAAG 163
Cdd:cd03352    31 GVVIGDGVVIGDDCVIHPNVTIYEG-----C-IIGDRVIIHSGAVIgsdgfgfapdgggwvkipqLGGVIIGDDVEIGAN 104


                  ...
gi 1317777326 164 AIV 166
Cdd:cd03352   105 TTI 107
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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