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Conserved domains on  [gi|966369367|ref|WP_058416947|]
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MULTISPECIES: acyltransferase [Pseudomonas]

Protein Classification

acyltransferase( domain architecture ID 11414744)

acyltransferase belonging to the transferase hexapeptide repeat family, catalyzes the transfer of an acyl group from an acyl-CoA to a substrate

CATH:  2.160.10.10
EC:  2.3.-.-
Gene Ontology:  GO:0046677|GO:0016746|GO:0120225
PubMed:  15500694
SCOP:  4002841

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
124-255 3.54e-37

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


:

Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 128.45  E-value: 3.54e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367 124 LRIGGAKIGKGSTVWRNTEVLGVDsLRIGNDSTVGWHCQLDARGGLVIGDHVTIASHVLIIAGGHDLNEPE-FWAVGGPV 202
Cdd:COG0110    4 LLLFGARIGDGVVIGPGVRIYGGN-ITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPAtFPLRTGPV 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 966369367 203 FIGDYAWICSRALLSFGADIGEGAVVGGNSVVSKPVPPYAIVSGPNAEIKGER 255
Cdd:COG0110   83 TIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKR 135
 
Name Accession Description Interval E-value
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
124-255 3.54e-37

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 128.45  E-value: 3.54e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367 124 LRIGGAKIGKGSTVWRNTEVLGVDsLRIGNDSTVGWHCQLDARGGLVIGDHVTIASHVLIIAGGHDLNEPE-FWAVGGPV 202
Cdd:COG0110    4 LLLFGARIGDGVVIGPGVRIYGGN-ITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPAtFPLRTGPV 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 966369367 203 FIGDYAWICSRALLSFGADIGEGAVVGGNSVVSKPVPPYAIVSGPNAEIKGER 255
Cdd:COG0110   83 TIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKR 135
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 148-251 2.36e-34

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: 119.87  E-value: 2.36e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367 148 SLRIGNDSTVGWHCQLDARGGLVIGDHVTIASHVLIIAGGHDLNEPEF----WAVGGPVFIGDYAWICSRALLSFGADIG 223
Cdd:cd04647    1 NISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDHNHDIDDPERpieqGVTSAPIVIGDDVWIGANVVILPGVTIG 80

                         90       100
                 ....*....|....*....|....*...
gi 966369367 224 EGAVVGGNSVVSKPVPPYAIVSGPNAEI 251
Cdd:cd04647   81 DGAVVGAGSVVTKDVPPNSIVAGNPAKV 108
PRK10502 PRK10502
putative acyl transferase; Provisional
 114-255 3.29e-22

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 90.78  E-value: 3.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367 114 IPSHTLRLLWLRIGGAKIGKG----STV-----WRntevlgvdsLRIGNDSTVGWHCQLDARGGLVIGDHVTIASHVLII 184
Cdd:PRK10502  37 QPLYRWRAFLLRLFGAKIGKGvvirPSVritypWK---------LTIGDYAWIGDDVWLYNLGEITIGAHCVISQKSYLC 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966369367 185 AGGHDLNEPEFWAVGGPVFIGDYAWICSRALLSFGADIGEGAVVGGNSVVSKPVPPYAIVSGPNAEIKGER 255
Cdd:PRK10502 108 TGSHDYSDPHFDLNTAPIVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIRPR 178
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 129-246 7.24e-13

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: 65.59  E-value: 7.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367  129 AKIGKGSTVWRNTeVLGVDSlRIGN------DSTVGWHCqldargglVIGDHVTIASHVlIIAGGhdlnepefwavggpV 202
Cdd:TIGR03570 100 ASIGEGTVIMAGA-VINPDV-RIGDnviintGAIVEHDC--------VIGDFVHIAPGV-TLSGG--------------V 154

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 966369367  203 FIGDYAWICSRALLSFGADIGEGAVVGGNSVVSKPVPPYAIVSG 246
Cdd:TIGR03570 155 VIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVG 198
 
Name Accession Description Interval E-value
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
124-255 3.54e-37

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 128.45  E-value: 3.54e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367 124 LRIGGAKIGKGSTVWRNTEVLGVDsLRIGNDSTVGWHCQLDARGGLVIGDHVTIASHVLIIAGGHDLNEPE-FWAVGGPV 202
Cdd:COG0110    4 LLLFGARIGDGVVIGPGVRIYGGN-ITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPAtFPLRTGPV 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 966369367 203 FIGDYAWICSRALLSFGADIGEGAVVGGNSVVSKPVPPYAIVSGPNAEIKGER 255
Cdd:COG0110   83 TIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKR 135
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 148-251 2.36e-34

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: 119.87  E-value: 2.36e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367 148 SLRIGNDSTVGWHCQLDARGGLVIGDHVTIASHVLIIAGGHDLNEPEF----WAVGGPVFIGDYAWICSRALLSFGADIG 223
Cdd:cd04647    1 NISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDHNHDIDDPERpieqGVTSAPIVIGDDVWIGANVVILPGVTIG 80

                         90       100
                 ....*....|....*....|....*...
gi 966369367 224 EGAVVGGNSVVSKPVPPYAIVSGPNAEI 251
Cdd:cd04647   81 DGAVVGAGSVVTKDVPPNSIVAGNPAKV 108
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 149-249 8.99e-25

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: 94.98  E-value: 8.99e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367 149 LRIGNDSTVGWHCQLDARGGLVIGDHVTIASHVLIIAGGHDLNEPEFWAVGGPVFIGDYAWICSRALLSFGADIGEGAVV 228
Cdd:cd05825    4 LTIGDNSWIGEGVWIYNLAPVTIGSDACISQGAYLCTGSHDYRSPAFPLITAPIVIGDGAWVAAEAFVGPGVTIGEGAVV 83

                         90       100
                 ....*....|....*....|.
gi 966369367 229 GGNSVVSKPVPPYAIVSGPNA 249
Cdd:cd05825   84 GARSVVVRDLPAWTVYAGNPA 104
PRK10502 PRK10502
putative acyl transferase; Provisional
 114-255 3.29e-22

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 90.78  E-value: 3.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367 114 IPSHTLRLLWLRIGGAKIGKG----STV-----WRntevlgvdsLRIGNDSTVGWHCQLDARGGLVIGDHVTIASHVLII 184
Cdd:PRK10502  37 QPLYRWRAFLLRLFGAKIGKGvvirPSVritypWK---------LTIGDYAWIGDDVWLYNLGEITIGAHCVISQKSYLC 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966369367 185 AGGHDLNEPEFWAVGGPVFIGDYAWICSRALLSFGADIGEGAVVGGNSVVSKPVPPYAIVSGPNAEIKGER 255
Cdd:PRK10502 108 TGSHDYSDPHFDLNTAPIVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIRPR 178
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 169-246 3.95e-16

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: 73.35  E-value: 3.95e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367 169 LVIGDHVTIASHVLIIAGG-HDLN---------EPEFWAVG---------GPVFIGDYAWICSRALLSFGADIGEGAVVG 229
Cdd:cd03349   22 LSIGKFCSIAPGVKIGLGGnHPTDwvstypfyiFGGEWEDDakfddwpskGDVIIGNDVWIGHGATILPGVTIGDGAVIA 101

                         90
                 ....*....|....*..
gi 966369367 230 GNSVVSKPVPPYAIVSG 246
Cdd:cd03349  102 AGAVVTKDVPPYAIVGG 118
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 151-253 4.22e-16

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: 72.53  E-value: 4.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367 151 IGNDSTVGWHCQLDarGGLVIGDHVTIASHVLIIAG---------GH------DLN----EPEFWAVGGPVfIGDYAWIC 211
Cdd:cd03358    1 IGDNCIIGTNVFIE--NDVKIGDNVKIQSNVSIYEGvtieddvfiGPnvvftnDLYprskIYRKWELKGTT-VKRGASIG 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 966369367 212 SRALLSFGADIGEGAVVGGNSVVSKPVPPYAIVSGPNAEIKG 253
Cdd:cd03358   78 ANATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 149-246 3.23e-15

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: 71.30  E-value: 3.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367 149 LRIGNDSTVGWHCQ-LDarGGLV-IGDHVTIASHVLIIAGGHDLnEPE----FWAVGGPVFIGDYAWICSRALLSFGADI 222
Cdd:cd03357   63 IHIGDNFYANFNCTiLD--VAPVtIGDNVLIGPNVQIYTAGHPL-DPEernrGLEYAKPITIGDNVWIGGGVIILPGVTI 139

                         90       100
                 ....*....|....*....|....
gi 966369367 223 GEGAVVGGNSVVSKPVPPYAIVSG 246
Cdd:cd03357  140 GDNSVIGAGSVVTKDIPANVVAAG 163
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 129-246 7.88e-14

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: 68.28  E-value: 7.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367 129 AKIGKGSTVWRNTeVLGVDSlRIGND------STVGWHCqldargglVIGDHVTIASHVlIIAGGhdlnepefwavggpV 202
Cdd:cd03360   97 AVIGEGCVIMAGA-VINPDA-RIGDNviintgAVIGHDC--------VIGDFVHIAPGV-VLSGG--------------V 151

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 966369367 203 FIGDYAWICSRALLSFGADIGEGAVVGGNSVVSKPVPPYAIVSG 246
Cdd:cd03360  152 TIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVG 195
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 129-246 7.24e-13

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: 65.59  E-value: 7.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367  129 AKIGKGSTVWRNTeVLGVDSlRIGN------DSTVGWHCqldargglVIGDHVTIASHVlIIAGGhdlnepefwavggpV 202
Cdd:TIGR03570 100 ASIGEGTVIMAGA-VINPDV-RIGDnviintGAIVEHDC--------VIGDFVHIAPGV-TLSGG--------------V 154

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 966369367  203 FIGDYAWICSRALLSFGADIGEGAVVGGNSVVSKPVPPYAIVSG 246
Cdd:TIGR03570 155 VIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVG 198
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 123-260 1.85e-12

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: 65.53  E-value: 1.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367 123 WLRIG-GAKIGKGSTVWRNTeVLGVDSLRIGND------STVGWHCqldargglVIGDHVTIASHVLIiaGGHdlnepef 195
Cdd:cd03351   77 RLEIGdNNTIREFVTIHRGT-AQGGGVTRIGNNnllmayVHVAHDC--------VIGNNVILANNATL--AGH------- 138

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966369367 196 wavggpVFIGDYAWICSRALLSFGADIGEGAVVGGNSVVSKPVPPYAIVSGPNAEIKGERARGLK 260
Cdd:cd03351  139 ------VEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARLRGLNLVGLK 197
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 126-254 5.71e-12

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: 62.04  E-value: 5.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367 126 IGGAKIGKGSTVWRNTEVLG-VDSLRIGNDSTVGWHCQL--DARGGLVIGDHVTIASHVlIIAGGHdlnepefwavggpv 202
Cdd:cd04645   15 IGDVTLGEGSSVWFGAVLRGdVNPIRIGERTNIQDGSVLhvDPGYPTIIGDNVTVGHGA-VLHGCT-------------- 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 966369367 203 fIGDYAWICSRALLSFGADIGEGAVVGGNSVVS--KPVPPYAIVSGPNAEIKGE 254
Cdd:cd04645   80 -IGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPpgKVIPPGSLVAGSPAKVVRE 132
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 171-251 1.00e-10

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 59.44  E-value: 1.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367 171 IGDHVTIASHVLIIAGGHDLNEPEFWA---VGGPVFIGDYAWICSRALLSFGADIGEGAVVGGNSVVSKPVPPYAIVSGP 247
Cdd:PRK10092  96 IGDNCMLAPGVHIYTATHPLDPVARNSgaeLGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGN 175


                 ....
gi 966369367 248 NAEI 251
Cdd:PRK10092 176 PARI 179
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 144-247 1.74e-10

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: 56.68  E-value: 1.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367 144 LGVDslrIGNDSTVGWHCQLDARGGLVIGDHVTIASHVLI-----IAGGHDLNEPefwavGGPVfIGDYAWICSRALLSF 218
Cdd:cd03354    1 TGID---IHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIyqgvtLGGKGKGGGK-----RHPT-IGDNVVIGAGAKILG 71

                         90       100
                 ....*....|....*....|....*....
gi 966369367 219 GADIGEGAVVGGNSVVSKPVPPYAIVSGP 247
Cdd:cd03354   72 NITIGDNVKIGANAVVTKDVPANSTVVGV 100
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 170-260 2.18e-10

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: 59.65  E-value: 2.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367 170 VIGDHVTIASHVLIiaGGHdlnepefwavggpVFIGDYAWI---------CSrallsfgadIGEGAVVGGNSVVSKPVPP 240
Cdd:COG1043  124 VVGNNVILANNATL--AGH-------------VEVGDHAIIgglsavhqfVR---------IGAHAMVGGGSGVVKDVPP 179

                         90       100
                 ....*....|....*....|
gi 966369367 241 YAIVSGPNAEIKGERARGLK 260
Cdd:COG1043  180 YVLAAGNPARLRGLNLVGLK 199
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 126-254 6.54e-10

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 56.57  E-value: 6.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367 126 IGGAKIGKGSTVWRNTEVLG-VDSLRIGNDSTVGWHCQL--DARGGLVIGDHVTIASHVlIIAGGHdlnepefwavggpv 202
Cdd:COG0663   26 IGDVTIGEDVSVWPGAVLRGdVGPIRIGEGSNIQDGVVLhvDPGYPLTIGDDVTIGHGA-ILHGCT-------------- 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 966369367 203 fIGDYAWICSRALLSFGADIGEGAVVGGNSVVS--KPVPPYAIVSGPNAEIKGE 254
Cdd:COG0663   91 -IGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTegKVVPPGSLVVGSPAKVVRE 143
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 169-246 8.32e-10

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 57.32  E-value: 8.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367 169 LVIGDHVTIASHVLIIAGGHDLN-----EPEFWAVggPVFIGDYAWICSRALLSFGADIGEGAVVGGNSVVSKPVPPYAI 243
Cdd:PRK09527  96 VTIGDNVLIAPNVTLSVTGHPVHhelrkNGEMYSF--PITIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVV 173


                 ...
gi 966369367 244 VSG 246
Cdd:PRK09527 174 AAG 176
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 123-260 1.13e-09

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 57.34  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367 123 WLRIG-GAKIGKGSTVWRNTEVLGVDslRIGND------STVGWHCQldargglvIGDHVTIASHVLIiaGGHdlnepef 195
Cdd:PRK12461  77 RLEIGdRNVIREGVTIHRGTKGGGVT--RIGNDnllmaySHVAHDCQ--------IGNNVILVNGALL--AGH------- 137

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966369367 196 wavggpVFIGDYAWICSRALLSFGADIGEGAVVGGNSVVSKPVPPYAIVSGPNAEIKGERARGLK 260
Cdd:PRK12461 138 ------VTVGDRAIISGNCLVHQFCRIGALAMMAGGSRISKDVPPYCMMAGHPTNVHGLNAVGLR 196
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 126-260 4.09e-09

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


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 55.73  E-value: 4.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367  126 IGGAKIGKGSTVWRNTeVLGVD-----------SLRIGNDST-------------------VGWHCQLDARGGL----VI 171
Cdd:TIGR01852  44 LGHTTIGEGTRIFPGA-VIGGVpqdlkykgektRLIIGDNNTirefvtinrgtasgggvtrIGNNNLLMAYSHIahdcVV 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367  172 GDHVTIASHVLIiaGGHdlnepefwavggpVFIGDYAWICSRALLSFGADIGEGAVVGGNSVVSKPVPPYAIVSGPNAEI 251
Cdd:TIGR01852 123 GNHVILANNATL--AGH-------------VEVGDYAIIGGLVAVHQFVRIGRYAMIGGLSAVSKDVPPYCLAEGNRARL 187


                  ....*....
gi 966369367  252 KGERARGLK 260
Cdd:TIGR01852 188 RGLNIVGLR 196
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
150-260 5.97e-09

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 55.49  E-value: 5.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367 150 RIGND------STVGWHCqldargglVIGDHVTIASHVLIiaGGHdlnepefwavggpVFIGDYAWI--CSrALLSFgAD 221
Cdd:PRK05289 107 RIGDNnllmayVHVAHDC--------VVGNHVILANNATL--AGH-------------VEVGDYAIIggLT-AVHQF-VR 161

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 966369367 222 IGEGAVVGGNSVVSKPVPPYAIVSGPNAEIKGERARGLK 260
Cdd:PRK05289 162 IGAHAMVGGMSGVSQDVPPYVLAEGNPARLRGLNLVGLK 200
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 142-251 7.87e-09

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 54.11  E-value: 7.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367 142 EVLGVDSLRIGNDSTVGWHCQLDARGGLVIGDHVTIASHVLIIAGGH-DLNEPEFWAVGG-----------PVFIGDYAW 209
Cdd:PRK09677  59 DAFGRGKLFFGDNVQVNDYVHIACIESITIGRDTLIASKVFITDHNHgSFKHSDDFSSPNlppdmrtlessAVVIGQRVW 138

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 966369367 210 ICSRALLSFGADIGEGAVVGGNSVVSKPVPPYAIVSGPNAEI 251
Cdd:PRK09677 139 IGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKI 180
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 155-234 1.09e-08

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: 51.10  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367 155 STVGWHCQLDA----RGGLVIGDHVTIASHVLIIAGGHDLNepefwavGGPVFIGDYAWICSRALLSFGADIGEGAVVGG 230
Cdd:cd00208    1 VFIGEGVKIHPkaviRGPVVIGDNVNIGPGAVIGAATGPNE-------KNPTIIGDNVEIGANAVIHGGVKIGDNAVIGA 73


                 ....
gi 966369367 231 NSVV 234
Cdd:cd00208   74 GAVV 77
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 170-255 1.76e-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: 50.08  E-value: 1.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367 170 VIGDHVTIASHVLIIAGGhdlnepefWAVGG--PVfIGDYAWICSRALLsFGAD-IGEGAVVGGNSVVSKPVPPYAIVSG 246
Cdd:COG1045   93 VIGDNVTIYQGVTLGGTG--------KEKGKrhPT-IGDNVVIGAGAKI-LGPItIGDNAKIGANSVVLKDVPPGSTVVG 162


                 ....*....
gi 966369367 247 PNAEIKGER 255
Cdd:COG1045  163 VPARIVKRK 171
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 126-251 2.02e-07

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: 49.49  E-value: 2.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367 126 IGGAKIGKGSTVWRNTEVLG-VDSLRIGNDSTVGWHCQLDARGG--LVIGDHVTIAsHVLIIAGGHdlnepefwavggpv 202
Cdd:cd04650   16 IGDVVIGELTSVWHYAVIRGdNDSIYIGKYSNVQENVSIHTDHGypTEIGDYVTIG-HNAVVHGAK-------------- 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 966369367 203 fIGDYAWICSRALLSFGADIGEGAVVGGNSVVS--KPVPPYAIVSGPNAEI 251
Cdd:cd04650   81 -VGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTpgKEIPDYSLVLGVPAKV 130
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 150-246 1.69e-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: 47.40  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367 150 RIGNDSTVGWHCQLDaRGGL---VIGDHVTIASHVLI-----------IAGGHdlnepefwAVGGPVFIGDYAWICSRAL 215
Cdd:cd03352   94 IIGDDVEIGANTTID-RGALgdtVIGDGTKIDNLVQIahnvrigenclIAAQV--------GIAGSTTIGDNVIIGGQVG 164

                         90       100       110
                 ....*....|....*....|....*....|.
gi 966369367 216 LSFGADIGEGAVVGGNSVVSKPVPPYAIVSG 246
Cdd:cd03352  165 IAGHLTIGDGVVIGAGSGVTSIVPPGEYVSG 195
cysE PRK11132
serine acetyltransferase; Provisional
 221-253 2.26e-04

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 41.61  E-value: 2.26e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 966369367 221 DIGEGAVVGGNSVVSKPVPPYAIVSGPNAEIKG 253
Cdd:PRK11132 213 EVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVG 245
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 201-243 5.08e-04

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 40.90  E-value: 5.08e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 966369367 201 PVFIGDYAWICSRALLSFGADIGEGAVVGGNSVVSKPVPPYAI 243
Cdd:PRK14357 383 PTFIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSL 425
PLN02739 PLN02739
serine acetyltransferase
 139-253 7.44e-04

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 40.40  E-value: 7.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367 139 RNTEVLGVDslrIGNDSTVGWHCQLDARGGLVIGDHVTIASHVLIIAG------GHDLNE--PEfwavggpvfIGDYAWI 210
Cdd:PLN02739 199 RVSEVFGID---IHPAARIGKGILLDHGTGVVIGETAVIGDRVSILHGvtlggtGKETGDrhPK---------IGDGALL 266

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 966369367 211 CSRALLSFGADIGEGAVVGGNSVVSKPVPPYAIVSGPNAEIKG 253
Cdd:PLN02739 267 GACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIG 309
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 171-245 8.61e-04

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: 38.52  E-value: 8.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367 171 IGDHVTIASHVLIiagGHDLNEPEfwavGGPVFIGDYAWICSRALLSFGADIGEGAVVGGNSVVSK-------------- 236
Cdd:cd03350   52 IGKNVHLSAGAVI---GGVLEPLQ----ATPVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTQstpiydretgeiyy 124

                         90
                 ....*....|
gi 966369367 237 -PVPPYAIVS 245
Cdd:cd03350  125 gRVPPGSVVV 134
PLN02694 PLN02694
serine O-acetyltransferase
 101-262 1.59e-03

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 39.24  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367 101 RTWEQAYNILICKIPSHTLRLLWLRIG-GAKIGKGSTVWRNTEVLGVDSLRIGNDSTVGWHCQLDARGGLVIGDHVTIAS 179
Cdd:PLN02694 138 KLWTQSRRPLALALHSRISDVFAVDIHpAAKIGKGILFDHATGVVIGETAVIGNNVSILHHVTLGGTGKACGDRHPKIGD 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367 180 HVLIIAGGHDLNEpefwavggpvfigdyawicsrallsfgADIGEGAVVGGNSVVSKPVPPYAIVSGPNAEIKGERARGL 259
Cdd:PLN02694 218 GVLIGAGATILGN---------------------------VKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLVGGKEKPA 270


                 ...
gi 966369367 260 KYK 262
Cdd:PLN02694 271 KHE 273
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 122-246 1.78e-03

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: 39.73  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367  122 LWLRIGGAKIGKGstVWRNTEVLGVDSL-RIGNDSTVGWHCQLDA---RGGLVIGDHVTiashvliiagghdlnepefwa 197
Cdd:TIGR02353 591 AILRLLGVKIGRG--VYIDGTDLTERDLvTIGDDSTLNEGSVIQThlfEDRVMKSDTVT--------------------- 647

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 966369367  198 vggpvfIGDYAWICSRALLSFGADIGEGAVVGGNSVVSK--PVPPYAIVSG 246
Cdd:TIGR02353 648 ------IGDGATLGPGAIVLYGVVMGEGSVLGPDSLVMKgeEVPAHTRWRG 692
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 127-183 6.31e-03

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: 34.92  E-value: 6.31e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966369367 127 GGAKIGKGSTVWRNTEVLGVDSLRIGNDSTVGWHCQLDAR----GGLVIGDHVTIASHVLI 183
Cdd:cd00208   17 GPVVIGDNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGANavihGGVKIGDNAVIGAGAVV 77
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 147-230 8.58e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 37.04  E-value: 8.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367 147 DSLRIGNDSTVGWHCqldargglVIGDHVTIASHVLIIAGghdlnepefwAVGGP-VFIGDYAWICSRALLSFGADIGE- 224
Cdd:PRK00892 111 PSAKIGEGVSIGPNA--------VIGAGVVIGDGVVIGAG----------AVIGDgVKIGADCRLHANVTIYHAVRIGNr 172

                         90
                 ....*....|.
gi 966369367 225 -----GAVVGG 230
Cdd:PRK00892 173 viihsGAVIGS 183
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 147-230 8.81e-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: 36.92  E-value: 8.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966369367 147 DSLRIGNDSTVGWHCQLDArgGLVIGDHVTIASHVLIiagGHDlnepefwavggpVFIGDYAWICSRALLSFGADIGE-- 224
Cdd:COG1044  107 PSAKIGEGVSIGPFAVIGA--GVVIGDGVVIGPGVVI---GDG------------VVIGDDCVLHPNVTIYERCVIGDrv 169

                         90
                 ....*....|
gi 966369367 225 ----GAVVGG 230
Cdd:COG1044  170 iihsGAVIGA 179
 
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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