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Conserved domains on  [gi|2542751027|ref|WP_298698977|]
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sugar O-acetyltransferase [uncultured Rothia sp.]

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 ...
 49-188 1.15e-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: 182.24  E-value: 1.15e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  49 EQAQAMHVYREHLGHLGEHSHIRPGARFDYGVNTYIGDGSFFNFGCVFLDVCPIRIGSTVLVGNNVQFLTPTHPLNPVDR 128
Cdd:cd03357    30 DAEERRELLKELFGSVGENVYIEPPFHCDYGYNIHIGDNFYANFNCTILDVAPVTIGDNVLIGPNVQIYTAGHPLDPEER 109

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027 129 AAYWEGGEPITVEDNVWIGGGAIILGGVTVGKNSVIGAGTVVTEDVPENSLVVGNPGRVI 188
Cdd:cd03357   110 NRGLEYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
 
Name Accession Description Interval E-value
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 49-188 1.15e-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: 182.24  E-value: 1.15e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  49 EQAQAMHVYREHLGHLGEHSHIRPGARFDYGVNTYIGDGSFFNFGCVFLDVCPIRIGSTVLVGNNVQFLTPTHPLNPVDR 128
Cdd:cd03357    30 DAEERRELLKELFGSVGENVYIEPPFHCDYGYNIHIGDNFYANFNCTILDVAPVTIGDNVLIGPNVQIYTAGHPLDPEER 109

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027 129 AAYWEGGEPITVEDNVWIGGGAIILGGVTVGKNSVIGAGTVVTEDVPENSLVVGNPGRVI 188
Cdd:cd03357   110 NRGLEYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 14-191 3.76e-45

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 148.42  E-value: 3.76e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  14 RMVSGAAYMPDAECAAQtKRIHAATVLAE-EHYARGEQAQAMHVYREHLGHLGEhSHIRPGARFDYGVNTYIGDGSFFNF 92
Cdd:PRK10092    7 KMIAGELYRSADETLSR-DRLRARQLIHRyNHSLPDEHTLRQQILADLFGQVTE-AYIEPTFRCDYGYNIFLGNNFYANF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  93 GCVFLDVCPIRIGSTVLVGNNVQFLTPTHPLNPVDRAAYWEGGEPITVEDNVWIGGGAIILGGVTVGKNSVIGAGTVVTE 172
Cdd:PRK10092   85 DCVMLDVCPIRIGDNCMLAPGVHIYTATHPLDPVARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTK 164

                         170
                  ....*....|....*....
gi 2542751027 173 DVPENSLVVGNPGRVIRTL 191
Cdd:PRK10092  165 DVPDNVVVGGNPARIIKKL 183
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
54-196 2.51e-39

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 132.30  E-value: 2.51e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  54 MHVYREHLGHLGEHSHIRPGARFdYGVNTYIGDGSFFNFGCVFLDVCPIRIGSTVLVGNNVQFLTPTHPLNpvDRAAYWE 133
Cdd:COG0110     1 MKLLLLFGARIGDGVVIGPGVRI-YGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPID--DPATFPL 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2542751027 134 GGEPITVEDNVWIGGGAIILGGVTVGKNSVIGAGTVVTEDVPENSLVVGNPGRVIRTLDENER 196
Cdd:COG0110    78 RTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEEER 140
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 59-184 1.59e-08

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: 1.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  59 EHLGHLGEHSHIRPGARFdyGVNTYIGDGSFfnfgcvfldvcpIRIGSTVLVGnnvqfltpthplnpvdraayweggepi 138
Cdd:TIGR03570 133 EHDCVIGDFVHIAPGVTL--SGGVVIGEGVF------------IGAGATIIQG--------------------------- 171

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2542751027 139 tvednvwigggaiilggVTVGKNSVIGAGTVVTEDVPENSLVVGNP 184
Cdd:TIGR03570 172 -----------------VTIGAGAIVGAGAVVTKDIPDGGVVVGVP 200
 
Name Accession Description Interval E-value
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 49-188 1.15e-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: 182.24  E-value: 1.15e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  49 EQAQAMHVYREHLGHLGEHSHIRPGARFDYGVNTYIGDGSFFNFGCVFLDVCPIRIGSTVLVGNNVQFLTPTHPLNPVDR 128
Cdd:cd03357    30 DAEERRELLKELFGSVGENVYIEPPFHCDYGYNIHIGDNFYANFNCTILDVAPVTIGDNVLIGPNVQIYTAGHPLDPEER 109

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027 129 AAYWEGGEPITVEDNVWIGGGAIILGGVTVGKNSVIGAGTVVTEDVPENSLVVGNPGRVI 188
Cdd:cd03357   110 NRGLEYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 14-191 3.76e-45

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 148.42  E-value: 3.76e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  14 RMVSGAAYMPDAECAAQtKRIHAATVLAE-EHYARGEQAQAMHVYREHLGHLGEhSHIRPGARFDYGVNTYIGDGSFFNF 92
Cdd:PRK10092    7 KMIAGELYRSADETLSR-DRLRARQLIHRyNHSLPDEHTLRQQILADLFGQVTE-AYIEPTFRCDYGYNIFLGNNFYANF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  93 GCVFLDVCPIRIGSTVLVGNNVQFLTPTHPLNPVDRAAYWEGGEPITVEDNVWIGGGAIILGGVTVGKNSVIGAGTVVTE 172
Cdd:PRK10092   85 DCVMLDVCPIRIGDNCMLAPGVHIYTATHPLDPVARNSGAELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTK 164

                         170
                  ....*....|....*....
gi 2542751027 173 DVPENSLVVGNPGRVIRTL 191
Cdd:PRK10092  165 DVPDNVVVGGNPARIIKKL 183
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
54-196 2.51e-39

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 132.30  E-value: 2.51e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  54 MHVYREHLGHLGEHSHIRPGARFdYGVNTYIGDGSFFNFGCVFLDVCPIRIGSTVLVGNNVQFLTPTHPLNpvDRAAYWE 133
Cdd:COG0110     1 MKLLLLFGARIGDGVVIGPGVRI-YGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPID--DPATFPL 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2542751027 134 GGEPITVEDNVWIGGGAIILGGVTVGKNSVIGAGTVVTEDVPENSLVVGNPGRVIRTLDENER 196
Cdd:COG0110    78 RTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEEER 140
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 9-199 1.47e-30

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 111.63  E-value: 1.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027   9 GDIFNRMVSGaayMPDaecaaqtKRIHAATVLAEEHYAR-GEQAQAMHVYREHLGHLGEHSHIRPGARFDYGVNTYIGDG 87
Cdd:PRK09527   12 GKLFTDMCEG---LPE-------KRLRGKTLMYEFNHSHpSEVEKRESLIKEMFATVGENAWVEPPVYFSYGSNIHIGRN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  88 SFFNFGCVFLDVCPIRIGSTVLVGNNVQFLTPTHPLNPVDRaaywEGGE----PITVEDNVWIGGGAIILGGVTVGKNSV 163
Cdd:PRK09527   82 FYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGHPVHHELR----KNGEmysfPITIGNNVWIGSHVVINPGVTIGDNSV 157

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2542751027 164 IGAGTVVTEDVPENSLVVGNPGRVIRTLDENERPAY 199
Cdd:PRK09527  158 IGAGSVVTKDIPPNVVAAGVPCRVIREINDRDKQYY 193
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 84-188 3.89e-30

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: 107.54  E-value: 3.89e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  84 IGDGSFFNFGCVFLDVCPIRIGSTVLVGNNVQFLTPTHPLNPVDRAAY-WEGGEPITVEDNVWIGGGAIILGGVTVGKNS 162
Cdd:cd04647     4 IGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDHNHDIDDPERPIEqGVTSAPIVIGDDVWIGANVVILPGVTIGDGA 83

                          90       100
                  ....*....|....*....|....*.
gi 2542751027 163 VIGAGTVVTEDVPENSLVVGNPGRVI 188
Cdd:cd04647    84 VVGAGSVVTKDVPPNSIVAGNPAKVI 109
PRK10502 PRK10502
putative acyl transferase; Provisional
 65-190 1.53e-16

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 74.22  E-value: 1.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  65 GEHSHIRPGARFDYGVNTYIGDGSFFNFGCVFLDVCPIRIGSTVLVGNNVQFLTPTHPLnpvDRAAYWEGGEPITVEDNV 144
Cdd:PRK10502   55 GKGVVIRPSVRITYPWKLTIGDYAWIGDDVWLYNLGEITIGAHCVISQKSYLCTGSHDY---SDPHFDLNTAPIVIGEGC 131

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2542751027 145 WIGGGAIILGGVTVGKNSVIGAGTVVTEDVPENSLVVGNPGRVIRT 190
Cdd:PRK10502  132 WLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIRP 177
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 79-189 1.37e-14

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: 67.53  E-value: 1.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  79 GVNTYIGDGSFFNFGCVFLDVCPIR----IGSTVLVGNNVqFLTP----THPLNPvdRAAYWEGGE--PITVEDNVWIGG 148
Cdd:cd03358     2 GDNCIIGTNVFIENDVKIGDNVKIQsnvsIYEGVTIEDDV-FIGPnvvfTNDLYP--RSKIYRKWElkGTTVKRGASIGA 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2542751027 149 GAIILGGVTVGKNSVIGAGTVVTEDVPENSLVVGNPGRVIR 189
Cdd:cd03358    79 NATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 81-189 3.32e-13

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: 64.49  E-value: 3.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  81 NTYIGDGSFFNFGCVFLDVCPIRIGSTVLVGNNVQFLT-PTHPLNPV------DRAAYWEGGE---------PITVEDNV 144
Cdd:cd03349     1 NISVGDYSYGSGPDCDVGGDKLSIGKFCSIAPGVKIGLgGNHPTDWVstypfyIFGGEWEDDAkfddwpskgDVIIGNDV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2542751027 145 WIGGGAIILGGVTVGKNSVIGAGTVVTEDVPENSLVVGNPGRVIR 189
Cdd:cd03349    81 WIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIR 125
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 70-190 3.90e-13

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: 64.72  E-value: 3.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  70 IRPGARfdygvntyIGDGSFF--NFGCVfldvcpirIGSTVLVGNNVQFL------------TPTHPlnpvdraaywegg 135
Cdd:COG1045    68 IHPGAT--------IGRGFFIdhGTGVV--------IGETAVIGDNVTIYqgvtlggtgkekGKRHP------------- 118

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2542751027 136 epiTVEDNVWIGGGAIILGGVTVGKNSVIGAGTVVTEDVPENSLVVGNPGRVIRT 190
Cdd:COG1045   119 ---TIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVKR 170
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 84-188 1.54e-12

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: 61.47  E-value: 1.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  84 IGDGSFFNFGCVFLDVCPIRIGSTVLVGNNVQFLTPTH----PLNPVDRAayweggePITVEDNVWIGGGAIILGGVTVG 159
Cdd:cd05825     6 IGDNSWIGEGVWIYNLAPVTIGSDACISQGAYLCTGSHdyrsPAFPLITA-------PIVIGDGAWVAAEAFVGPGVTIG 78

                          90       100
                  ....*....|....*....|....*....
gi 2542751027 160 KNSVIGAGTVVTEDVPENSLVVGNPGRVI 188
Cdd:cd05825    79 EGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 84-196 1.50e-11

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: 60.12  E-value: 1.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  84 IGDGSFFNFGCVfL--DVCPIRIG----------------STVLVGNNVqflTPTHplNPVDRAAyweggepiTVEDNVW 145
Cdd:cd04645    20 LGEGSSVWFGAV-LrgDVNPIRIGertniqdgsvlhvdpgYPTIIGDNV---TVGH--GAVLHGC--------TIGDNCL 85

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2542751027 146 IGGGAIILGGVTVGKNSVIGAGTVVTED--VPENSLVVGNPGRVIRTLDENER 196
Cdd:cd04645    86 IGMGAIILDGAVIGKGSIVAAGSLVPPGkvIPPGSLVAGSPAKVVRELTDEEI 138
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 69-184 3.87e-11

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: 57.84  E-value: 3.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  69 HIRPGARFDYGVntYIGDGSffnfGCVfldvcpirIGSTVLVGNNV---QFLTpthplnpVDRAAYWEGGEPITVEDNVW 145
Cdd:cd03354     4 DIHPGAKIGPGL--FIDHGT----GIV--------IGETAVIGDNCtiyQGVT-------LGGKGKGGGKRHPTIGDNVV 62

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2542751027 146 IGGGAIILGGVTVGKNSVIGAGTVVTEDVPENSLVVGNP 184
Cdd:cd03354    63 IGAGAKILGNITIGDNVKIGANAVVTKDVPANSTVVGVP 101
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 156-196 4.37e-11

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 59.27  E-value: 4.37e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2542751027 156 VTVGKNSVIGAGTVVTED--VPENSLVVGNPGRVIRTLDENER 196
Cdd:COG0663   107 AVIGDGSIVGAGALVTEGkvVPPGSLVVGSPAKVVRELTEEEI 149
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 74-192 1.27e-09

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 55.65  E-value: 1.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  74 ARFDYGVNTYIGDgsFFNFGCVFldvcPIRIGSTVLVGNNVqFLT------PTHP-------LNPVDRAAyweGGEPITV 140
Cdd:PRK09677   64 GKLFFGDNVQVND--YVHIACIE----SITIGRDTLIASKV-FITdhnhgsFKHSddfsspnLPPDMRTL---ESSAVVI 133

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2542751027 141 EDNVWIGGGAIILGGVTVGKNSVIGAGTVVTEDVPENSLVVGNPGRVIRTLD 192
Cdd:PRK09677  134 GQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKKYN 185
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 63-184 2.08e-09

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: 55.18  E-value: 2.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  63 HLGEHSHIRPGARFdyGVNTYIGDGSFFNFGCVfldvcpirIGSTVLVGNNVqFLTPTHPLNpvdraayweGGepITVED 142
Cdd:cd03360    98 VIGEGCVIMAGAVI--NPDARIGDNVIINTGAV--------IGHDCVIGDFV-HIAPGVVLS---------GG--VTIGE 155

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2542751027 143 NVWIGGGAIILGGVTVGKNSVIGAGTVVTEDVPENSLVVGNP 184
Cdd:cd03360   156 GAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 63-182 1.55e-08

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 53.88  E-value: 1.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  63 HLGEHSHIrpG-------ARFDYGVN----TYIGD---GSFFNFGC--VFldvC--------PIRIGSTVLVGNNVQFLT 118
Cdd:COG1207   337 VLGEGVKI--GnfvevknSTIGEGSKvnhlSYIGDaeiGEGVNIGAgtIT---CnydgvnkhRTVIGDGAFIGSNTNLVA 411

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2542751027 119 PthplnpvdraayweggepitvednvwigggaiilggVTVGKNSVIGAGTVVTEDVPENSLVVG 182
Cdd:COG1207   412 P------------------------------------VTIGDGATIGAGSTITKDVPAGALAIA 439
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 59-184 1.59e-08

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: 1.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  59 EHLGHLGEHSHIRPGARFdyGVNTYIGDGSFfnfgcvfldvcpIRIGSTVLVGnnvqfltpthplnpvdraayweggepi 138
Cdd:TIGR03570 133 EHDCVIGDFVHIAPGVTL--SGGVVIGEGVF------------IGAGATIIQG--------------------------- 171

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2542751027 139 tvednvwigggaiilggVTVGKNSVIGAGTVVTEDVPENSLVVGNP 184
Cdd:TIGR03570 172 -----------------VTIGAGAIVGAGAVVTKDIPDGGVVVGVP 200
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 63-182 3.27e-08

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 51.65  E-value: 3.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  63 HLGEHSHIRPGARFDYGVN---------------------TYIGD---GSFFNFGC--VFldvC--------PIRIGSTV 108
Cdd:cd03353    75 TVGPFAHLRPGTVLGEGVHignfveikkstigegskanhlSYLGDaeiGEGVNIGAgtIT---CnydgvnkhRTVIGDNV 151

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2542751027 109 LVGNNVQFLTPthplnpvdraayweggepitvednvwigggaiilggVTVGKNSVIGAGTVVTEDVPENSLVVG 182
Cdd:cd03353   152 FIGSNSQLVAP------------------------------------VTIGDGATIAAGSTITKDVPPGALAIA 189
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 158-195 2.19e-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: 48.72  E-value: 2.19e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2542751027 158 VGKNSVIGAGTVVTE--DVPENSLVVGNPGRVIRTLDENE 195
Cdd:cd04650    99 IGDHVIIGAGAVVTPgkEIPDYSLVLGVPAKVVRKLTEEE 138
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 137-189 4.36e-07

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 49.76  E-value: 4.36e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2542751027 137 PITVEDNVWIGGGAIILGGVTVGKNSVIGAGTVVTEDVPENSLVVGNPGRVIR 189
Cdd:PRK14357  383 PTFIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQIVK 435
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 82-190 1.65e-06

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 47.82  E-value: 1.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  82 TYIGD---GSFFNFGCVFLdVC--------PIRIGSTVLVGNNVQFLTPthplnpvdraayweggepitvednvwiggga 150
Cdd:PRK14355  368 TYLGDatiGRNVNIGCGTI-TCnydgvkkhRTVIEDDVFVGSDVQFVAP------------------------------- 415

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2542751027 151 iilggVTVGKNSVIGAGTVVTEDVPENSLVVGNPGRVIRT 190
Cdd:PRK14355  416 -----VTVGRNSLIAAGTTVTKDVPPDSLAIARSPQVNKE 450
PLN02739 PLN02739
serine acetyltransferase
 70-205 1.99e-06

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 47.72  E-value: 1.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  70 IRPGARfdygvntyIGDGSFFNFGCvfldvcPIRIGSTVLVGNNVQFLtptHPLNpVDRAAYWEGGEPITVEDNVWIGGG 149
Cdd:PLN02739  208 IHPAAR--------IGKGILLDHGT------GVVIGETAVIGDRVSIL---HGVT-LGGTGKETGDRHPKIGDGALLGAC 269

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2542751027 150 AIILGGVTVGKNSVIGAGTVVTEDVPENSLVVGNPGRVIRTLDENErPAYPHTYSA 205
Cdd:PLN02739  270 VTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFVDEQD-PSLTMEYDA 324
PLN02694 PLN02694
serine O-acetyltransferase
 70-210 3.08e-06

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 46.94  E-value: 3.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  70 IRPGARfdygvntyIGDGSFFNFGCvfldvcPIRIGSTVLVGNNVQFLTPThPLNPVDRAAyweGGEPITVEDNVWIGGG 149
Cdd:PLN02694  163 IHPAAK--------IGKGILFDHAT------GVVIGETAVIGNNVSILHHV-TLGGTGKAC---GDRHPKIGDGVLIGAG 224

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2542751027 150 AIILGGVTVGKNSVIGAGTVVTEDVPENSLVVGNPGRVIrtlDENERPAYPHTYSAEALEE 210
Cdd:PLN02694  225 ATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLV---GGKEKPAKHEECPGESMDH 282
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 65-182 3.86e-06

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 46.75  E-value: 3.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  65 GEHSHIRPGARFDYGVN---------------------TYIGD---GSFFNFGCvfldvcpirigSTVLV---GNNvQFL 117
Cdd:PRK14354  326 GPFAHLRPGSVIGEEVKignfveikkstigegtkvshlTYIGDaevGENVNIGC-----------GTITVnydGKN-KFK 393

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2542751027 118 TpthplnpvdraayweggepiTVEDNVWIGGGAIILGGVTVGKNSVIGAGTVVTEDVPENSLVVG 182
Cdd:PRK14354  394 T--------------------IIGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDALAIA 438
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 63-195 7.43e-06

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


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 44.28  E-value: 7.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  63 HLGEHSHIRPGA--RFDYGVnTYIGDGSFFNFGCVFldvcPIRIGSTVLVGNNvqfltpTHplnpVDRAAYWEGGepiTV 140
Cdd:cd04745    20 IIGKNCYIGPHAslRGDFGR-IVIRDGANVQDNCVI----HGFPGQDTVLEEN------GH----IGHGAILHGC---TI 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2542751027 141 EDNVWIGGGAIILGGVTVGKNSVIGAGTVVTE--DVPENSLVVGNPGRVIRTLDENE 195
Cdd:cd04745    82 GRNALVGMNAVVMDGAVIGEESIVGAMAFVKAgtVIPPRSLIAGSPAKVIRELSDEE 138
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 156-213 8.24e-06

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 45.70  E-value: 8.24e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2542751027 156 VTVGKNSVIGAGTVVTEDVPENSLVV-GNPGRVIRTLDENERPAYPhtySAEALEEARA 213
Cdd:PRK14352  418 VTVGDGAYTGAGTVIREDVPPGALAVsEGPQRNIEGWVQRKRPGTP---AAEAAEAASE 473
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 64-181 2.07e-05

2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP succinyltransferase): THDP N-succinyltransferase catalyzes the conversion of tetrahydrodipicolinate and succinyl-CoA to N-succinyltetrahydrodipicolinate and CoA. It is the committed step in the succinylase pathway by which bacteria synthesize L-lysine and meso-diaminopimelate, a component of peptidoglycan. The enzyme is homotrimeric and each subunit contains an N-terminal region with alpha helices and hairpin loops, as well as a C-terminal region with a left-handed parallel alpha-helix (LbH) structural motif encoded by hexapeptide repeat motifs.


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 42.75  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  64 LGEHSHIRPGARFDYGvnTYIGDGSFFNFGCVfldvcpirIGSTVLVGNNVQFLTPTH---PLNPVDRAayweggePITV 140
Cdd:cd03350    16 IGPGAVLMMPSYVNIG--AYVDEGTMVDSWAT--------VGSCAQIGKNVHLSAGAViggVLEPLQAT-------PVII 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2542751027 141 EDNVWIGGGAIILGGVTVGKNSVIGAGTVVT---------------EDVPENSLVV 181
Cdd:cd03350    79 EDDVFIGANCEVVEGVIVGKGAVLAAGVVLTqstpiydretgeiyyGRVPPGSVVV 134
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 156-182 2.70e-05

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 44.33  E-value: 2.70e-05
                          10        20
                  ....*....|....*....|....*..
gi 2542751027 156 VTVGKNSVIGAGTVVTEDVPENSLVVG 182
Cdd:PRK14356  417 VTIGDGALVGAGSVITKDVPDGSLAIA 443
PLN02296 PLN02296
carbonate dehydratase
 84-196 2.83e-05

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 43.96  E-value: 2.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  84 IGDGSFFNFGCVFL-DVCPIRIGStvlvGNNVQFLTPTHplnpVDRAAYWEGGEPI-----------------TVEDNVW 145
Cdd:PLN02296   73 VGRGSSIWYGCVLRgDVNSISVGS----GTNIQDNSLVH----VAKTNLSGKVLPTiigdnvtighsavlhgcTVEDEAF 144

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2542751027 146 IGGGAIILGGVTVGKNSVIGAGTVVTED--VPENSLVVGNPGRVIRTLDENER 196
Cdd:PLN02296  145 VGMGATLLDGVVVEKHAMVAAGALVRQNtrIPSGEVWAGNPAKFLRKLTEEEI 197
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 83-171 3.38e-05

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: 40.70  E-value: 3.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  83 YIGDGSFFNFGCVFLDvcPIRIGSTVLVGNNVQFLTPTHPlnpvdraaywEGGEPITVEDNVWIGGGAIILGGVTVGKNS 162
Cdd:cd00208     2 FIGEGVKIHPKAVIRG--PVVIGDNVNIGPGAVIGAATGP----------NEKNPTIIGDNVEIGANAVIHGGVKIGDNA 69


                  ....*....
gi 2542751027 163 VIGAGTVVT 171
Cdd:cd00208    70 VIGAGAVVT 78
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 156-189 5.15e-05

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 43.38  E-value: 5.15e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2542751027 156 VTVGKNSVIGAGTVVTEDVPENSLVVGNPGRVIR 189
Cdd:PRK14360  409 ITLGEDVTVAAGSTITKDVPDNSLAIARSRQVIK 442
PRK10191 PRK10191
putative acyl transferase; Provisional
 156-187 5.71e-05

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 41.80  E-value: 5.71e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2542751027 156 VTVGKNSVIGAGTVVTEDVPENSLVVGNPGRV 187
Cdd:PRK10191  111 ITIGNNVTVGAGSVVLDSVPDNALVVGEKARV 142
PLN02357 PLN02357
serine acetyltransferase
 70-188 8.40e-05

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 42.56  E-value: 8.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  70 IRPGARfdygvntyIGDGsffnfgcVFLD-VCPIRIGSTVLVGNNVQFLTPThPLNPVDRAAyweGGEPITVEDNVWIGG 148
Cdd:PLN02357  229 IHPGAK--------IGQG-------ILLDhATGVVIGETAVVGNNVSILHNV-TLGGTGKQS---GDRHPKIGDGVLIGA 289

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2542751027 149 GAIILGGVTVGKNSVIGAGTVVTEDVPENSLVVGNPGRVI 188
Cdd:PLN02357  290 GTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLI 329
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 156-190 9.41e-05

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 42.54  E-value: 9.41e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2542751027 156 VTVGKNSVIGAGTVVTEDVPENSLVVGNPGRVIRT 190
Cdd:PRK14353  399 VTIGDGAYIASGSVITEDVPDDALALGRARQETKP 433
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 156-181 1.38e-04

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 41.94  E-value: 1.38e-04
                          10        20
                  ....*....|....*....|....*.
gi 2542751027 156 VTVGKNSVIGAGTVVTEDVPENSLVV 181
Cdd:PRK09451  413 VTVGKGATIGAGTTVTRDVAENELVI 438
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 66-187 4.35e-04

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: 40.11  E-value: 4.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  66 EHSHIRPGARFDYGVnTYIGDGsffnfgCVFLDVCPI----RIGSTVLVGNNVQFltpthplnpvdraayweGGEpITVE 141
Cdd:cd03351    88 EFVTIHRGTAQGGGV-TRIGNN------NLLMAYVHVahdcVIGNNVILANNATL-----------------AGH-VEIG 142

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2542751027 142 DNVWIGGGAIILGGVTVGKNSVIGAGTVVTEDVPENSLVVGNPGRV 187
Cdd:cd03351   143 DYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARL 188
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 64-215 1.02e-03

Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p25 is part of the pointed-end subcomplex in dynactin that also includes p26, p27, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100049 [Multi-domain]  Cd Length: 161  Bit Score: 38.35  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542751027  64 LGEHSHIRPGARFDYGVNTY----IGDGSFFNFGCVfldVCPIRIGSTVLVGNNVQFltpthplnpvdraaywegGEPIT 139
Cdd:cd03359    51 LSEGCVIRPPFKKFSKGVAFfplhIGDYVFIGENCV---VNAAQIGSYVHIGKNCVI------------------GRRCI 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2542751027 140 VEDNVWigggaiilggvtVGKNSVIGAGTVvtedVPENSLVVGNPGRVIRTLdenerpayPHTYSAEALEEARAFY 215
Cdd:cd03359   110 IKDCVK------------ILDGTVVPPDTV----IPPYSVVSGRPARFIGEL--------PECTQELMEEETKEYY 161
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 139-184 3.87e-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: 3.87e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2542751027 139 TVEDNVWIGGGAIILGGVTVGKNSVIGAGTVVTEDVPENSLVVGNP 184
Cdd:cd03352   152 TIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTP 197
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 104-181 7.87e-03

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 36.89  E-value: 7.87e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2542751027 104 IGSTVLVGNNVQFLTPthplnpvdraayweggepITVEDNVwigggaiilggvtvgknsVIGAGTVVTEDVPENSLVV 181
Cdd:PRK14359  370 IGKNVFIGSDTQLVAP------------------VNIEDNV------------------LIAAGSTVTKDVPKGSLAI 411
 
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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