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Conserved domains on  [gi|1543020207|gb|AZQ85451|]
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acyltransferase [Colwellia sp. Arc7-635]

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];
1-111 2.34e-34

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


:

Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 115.74  E-value: 2.34e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   1 MQIGANTYIGRNSSLSCH--VSIANDVLVASNVSFVGGDHKIDNISTNINLSGRdeikcITVESNVWIGHGVIVMHGVTL 78
Cdd:COG0110    28 ITIGDNVYIGPGVTIDDPggITIGDNVLIGPGVTILTGNHPIDDPATFPLRTGP-----VTIGDDVWIGAGATILPGVTI 102

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1543020207  79 RTGSVIAAGSIVTKDVPENAIYGGNPAKLIRFR 111
Cdd:COG0110   103 GDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKR 135
 
Name Accession Description Interval E-value
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
1-111 2.34e-34

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 115.74  E-value: 2.34e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   1 MQIGANTYIGRNSSLSCH--VSIANDVLVASNVSFVGGDHKIDNISTNINLSGRdeikcITVESNVWIGHGVIVMHGVTL 78
Cdd:COG0110    28 ITIGDNVYIGPGVTIDDPggITIGDNVLIGPGVTILTGNHPIDDPATFPLRTGP-----VTIGDDVWIGAGATILPGVTI 102

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1543020207  79 RTGSVIAAGSIVTKDVPENAIYGGNPAKLIRFR 111
Cdd:COG0110   103 GDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKR 135
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 3-108 1.25e-32

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: 110.24  E-value: 1.25e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   3 IGANTYIGRNSSLSCH--VSIANDVLVASNVSFVGGDHKIDNISTNINlsGRDEIKCITVESNVWIGHGVIVMHGVTLRT 80
Cdd:cd04647     4 IGDNVYIGPGCVISAGggITIGDNVLIGPNVTIYDHNHDIDDPERPIE--QGVTSAPIVIGDDVWIGANVVILPGVTIGD 81

                          90       100
                  ....*....|....*....|....*...
gi 1543020207  81 GSVIAAGSIVTKDVPENAIYGGNPAKLI 108
Cdd:cd04647    82 GAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
phn_thr-fam TIGR03308
phosphonate metabolism protein, transferase hexapeptide repeat family; This family of proteins ...
 2-111 2.50e-20

phosphonate metabolism protein, transferase hexapeptide repeat family; This family of proteins contains copies of the Bacterial transferase hexapeptide repeat family (pfam00132) and is only found in operons encoding the phosphonate C-P lyase system (GenProp0232). Many C-P lyase operons, however, lack a homolog of this protein.


Pssm-ID: 132351 [Multi-domain]  Cd Length: 204  Bit Score: 81.36  E-value: 2.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   2 QIGANT-----------YIGRNSSLSChVSIANDVLVASNVSFVGGDHKID-----NISTNINLSGRDE----------- 54
Cdd:TIGR03308  27 EIGERTrlrevalgdysYVMRDCDIIY-TTIGKFCSIAAMVRINATNHPMErptlhHFTYRAAMYFDDAsddadffawrr 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1543020207  55 IKCITVESNVWIGHGVIVMHGVTLRTGSVIAAGSIVTKDVPENAIYGGNPAKLIRFR 111
Cdd:TIGR03308 106 AKRVTIGHDVWIGHGAVILPGVTIGNGAVIAAGAVVTKDVAPYTIVAGVPAKLIRRR 162
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 4-109 1.66e-19

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 78.70  E-value: 1.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   4 GANTYIGRNSSLS--------CHVSIANDVLVASNVSFVGGDHKIDNISTNinlSGRDEIKCITVESNVWIGHGVIVMHG 75
Cdd:PRK10092   71 GYNIFLGNNFYANfdcvmldvCPIRIGDNCMLAPGVHIYTATHPLDPVARN---SGAELGKPVTIGNNVWIGGRAVINPG 147

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1543020207  76 VTLRTGSVIAAGSIVTKDVPENAIYGGNPAKLIR 109
Cdd:PRK10092  148 VTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIK 181
 
Name Accession Description Interval E-value
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
1-111 2.34e-34

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 115.74  E-value: 2.34e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   1 MQIGANTYIGRNSSLSCH--VSIANDVLVASNVSFVGGDHKIDNISTNINLSGRdeikcITVESNVWIGHGVIVMHGVTL 78
Cdd:COG0110    28 ITIGDNVYIGPGVTIDDPggITIGDNVLIGPGVTILTGNHPIDDPATFPLRTGP-----VTIGDDVWIGAGATILPGVTI 102

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1543020207  79 RTGSVIAAGSIVTKDVPENAIYGGNPAKLIRFR 111
Cdd:COG0110   103 GDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKR 135
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 3-108 1.25e-32

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: 110.24  E-value: 1.25e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   3 IGANTYIGRNSSLSCH--VSIANDVLVASNVSFVGGDHKIDNISTNINlsGRDEIKCITVESNVWIGHGVIVMHGVTLRT 80
Cdd:cd04647     4 IGDNVYIGPGCVISAGggITIGDNVLIGPNVTIYDHNHDIDDPERPIE--QGVTSAPIVIGDDVWIGANVVILPGVTIGD 81

                          90       100
                  ....*....|....*....|....*...
gi 1543020207  81 GSVIAAGSIVTKDVPENAIYGGNPAKLI 108
Cdd:cd04647    82 GAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 2-111 1.85e-30

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: 105.70  E-value: 1.85e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   2 QIGANTYIGR--NSSLSCHVSIANDVLVASNVSFV-GGDHKIDNIST------------NINLSGRDEIKCITVESNVWI 66
Cdd:cd03349     3 SVGDYSYGSGpdCDVGGDKLSIGKFCSIAPGVKIGlGGNHPTDWVSTypfyifggewedDAKFDDWPSKGDVIIGNDVWI 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1543020207  67 GHGVIVMHGVTLRTGSVIAAGSIVTKDVPENAIYGGNPAKLIRFR 111
Cdd:cd03349    83 GHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRYR 127
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 3-108 4.50e-29

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: 102.89  E-value: 4.50e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   3 IGANTYIGRNSSL--SCHVSIANDVLVASNVSFVGGDHKIDNISTNINLsgrdEI-KCITVESNVWIGHGVIVMHGVTLR 79
Cdd:cd03357    65 IGDNFYANFNCTIldVAPVTIGDNVLIGPNVQIYTAGHPLDPEERNRGL----EYaKPITIGDNVWIGGGVIILPGVTIG 140

                          90       100
                  ....*....|....*....|....*....
gi 1543020207  80 TGSVIAAGSIVTKDVPENAIYGGNPAKLI 108
Cdd:cd03357   141 DNSVIGAGSVVTKDIPANVVAAGNPARVI 169
phn_thr-fam TIGR03308
phosphonate metabolism protein, transferase hexapeptide repeat family; This family of proteins ...
 2-111 2.50e-20

phosphonate metabolism protein, transferase hexapeptide repeat family; This family of proteins contains copies of the Bacterial transferase hexapeptide repeat family (pfam00132) and is only found in operons encoding the phosphonate C-P lyase system (GenProp0232). Many C-P lyase operons, however, lack a homolog of this protein.


Pssm-ID: 132351 [Multi-domain]  Cd Length: 204  Bit Score: 81.36  E-value: 2.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   2 QIGANT-----------YIGRNSSLSChVSIANDVLVASNVSFVGGDHKID-----NISTNINLSGRDE----------- 54
Cdd:TIGR03308  27 EIGERTrlrevalgdysYVMRDCDIIY-TTIGKFCSIAAMVRINATNHPMErptlhHFTYRAAMYFDDAsddadffawrr 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1543020207  55 IKCITVESNVWIGHGVIVMHGVTLRTGSVIAAGSIVTKDVPENAIYGGNPAKLIRFR 111
Cdd:TIGR03308 106 AKRVTIGHDVWIGHGAVILPGVTIGNGAVIAAGAVVTKDVAPYTIVAGVPAKLIRRR 162
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 4-109 1.66e-19

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 78.70  E-value: 1.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   4 GANTYIGRNSSLS--------CHVSIANDVLVASNVSFVGGDHKIDNISTNinlSGRDEIKCITVESNVWIGHGVIVMHG 75
Cdd:PRK10092   71 GYNIFLGNNFYANfdcvmldvCPIRIGDNCMLAPGVHIYTATHPLDPVARN---SGAELGKPVTIGNNVWIGGRAVINPG 147

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1543020207  76 VTLRTGSVIAAGSIVTKDVPENAIYGGNPAKLIR 109
Cdd:PRK10092  148 VTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIK 181
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 4-109 2.46e-18

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 76.20  E-value: 2.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   4 GANTYIGRNSSLSCH--------VSIANDVLVASNVSFVGGDHKIDNistNINLSGRDEIKCITVESNVWIGHGVIVMHG 75
Cdd:PRK09527   73 GSNIHIGRNFYANFNltivddytVTIGDNVLIAPNVTLSVTGHPVHH---ELRKNGEMYSFPITIGNNVWIGSHVVINPG 149

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1543020207  76 VTLRTGSVIAAGSIVTKDVPENAIYGGNPAKLIR 109
Cdd:PRK09527  150 VTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIR 183
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 3-109 2.74e-17

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: 71.38  E-value: 2.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   3 IGANTYIGRNSSLSCHVSIANDVLVASNVsFVGGDHKIDN--------ISTNINLSGR-----DEIKCITVESNVWIGHG 69
Cdd:cd03358     1 IGDNCIIGTNVFIENDVKIGDNVKIQSNV-SIYEGVTIEDdvfigpnvVFTNDLYPRSkiyrkWELKGTTVKRGASIGAN 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1543020207  70 VIVMHGVTLRTGSVIAAGSIVTKDVPENAIYGGNPAKLIR 109
Cdd:cd03358    80 ATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
PRK10502 PRK10502
putative acyl transferase; Provisional
 3-114 6.18e-17

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 72.29  E-value: 6.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   3 IGANTYIGRNS---SLScHVSIANDVLVASNVSFVGGDHKIDNISTNINLSGrdeikcITVESNVWIGHGVIVMHGVTLR 79
Cdd:PRK10502   74 IGDYAWIGDDVwlyNLG-EITIGAHCVISQKSYLCTGSHDYSDPHFDLNTAP------IVIGEGCWLAADVFVAPGVTIG 146

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1543020207  80 TGSVIAAGSIVTKDVPENAIYGGNPAKLIRFRKLP 114
Cdd:PRK10502  147 SGAVVGARSSVFKSLPANTICRGNPAVPIRPRVET 181
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 2-108 1.33e-15

wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar proteins. WcaF is part of the gene cluster responsible for the biosynthesis of the extracellular polysaccharide colanic acid. The wcaF protein is predicted to contain a left-handed parallel beta-helix (LbH) domain encoded by imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Many are trimeric in their active forms.


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 66.86  E-value: 1.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   2 QIGANTYIGRNSSLSC--HVSIANDVLVASNVSFVGGDHKIDNISTNINLsgrdeiKCITVESNVWIGHGVIVMHGVTLR 79
Cdd:cd05825     5 TIGDNSWIGEGVWIYNlaPVTIGSDACISQGAYLCTGSHDYRSPAFPLIT------APIVIGDGAWVAAEAFVGPGVTIG 78

                          90       100
                  ....*....|....*....|....*....
gi 1543020207  80 TGSVIAAGSIVTKDVPENAIYGGNPAKLI 108
Cdd:cd05825    79 EGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 2-105 1.80e-15

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: 68.67  E-value: 1.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   2 QIGANTYIGRNSSLSCHVSIANDVLVASNVSfVGGDHKIDN---ISTNINLSGrdeikCITVESNVWIGHGVIVMHGVTL 78
Cdd:TIGR03570 101 SIGEGTVIMAGAVINPDVRIGDNVIINTGAI-VEHDCVIGDfvhIAPGVTLSG-----GVVIGEGVFIGAGATIIQGVTI 174

                          90       100
                  ....*....|....*....|....*..
gi 1543020207  79 RTGSVIAAGSIVTKDVPENAIYGGNPA 105
Cdd:TIGR03570 175 GAGAIVGAGAVVTKDIPDGGVVVGVPA 201
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 3-104 5.59e-15

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: 67.12  E-value: 5.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   3 IGANTYIGRNSSLSCHVSIANDVLVASNVsfvggdhkidNISTNINLSGRdeikcITVESNVWIGHGVIVMHGVTLRTGS 82
Cdd:cd03360   111 INPDARIGDNVIINTGAVIGHDCVIGDFV----------HIAPGVVLSGG-----VTIGEGAFIGAGATIIQGVTIGAGA 175

                          90       100
                  ....*....|....*....|..
gi 1543020207  83 VIAAGSIVTKDVPENAIYGGNP 104
Cdd:cd03360   176 IIGAGAVVTKDVPDGSVVVGNP 197
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 1-111 6.10e-15

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 67.21  E-value: 6.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   1 MQIGANTYIGRNSSLSC--HVSIANDVLVASNVSFVGGDH-----KIDNISTNINLSGRD-EIKCITVESNVWIGHGVIV 72
Cdd:PRK09677   66 LFFGDNVQVNDYVHIACieSITIGRDTLIASKVFITDHNHgsfkhSDDFSSPNLPPDMRTlESSAVVIGQRVWIGENVTI 145

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1543020207  73 MHGVTLRTGSVIAAGSIVTKDVPENAIYGGNPAKLIRFR 111
Cdd:PRK09677  146 LPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKKY 184
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 3-109 3.71e-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: 58.96  E-value: 3.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   3 IGANTYIGRNSSLscHVSIANDVLVASNVSfVGgdHKidnistninlsgrdeikCI----TVESNVWIGHGVIVMHGVTL 78
Cdd:cd04645    41 IGERTNIQDGSVL--HVDPGYPTIIGDNVT-VG--HG-----------------AVlhgcTIGDNCLIGMGAIILDGAVI 98

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1543020207  79 RTGSVIAAGSIVT--KDVPENAIYGGNPAKLIR 109
Cdd:cd04645    99 GKGSIVAAGSLVPpgKVIPPGSLVAGSPAKVVR 131
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 59-109 1.38e-11

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 57.73  E-value: 1.38e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1543020207  59 TVESNVWIGHGVIVMHGVTLRTGSVIAAGSIVT--KDVPENAIYGGNPAKLIR 109
Cdd:COG0663    90 TIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTegKVVPPGSLVVGSPAKVVR 142
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 59-112 1.48e-10

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: 55.09  E-value: 1.48e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1543020207  59 TVESNVWIGHGVIVMHGVTLRTGSVIAAGSIVTKDVPENAIYGGNPAKLIRFRK 112
Cdd:COG1045   119 TIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVKRKG 172
PLN02739 PLN02739
serine acetyltransferase
 4-110 1.92e-09

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 53.50  E-value: 1.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   4 GANTYIGRNSSLSCHVSIANDVLVASNVSFVGGDHKidNISTNINLSGrdeikCITVESNVWIGhgvivmhgvtlrTGSV 83
Cdd:PLN02739  223 GTGVVIGETAVIGDRVSILHGVTLGGTGKETGDRHP--KIGDGALLGA-----CVTILGNISIG------------AGAM 283

                          90       100
                  ....*....|....*....|....*..
gi 1543020207  84 IAAGSIVTKDVPENAIYGGNPAKLIRF 110
Cdd:PLN02739  284 VAAGSLVLKDVPSHSMVAGNPAKLIGF 310
PLN02296 PLN02296
carbonate dehydratase
 1-109 5.46e-09

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 52.05  E-value: 5.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   1 MQIGANTYIGRNSSLscHVSIANdvlvasnvsfVGGDHKIDNISTNINLSGRDEIKCITVESNVWIGHGVIVMHGVTLRT 80
Cdd:PLN02296   92 ISVGSGTNIQDNSLV--HVAKTN----------LSGKVLPTIIGDNVTIGHSAVLHGCTVEDEAFVGMGATLLDGVVVEK 159

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1543020207  81 GSVIAAGSIVTKD--VPENAIYGGNPAKLIR 109
Cdd:PLN02296  160 HAMVAAGALVRQNtrIPSGEVWAGNPAKFLR 190
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 56-104 6.30e-08

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: 46.66  E-value: 6.30e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1543020207  56 KCITVESNVWIGHGVIVMHGVTLRTGSVIAAGSIVTKDVPENAIYGGNP 104
Cdd:cd03354    53 RHPTIGDNVVIGAGAKILGNITIGDNVKIGANAVVTKDVPANSTVVGVP 101
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 3-109 1.16e-07

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: 47.79  E-value: 1.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   3 IGANTYIGR----NSSLSCHVSIANDVLVASNVSFvgGDHKIdnISTNINLSGrdeikCITVESNVWIGHGVIVMHGVTL 78
Cdd:cd03352   101 IGANTTIDRgalgDTVIGDGTKIDNLVQIAHNVRI--GENCL--IAAQVGIAG-----STTIGDNVIIGGQVGIAGHLTI 171

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1543020207  79 RTGSVIAAGSIVTKDVPENAIYGGNPAKLIR 109
Cdd:cd03352   172 GDGVVIGAGSGVTSIVPPGEYVSGTPAQPHR 202
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 59-114 3.68e-06

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 43.85  E-value: 3.68e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1543020207  59 TVESNVWIGHGV-IVMHgVTLRTGSVIAAGSIVTKDVPENAIYGGNPAK--------LIRFRKLP 114
Cdd:COG1044   260 KIGDNVVIGGQVgIAGH-LTIGDGVIIGAQSGVTKSIPEGGVYSGSPAQphrewlrnAAALRRLP 323
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 7-107 3.95e-06

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: 43.96  E-value: 3.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   7 TYIGRNSSLSCHVSIANDVLVasnvsfvgGDHKIdnISTNINLSGrdeikCITVESNVWIGHGVIVMHGVTLRTGSVIAA 86
Cdd:cd03351   103 TRIGNNNLLMAYVHVAHDCVI--------GNNVI--LANNATLAG-----HVEIGDYAIIGGLSAVHQFCRIGRHAMVGG 167

                          90       100
                  ....*....|....*....|.
gi 1543020207  87 GSIVTKDVPENAIYGGNPAKL 107
Cdd:cd03351   168 GSGVVQDVPPYVIAAGNRARL 188
PLN02472 PLN02472
uncharacterized protein
 59-109 1.01e-05

uncharacterized protein


Pssm-ID: 215263 [Multi-domain]  Cd Length: 246  Bit Score: 42.64  E-value: 1.01e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1543020207  59 TVESNVWIGHGVIVMHGVTLRTGSVIAAGSIVT--KDVPENAIYGGNPAKLIR 109
Cdd:PLN02472  145 TIEPECIIGQHSILMEGSLVETHSILEAGSVLPpgRRIPTGELWAGNPARFVR 197
PLN02357 PLN02357
serine acetyltransferase
 64-108 2.37e-05

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 41.79  E-value: 2.37e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1543020207  64 VWIGHGVIVMHGVTLRTGSVIAAGSIVTKDVPENAIYGGNPAKLI 108
Cdd:PLN02357  285 VLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLI 329
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 6-99 2.60e-05

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 41.74  E-value: 2.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   6 NTYIGRNSSLScHVSIANDVLVASNVSFVGGdhkidniSTNINLSGRDEIKCItVESNVWIGHGVIVMHGVTLRTGSVIA 85
Cdd:PRK14354  351 KSTIGEGTKVS-HLTYIGDAEVGENVNIGCG-------TITVNYDGKNKFKTI-IGDNAFIGCNSNLVAPVTVGDNAYIA 421

                          90
                  ....*....|....
gi 1543020207  86 AGSIVTKDVPENAI 99
Cdd:PRK14354  422 AGSTITKDVPEDAL 435
PLN02694 PLN02694
serine O-acetyltransferase
 64-114 3.15e-05

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 41.55  E-value: 3.15e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1543020207  64 VWIGHGVIVMHGVTLRTGSVIAAGSIVTKDVPENAIYGGNPAKLIRFRKLP 114
Cdd:PLN02694  219 VLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLVGGKEKP 269
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 3-91 6.17e-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: 38.38  E-value: 6.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   3 IGANTYIGRNSSLSCHVSIANDVLVASNVSFVGGDHKIDNISTninlsgrdeikciTVESNVWIGHGVIVMHGVTLRTGS 82
Cdd:cd00208     3 IGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGPNEKNPT-------------IIGDNVEIGANAVIHGGVKIGDNA 69


                  ....*....
gi 1543020207  83 VIAAGSIVT 91
Cdd:cd00208    70 VIGAGAVVT 78
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 2-116 8.23e-05

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 40.50  E-value: 8.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   2 QIGANTYIGrNSSLSCH--VSIANDVLVASNVSFVGgdHKIDnistninlSGRDEIKCITVESNVWIGHGVIVMHGVTLR 79
Cdd:TIGR02353 114 KIGKGVDIG-SLPPVCTdlLTIGAGTIVRKEVMLLG--YRAE--------RGRLHTGPVTLGRDAFIGTRSTLDIDTSIG 182

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1543020207  80 TGSVIAAGSIVTKD--VPENAIYGGNPAKLIRF--RKLPNS 116
Cdd:TIGR02353 183 DGAQLGHGSALQGGqsIPDGERWHGSPAQKTGAdyRKVQPA 223
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 58-105 1.26e-04

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 39.73  E-value: 1.26e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1543020207  58 ITVESNVWIGHGVIVMHGVTLRTGSVIAAGSIVTK--DVPENAIYGGNPA 105
Cdd:TIGR02353 646 VTIGDGATLGPGAIVLYGVVMGEGSVLGPDSLVMKgeEVPAHTRWRGNPA 695
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 2-99 1.69e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 39.34  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   2 QIGANTYIG------RNSSLSCHVSIANDVLV----------ASNVSFVGGDhkidNISTNINLsGRDEIKC-------- 57
Cdd:PRK14355  322 VVGDDVAIGpmahlrPGTELSAHVKIGNFVETkkivmgegskASHLTYLGDA----TIGRNVNI-GCGTITCnydgvkkh 396

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1543020207  58 -ITVESNVWIGHGVIVMHGVTLRTGSVIAAGSIVTKDVPENAI 99
Cdd:PRK14355  397 rTVIEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPPDSL 439
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 59-98 1.77e-04

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: 39.24  E-value: 1.77e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1543020207  59 TVESNVWIGHGVIVMHGVTLRTGSVIAAGSIVTKDVPENA 98
Cdd:COG1207   396 VIGDGAFIGSNTNLVAPVTIGDGATIGAGSTITKDVPAGA 435
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 7-107 2.44e-04

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: 38.85  E-value: 2.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   7 TYIGRNSSLSCHVSIANDVLVasnvsfvgGDHKIdnISTNINLSGRdeikcITVESNVWIGHGVIVMHGVTLRTGSVIAA 86
Cdd:COG1043   105 TRIGDDNLLMAYVHVAHDCVV--------GNNVI--LANNATLAGH-----VEVGDHAIIGGLSAVHQFVRIGAHAMVGG 169

                          90       100
                  ....*....|....*....|.
gi 1543020207  87 GSIVTKDVPENAIYGGNPAKL 107
Cdd:COG1043   170 GSGVVKDVPPYVLAAGNPARL 190
PRK10191 PRK10191
putative acyl transferase; Provisional
 2-107 3.71e-04

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 37.56  E-value: 3.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   2 QIGANTYIGRnsslscHVSIANDVLVASNVSFVGGDHKIDNISTNINLSGRDEIKCITVESNVWIGHGVIVMHGVTLRTG 81
Cdd:PRK10191   43 EIQAAATIGR------RFTIHHGYAVVINKNVVAGDDFTIRHGVTIGNRGADNMACPHIGNGVELGANVIILGDITIGNN 116

                          90       100
                  ....*....|....*....|....*.
gi 1543020207  82 SVIAAGSIVTKDVPENAIYGGNPAKL 107
Cdd:PRK10191  117 VTVGAGSVVLDSVPDNALVVGEKARV 142
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 3-109 4.36e-04

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: 37.73  E-value: 4.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   3 IGANTYIGRNSSLSchvsiandvlvasnvsfvgGD------HKIDNISTNINLSGRDEIKCItVESNVWIGHGVIVmHGV 76
Cdd:cd04745    21 IGKNCYIGPHASLR-------------------GDfgriviRDGANVQDNCVIHGFPGQDTV-LEENGHIGHGAIL-HGC 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1543020207  77 TLRTG------------------SVIAAGSIVTK--DVPENAIYGGNPAKLIR 109
Cdd:cd04745    80 TIGRNalvgmnavvmdgavigeeSIVGAMAFVKAgtVIPPRSLIAGSPAKVIR 132
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 6-99 4.67e-04

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 38.21  E-value: 4.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   6 NTYIGRNSSLScHVSIANDVLVASNVSFVGGdhkidniSTNINLSGRDEIKCItVESNVWIGHGVIVMHGVTLRTGSVIA 85
Cdd:PRK14357  341 KSTIGENTKAQ-HLTYLGDATVGKNVNIGAG-------TITCNYDGKKKNPTF-IEDGAFIGSNSSLVAPVRIGKGALIG 411

                          90
                  ....*....|....
gi 1543020207  86 AGSIVTKDVPENAI 99
Cdd:PRK14357  412 AGSVITEDVPPYSL 425
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 59-98 1.13e-03

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: 36.63  E-value: 1.13e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1543020207  59 TVESNVWIGHGVIVMHGVTLRTGSVIAAGSIVTKDVPENA 98
Cdd:cd03353   146 VIGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGA 185
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 6-97 1.35e-03

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 36.93  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   6 NTYIGRNSSLScHVSIANDVLVASNVSFVGGdhkidniSTNINLSGRDEIKCItVESNVWIGHGVIVMHGVTLRTGSVIA 85
Cdd:PRK09451  352 KARLGKGSKAG-HLTYLGDAEIGDNVNIGAG-------TITCNYDGANKFKTI-IGDDVFVGSDTQLVAPVTVGKGATIG 422

                          90
                  ....*....|..
gi 1543020207  86 AGSIVTKDVPEN 97
Cdd:PRK09451  423 AGTTVTRDVAEN 434
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 64-99 6.25e-03

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 35.08  E-value: 6.25e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1543020207  64 VWIGHGVIVMHGVTLRTGSVIAAGSIVTKDVPENAI 99
Cdd:PRK14356  405 AFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSL 440
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 57-117 6.49e-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: 34.50  E-value: 6.49e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1543020207  57 CITVESNVWIGHGVIVMHGVTLRTGSVIAAGSIvtkdVPENAIYGGNPAKLIRFrkLPNSY 117
Cdd:cd03359    95 YVHIGKNCVIGRRCIIKDCVKILDGTVVPPDTV----IPPYSVVSGRPARFIGE--LPECT 149
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 59-99 7.47e-03

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 34.45  E-value: 7.47e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1543020207  59 TVESNVWIGHGVIVMHGVTLRTGSVIAAGSIVTKDVPENAI 99
Cdd:PRK14353  382 EIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDAL 422
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 2-84 9.79e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 34.34  E-value: 9.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020207   2 QIGANTYIGRNSSLSCHVSIANDVLVASNVsFVGGDHKIdnistninlsGRDeikCItVESNVWIGHGVIVMHGVTLRTG 81
Cdd:PRK00892  114 KIGEGVSIGPNAVIGAGVVIGDGVVIGAGA-VIGDGVKI----------GAD---CR-LHANVTIYHAVRIGNRVIIHSG 178


                  ...
gi 1543020207  82 SVI 84
Cdd:PRK00892  179 AVI 181
 
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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