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Conserved domains on  [gi|306869122|gb|EFN00924|]
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hypothetical protein appser12_9570 [Actinobacillus pleuropneumoniae serovar 12 str. 1096]

Protein Classification

LbetaH domain-containing protein( domain architecture ID 372)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LbetaH super family cl00160
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 47-180 1.18e-57

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


The actual alignment was detected with superfamily member cd03357:

Pssm-ID: 469633 [Multi-domain]  Cd Length: 169  Bit Score: 178.77  E-value: 1.18e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869122  47 QRLLSEITQsHIDETLHVNLPLYCDFGRHLRIGKNVFINTACVFTDLGGITLEDNVLLAPRVNIITVNHPTDPQTRR--G 124
Cdd:cd03357   35 RELLKELFG-SVGENVYIEPPFHCDYGYNIHIGDNFYANFNCTILDVAPVTIGDNVLIGPNVQIYTAGHPLDPEERNrgL 113

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 306869122 125 VIVKPVIVKQNAWIGAGATILPSVTVGKNAIVAAGSVVTKDVPANTIVAGVPAKIV 180
Cdd:cd03357  114 EYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
 
Name Accession Description Interval E-value
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 47-180 1.18e-57

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: 178.77  E-value: 1.18e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869122  47 QRLLSEITQsHIDETLHVNLPLYCDFGRHLRIGKNVFINTACVFTDLGGITLEDNVLLAPRVNIITVNHPTDPQTRR--G 124
Cdd:cd03357   35 RELLKELFG-SVGENVYIEPPFHCDYGYNIHIGDNFYANFNCTILDVAPVTIGDNVLIGPNVQIYTAGHPLDPEERNrgL 113

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 306869122 125 VIVKPVIVKQNAWIGAGATILPSVTVGKNAIVAAGSVVTKDVPANTIVAGVPAKIV 180
Cdd:cd03357  114 EYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
57-185 1.40e-49

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 156.95  E-value: 1.40e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869122  57 HIDETLHVNLPLYCdFGRHLRIGKNVFINTACVFTDLGGITLEDNVLLAPRVNIITVNHPTDPQTRRGVIVKPVIVKQNA 136
Cdd:COG0110   10 RIGDGVVIGPGVRI-YGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPATFPLRTGPVTIGDDV 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 306869122 137 WIGAGATILPSVTVGKNAIVAAGSVVTKDVPANTIVAGVPAKIVKIIDE 185
Cdd:COG0110   89 WIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDE 137
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 41-181 6.81e-38

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 128.78  E-value: 6.81e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869122  41 QTQADIQRLLSEITQSHIDETLHvnlplyCDFGRHLRIGKNVFINTACVFTDLGGITLEDNVLLAPRVNIITVNHPTDPQ 120
Cdd:PRK10092  45 LRQQILADLFGQVTEAYIEPTFR------CDYGYNIFLGNNFYANFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPLDPV 118

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 306869122 121 TRRG--VIVKPVIVKQNAWIGAGATILPSVTVGKNAIVAAGSVVTKDVPANTIVAGVPAKIVK 181
Cdd:PRK10092 119 ARNSgaELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIK 181
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 77-177 4.86e-20

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: 82.93  E-value: 4.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869122   77 RIGKNVFINTACVFT-DlggITLEDNVLLAPRVNIitvnhptdpqTRRgvivkpVIVKQNAWIGAGATILPSVTVGKNAI 155
Cdd:TIGR03570 119 RIGDNVIINTGAIVEhD---CVIGDFVHIAPGVTL----------SGG------VVIGEGVFIGAGATIIQGVTIGAGAI 179

                          90       100
                  ....*....|....*....|..
gi 306869122  156 VAAGSVVTKDVPANTIVAGVPA 177
Cdd:TIGR03570 180 VGAGAVVTKDIPDGGVVVGVPA 201
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
129-158 3.23e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.85  E-value: 3.23e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 306869122  129 PVIVKQNAWIGAGATILPSVTVGKNAIVAA 158
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 47-180 1.18e-57

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: 178.77  E-value: 1.18e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869122  47 QRLLSEITQsHIDETLHVNLPLYCDFGRHLRIGKNVFINTACVFTDLGGITLEDNVLLAPRVNIITVNHPTDPQTRR--G 124
Cdd:cd03357   35 RELLKELFG-SVGENVYIEPPFHCDYGYNIHIGDNFYANFNCTILDVAPVTIGDNVLIGPNVQIYTAGHPLDPEERNrgL 113

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 306869122 125 VIVKPVIVKQNAWIGAGATILPSVTVGKNAIVAAGSVVTKDVPANTIVAGVPAKIV 180
Cdd:cd03357  114 EYAKPITIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
57-185 1.40e-49

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 156.95  E-value: 1.40e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869122  57 HIDETLHVNLPLYCdFGRHLRIGKNVFINTACVFTDLGGITLEDNVLLAPRVNIITVNHPTDPQTRRGVIVKPVIVKQNA 136
Cdd:COG0110   10 RIGDGVVIGPGVRI-YGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNHPIDDPATFPLRTGPVTIGDDV 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 306869122 137 WIGAGATILPSVTVGKNAIVAAGSVVTKDVPANTIVAGVPAKIVKIIDE 185
Cdd:COG0110   89 WIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDE 137
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 75-180 7.98e-45

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: 144.14  E-value: 7.98e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869122  75 HLRIGKNVFINTACVFTDLGGITLEDNVLLAPRVNIITVNHPTDPQTRR---GVIVKPVIVKQNAWIGAGATILPSVTVG 151
Cdd:cd04647    1 NISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYDHNHDIDDPERPieqGVTSAPIVIGDDVWIGANVVILPGVTIG 80

                         90       100
                 ....*....|....*....|....*....
gi 306869122 152 KNAIVAAGSVVTKDVPANTIVAGVPAKIV 180
Cdd:cd04647   81 DGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 41-181 6.81e-38

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 128.78  E-value: 6.81e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869122  41 QTQADIQRLLSEITQSHIDETLHvnlplyCDFGRHLRIGKNVFINTACVFTDLGGITLEDNVLLAPRVNIITVNHPTDPQ 120
Cdd:PRK10092  45 LRQQILADLFGQVTEAYIEPTFR------CDYGYNIFLGNNFYANFDCVMLDVCPIRIGDNCMLAPGVHIYTATHPLDPV 118

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 306869122 121 TRRG--VIVKPVIVKQNAWIGAGATILPSVTVGKNAIVAAGSVVTKDVPANTIVAGVPAKIVK 181
Cdd:PRK10092 119 ARNSgaELGKPVTIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIK 181
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 73-181 2.55e-31

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: 109.90  E-value: 2.55e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869122  73 GRHLRIGKNVFINTACVFTD----------LGGITLEDNVLLAPRVNIITVNHPTDPQTRRGViVKPVIVKQNAWIGAGA 142
Cdd:cd03358    2 GDNCIIGTNVFIENDVKIGDnvkiqsnvsiYEGVTIEDDVFIGPNVVFTNDLYPRSKIYRKWE-LKGTTVKRGASIGANA 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 306869122 143 TILPSVTVGKNAIVAAGSVVTKDVPANTIVAGVPAKIVK 181
Cdd:cd03358   81 TILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 58-189 7.77e-29

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 106.24  E-value: 7.77e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869122  58 IDETLHVNLPLYCDFGRHLRIGKNVFINTACVFTDLGGITLEDNVLLAPRVNIITVNHPTDPQTRRG--VIVKPVIVKQN 135
Cdd:PRK09527  58 VGENAWVEPPVYFSYGSNIHIGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGHPVHHELRKNgeMYSFPITIGNN 137

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 306869122 136 AWIGAGATILPSVTVGKNAIVAAGSVVTKDVPANTIVAGVPAKIVKIIDEVSNE 189
Cdd:PRK09527 138 VWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIREINDRDKQ 191
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 67-181 1.79e-24

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: 92.99  E-value: 1.79e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869122  67 PLYCDFGR-HLRIGKNVFIntacvftdlggitlednvllAPRVNIIT-VNHPTD-----PQTRRGVIV------------ 127
Cdd:cd03349   12 GPDCDVGGdKLSIGKFCSI--------------------APGVKIGLgGNHPTDwvstyPFYIFGGEWeddakfddwpsk 71

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 306869122 128 KPVIVKQNAWIGAGATILPSVTVGKNAIVAAGSVVTKDVPANTIVAGVPAKIVK 181
Cdd:cd03349   72 GDVIIGNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIR 125
PRK10502 PRK10502
putative acyl transferase; Provisional
 76-181 6.69e-23

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 90.01  E-value: 6.69e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869122  76 LRIGKNVFINTACVFTDLGGITLEDNVLLAPRVNIITVNHptDPQTRR-GVIVKPVIVKQNAWIGAGATILPSVTVGKNA 154
Cdd:PRK10502  72 LTIGDYAWIGDDVWLYNLGEITIGAHCVISQKSYLCTGSH--DYSDPHfDLNTAPIVIGEGCWLAADVFVAPGVTIGSGA 149

                         90       100
                 ....*....|....*....|....*..
gi 306869122 155 IVAAGSVVTKDVPANTIVAGVPAKIVK 181
Cdd:PRK10502 150 VVGARSSVFKSLPANTICRGNPAVPIR 176
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 74-180 3.77e-22

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: 86.12  E-value: 3.77e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869122  74 RHLRIGKNVFINTACVFTDLGGITLEDNVLLAPRVNIITVNHPTDPQTRrGVIVKPVIVKQNAWIGAGATILPSVTVGKN 153
Cdd:cd05825    2 WNLTIGDNSWIGEGVWIYNLAPVTIGSDACISQGAYLCTGSHDYRSPAF-PLITAPIVIGDGAWVAAEAFVGPGVTIGEG 80

                         90       100
                 ....*....|....*....|....*..
gi 306869122 154 AIVAAGSVVTKDVPANTIVAGVPAKIV 180
Cdd:cd05825   81 AVVGARSVVVRDLPAWTVYAGNPAVPV 107
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 76-188 2.23e-21

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 86.47  E-value: 2.23e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869122  76 LRIGKNVFINTACVFTDLGGITLEDNVLLAPRVNIITVNH-----PTD------PQTRRGVIVKPVIVKQNAWIGAGATI 144
Cdd:PRK09677  66 LFFGDNVQVNDYVHIACIESITIGRDTLIASKVFITDHNHgsfkhSDDfsspnlPPDMRTLESSAVVIGQRVWIGENVTI 145

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 306869122 145 LPSVTVGKNAIVAAGSVVTKDVPANTIVAGVPAKIVKIIDEVSN 188
Cdd:PRK09677 146 LPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKKYNHETK 189
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 77-177 4.86e-20

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: 82.93  E-value: 4.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869122   77 RIGKNVFINTACVFT-DlggITLEDNVLLAPRVNIitvnhptdpqTRRgvivkpVIVKQNAWIGAGATILPSVTVGKNAI 155
Cdd:TIGR03570 119 RIGDNVIINTGAIVEhD---CVIGDFVHIAPGVTL----------SGG------VVIGEGVFIGAGATIIQGVTIGAGAI 179

                          90       100
                  ....*....|....*....|..
gi 306869122  156 VAAGSVVTKDVPANTIVAGVPA 177
Cdd:TIGR03570 180 VGAGAVVTKDIPDGGVVVGVPA 201
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 77-181 1.08e-19

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: 81.67  E-value: 1.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869122  77 RIGKNVFIN---------TACVftdlggitlEDNVLLAPRVNIITVN------HPTdpqtrrgvivkpviVKQNAWIGAG 141
Cdd:COG1045   73 TIGRGFFIDhgtgvvigeTAVI---------GDNVTIYQGVTLGGTGkekgkrHPT--------------IGDNVVIGAG 129

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 306869122 142 ATILPSVTVGKNAIVAAGSVVTKDVPANTIVAGVPAKIVK 181
Cdd:COG1045  130 AKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVK 169
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 77-176 5.24e-19

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: 80.22  E-value: 5.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869122  77 RIGKNVFINTACVftdlggI----TLEDNVLLAPRVNIiTVNhptdpqtrrgvivkpVIVKQNAWIGAGATILPSVTVGK 152
Cdd:cd03360  116 RIGDNVIINTGAV------IghdcVIGDFVHIAPGVVL-SGG---------------VTIGEGAFIGAGATIIQGVTIGA 173

                         90       100
                 ....*....|....*....|....
gi 306869122 153 NAIVAAGSVVTKDVPANTIVAGVP 176
Cdd:cd03360  174 GAIIGAGAVVTKDVPDGSVVVGNP 197
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 66-176 1.14e-15

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: 69.01  E-value: 1.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869122  66 LPLYCDFGRHLRI--GKNVFINTACVFTDlgGITLEDNVLLAPRVNIITVNHPTdpqtrrgvivkpviVKQNAWIGAGAT 143
Cdd:cd03354    5 IHPGAKIGPGLFIdhGTGIVIGETAVIGD--NCTIYQGVTLGGKGKGGGKRHPT--------------IGDNVVIGAGAK 68

                         90       100       110
                 ....*....|....*....|....*....|...
gi 306869122 144 ILPSVTVGKNAIVAAGSVVTKDVPANTIVAGVP 176
Cdd:cd03354   69 ILGNITIGDNVKIGANAVVTKDVPANSTVVGVP 101
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 75-185 4.10e-14

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: 66.28  E-value: 4.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869122  75 HLRIGKNVFINTACVF--TDLGGITLEDNVllaprvniiTVNHptdpqtrrGVIVKPVIVKQNAWIGAGATILPSVTVGK 152
Cdd:cd04645   38 PIRIGERTNIQDGSVLhvDPGYPTIIGDNV---------TVGH--------GAVLHGCTIGDNCLIGMGAIILDGAVIGK 100

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 306869122 153 NAIVAAGSVVT--KDVPANTIVAGVPAKIVKIIDE 185
Cdd:cd04645  101 GSIVAAGSLVPpgKVIPPGSLVAGSPAKVVRELTD 135
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 77-178 7.58e-14

serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 65.78  E-value: 7.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869122   77 RIGKNVFINTACVFTDLGGITLEDNVLLAPRVNIITVN------HPTdpqtrrgvivkpviVKQNAWIGAGATILPSVTV 150
Cdd:TIGR01172  69 RIGRGVFIDHGTGVVIGETAVIGDDVTIYHGVTLGGTGkekgkrHPT--------------IGEGVMIGAGAKVLGNIEV 134

                          90       100
                  ....*....|....*....|....*...
gi 306869122  151 GKNAIVAAGSVVTKDVPANTIVAGVPAK 178
Cdd:TIGR01172 135 GENAKIGANSVVLKDVPPGATVVGVPAR 162
PLN02739 PLN02739
serine acetyltransferase
 27-185 1.08e-13

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 68.14  E-value: 1.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869122  27 AENAYKIAElsgKFQTQAdiQRLLSEITQSHIDETLHVnlplycDFGRHLRIGKNVFINTACvftdlgGITLEDNVLLAP 106
Cdd:PLN02739 174 ALQAYRVAH---KLWKQG--RKLLALALQSRVSEVFGI------DIHPAARIGKGILLDHGT------GVVIGETAVIGD 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869122 107 RVNII-------TVNHPTDPQTRRGvivkpvivkQNAWIGAGATILPSVTVGKNAIVAAGSVVTKDVPANTIVAGVPAKI 179
Cdd:PLN02739 237 RVSILhgvtlggTGKETGDRHPKIG---------DGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKL 307


                 ....*.
gi 306869122 180 VKIIDE 185
Cdd:PLN02739 308 IGFVDE 313
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 71-185 4.34e-13

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 63.89  E-value: 4.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869122  71 DFGRhLRIGKNVFINTACVF--TDLGGITLEDNVllaprvniiTVNHptdpqtrrGVIVKPVIVKQNAWIGAGATILPSV 148
Cdd:COG0663   46 DVGP-IRIGEGSNIQDGVVLhvDPGYPLTIGDDV---------TIGH--------GAILHGCTIGDNVLIGMGAIVLDGA 107

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 306869122 149 TVGKNAIVAAGSVVT--KDVPANTIVAGVPAKIVKIIDE 185
Cdd:COG0663  108 VIGDGSIVGAGALVTegKVVPPGSLVVGSPAKVVRELTE 146
cysE PRK11132
serine acetyltransferase; Provisional
 119-180 2.50e-12

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 63.56  E-value: 2.50e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 306869122 119 PQTRRGVIvkpvivkqnawIGAGATILPSVTVGKNAIVAAGSVVTKDVPANTIVAGVPAKIV 180
Cdd:PRK11132 194 PKIREGVM-----------IGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIV 244
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 77-189 1.30e-10

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: 56.99  E-value: 1.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869122  77 RIGKNVFINT-ACVFTDLGGITLE------DNVLLAPRVNIITVNHpTDPQTRRGVIVKPVIVKQNAWIGAGATILPSVT 149
Cdd:cd04745   20 IIGKNCYIGPhASLRGDFGRIVIRdganvqDNCVIHGFPGQDTVLE-ENGHIGHGAILHGCTIGRNALVGMNAVVMDGAV 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 306869122 150 VGKNAIVAAGSVVTK--DVPANTIVAGVPAKIVKiidEVSNE 189
Cdd:cd04745   99 IGEESIVGAMAFVKAgtVIPPRSLIAGSPAKVIR---ELSDE 137
PLN02694 PLN02694
serine O-acetyltransferase
 26-180 9.37e-10

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 56.57  E-value: 9.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869122  26 VAENAYKIAElsgKFQTQAdiQRLLSEITQSHIDETLHVnlplycDFGRHLRIGKNVFINTACvftdlgGITLEDNVLLA 105
Cdd:PLN02694 128 LACQAHRVAH---KLWTQS--RRPLALALHSRISDVFAV------DIHPAAKIGKGILFDHAT------GVVIGETAVIG 190

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 306869122 106 PRVNIItvNHPTDPQTRRGVIVKPVIVKQNAWIGAGATILPSVTVGKNAIVAAGSVVTKDVPANTIVAGVPAKIV 180
Cdd:PLN02694 191 NNVSIL--HHVTLGGTGKACGDRHPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLV 263
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 107-172 3.22e-09

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: 55.03  E-value: 3.22e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 306869122 107 RVNI----ITVN------HPTdpqtrrgvivkpvIVKQNAWIGAGATILPSVTVGKNAIVAAGSVVTKDVPANTIV 172
Cdd:COG1207  375 GVNIgagtITCNydgvnkHRT-------------VIGDGAFIGSNTNLVAPVTIGDGATIGAGSTITKDVPAGALA 437
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 107-172 8.19e-09

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: 52.81  E-value: 8.19e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 306869122 107 RVNI----ITVN------HPTdpqtrrgvivkpvIVKQNAWIGAGATILPSVTVGKNAIVAAGSVVTKDVPANTIV 172
Cdd:cd03353  125 GVNIgagtITCNydgvnkHRT-------------VIGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGALA 187
PLN02296 PLN02296
carbonate dehydratase
 78-185 8.45e-09

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 53.59  E-value: 8.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869122  78 IGKNVFINTACVFT-DLGGIT------LEDNVLL-APRVNIITVNHPTDPQTRRGVIVKPVI----VKQNAWIGAGATIL 145
Cdd:PLN02296  73 VGRGSSIWYGCVLRgDVNSISvgsgtnIQDNSLVhVAKTNLSGKVLPTIIGDNVTIGHSAVLhgctVEDEAFVGMGATLL 152

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 306869122 146 PSVTVGKNAIVAAGSVVTKD--VPANTIVAGVPAKIV-KIIDE 185
Cdd:PLN02296 153 DGVVVEKHAMVAAGALVRQNtrIPSGEVWAGNPAKFLrKLTEE 195
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 77-163 3.92e-08

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 48.40  E-value: 3.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869122  77 RIGKNVFINTACVFtdLGGITLEDNVLLAPRVNIITVNHPTDPqtrrgvivKPVIVKQNAWIGAGATILPSVTVGKNAIV 156
Cdd:cd00208    2 FIGEGVKIHPKAVI--RGPVVIGDNVNIGPGAVIGAATGPNEK--------NPTIIGDNVEIGANAVIHGGVKIGDNAVI 71


                 ....*..
gi 306869122 157 AAGSVVT 163
Cdd:cd00208   72 GAGAVVT 78
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 129-181 4.17e-08

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 52.07  E-value: 4.17e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 306869122 129 PVIVKQNAWIGAGATILPSVTVGKNAIVAAGSVVTKDVPANTIVAGVPAKIVK 181
Cdd:PRK14357 383 PTFIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQIVK 435
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 107-171 4.50e-08

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 51.76  E-value: 4.50e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 306869122 107 RVNI----ITVN------HPTdpqtrrgvivkpvIVKQNAWIGAGATILPSVTVGKNAIVAAGSVVTKDVPANTI 171
Cdd:PRK14354 374 NVNIgcgtITVNydgknkFKT-------------IIGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDAL 435
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 135-178 8.53e-08

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: 50.10  E-value: 8.53e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 306869122 135 NAWIGAGATILPSVTVGKNAIVAAGSVVTKDVPANTIVAGVPAK 178
Cdd:cd03352  156 NVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQ 199
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 67-178 1.07e-07

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: 50.90  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869122   67 PLYCDFGRHL--RIGKNVFINTAC-VFTDLggITLEDNVLLAPRVNIItvNHPTDpqtrRGVI-VKPVIVKQNAWIGAGA 142
Cdd:TIGR02353 102 PLYSLYLRALgaKIGKGVDIGSLPpVCTDL--LTIGAGTIVRKEVMLL--GYRAE----RGRLhTGPVTLGRDAFIGTRS 173

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 306869122  143 TILPSVTVGKNAIVAAGSVVTKD--VPANTIVAGVPAK 178
Cdd:TIGR02353 174 TLDIDTSIGDGAQLGHGSALQGGqsIPDGERWHGSPAQ 211
PLN02357 PLN02357
serine acetyltransferase
 138-180 1.42e-07

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 50.27  E-value: 1.42e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 306869122 138 IGAGATILPSVTVGKNAIVAAGSVVTKDVPANTIVAGVPAKIV 180
Cdd:PLN02357 287 IGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLI 329
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 77-177 6.32e-07

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: 48.59  E-value: 6.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869122   77 RIGKNVFINTACVF-TDLggITLEDNVllaprvniiTVNHPTDPQTR----RGVIVKPVIVKQNAWIGAGATILPSVTVG 151
Cdd:TIGR02353 599 KIGRGVYIDGTDLTeRDL--VTIGDDS---------TLNEGSVIQTHlfedRVMKSDTVTIGDGATLGPGAIVLYGVVMG 667

                          90       100
                  ....*....|....*....|....*...
gi 306869122  152 KNAIVAAGSVVTK--DVPANTIVAGVPA 177
Cdd:TIGR02353 668 EGSVLGPDSLVMKgeEVPAHTRWRGNPA 695
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 136-171 6.88e-07

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 48.57  E-value: 6.88e-07
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 306869122 136 AWIGAGATILPSVTVGKNAIVAAGSVVTKDVPANTI 171
Cdd:PRK14356 405 AFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSL 440
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 132-185 8.97e-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: 46.41  E-value: 8.97e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 306869122 132 VKQNAWIGAGATILPSVTVGKNAIVAAGSVVT--KDVPANTIVAGVPAKIVKIIDE 185
Cdd:cd04650   81 VGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTpgKEIPDYSLVLGVPAKVVRKLTE 136
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 130-180 1.17e-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: 47.43  E-value: 1.17e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 306869122 130 VIVKQNAWIGAGATILPSVTVGKNAIVAAGSVVTKDVPANTIVAGVPAKIV 180
Cdd:cd03351  139 VEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARLR 189
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 135-181 2.09e-06

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 46.78  E-value: 2.09e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 306869122 135 NAWIGAGATILPSVTVGKNAIVAAGSVVTKDVPANTIVAGVPAKIVK 181
Cdd:PRK14353 386 GAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALGRARQETK 432
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 128-177 4.91e-06

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: 44.29  E-value: 4.91e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 306869122 128 KPVIVKQNAWIGAGATILPSVTVGKNAIVAAGSVVTK---------------DVPAN-TIVAGVPA 177
Cdd:cd03350   74 TPVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTQstpiydretgeiyygRVPPGsVVVAGSLP 139
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 138-178 7.49e-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: 45.01  E-value: 7.49e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 306869122 138 IGAGATILPSVTVGKNAIVAAGSVVTKDVPANTIVAGVPAK 178
Cdd:COG1044  267 IGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSGSPAQ 307
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 104-181 4.01e-05

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 42.99  E-value: 4.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869122 104 LAPRVNI----ITVNHPtdpqtrrGVIVKPVIVKQNAWIGAGATILPSVTVGKNAIVAAGSVVTKDVPANTIVAGVPAKI 179
Cdd:PRK14360 368 LGEQVNIgagtITANYD-------GVKKHRTVIGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLAIARSRQV 440


                 ..
gi 306869122 180 VK 181
Cdd:PRK14360 441 IK 442
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 75-171 7.53e-05

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 42.42  E-value: 7.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 306869122  75 HLRIGKnvFINTACVFTDLGG----ITLEDNVLLAPRVNI----ITVNHPtdpqtrrGVIVKPVIVKQNAWIGAGATILP 146
Cdd:PRK14355 344 HVKIGN--FVETKKIVMGEGSkashLTYLGDATIGRNVNIgcgtITCNYD-------GVKKHRTVIEDDVFVGSDVQFVA 414

                         90       100
                 ....*....|....*....|....*
gi 306869122 147 SVTVGKNAIVAAGSVVTKDVPANTI 171
Cdd:PRK14355 415 PVTVGRNSLIAAGTTVTKDVPPDSL 439
PRK10191 PRK10191
putative acyl transferase; Provisional
 129-183 1.44e-04

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 40.26  E-value: 1.44e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 306869122 129 PVIvKQNAWIGAGATILPSVTVGKNAIVAAGSVVTKDVPANTIVAGVPAKiVKII 183
Cdd:PRK10191  93 PHI-GNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKAR-VKVI 145
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
130-179 2.44e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 40.47  E-value: 2.44e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 306869122 130 VIVKQNAWIGAGATILPSVTVGKNAIVAAGSVVTKDVPANTIVAGVPAKI 179
Cdd:PRK05289 142 VEVGDYAIIGGLTAVHQFVRIGAHAMVGGMSGVSQDVPPYVLAEGNPARL 191
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 131-172 1.53e-03

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 38.47  E-value: 1.53e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 306869122 131 IVKQNAWIGAGATILPSVTVGKNAIVAAGSVVTKDVPANTIV 172
Cdd:PRK09451 396 IIGDDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDVAENELV 437
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 138-178 1.95e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 37.81  E-value: 1.95e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 306869122 138 IGAGATILPSVTVGKNAIVAAGSVVTKDVPA-NTIVAGVPAK 178
Cdd:PRK00892 270 IGGQVGIAGHLEIGDGVTITAMSGVTKSIPEpGEYSSGIPAQ 311
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 129-180 2.39e-03

Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; Tetrahydrodipicolinate N-succinyltransferase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 441774 [Multi-domain]  Cd Length: 268  Bit Score: 37.40  E-value: 2.39e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 306869122 129 PVIVKQNAWIGAGATILPSVTVGKNAIVAAGSVVTK-----DVPANTIVAG-VPAKIV 180
Cdd:COG2171  170 PVIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLTAstkiyDRVTGEVYYGrVPAGSV 227
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
129-158 3.23e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.85  E-value: 3.23e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 306869122  129 PVIVKQNAWIGAGATILPSVTVGKNAIVAA 158
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
130-164 7.98e-03

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 32.80  E-value: 7.98e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 306869122  130 VIVKQNAWIGAGATIlpSVTVGKNAIVAAGSVVTK 164
Cdd:pfam14602   1 VIIGDNCLIGANSGI--GVSLGDNCVVGAGVVITA 33
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 129-180 8.25e-03

2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 35.94  E-value: 8.25e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 306869122 129 PVIVKQNAWIGAGATILPSVTVGKNAIVAAGSVVTK-----DVPANTIVAG-VPAKIV 180
Cdd:PRK11830 176 PVIIEDNCFIGARSEVVEGVIVEEGSVLGMGVFLGQstkiyDRETGEVHYGrVPAGSV 233
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 138-172 8.62e-03

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 36.07  E-value: 8.62e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 306869122 138 IGAGATILPSVTVGKNAIVAAGSVVTKDVPANTIV 172
Cdd:PRK14352 408 TGSDTMFVAPVTVGDGAYTGAGTVIREDVPPGALA 442
 
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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