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Conserved domains on  [gi|1072035592|gb|AOT19534|]
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serine acetyltransferase [Pseudoalteromonas luteoviolacea]

Protein Classification

acyltransferase( domain architecture ID 10213561)

acyltransferase belonging to the transferase hexapeptide repeat family, catalyzes the transfer of an acyl group from an acyl-CoA to a substrate; similar to O-antigen biosynthesis protein WlbB, a bacterial N-acetyltransferase involved in the biosynthesis of 2,3-diacetamido-2,3-dideoxy-D-mannuronic acid

CATH:  2.160.10.10
EC:  2.3.1.-
Gene Ontology:  GO:0016746|GO:0120225
PubMed:  15500694

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 35-153 1.87e-61

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: 186.55  E-value: 1.87e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  35 IGKGCSLGQNVFVGNKVTIGNNVKVQNNVSVYDNVYLEDDVFCGPSMVFTNVYNPRSFIERKTEYRDTIVKKGATLGANC 114
Cdd:cd03358     1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKIYRKWELKGTTVKRGASIGANA 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1072035592 115 TVVCGVTIGEYSLVGAGAVINKDVKPFALMVGVPAKQIG 153
Cdd:cd03358    81 TILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
LbetaH super family cl00160
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 2-65 6.92e-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.


The actual alignment was detected with superfamily member cd00208:

Pssm-ID: 469633 [Multi-domain]  Cd Length: 78  Bit Score: 39.54  E-value: 6.92e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1072035592   2 NYQVHASAIIDDGAQIGDDTRVWHFAHVCG--------GAQIGKGCSLGQNVFVGNKVTIGNNVKVQNNVSV 65
Cdd:cd00208     6 GVKIHPKAVIRGPVVIGDNVNIGPGAVIGAatgpneknPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVV 77
 
Name Accession Description Interval E-value
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 35-153 1.87e-61

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: 186.55  E-value: 1.87e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  35 IGKGCSLGQNVFVGNKVTIGNNVKVQNNVSVYDNVYLEDDVFCGPSMVFTNVYNPRSFIERKTEYRDTIVKKGATLGANC 114
Cdd:cd03358     1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKIYRKWELKGTTVKRGASIGANA 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1072035592 115 TVVCGVTIGEYSLVGAGAVINKDVKPFALMVGVPAKQIG 153
Cdd:cd03358    81 TILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
32-157 3.53e-33

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 115.35  E-value: 3.53e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  32 GAQIGKGCSLGQNVFV-GNKVTIGNNVKVQNNVSVYD--NVYLEDDVFCGPSMVFTNVYNPRSFIERKTEY-RDTIVKKG 107
Cdd:COG0110     8 GARIGDGVVIGPGVRIyGGNITIGDNVYIGPGVTIDDpgGITIGDNVLIGPGVTILTGNHPIDDPATFPLRtGPVTIGDD 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1072035592 108 ATLGANCTVVCGVTIGEYSLVGAGAVINKDVKPFALMVGVPAKQIGWISK 157
Cdd:COG0110    88 VWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDE 137
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 5-149 9.11e-16

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: 71.76  E-value: 9.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592   5 VHASAIIDDGAQIGDDTRVWHFAHVCGGAQIGKGCSLGQNVFVGNKVTIGNNVKVQNNVSVYDNVYLEDDVFcgpsmvft 84
Cdd:TIGR03570  90 IHPSAIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVIGEGVF-------- 161

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1072035592  85 nvynprsfierkteyrdtivkkgatLGANCTVVCGVTIGEYSLVGAGAVINKDVKPFALMVGVPA 149
Cdd:TIGR03570 162 -------------------------IGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 5-75 1.58e-14

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 70.17  E-value: 1.58e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1072035592   5 VHASAIIDDGAQIGDDTRVWHFAHVCGGAQIGKGCSLGQNVFVGNKVTIGNNVKVQNNVSVYDNVYLEDDV 75
Cdd:PRK00892  103 IHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNRV 173
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 2-65 6.92e-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: 39.54  E-value: 6.92e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1072035592   2 NYQVHASAIIDDGAQIGDDTRVWHFAHVCG--------GAQIGKGCSLGQNVFVGNKVTIGNNVKVQNNVSV 65
Cdd:cd00208     6 GVKIHPKAVIRGPVVIGDNVNIGPGAVIGAatgpneknPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVV 77
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
14-42 2.86e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.85  E-value: 2.86e-03
                          10        20
                  ....*....|....*....|....*....
gi 1072035592  14 GAQIGDDTRVWHFAHVCGGAQIGKGCSLG 42
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIG 29
 
Name Accession Description Interval E-value
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 35-153 1.87e-61

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: 186.55  E-value: 1.87e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  35 IGKGCSLGQNVFVGNKVTIGNNVKVQNNVSVYDNVYLEDDVFCGPSMVFTNVYNPRSFIERKTEYRDTIVKKGATLGANC 114
Cdd:cd03358     1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKIYRKWELKGTTVKRGASIGANA 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1072035592 115 TVVCGVTIGEYSLVGAGAVINKDVKPFALMVGVPAKQIG 153
Cdd:cd03358    81 TILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
32-157 3.53e-33

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 115.35  E-value: 3.53e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  32 GAQIGKGCSLGQNVFV-GNKVTIGNNVKVQNNVSVYD--NVYLEDDVFCGPSMVFTNVYNPRSFIERKTEY-RDTIVKKG 107
Cdd:COG0110     8 GARIGDGVVIGPGVRIyGGNITIGDNVYIGPGVTIDDpgGITIGDNVLIGPGVTILTGNHPIDDPATFPLRtGPVTIGDD 87

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1072035592 108 ATLGANCTVVCGVTIGEYSLVGAGAVINKDVKPFALMVGVPAKQIGWISK 157
Cdd:COG0110    88 VWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDE 137
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 35-152 3.47e-23

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: 88.67  E-value: 3.47e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  35 IGKGCSLGQNVFV--GNKVTIGNNVKVQNNVSVYDNvyleddvfcgpsmvFTNVYNPRSFIERKTEYRDTIVKKGATLGA 112
Cdd:cd04647     4 IGDNVYIGPGCVIsaGGGITIGDNVLIGPNVTIYDH--------------NHDIDDPERPIEQGVTSAPIVIGDDVWIGA 69

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1072035592 113 NCTVVCGVTIGEYSLVGAGAVINKDVKPFALMVGVPAKQI 152
Cdd:cd04647    70 NVVILPGVTIGDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 5-150 3.08e-16

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: 75.05  E-value: 3.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592   5 VHASAIIDDGAQIGDDTRVWHFAHVCGGAQIGKGCSLGQNVFVGNKVTIGNNVKVQNNVSVYDNVYLEDDVFCGPSMV-- 82
Cdd:COG1044    99 IHPSAVIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVIGDRVIIHSGAVig 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  83 -----FTNVYNPR---------------------SFIERKTeYRDTIVKKGA------------TLGANCtVVCG----- 119
Cdd:COG1044   179 adgfgFAPDEDGGwvkipqlgrvvigddveiganTTIDRGA-LGDTVIGDGTkidnlvqiahnvRIGEHT-AIAAqvgia 256

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1072035592 120 --VTIGEYSL------------------VGAGAVINKDVKPFALMVGVPAK 150
Cdd:COG1044   257 gsTKIGDNVViggqvgiaghltigdgviIGAQSGVTKSIPEGGVYSGSPAQ 307
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 5-149 9.11e-16

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: 71.76  E-value: 9.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592   5 VHASAIIDDGAQIGDDTRVWHFAHVCGGAQIGKGCSLGQNVFVGNKVTIGNNVKVQNNVSVYDNVYLEDDVFcgpsmvft 84
Cdd:TIGR03570  90 IHPSAIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVIGEGVF-------- 161

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1072035592  85 nvynprsfierkteyrdtivkkgatLGANCTVVCGVTIGEYSLVGAGAVINKDVKPFALMVGVPA 149
Cdd:TIGR03570 162 -------------------------IGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 27-148 1.01e-14

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 69.05  E-value: 1.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  27 AHVCGGAQIGKGCSLGQNVFVGNKVTIGNNVKVQNNVSV-YDNVyLEDDVFCGPSMVFT-NVynprsfierkteyrdtIV 104
Cdd:cd03360    91 AVVSPSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIgHDCV-IGDFVHIAPGVVLSgGV----------------TI 153

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1072035592 105 KKGATLGANCTVVCGVTIGEYSLVGAGAVINKDVKPFALMVGVP 148
Cdd:cd03360   154 GEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 33-152 1.03e-14

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: 68.22  E-value: 1.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  33 AQIGKGCSLGQNVFV--GNKVTIGNNVKVQNNVSVYDN--VYLEDDVFCGPSMVFTNVYNPRSFIERKT--EY-RDTIVK 105
Cdd:cd03357    43 GSVGENVYIEPPFHCdyGYNIHIGDNFYANFNCTILDVapVTIGDNVLIGPNVQIYTAGHPLDPEERNRglEYaKPITIG 122

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1072035592 106 KGATLGANCTVVCGVTIGEYSLVGAGAVINKDVKPFALMVGVPAKQI 152
Cdd:cd03357   123 DNVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 5-75 1.58e-14

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 70.17  E-value: 1.58e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1072035592   5 VHASAIIDDGAQIGDDTRVWHFAHVCGGAQIGKGCSLGQNVFVGNKVTIGNNVKVQNNVSVYDNVYLEDDV 75
Cdd:PRK00892  103 IHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNRV 173
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 4-150 6.38e-13

UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this family catalyze the transfer of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to UDP-GlcNAc. It is the first enzyme in the lipid A biosynthetic pathway and is also referred to as LpxA. Lipid A is essential for the growth of Escherichia coli and related bacteria. It is also essential for maintaining the integrity of the outer membrane. UDP-GlcNAc acyltransferase is a homotrimer of left-handed parallel beta helix (LbH) subunits. Each subunit contains an N-terminal LbH region with 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal alpha-helical region.


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 65.15  E-value: 6.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592   4 QVHASAIIDDGAQIGDDTRVWHFAHVCGGAQIGKGCSLGQNVFVGNKVTIGNNVKVQNNVSV----YDNVYLEDDVFC-- 77
Cdd:cd03351     1 MIHPTAIVDPGAKIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIgeapQDLKYKGEPTRLei 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  78 GPSMVFtnvynpRSF--IERKTE----------------Y----------RDTIVKKGATLGANCTV----VCG------ 119
Cdd:cd03351    81 GDNNTI------REFvtIHRGTAqgggvtrignnnllmaYvhvahdcvigNNVILANNATLAGHVEIgdyaIIGglsavh 154

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1072035592 120 --VTIGEYSLVGAGAVINKDVKPFALMVGVPAK 150
Cdd:cd03351   155 qfCRIGRHAMVGGGSGVVQDVPPYVIAAGNRAR 187
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 23-153 3.63e-12

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: 61.64  E-value: 3.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  23 VWHFAHVCGGAQIGKGCSLGQNVFV--GNKVTIGNNVKVQNNVSVYDNVYLeddvfcGPsmvftnvynpRSFIERKteyR 100
Cdd:COG1045    56 LSERARFLTGIDIHPGATIGRGFFIdhGTGVVIGETAVIGDNVTIYQGVTL------GG----------TGKEKGK---R 116

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1072035592 101 DTIVKKGATLGANCTVVCGVTIGEYSLVGAGAVINKDVKPFALMVGVPAKQIG 153
Cdd:COG1045   117 HPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVK 169
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 2-154 4.03e-12

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 63.79  E-value: 4.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592   2 NYQVHASAIIDdgAQIGDDTRVWHFAHVCGGAQIGKGCSLGQNVFVgNKVTIGNNVKVqNNVSVYDNVYLEDDVFCGPSM 81
Cdd:PRK14360  303 NVTVLYSVVSD--SQIGDGVKIGPYAHLRPEAQIGSNCRIGNFVEI-KKSQLGEGSKV-NHLSYIGDATLGEQVNIGAGT 378

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1072035592  82 VFTNvYNPrsfiERKTEyrdTIVKKGATLGANCTVVCGVTIGEYSLVGAGAVINKDVKPFALMVGvPAKQI---GW 154
Cdd:PRK14360  379 ITAN-YDG----VKKHR---TVIGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLAIA-RSRQVikeNW 445
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 7-151 4.62e-12

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: 61.67  E-value: 4.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592   7 ASAIIDDGAQIGDDTRVWHFAHVCGGAQIGKGCSLGQNVFVGNkVTIGNNVKVQNNvSVYDNVYLEDDVFCGP------- 79
Cdd:cd03353     8 ETTYIDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIKD-STIGDGVVIKAS-SVIEGAVIGNGATVGPfahlrpg 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  80 SMVFTNVY--NprsFIERKT---------------------------------------EYRdTIVKKGATLGANCTVVC 118
Cdd:cd03353    86 TVLGEGVHigN---FVEIKKstigegskanhlsylgdaeigegvnigagtitcnydgvnKHR-TVIGDNVFIGSNSQLVA 161

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1072035592 119 GVTIGEYSLVGAGAVINKDVKPFALMVGVpAKQ 151
Cdd:cd03353   162 PVTIGDGATIAAGSTITKDVPPGALAIAR-ARQ 193
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 15-150 6.35e-12

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: 61.66  E-value: 6.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  15 AQIGDDTRVWHFAHVCGGAQIGKGCSLGQNVFVGNKVTIGNNVKVQNNVSVYDNVYLEDDVFCGPSMV-----FTNVYNP 89
Cdd:cd03352     2 AKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVigsdgFGFAPDG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  90 RSF----------IERKTE-----------YRDTIVKKG------------------------------ATLGANCT--- 115
Cdd:cd03352    82 GGWvkipqlggviIGDDVEiganttidrgaLGDTVIGDGtkidnlvqiahnvrigencliaaqvgiagsTTIGDNVIigg 161

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1072035592 116 ---VVCGVTIGEYSLVGAGAVINKDVKPFALMVGVPAK 150
Cdd:cd03352   162 qvgIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQ 199
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 4-150 6.39e-12

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: 62.34  E-value: 6.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592   4 QVHASAIIDDGAQIGDDTRVWHFAHVCGGAQIGKGCSLGQNVFVGNKVTIGNNVKV----------Q------------- 60
Cdd:COG1043     3 MIHPTAIVDPGAKLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIfpfasigeepQdlkykgeptrlei 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  61 --NNV------------------SVYDNVYLeddvfcgpsMVFTNV------YNprsfierkteyrDTIVKKGATLGANC 114
Cdd:COG1043    83 gdNNTirefvtihrgtvqgggvtRIGDDNLL---------MAYVHVahdcvvGN------------NVILANNATLAGHV 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1072035592 115 TV--------VCGV----TIGEYSLVGAGAVINKDVKPFALMVGVPAK 150
Cdd:COG1043   142 EVgdhaiiggLSAVhqfvRIGAHAMVGGGSGVVKDVPPYVLAAGNPAR 189
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 4-154 8.94e-12

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: 62.74  E-value: 8.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592   4 QVHASAIIDDgAQIGDDTRVwHFAHVCGgAQIGKGCS------------LGQNVFVGN-----KVTIGNNVKVqNNVSvy 66
Cdd:COG1207   292 VIGPNCTLKD-STIGDGVVI-KYSVIED-AVVGAGATvgpfarlrpgtvLGEGVKIGNfvevkNSTIGEGSKV-NHLS-- 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  67 dnvYLED-----DVFCGPSMVFTNvYNprsfieRKTEYRdTIVKKGATLGANCTVVCGVTIGEYSLVGAGAVINKDVKPF 141
Cdd:COG1207   366 ---YIGDaeigeGVNIGAGTITCN-YD------GVNKHR-TVIGDGAFIGSNTNLVAPVTIGDGATIGAGSTITKDVPAG 434

                         170
                  ....*....|....*.
gi 1072035592 142 ALMVGVpAKQI---GW 154
Cdd:COG1207   435 ALAIAR-ARQRnieGW 449
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 35-154 1.59e-11

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: 59.09  E-value: 1.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  35 IGKGCSLGQNVfvgnKVTIGNNVKVqNNVSVYdnvyleddvfcgPSMVFTNVYNPRSFIERKTEYRDTIVKKGATLGANC 114
Cdd:cd03349    24 IGKFCSIAPGV----KIGLGGNHPT-DWVSTY------------PFYIFGGEWEDDAKFDDWPSKGDVIIGNDVWIGHGA 86

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1072035592 115 TVVCGVTIGEYSLVGAGAVINKDVKPFALMVGVPAKQIGW 154
Cdd:cd03349    87 TILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRY 126
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 4-152 2.93e-11

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 58.89  E-value: 2.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592   4 QVHASAIIDDGAQ------IGDDTRVWHFAhvcggaqigkgcslgqnVFVG--NKVTIGNNVKVQNNVSV-----YDnVY 70
Cdd:COG0663    12 QIHPSAFVAPTAVvigdvtIGEDVSVWPGA-----------------VLRGdvGPIRIGEGSNIQDGVVLhvdpgYP-LT 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  71 LEDDVFCGP-SMVftnvynprsfierkteyrdtivkKGATLGANC------TVVCGVTIGEYSLVGAGAVI--NKDVKPF 141
Cdd:COG0663    74 IGDDVTIGHgAIL-----------------------HGCTIGDNVligmgaIVLDGAVIGDGSIVGAGALVteGKVVPPG 130

                         170
                  ....*....|.
gi 1072035592 142 ALMVGVPAKQI 152
Cdd:COG0663   131 SLVVGSPAKVV 141
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
1-150 4.24e-11

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 60.11  E-value: 4.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592   1 MNYQVHASAIIDDGAQIGDDTRVWHFAHVCGGAQIGKGCSLGQNVFVGNKVTIGNNVKVQNNVSV--------YDNvyle 72
Cdd:PRK05289    1 MMAKIHPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIgedpqdlkYKG---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  73 ddvfcGPSMVFTNVYNP-RSF--IERKTE----------------Y----------RDTIVKKGATLGANCTV------- 116
Cdd:PRK05289   77 -----EPTRLVIGDNNTiREFvtINRGTVqgggvtrigdnnllmaYvhvahdcvvgNHVILANNATLAGHVEVgdyaiig 151

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1072035592 117 -VCGV----TIGEYSLVGAGAVINKDVKPFALMVGVPAK 150
Cdd:PRK05289  152 gLTAVhqfvRIGAHAMVGGMSGVSQDVPPYVLAEGNPAR 190
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-159 8.87e-11

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 59.85  E-value: 8.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592   5 VHASAIIDdgAQIGDDTRVWHFAHvcggaqIGKGCSLGQNVFVGN-----KVTIGNNVKVQN-----NVSVYDNVyledD 74
Cdd:PRK14354  309 ITNSVIEE--SKVGDNVTVGPFAH------LRPGSVIGEEVKIGNfveikKSTIGEGTKVSHltyigDAEVGENV----N 376

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  75 VFCGpsMVFTNvYNPrsfierKTEYRdTIVKKGATLGANCTVVCGVTIGEYSLVGAGAVINKDVKPFALMVGvPAKQI-- 152
Cdd:PRK14354  377 IGCG--TITVN-YDG------KNKFK-TIIGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDALAIA-RARQVnk 445


                  ....*...
gi 1072035592 153 -GWISKFG 159
Cdd:PRK14354  446 eGYVKKLP 453
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 32-148 2.14e-10

Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetylserine, as the first step of a two-step biosynthetic pathway in bacteria and plants leading to the formation of L-cysteine. This reaction represents a key metabolic point of regulation for the cysteine biosynthetic pathway due to its feedback inhibition by cysteine. The enzyme is a 175 kDa homohexamer, composed of a dimer of homotrimers. Each subunit contains an N-terminal alpha helical region and a C-terminal left-handed beta-helix (LbH) subdomain with 5 turns, each containing a hexapeptide repeat motif characteristic of the acyltransferase superfamily of enzymes. The trimer interface mainly involves the C-terminal LbH subdomain while the dimer (of trimers) interface is mediated by the N-terminal alpha helical subdomain.


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 55.14  E-value: 2.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  32 GAQIGKGCSL--GQNVFVGNKVTIGNNVKVQNNVSVydnvyleddvfcGPSMVFTNVYNPrsfierkteyrdtIVKKGAT 109
Cdd:cd03354     8 GAKIGPGLFIdhGTGIVIGETAVIGDNCTIYQGVTL------------GGKGKGGGKRHP-------------TIGDNVV 62

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1072035592 110 LGANCTVVCGVTIGEYSLVGAGAVINKDVKPFALMVGVP 148
Cdd:cd03354    63 IGAGAKILGNITIGDNVKIGANAVVTKDVPANSTVVGVP 101
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 2-153 2.31e-10

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 57.72  E-value: 2.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592   2 NYQVHASAIIDDGAQIGDDTRVWHFAHVCGGAQIGKGCSLGQNVFVGN------------KVTIGNNVKVQNNVSVY--- 66
Cdd:PRK12461   17 GVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGDepqdftykgeesRLEIGDRNVIREGVTIHrgt 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  67 ---------------DNVYLEDDVFCGPSMVFTNVYNPRSFIErkteyrdtiVKKGATLGANCTVVCGVTIGEYSLVGAG 131
Cdd:PRK12461   97 kgggvtrigndnllmAYSHVAHDCQIGNNVILVNGALLAGHVT---------VGDRAIISGNCLVHQFCRIGALAMMAGG 167

                         170       180
                  ....*....|....*....|..
gi 1072035592 132 AVINKDVKPFALMVGVPAKQIG 153
Cdd:PRK12461  168 SRISKDVPPYCMMAGHPTNVHG 189
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 14-162 4.37e-10

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 57.85  E-value: 4.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  14 GAQIGDDTRVWHFAhvcggaQIGKGCSLGQNVFVGN-----KVTIGNNVKVQNnVSVYDNVYLEDDVFCGPSMVFTNvyn 88
Cdd:PRK14357  306 KSVIEDDVSVGPFS------RLREGTVLKKSVKIGNfveikKSTIGENTKAQH-LTYLGDATVGKNVNIGAGTITCN--- 375

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1072035592  89 prsfIERKTEYRdTIVKKGATLGANCTVVCGVTIGEYSLVGAGAVINKDVKPFALMVGvPAKQI---GWISKFGEQL 162
Cdd:PRK14357  376 ----YDGKKKNP-TFIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALG-RARQIvkeGWVLKKRKEE 446
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 15-146 6.30e-10

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 57.43  E-value: 6.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  15 AQIGDDTRVWHFAHVcGGAQIGKGCSLG------------QNVFVGN-----KVTIGNNVKVqNNVSVYDNVYLEDDVFC 77
Cdd:PRK14356  305 AVVSSGATIHSFSHL-EGAEVGDGCSVGpyarlrpgavleEGARVGNfvemkKAVLGKGAKA-NHLTYLGDAEIGAGANI 382

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1072035592  78 GPSMVFTNvYnprsfiERKTEYRdTIVKKGATLGANCTVVCGVTIGEYSLVGAGAVINKDVKPFALMVG 146
Cdd:PRK14356  383 GAGTITCN-Y------DGVNKHR-TVIGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSLAIA 443
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 40-161 7.72e-10

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 55.78  E-value: 7.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  40 SLGQNVFVGNK--------------VTIGNNVKVQNNVS-------VYDNVYLEDDVFCGPSMVFTNVYnprsfierkte 98
Cdd:PRK09527   71 SYGSNIHIGRNfyanfnltivddytVTIGDNVLIAPNVTlsvtghpVHHELRKNGEMYSFPITIGNNVW----------- 139

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1072035592  99 yrdtivkkgatLGANCTVVCGVTIGEYSLVGAGAVINKDVKPFALMVGVPAKQIGWISKFGEQ 161
Cdd:PRK09527  140 -----------IGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIREINDRDKQ 191
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 11-143 1.91e-09

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 55.91  E-value: 1.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  11 IDDGAQIGDDTRVWHFAHVCGGAQIGKGCSLGQNVFVGNkVTIGNNVKVQNNvSVYDNVYLEDDVFCGPsMVFT---NVY 87
Cdd:PRK14355  265 IDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVIKG-CRIGDDVTVKAG-SVLEDSVVGDDVAIGP-MAHLrpgTEL 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  88 NPRSFIERKTEYRDTIVKKG-----------ATLGANCTVVCG-------------------------------VTIGEY 125
Cdd:PRK14355  342 SAHVKIGNFVETKKIVMGEGskashltylgdATIGRNVNIGCGtitcnydgvkkhrtvieddvfvgsdvqfvapVTVGRN 421

                         170
                  ....*....|....*...
gi 1072035592 126 SLVGAGAVINKDVKPFAL 143
Cdd:PRK14355  422 SLIAAGTTVTKDVPPDSL 439
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 51-135 2.16e-09

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 51.87  E-value: 2.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  51 VTIGNNVKVQNNVSVYDNVYLEDDVFCGPSMVFTNVYNPrsfierkTEYRDTIVKKGATLGANCTVVCGVTIGEYSLVGA 130
Cdd:cd00208     1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGP-------NEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGA 73


                  ....*
gi 1072035592 131 GAVIN 135
Cdd:cd00208    74 GAVVT 78
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 11-162 2.16e-09

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 55.64  E-value: 2.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  11 IDDGAQIgddtRVW-HF--AHVCGGAQIGK------GCSLGQNVFVGN-----KVTIGNNVKVqNNVSvydnvYLeDDVF 76
Cdd:PRK14353  289 VASGAVI----HAFsHLegAHVGEGAEVGPyarlrpGAELGEGAKVGNfvevkNAKLGEGAKV-NHLT-----YI-GDAT 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  77 CGPSmvfTNV------YNPRSFIERKTEyrdtiVKKGATLGANCTVVCGVTIGEYSLVGAGAVINKDVKPFALMVGvPAK 150
Cdd:PRK14353  358 IGAG---ANIgagtitCNYDGFNKHRTE-----IGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALG-RAR 428

                         170
                  ....*....|....*
gi 1072035592 151 QI---GWISKFGEQL 162
Cdd:PRK14353  429 QEtkpGWAKKLRERL 443
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 22-152 2.08e-08

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 51.80  E-value: 2.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  22 RVWHFAHVCGGAQIGKGCSLGQNVFVGNKVTIGNNVKVQNNVSV--YDNVYLEDDVFCGpSMVFTNVYNPRSF------- 92
Cdd:PRK09677   37 YIRNDGSINFGEGFTSGVGLRLDAFGRGKLFFGDNVQVNDYVHIacIESITIGRDTLIA-SKVFITDHNHGSFkhsddfs 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1072035592  93 ------IERKTEYRDTIVKKGATLGANCTVVCGVTIGEYSLVGAGAVINKDVKPFALMVGVPAKQI 152
Cdd:PRK09677  116 spnlppDMRTLESSAVVIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKII 181
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 9-141 9.75e-08

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: 48.92  E-value: 9.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592   9 AIIDDGAQIGDDTRVWHFAHVCGGAQIGKGCSLGQNVFVGNKVTIGNNVKVQNNVSVydnvyleddvfcgpsmvfTNVYN 88
Cdd:cd03350     8 AIIRDGAFIGPGAVLMMPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVI------------------GGVLE 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1072035592  89 PrsfierkTEYRDTIVKKGATLGANCTVVCGVTIGEYSLVGAGAVINKDVKPF 141
Cdd:cd03350    70 P-------LQATPVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTQSTPIY 115
PRK10502 PRK10502
putative acyl transferase; Provisional
 32-150 1.32e-07

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 49.18  E-value: 1.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  32 GAQIGKGC--------------SLGQNVFVGNKVTIGN--NVKVQNNVSVYDNVYLeddvfCGPSMVFTNvynpRSFier 95
Cdd:PRK10502   51 GAKIGKGVvirpsvritypwklTIGDYAWIGDDVWLYNlgEITIGAHCVISQKSYL-----CTGSHDYSD----PHF--- 118

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  96 kteyrDTIVK-----KGATLGANCTVVCGVTIGEYSLVGAGAVINKDVKPFALMVGVPAK 150
Cdd:PRK10502  119 -----DLNTApivigEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAV 173
PLN02739 PLN02739
serine acetyltransferase
 32-157 1.50e-07

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 50.42  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  32 GAQIGKGCSL--GQNVFVGNKVTIGNNVKVQNNVSVydnvyleddvfcgpsmvftnvynprSFIERKTEYRDTIVKKGAT 109
Cdd:PLN02739  211 AARIGKGILLdhGTGVVIGETAVIGDRVSILHGVTL-------------------------GGTGKETGDRHPKIGDGAL 265

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1072035592 110 LGANCTVVCGVTIGEYSLVGAGAVINKDVKPFALMVGVPAKQIGWISK 157
Cdd:PLN02739  266 LGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFVDE 313
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 5-152 2.34e-07

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


Pssm-ID: 100055 [Multi-domain]  Cd Length: 154  Bit Score: 48.34  E-value: 2.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592   5 VHASAIIDDGAQIGDDTRVWHFAHVCG---GAQIGKGCSLGQNVFV----GNKVTIGNNVKVQNNVSVYDnvyleddvfc 77
Cdd:cd04650     9 VHPTSYVIGDVVIGELTSVWHYAVIRGdndSIYIGKYSNVQENVSIhtdhGYPTEIGDYVTIGHNAVVHG---------- 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1072035592  78 gpSMVFTNVynprsfierkteyrdtIVKKGATLganctvVCGVTIGEYSLVGAGAVI--NKDVKPFALMVGVPAKQI 152
Cdd:cd04650    79 --AKVGNYV----------------IVGMGAIL------LNGAKIGDHVIIGAGAVVtpGKEIPDYSLVLGVPAKVV 131
PLN02694 PLN02694
serine O-acetyltransferase
 33-165 4.43e-07

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 48.87  E-value: 4.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  33 AQIGKGCSL--GQNVFVGNKVTIGNNVKVQNNVSVYDNVYLEDDvfcgpsmvftnvynprsfierkteyRDTIVKKGATL 110
Cdd:PLN02694  167 AKIGKGILFdhATGVVIGETAVIGNNVSILHHVTLGGTGKACGD-------------------------RHPKIGDGVLI 221

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1072035592 111 GANCTVVCGVTIGEYSLVGAGAVINKDVKPFALMVGVPAKQIGWISKFGEQLDLP 165
Cdd:PLN02694  222 GAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLVGGKEKPAKHEECP 276
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 107-152 5.12e-07

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: 46.06  E-value: 5.12e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1072035592 107 GATLGANCTVVCGVTIGEYSLVGAGAVINKDVKPFALMVGVPAKQI 152
Cdd:cd05825    62 GAWVAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
PLN02357 PLN02357
serine acetyltransferase
 32-153 5.37e-07

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 48.72  E-value: 5.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  32 GAQIGKGCSL--GQNVFVGNKVTIGNNVKVQNNVSVYDNVYLEDDvfcgpsmvftnvynprsfierkteyRDTIVKKGAT 109
Cdd:PLN02357  232 GAKIGQGILLdhATGVVIGETAVVGNNVSILHNVTLGGTGKQSGD-------------------------RHPKIGDGVL 286

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1072035592 110 LGANCTVVCGVTIGEYSLVGAGAVINKDVKPFALMVGVPAKQIG 153
Cdd:PLN02357  287 IGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLIG 330
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 4-152 3.44e-06

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: 44.71  E-value: 3.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592   4 QVHASAIIDDGAQigddtrvwhfahVCGGAQIGKGCSLGQNVFV---GNKVTIGNNVKVQNNVSVydnvyleddvfcgps 80
Cdd:cd04645     1 EIDPSAFIAPNAT------------VIGDVTLGEGSSVWFGAVLrgdVNPIRIGERTNIQDGSVL--------------- 53

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  81 mvftnvynprsfieRKTEYRDTIVKKGATLGANCTVVcGVTIGEYSLVGAGAVI--------------------NKDVKP 140
Cdd:cd04645    54 --------------HVDPGYPTIIGDNVTVGHGAVLH-GCTIGDNCLIGMGAIIldgavigkgsivaagslvppGKVIPP 118

                         170
                  ....*....|..
gi 1072035592 141 FALMVGVPAKQI 152
Cdd:cd04645   119 GSLVAGSPAKVV 130
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 13-157 2.07e-05

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 44.16  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  13 DGAQIGDDTRVWHFAHVCGGAQIGKGCSLGqnVFVGNK-VTIGNNVKVQNNVSVYDNVyLEDDVFCGPSMVFTNvYNPrs 91
Cdd:PRK14352  321 SESEIGAGATVGPFTYLRPGTVLGEEGKLG--AFVETKnATIGRGTKVPHLTYVGDAD-IGEHSNIGASSVFVN-YDG-- 394

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1072035592  92 fiERKteyRDTIVKKGATLGANCTVVCGVTIGEYSLVGAGAVINKDVKPFALMV-GVPAKQI-GWISK 157
Cdd:PRK14352  395 --VNK---HRTTIGSHVRTGSDTMFVAPVTVGDGAYTGAGTVIREDVPPGALAVsEGPQRNIeGWVQR 457
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 46-134 3.38e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 43.20  E-value: 3.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  46 FVGNKVTIGNNVKVQNNVSVYDNVYLEDDVFCGPSmvftnvynprSFIerkteYRDTIVKKGATLGANCTVVCGVTIGEY 125
Cdd:PRK00892  108 VIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAG----------AVI-----GDGVKIGADCRLHANVTIYHAVRIGNR 172


                  ....*....
gi 1072035592 126 SLVGAGAVI 134
Cdd:PRK00892  173 VIIHSGAVI 181
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 5-134 4.70e-05

Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix (LbH) domain: Proteins in this family show simlarity to glucose-1-phosphate adenylyltransferases in that they contain N-terminal catalytic domains that resemble a dinucleotide-binding Rossmann fold and C-terminal LbH fold domains. Members in this family are predicted to be glucose-1-phosphate thymidylyltransferases, which are involved in the dTDP-L-rhamnose biosynthetic pathway. Glucose-1-phosphate thymidylyltransferase catalyzes the synthesis of deoxy-thymidine di-phosphate (dTDP)-L-rhamnose, an important component of the cell wall of many microorganisms. The C-terminal LbH domain contains multiple 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.


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 41.80  E-value: 4.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592   5 VHASAIIDDGAQ------IGDDTRVWHFAHVCGGAQIGKGCSLGQNVFVGNKVtIGNNVKVQNNVSVYDNVyLEDDVFCG 78
Cdd:cd05636    20 IGEGAIVRSGAYiegpviIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSI-IMDGTKVPHLNYVGDSV-LGENVNLG 97

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1072035592  79 PSMVFTNVYNPRSF--IERKTEYRDTIVKK-GATLGANCTVVC------GVTIGEYSLVGAGAVI 134
Cdd:cd05636    98 AGTITANLRFDDKPvkVRLKGERVDTGRRKlGAIIGDGVKTGInvslnpGVKIGPGSWVYPGCVV 162
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 2-65 6.92e-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: 39.54  E-value: 6.92e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1072035592   2 NYQVHASAIIDDGAQIGDDTRVWHFAHVCG--------GAQIGKGCSLGQNVFVGNKVTIGNNVKVQNNVSV 65
Cdd:cd00208     6 GVKIHPKAVIRGPVVIGDNVNIGPGAVIGAatgpneknPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVV 77
cysE PRK11132
serine acetyltransferase; Provisional
 104-153 1.24e-04

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 41.61  E-value: 1.24e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1072035592 104 VKKGATLGANCTVVCGVTIGEYSLVGAGAVINKDVKPFALMVGVPAKQIG 153
Cdd:PRK11132  196 IREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVG 245
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 35-130 1.46e-04

Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 38.76  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  35 IGKGCSLGQNVFVGNKVtIGNNVKVQNNVSVYDnvyleddvfcgpSMVFTNVYnprsfIERKTEYRDTIVKKGATLGANC 114
Cdd:cd03356     2 IGESTVIGENAIIKNSV-IGDNVRIGDGVTITN------------SILMDNVT-----IGANSVIVDSIIGDNAVIGENV 63

                          90
                  ....*....|....*.
gi 1072035592 115 TVVCGVTIGEYSLVGA 130
Cdd:cd03356    64 RVVNLCIIGDDVVVED 79
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 35-124 3.33e-04

eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 37.94  E-value: 3.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  35 IGKGCSLGQNVFVGNKV-----TIGNNVKVQNNVsVYDNVYLEDDVFCGPSMVFTNVynprsfierkteyrdtIVKKGAT 109
Cdd:cd05787     2 IGRGTSIGEGTTIKNSVigrncKIGKNVVIDNSY-IWDDVTIEDGCTIHHSIVADGA----------------VIGKGCT 64

                          90
                  ....*....|....*
gi 1072035592 110 LGANCTVVCGVTIGE 124
Cdd:cd05787    65 IPPGSLISFGVVIGD 79
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 9-54 5.40e-04

eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 37.17  E-value: 5.40e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1072035592   9 AIIDDGAQIGDDTRVWHfAHVCGGAQIGKGCSLGQNVFVGNKVTIG 54
Cdd:cd05787    34 SYIWDDVTIEDGCTIHH-SIVADGAVIGKGCTIPPGSLISFGVVIG 78
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 14-139 1.10e-03

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


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 38.63  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  14 GAQIGDDTRVWHFAHVCGGAQIGKGCSLGQNVFVGnkvtiGNNVKVQNNvsvydNVYLEDDVFcgpsmvftnvynprsfi 93
Cdd:PRK11830  132 GAYVDEGTMVDTWATVGSCAQIGKNVHLSGGVGIG-----GVLEPLQAN-----PVIIEDNCF----------------- 184

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1072035592  94 erkteyrdtivkkgatLGANCTVVCGVTIGEYSLVGAGAVINKDVK 139
Cdd:PRK11830  185 ----------------IGARSEVVEGVIVEEGSVLGMGVFLGQSTK 214
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 30-152 1.67e-03

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 37.49  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  30 CGGAQIGKG--CSLGQNVFVGNK--------------VTIGNNVKVQNNVSVYDNVYLEDDV-------FCGPSMVFTNV 86
Cdd:PRK10092   57 VTEAYIEPTfrCDYGYNIFLGNNfyanfdcvmldvcpIRIGDNCMLAPGVHIYTATHPLDPVarnsgaeLGKPVTIGNNV 136

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1072035592  87 YnprsfierkteyrdtivkkgatLGANCTVVCGVTIGEYSLVGAGAVINKDVKPFALMVGVPAKQI 152
Cdd:PRK10092  137 W----------------------IGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARII 180
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
14-42 2.86e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.85  E-value: 2.86e-03
                          10        20
                  ....*....|....*....|....*....
gi 1072035592  14 GAQIGDDTRVWHFAHVCGGAQIGKGCSLG 42
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIG 29
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 106-139 3.71e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 37.04  E-value: 3.71e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1072035592 106 KGATLGANCTVVCGVTIGEYSLVGAGAVINKDVK 139
Cdd:PRK00892  117 EGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVK 150
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 14-134 3.82e-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: 37.02  E-value: 3.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  14 GAQIGDDTRV--WhfAHVCGGAQIGKGCSLGQNVFVG--------NKVTIgnnvkvqnnvsvydnvylEDDVFcgpsmvf 83
Cdd:COG2171   126 GAYVDEGTMVdtW--ATVGSCAQIGKNVHLSGGAGIGgvleplqaAPVII------------------EDNCF------- 178

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1072035592  84 tnvynprsfierkteyrdtivkkgatLGANCTVVCGVTIGEYSLVGAGAVI 134
Cdd:COG2171   179 --------------------------IGARSGVVEGVIVGEGAVLGAGVYL 203
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 15-82 3.91e-03

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 34.92  E-value: 3.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1072035592  15 AQIGDDTRVWHFAHVCGGAQIGKGCSLGQNVFVGN--------KVTIGNNVKVQNNVSVYDNVYLEDDVFCGPSMV 82
Cdd:cd00208     1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAatgpneknPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAV 76
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 27-157 4.91e-03

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: 36.19  E-value: 4.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592  27 AHVCGGAQIGKGCSLGQNVFV---GNKVTIGNNVKVQNNVSVY----DNVYLEDDVFCGPSMVFtnvynprsfierktey 99
Cdd:cd04745    13 AVLIGDVIIGKNCYIGPHASLrgdFGRIVIRDGANVQDNCVIHgfpgQDTVLEENGHIGHGAIL---------------- 76

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592 100 RDTIVKKGATLGANCTVVCGVTIGEYSLVGAGAVI--NKDVKPFALMVGVPAKQIGWISK 157
Cdd:cd04745    77 HGCTIGRNALVGMNAVVMDGAVIGEESIVGAMAFVkaGTVIPPRSLIAGSPAKVIRELSD 136
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 4-134 7.63e-03

Gamma carbonic anhydrases (CA): Carbonic anhydrases 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 distinct groups of carbonic anhydrases - alpha, beta and gamma - which show no significant sequence identity or structural similarity. Gamma CAs are homotrimeric enzymes, with each subunit containing a left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 35.68  E-value: 7.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1072035592   4 QVHASAIIDDGAQIGDDTRVWHFAHVCGGA----------QIGKGCSLGQNVFV----GNKVTIGNNVKVQNNVSVYDNV 69
Cdd:cd00710     4 VIDPSAYVHPTAVVIGDVIIGDNVFVGPGAsiradegtpiIIGANVNIQDGVVIhaleGYSVWIGKNVSIAHGAIVHGPA 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1072035592  70 YLEDDVFCG-PSMVFTnvynprsfierkteyrdtivkkgATLGANC-----TVVCGVTIGEYSLVGAGAVI 134
Cdd:cd00710    84 YIGDNCFIGfRSVVFN-----------------------AKVGDNCvighnAVVDGVEIPPGRYVPAGAVI 131
 
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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