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Conserved domains on  [gi|518429266|ref|WP_019599473|]
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MULTISPECIES: acyltransferase [Rhodonellum]

Protein Classification

acyltransferase( domain architecture ID 10444459)

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 ...
 37-155 1.86e-57

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: 176.54  E-value: 1.86e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  37 IGKGCNLGQNVVISPEVILGDNVKVQNNVSIYTGVTCDNDVFLGPSMVFTNVTNPRSAINRRDQYSKTHVGKGATIGANA 116
Cdd:cd03358    1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKIYRKWELKGTTVKRGASIGANA 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 518429266 117 TIVCGHDIGPFAFIGAGSVVTKTVPAYALLVGNPAKQIG 155
Cdd:cd03358   81 TILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
16-44 1.72e-04

Bacterial transferase hexapeptide (six repeats);


:

Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 37.32  E-value: 1.72e-04
                          10        20
                  ....*....|....*....|....*....
gi 518429266   16 GCEIGEGTKIWHFTHVMPNCKIGKGCNLG 44
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 ...
 37-155 1.86e-57

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: 176.54  E-value: 1.86e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  37 IGKGCNLGQNVVISPEVILGDNVKVQNNVSIYTGVTCDNDVFLGPSMVFTNVTNPRSAINRRDQYSKTHVGKGATIGANA 116
Cdd:cd03358    1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKIYRKWELKGTTVKRGASIGANA 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 518429266 117 TIVCGHDIGPFAFIGAGSVVTKTVPAYALLVGNPAKQIG 155
Cdd:cd03358   81 TILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
34-159 2.08e-33

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 116.12  E-value: 2.08e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  34 NCKIGKGCNLGQNVVISPE-VILGDNVKVQNNVSIYT--GVTCDNDVFLGPSMVFTNVTNPRSAINRRDQYSK-THVGKG 109
Cdd:COG0110    8 GARIGDGVVIGPGVRIYGGnITIGDNVYIGPGVTIDDpgGITIGDNVLIGPGVTILTGNHPIDDPATFPLRTGpVTIGDD 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 518429266 110 ATIGANATIVCGHDIGPFAFIGAGSVVTKTVPAYALLVGNPAKQIGWMSE 159
Cdd:COG0110   88 VWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDE 137
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 8-151 2.50e-22

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: 89.09  E-value: 2.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266    8 HPTAVIDEGCEIGEGTKIWHFTHVMPNCKIGKGCNLGQNVVISPEVILGDNVkvqnnvSIYTGVTCDNDVflgpsmvftn 87
Cdd:TIGR03570  91 HPSAIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFV------HIAPGVTLSGGV---------- 154

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518429266   88 vtnprsainrrdqysktHVGKGATIGANATIVCGHDIGPFAFIGAGSVVTKTVPAYALLVGNPA 151
Cdd:TIGR03570 155 -----------------VIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
8-152 8.79e-16

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 72.82  E-value: 8.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266   8 HPTAVIDEGCEIGEGTKIWHFTHVMPNCKIGKGCNLGQNVVISPEVILGDNVKVQNNVSI--------YTG-----VTCD 74
Cdd:PRK05289   6 HPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIgedpqdlkYKGeptrlVIGD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  75 NDVFLgpsmvfTNVTnprsaINR--RDQYSKT------------HVGKGATIG-----ANATIVCGH----D-------- 123
Cdd:PRK05289  86 NNTIR------EFVT-----INRgtVQGGGVTrigdnnllmayvHVAHDCVVGnhvilANNATLAGHvevgDyaiigglt 154

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 518429266 124 -------IGPFAFIGAGSVVTKTVPAYALLVGNPAK 152
Cdd:PRK05289 155 avhqfvrIGAHAMVGGMSGVSQDVPPYVLAEGNPAR 190
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
16-44 1.72e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 37.32  E-value: 1.72e-04
                          10        20
                  ....*....|....*....|....*....
gi 518429266   16 GCEIGEGTKIWHFTHVMPNCKIGKGCNLG 44
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIG 29
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 12-61 2.23e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 41.01  E-value: 2.23e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 518429266  12 VIDEGCEIGEGTKIWHfTHVMPNCKIGKGCNLgQNVVISPEVILGDNVKV 61
Cdd:PRK05293 310 VLFQGVQVGEGSVVKD-SVIMPGAKIGENVVI-ERAIIGENAVIGDGVII 357
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
36-68 3.65e-03

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 33.95  E-value: 3.65e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 518429266   36 KIGKGCNLGQNVVISpeVILGDNVKVQNNVSIY 68
Cdd:pfam14602   2 IIGDNCLIGANSGIG--VSLGDNCVVGAGVVIT 32
 
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 ...
 37-155 1.86e-57

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: 176.54  E-value: 1.86e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  37 IGKGCNLGQNVVISPEVILGDNVKVQNNVSIYTGVTCDNDVFLGPSMVFTNVTNPRSAINRRDQYSKTHVGKGATIGANA 116
Cdd:cd03358    1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKIYRKWELKGTTVKRGASIGANA 80

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 518429266 117 TIVCGHDIGPFAFIGAGSVVTKTVPAYALLVGNPAKQIG 155
Cdd:cd03358   81 TILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
34-159 2.08e-33

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 116.12  E-value: 2.08e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  34 NCKIGKGCNLGQNVVISPE-VILGDNVKVQNNVSIYT--GVTCDNDVFLGPSMVFTNVTNPRSAINRRDQYSK-THVGKG 109
Cdd:COG0110    8 GARIGDGVVIGPGVRIYGGnITIGDNVYIGPGVTIDDpgGITIGDNVLIGPGVTILTGNHPIDDPATFPLRTGpVTIGDD 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 518429266 110 ATIGANATIVCGHDIGPFAFIGAGSVVTKTVPAYALLVGNPAKQIGWMSE 159
Cdd:COG0110   88 VWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDE 137
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 8-151 2.50e-22

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: 89.09  E-value: 2.50e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266    8 HPTAVIDEGCEIGEGTKIWHFTHVMPNCKIGKGCNLGQNVVISPEVILGDNVkvqnnvSIYTGVTCDNDVflgpsmvftn 87
Cdd:TIGR03570  91 HPSAIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFV------HIAPGVTLSGGV---------- 154

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518429266   88 vtnprsainrrdqysktHVGKGATIGANATIVCGHDIGPFAFIGAGSVVTKTVPAYALLVGNPA 151
Cdd:TIGR03570 155 -----------------VIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 8-150 3.16e-21

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: 86.00  E-value: 3.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266   8 HPTAVIDEGCEIGEGTKIWHFTHVMPNCKIGKGCNLGQNVVISPEVILGDNVkvqnnvSIYTGVTCDNDVflgpsmvftn 87
Cdd:cd03360   88 HPSAVVSPSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFV------HIAPGVVLSGGV---------- 151

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518429266  88 vtnprsainrrdqysktHVGKGATIGANATIVCGHDIGPFAFIGAGSVVTKTVPAYALLVGNP 150
Cdd:cd03360  152 -----------------TIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 34-154 6.05e-20

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: 80.19  E-value: 6.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  34 NCKIGKGCNLGQNVVISP--EVILGDNVKVQNNVSIYTGvtcdndvflgpsmvFTNVTNPRSAINRRDQYSKTHVGKGAT 111
Cdd:cd04647    1 NISIGDNVYIGPGCVISAggGITIGDNVLIGPNVTIYDH--------------NHDIDDPERPIEQGVTSAPIVIGDDVW 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 518429266 112 IGANATIVCGHDIGPFAFIGAGSVVTKTVPAYALLVGNPAKQI 154
Cdd:cd04647   67 IGANVVILPGVTIGDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 8-152 3.66e-17

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: 76.60  E-value: 3.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266   8 HPTAVIDEGCEIGEGTKIWHFTHVMPNCKIGKGCNLGQNVVISP------------------------------EVILGD 57
Cdd:COG1043    5 HPTAIVDPGAKLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGpttigknnrifpfasigeepqdlkykgeptRLEIGD 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  58 NVKVQNNVSIYTGVTCDN-------------------DVFLGPSMVFTN-------VtnprsainrrdqysktHVGKGAT 111
Cdd:COG1043   85 NNTIREFVTIHRGTVQGGgvtrigddnllmayvhvahDCVVGNNVILANnatlaghV----------------EVGDHAI 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 518429266 112 IGANATIvcgHD---IGPFAFIGAGSVVTKTVPAYALLVGNPAK 152
Cdd:COG1043  149 IGGLSAV---HQfvrIGAHAMVGGGSGVVKDVPPYVLAAGNPAR 189
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 34-154 4.09e-17

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: 74.77  E-value: 4.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  34 NCKIGKGCNLGQNVVI--SPEVILGDNVKVQNNVSIYTgvtcdndvflgpsmvftnVTNPRSAINRRD--QYSK-THVGK 108
Cdd:cd03357   62 NIHIGDNFYANFNCTIldVAPVTIGDNVLIGPNVQIYT------------------AGHPLDPEERNRglEYAKpITIGD 123

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 518429266 109 GATIGANATIVCGHDIGPFAFIGAGSVVTKTVPAYALLVGNPAKQI 154
Cdd:cd03357  124 NVWIGGGVIILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 33-155 4.46e-17

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: 74.73  E-value: 4.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  33 PNCKIGKGCNL--GQNVVISPEVILGDNVKvqnnvsIYTGVTcdndvfLGPsmvftnvtnprsainRRDQYSKTH--VGK 108
Cdd:COG1045   70 PGATIGRGFFIdhGTGVVIGETAVIGDNVT------IYQGVT------LGG---------------TGKEKGKRHptIGD 122

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 518429266 109 GATIGANATIVCGHDIGPFAFIGAGSVVTKTVPAYALLVGNPAKQIG 155
Cdd:COG1045  123 NVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVK 169
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 8-152 7.88e-17

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: 76.59  E-value: 7.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266   8 HPTAVIDEGCEIGEGTKIWHFTHVMPNCKIGKGCNLGQNVVISPEVILGDNVKVQNNVSIYTGVTCDNDVFLGPSMV--- 84
Cdd:COG1044  100 HPSAVIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVIGDRVIIHSGAViga 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  85 --FTNVTNPR-----------------------SAINR---RDqyskTHVGKG--------------------------- 109
Cdd:COG1044  180 dgFGFAPDEDggwvkipqlgrvvigddveiganTTIDRgalGD----TVIGDGtkidnlvqiahnvrigehtaiaaqvgi 255

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 518429266 110 ---ATIGANATI-----VCGH-DIGPFAFIGAGSVVTKTVPAYALLVGNPAK 152
Cdd:COG1044  256 agsTKIGDNVVIggqvgIAGHlTIGDGVIIGAQSGVTKSIPEGGVYSGSPAQ 307
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 8-152 3.01e-16

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: 74.01  E-value: 3.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266   8 HPTAVIDEGCEIGEGTKIWHFTHVMPNCKIGKGCNLGQNVVISPEVILGDNVKVQNNVSI--------YTGvtcdndvfl 79
Cdd:cd03351    3 HPTAIVDPGAKIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIgeapqdlkYKG--------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  80 GPSMVFT--------NVTnprsaINR--RDQYSKTHVGKG------------ATIG-----ANATIVCGH----D----- 123
Cdd:cd03351   74 EPTRLEIgdnntireFVT-----IHRgtAQGGGVTRIGNNnllmayvhvahdCVIGnnvilANNATLAGHveigDyaiig 148

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 518429266 124 ----------IGPFAFIGAGSVVTKTVPAYALLVGNPAK 152
Cdd:cd03351  149 glsavhqfcrIGRHAMVGGGSGVVQDVPPYVIAAGNRAR 187
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 8-152 6.64e-16

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: 72.06  E-value: 6.64e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266   8 HPTAVIDEGCEIGEGTKIWHFTHVMPNCKIGKGCNLGQNVVISPEVILGDNVKVQNNVSI------YT------------ 69
Cdd:cd03352   11 GPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIgsdgfgFApdgggwvkipql 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  70 -GVTCDNDVFLGpsmvfTNVTNPRSAIN--RRDQYSK----------------------------THVGKGATIGANATI 118
Cdd:cd03352   91 gGVIIGDDVEIG-----ANTTIDRGALGdtVIGDGTKidnlvqiahnvrigencliaaqvgiagsTTIGDNVIIGGQVGI 165

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 518429266 119 VcGH-DIGPFAFIGAGSVVTKTVPAYALLVGNPAK 152
Cdd:cd03352  166 A-GHlTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQ 199
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
8-152 8.79e-16

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 72.82  E-value: 8.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266   8 HPTAVIDEGCEIGEGTKIWHFTHVMPNCKIGKGCNLGQNVVISPEVILGDNVKVQNNVSI--------YTG-----VTCD 74
Cdd:PRK05289   6 HPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIgedpqdlkYKGeptrlVIGD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  75 NDVFLgpsmvfTNVTnprsaINR--RDQYSKT------------HVGKGATIG-----ANATIVCGH----D-------- 123
Cdd:PRK05289  86 NNTIR------EFVT-----INRgtVQGGGVTrigdnnllmayvHVAHDCVVGnhvilANNATLAGHvevgDyaiigglt 154

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 518429266 124 -------IGPFAFIGAGSVVTKTVPAYALLVGNPAK 152
Cdd:PRK05289 155 avhqfvrIGAHAMVGGMSGVSQDVPPYVLAEGNPAR 190
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 17-156 9.63e-15

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: 67.95  E-value: 9.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  17 CEIGEGTKI----WHFTHvmPNCKIGKGCNLGQNVVIspevILGDNVKVqNNVSIYtgvtcdndvflgPSMVFTNVTNPR 92
Cdd:cd03349    2 ISVGDYSYGsgpdCDVGG--DKLSIGKFCSIAPGVKI----GLGGNHPT-DWVSTY------------PFYIFGGEWEDD 62

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518429266  93 SAINRRDQYSKTHVGKGATIGANATIVCGHDIGPFAFIGAGSVVTKTVPAYALLVGNPAKQIGW 156
Cdd:cd03349   63 AKFDDWPSKGDVIIGNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRY 126
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 33-150 1.29e-14

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: 66.31  E-value: 1.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  33 PNCKIGKGCNL--GQNVVISPEVILGDNVkvqnnvSIYTGVTcdndvfLGPSMVFTNVTNPrsainrrdqysktHVGKGA 110
Cdd:cd03354    7 PGAKIGPGLFIdhGTGIVIGETAVIGDNC------TIYQGVT------LGGKGKGGGKRHP-------------TIGDNV 61

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 518429266 111 TIGANATIVCGHDIGPFAFIGAGSVVTKTVPAYALLVGNP 150
Cdd:cd03354   62 VIGAGAKILGNITIGDNVKIGANAVVTKDVPANSTVVGVP 101
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 17-162 6.62e-14

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 68.70  E-value: 6.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  17 CEIGEGTKIWHftHVMPNCKIGKGCNLGQNVVISPEVILGDNVKVQNNVSI---------------YTG-VTCDNDVFLG 80
Cdd:PRK14354 301 STIGDGVTITN--SVIEESKVGDNVTVGPFAHLRPGSVIGEEVKIGNFVEIkkstigegtkvshltYIGdAEVGENVNIG 378

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  81 PSMVFTNVtnprsainrrDQYSK--THVGKGATIGANATIVCGHDIGPFAFIGAGSVVTKTVPAYALLVGNpAKQI---G 155
Cdd:PRK14354 379 CGTITVNY----------DGKNKfkTIIGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDALAIAR-ARQVnkeG 447


                 ....*..
gi 518429266 156 WMSEFGH 162
Cdd:PRK14354 448 YVKKLPH 454
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 13-148 1.39e-13

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: 65.90  E-value: 1.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  13 IDEGCEIGEGTKIWHFTHVMPNCKIGKGCNLGQNVVISPEVIlGDNVKVQNNvSIYTGVTCDNDVFLGPsmvFTNVtNPR 92
Cdd:cd03353   12 IDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIKDSTI-GDGVVIKAS-SVIEGAVIGNGATVGP---FAHL-RPG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  93 SAINRrdqysKTHVG-----KGATIGANA----------------------TIVCGHD---------------------- 123
Cdd:cd03353   86 TVLGE-----GVHIGnfveiKKSTIGEGSkanhlsylgdaeigegvnigagTITCNYDgvnkhrtvigdnvfigsnsqlv 160

                        170       180
                 ....*....|....*....|....*....
gi 518429266 124 ----IGPFAFIGAGSVVTKTVPAYALLVG 148
Cdd:cd03353  161 apvtIGDGATIAAGSTITKDVPPGALAIA 189
PLN02739 PLN02739
serine acetyltransferase
 31-159 1.40e-13

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 67.75  E-value: 1.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  31 VMPNCKIGKGCNL--GQNVVISPEVILGDNVkvqnnvSIYTGVTcdndvfLGPSMVFTNVTNPRsainrrdqyskthVGK 108
Cdd:PLN02739 208 IHPAARIGKGILLdhGTGVVIGETAVIGDRV------SILHGVT------LGGTGKETGDRHPK-------------IGD 262

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 518429266 109 GATIGANATIVCGHDIGPFAFIGAGSVVTKTVPAYALLVGNPAKQIGWMSE 159
Cdd:PLN02739 263 GALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFVDE 313
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 6-159 3.42e-13

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: 63.97  E-value: 3.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266   6 FAHPTAVIDEGCEIGEGTKIWhfthvmPNC---------KIGKGCNLGQNVVI--SPE--VILGDNVKVQNNVSIYtGVT 72
Cdd:cd04645    7 FIAPNATVIGDVTLGEGSSVW------FGAvlrgdvnpiRIGERTNIQDGSVLhvDPGypTIIGDNVTVGHGAVLH-GCT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  73 CDNDVFlgpsmvftnvtnprsainrrdqyskthVGKGATIGANATIvcghdiGPFAFIGAGSVVT--KTVPAYALLVGNP 150
Cdd:cd04645   80 IGDNCL---------------------------IGMGAIILDGAVI------GKGSIVAAGSLVPpgKVIPPGSLVAGSP 126


                 ....*....
gi 518429266 151 AKQIGWMSE 159
Cdd:cd04645  127 AKVVRELTD 135
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 9-142 5.94e-13

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 65.93  E-value: 5.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266   9 PTAVIDEGCEIGEGTKIWHFTHVMPNCKIGKGCNLGQNVVISPEVILGDNVKVQNNVSI------YT------------- 69
Cdd:PRK00892 123 PNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVIgsdgfgFAndrggwvkipqlg 202

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  70 GVTCDNDVFLGpsmvfTNVTNPRSAInrRD----QYSK----------------------------THVGKGATIGANAT 117
Cdd:PRK00892 203 RVIIGDDVEIG-----ANTTIDRGAL--DDtvigEGVKidnlvqiahnvvigrhtaiaaqvgiagsTKIGRYCMIGGQVG 275

                        170       180
                 ....*....|....*....|....*.
gi 518429266 118 IVcGH-DIGPFAFIGAGSVVTKTVPA 142
Cdd:PRK00892 276 IA-GHlEIGDGVTITAMSGVTKSIPE 300
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 17-156 1.73e-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: 64.66  E-value: 1.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  17 CEIGEGTKIwHFTHVMpNCKIGKGCNLGQNVVISPEVILGDNVKVQN-----NVSI----------YTGvtcD----NDV 77
Cdd:COG1207  302 STIGDGVVI-KYSVIE-DAVVGAGATVGPFARLRPGTVLGEGVKIGNfvevkNSTIgegskvnhlsYIG---DaeigEGV 376

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  78 FLGPSMVFTNvtnprsainrrdqY-----SKTHVGKGATIGANATIVCGHDIGPFAFIGAGSVVTKTVPAYALLVGNpAK 152
Cdd:COG1207  377 NIGAGTITCN-------------YdgvnkHRTVIGDGAFIGSNTNLVAPVTIGDGATIGAGSTITKDVPAGALAIAR-AR 442


                 ....*..
gi 518429266 153 QI---GW 156
Cdd:COG1207  443 QRnieGW 449
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 8-118 2.27e-12

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 64.00  E-value: 2.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266   8 HPTAVIDEGCEIGEGTKIWHFTHVMPNCKIGKGCNLGQNVVISPEVILGDNVKVQNNVSIYTGVTCDNDVFLGPSMV--- 84
Cdd:PRK00892 104 HPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVigs 183

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 518429266  85 ----FtnvtnprsaINRRDQYSKT-HVGK-----GATIGANATI 118
Cdd:PRK00892 184 dgfgF---------ANDRGGWVKIpQLGRviigdDVEIGANTTI 218
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 17-156 3.06e-12

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 64.18  E-value: 3.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  17 CEIGEGTKIWHFTHVMPNCKIGKGCNLGQNVVISPEVIlGDNVKVqNNVSiytgvtcdndvFLGPSMVFTNVTNPRSAIN 96
Cdd:PRK14360 314 SQIGDGVKIGPYAHLRPEAQIGSNCRIGNFVEIKKSQL-GEGSKV-NHLS-----------YIGDATLGEQVNIGAGTIT 380

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518429266  97 RR-DQYSK--THVGKGATIGANATIVCGHDIGPFAFIGAGSVVTKTVPAYALLVGNpAKQI---GW 156
Cdd:PRK14360 381 ANyDGVKKhrTVIGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLAIAR-SRQVikeNW 445
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 11-148 1.10e-11

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 62.43  E-value: 1.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  11 AVIDEGC-----EIGEGTKIWHFTHVmPNCKIGKGCNLGQNVVISPEVILGDNVKVQNNVSIYTGVTC------------ 73
Cdd:PRK14356 294 AVIHSHCwlrdaVVSSGATIHSFSHL-EGAEVGDGCSVGPYARLRPGAVLEEGARVGNFVEMKKAVLGkgakanhltylg 372

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518429266  74 DNDVFLGPSMVFTNVTNPRSAINRRdqysKTHVGKGATIGANATIVCGHDIGPFAFIGAGSVVTKTVPAYALLVG 148
Cdd:PRK14356 373 DAEIGAGANIGAGTITCNYDGVNKH----RTVIGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSLAIA 443
PLN02694 PLN02694
serine O-acetyltransferase
 31-155 1.17e-11

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 61.97  E-value: 1.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  31 VMPNCKIGKGCNLGQnvviSPEVILGDNVKVQNNVSIYTGVTcdndvfLGPSMVFTNVTNPRsainrrdqyskthVGKGA 110
Cdd:PLN02694 163 IHPAAKIGKGILFDH----ATGVVIGETAVIGNNVSILHHVT------LGGTGKACGDRHPK-------------IGDGV 219

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 518429266 111 TIGANATIVCGHDIGPFAFIGAGSVVTKTVPAYALLVGNPAKQIG 155
Cdd:PLN02694 220 LIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLVG 264
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 10-156 1.81e-11

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 61.70  E-value: 1.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  10 TAVIDEGCEIGEGTKIWHFTHVMPNCKIGKGCNLGQNVVISpEVILGDNVKV----------QNNVSI------YTGVTC 73
Cdd:PRK14357 249 TTYIHYDVEIGMDTIIYPMTFIEGKTRIGEDCEIGPMTRIV-DCEIGNNVKIirseceksviEDDVSVgpfsrlREGTVL 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  74 DNDV-----------------------FLGPSMVFTNVTNPRSAIN-RRDQYSK--THVGKGATIGANATIVCGHDIGPF 127
Cdd:PRK14357 328 KKSVkignfveikkstigentkaqhltYLGDATVGKNVNIGAGTITcNYDGKKKnpTFIEDGAFIGSNSSLVAPVRIGKG 407

                        170       180       190
                 ....*....|....*....|....*....|..
gi 518429266 128 AFIGAGSVVTKTVPAYALLVGNpAKQI---GW 156
Cdd:PRK14357 408 ALIGAGSVITEDVPPYSLALGR-ARQIvkeGW 438
PLN02357 PLN02357
serine acetyltransferase
 33-155 3.72e-11

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 60.67  E-value: 3.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  33 PNCKIGKGCNL--GQNVVISPEVILGDNVKVQNNVSIY-TGVTCDndvflgpsmvftnvtnprsainrrDQYSKthVGKG 109
Cdd:PLN02357 231 PGAKIGQGILLdhATGVVIGETAVVGNNVSILHNVTLGgTGKQSG------------------------DRHPK--IGDG 284

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 518429266 110 ATIGANATIVCGHDIGPFAFIGAGSVVTKTVPAYALLVGNPAKQIG 155
Cdd:PLN02357 285 VLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLIG 330
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 9-164 3.94e-11

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 60.65  E-value: 3.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266   9 PTAVIDEGCEIGEGTKIWHFTHVmPNCKIGKGCNLGQNVVISPEVILGDNVKVQN-----NVSIYTGV-----TCDNDVF 78
Cdd:PRK14353 279 PNVVFGPGVTVASGAVIHAFSHL-EGAHVGEGAEVGPYARLRPGAELGEGAKVGNfvevkNAKLGEGAkvnhlTYIGDAT 357

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  79 LGPSmvfTNVTNPRSAINRrDQYSK--THVGKGATIGANATIVCGHDIGPFAFIGAGSVVTKTVPAYALLVGNpAKQI-- 154
Cdd:PRK14353 358 IGAG---ANIGAGTITCNY-DGFNKhrTEIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALGR-ARQEtk 432

                        170
                 ....*....|.
gi 518429266 155 -GWMSEFGHRL 164
Cdd:PRK14353 433 pGWAKKLRERL 443
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 8-155 4.02e-11

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 60.04  E-value: 4.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266   8 HPTAVIDEGCEIGEGTKIWHFTHVMPNCKIGKGCNLGQNVVISPEVILGDNVKVQNNVSI--------YTG-----VTCD 74
Cdd:PRK12461   3 HPTAVIDPSAKLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVgdepqdftYKGeesrlEIGD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  75 NDVFLgpsmvfTNVTnprsaINRRDQ-------------YSKTHVGKGATIG-----ANATIVCGH-------------- 122
Cdd:PRK12461  83 RNVIR------EGVT-----IHRGTKgggvtrigndnllMAYSHVAHDCQIGnnvilVNGALLAGHvtvgdraiisgncl 151

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 518429266 123 -----DIGPFAFIGAGSVVTKTVPAYALLVGNPAKQIG 155
Cdd:PRK12461 152 vhqfcRIGALAMMAGGSRISKDVPPYCMMAGHPTNVHG 189
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 6-154 4.07e-11

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 58.50  E-value: 4.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266   6 FAHPTAVI--DegCEIGEGTKIWhfthvmPNC---------KIGKGCNLGQNVVI-----SPeVILGDNVKVQNNVSIYt 69
Cdd:COG0663   18 FVAPTAVVigD--VTIGEDVSVW------PGAvlrgdvgpiRIGEGSNIQDGVVLhvdpgYP-LTIGDDVTIGHGAILH- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  70 GVTCDNDVFLGP-SMVFTnvtnprsainrrdqyskthvgkGATIGANativcghdigpfAFIGAGSVVT--KTVPAYALL 146
Cdd:COG0663   88 GCTIGDNVLIGMgAIVLD----------------------GAVIGDG------------SIVGAGALVTegKVVPPGSLV 133


                 ....*...
gi 518429266 147 VGNPAKQI 154
Cdd:COG0663  134 VGSPAKVV 141
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 10-157 2.37e-10

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 58.60  E-value: 2.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  10 TAVIDEGCEIGEGTKIWHFTHVMPNCKIGKGCNLGQNVVISpEVILGDNVKVQNNvSIYTGVTCDNDVFLGPsMVFT--- 86
Cdd:PRK14355 262 TTYIDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVIK-GCRIGDDVTVKAG-SVLEDSVVGDDVAIGP-MAHLrpg 338

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  87 NVTNPRSAINRRDQYSKTHVGKG-----------ATIGAN-----ATIVCGHD--------------------------I 124
Cdd:PRK14355 339 TELSAHVKIGNFVETKKIVMGEGskashltylgdATIGRNvnigcGTITCNYDgvkkhrtvieddvfvgsdvqfvapvtV 418

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 518429266 125 GPFAFIGAGSVVTKTVPAYALLVGNpAKQI---GWM 157
Cdd:PRK14355 419 GRNSLIAAGTTVTKDVPPDSLAIAR-SPQVnkeGWK 453
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 4-159 5.97e-10

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: 55.27  E-value: 5.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266   4 KFFAHPTAVIDEGCEIGEGTKIWHFTHVMpnckigkgcnlGQNVVISpeviLGDNVKVQNNVSIYTGvtcdndvFLGPSM 83
Cdd:cd04650    6 KAYVHPTSYVIGDVVIGELTSVWHYAVIR-----------GDNDSIY----IGKYSNVQENVSIHTD-------HGYPTE 63

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518429266  84 VFTNVTNPRSAInrrdqYSKTHVGKGATIGANATIVCGHDIGPFAFIGAGSVVT--KTVPAYALLVGNPAKQIGWMSE 159
Cdd:cd04650   64 IGDYVTIGHNAV-----VHGAKVGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTpgKEIPDYSLVLGVPAKVVRKLTE 136
cysE PRK11132
serine acetyltransferase; Provisional
 31-155 7.64e-10

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 56.63  E-value: 7.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  31 VMPNCKIGKGCNLGQNVVIspevILGDNVKVQNNVSIYTGVTcdndvfLGPsmvftnvTNPRSAinrrDQYSKthVGKGA 110
Cdd:PRK11132 144 IHPAAKIGRGIMLDHATGI----VIGETAVIENDVSILQSVT------LGG-------TGKTSG----DRHPK--IREGV 200

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 518429266 111 TIGANATIVCGHDIGPFAFIGAGSVVTKTVPAYALLVGNPAKQIG 155
Cdd:PRK11132 201 MIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVG 245
PRK10502 PRK10502
putative acyl transferase; Provisional
 40-152 2.23e-09

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 54.19  E-value: 2.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  40 GCNLGQNVVISPEV--------ILGDNVKVQNNVSIYT--GVTCDNDVFLGP-SMVFT---NVTNPRSAINRRdqysKTH 105
Cdd:PRK10502  51 GAKIGKGVVIRPSVritypwklTIGDYAWIGDDVWLYNlgEITIGAHCVISQkSYLCTgshDYSDPHFDLNTA----PIV 126

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 518429266 106 VGKGATIGANATIVCGHDIGPFAFIGAGSVVTKTVPAYALLVGNPAK 152
Cdd:PRK10502 127 IGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAV 173
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 9-156 4.08e-09

bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 54.99  E-value: 4.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266   9 PTAVIdEGCEIGEGTKIWHFTHVMPNCKIGKGCNLGqNVVISPEVILGDNVKVqNNVSIYTGVTCDNDVFLGPSMVFTNV 88
Cdd:PRK14358 316 PHSVL-EGAEVGAGSDVGPFARLRPGTVLGEGVHIG-NFVETKNARLDAGVKA-GHLAYLGDVTIGAETNVGAGTIVANF 392

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  89 tnprSAINRRdqysKTHVGKGATIGANATIVCGHDIGPFAFIGAGSVVTKTVPAYALLV--GNPAKQIGW 156
Cdd:PRK14358 393 ----DGVNKH----QSKVGAGVFIGSNTTLIAPRVVGDAAFIAAGSAVHDDVPEGAMAVarGKQRNLEGW 454
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 105-154 4.29e-09

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: 51.84  E-value: 4.29e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 518429266 105 HVGKGATIGANATIVCGHDIGPFAFIGAGSVVTKTVPAYALLVGNPAKQI 154
Cdd:cd05825   58 VIGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 38-154 6.23e-09

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 53.34  E-value: 6.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  38 GKGCNLgqNVVISPEVILGDNVKVQNNVSIYT--GVTCDNDVFLGpSMVF------------TNVTNPR-SAINRRDQYS 102
Cdd:PRK09677  53 GVGLRL--DAFGRGKLFFGDNVQVNDYVHIACieSITIGRDTLIA-SKVFitdhnhgsfkhsDDFSSPNlPPDMRTLESS 129

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 518429266 103 KTHVGKGATIGANATIVCGHDIGPFAFIGAGSVVTKTVPAYALLVGNPAKQI 154
Cdd:PRK09677 130 AVVIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKII 181
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 6-159 1.95e-08

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: 51.21  E-value: 1.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266   6 FAHPTAVIdegceIGegtkiwhfthvmpNCKIGKGCNLGQNVVISP---EVILGDNVKVQNNVSIYtgvtcdndVFLGps 82
Cdd:cd04745    8 FVHPTAVL-----IG-------------DVIIGKNCYIGPHASLRGdfgRIVIRDGANVQDNCVIH--------GFPG-- 59

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518429266  83 mvFTNVTNPRSAINRRDQYSKTHVGKGATIGANATIVCGHDIGPFAFIGAGSVVTK--TVPAYALLVGNPAKQIGWMSE 159
Cdd:cd04745   60 --QDTVLEENGHIGHGAILHGCTIGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAgtVIPPRSLIAGSPAKVIRELSD 136
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 52-154 1.28e-07

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 49.43  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  52 EVILGDNVKVQNNVSIYTGvtcdndvflgpsmvftnvTNPRSAINRRdqySKTHVGKGATIGAN------ATIVCGHDIG 125
Cdd:PRK10092  93 PIRIGDNCMLAPGVHIYTA------------------THPLDPVARN---SGAELGKPVTIGNNvwiggrAVINPGVTIG 151

                         90       100
                 ....*....|....*....|....*....
gi 518429266 126 PFAFIGAGSVVTKTVPAYALLVGNPAKQI 154
Cdd:PRK10092 152 DNVVVASGAVVTKDVPDNVVVGGNPARII 180
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 43-154 1.75e-07

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 49.23  E-value: 1.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  43 LGQNVVISPEVI--------LGDNVKVQNNVSI---YTgVTCDNDVFLGPSMVFTNVTNPRSAINRR--DQYS-KTHVGK 108
Cdd:PRK09527  58 VGENAWVEPPVYfsygsnihIGRNFYANFNLTIvddYT-VTIGDNVLIAPNVTLSVTGHPVHHELRKngEMYSfPITIGN 136

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 518429266 109 GATIGANATIVCGHDIGPFAFIGAGSVVTKTVPAYALLVGNPAKQI 154
Cdd:PRK09527 137 NVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVI 182
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 35-137 3.36e-07

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: 46.09  E-value: 3.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  35 CKIGKGCNLGQNVVISPEVILGDNVKVQNNVSIYtGVTCDNdvflgpsmvftnvtnprsainrrdQYSKTHVGKGATIGA 114
Cdd:cd00208    1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIG-AATGPN------------------------EKNPTIIGDNVEIGA 55

                         90       100
                 ....*....|....*....|...
gi 518429266 115 NATIVCGHDIGPFAFIGAGSVVT 137
Cdd:cd00208   56 NAVIHGGVKIGDNAVIGAGAVVT 78
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 9-137 3.46e-07

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: 47.97  E-value: 3.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266   9 PTAVIDEGCEIGEGTKIWHFTHVMPNCKIGKGCNLGQNVVISPEVILGDNVKVQNNVSIYTGVTCDN------------- 75
Cdd:cd05636   10 EGVTIKGPVWIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSIIMDGtkvphlnyvgdsv 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518429266  76 ---DVFLGPSMVFTNVTNPRS--AINRRDQYSKTH-------VGKGATIGANATIVCGHDIGPFAFIGAGSVVT 137
Cdd:cd05636   90 lgeNVNLGAGTITANLRFDDKpvKVRLKGERVDTGrrklgaiIGDGVKTGINVSLNPGVKIGPGSWVYPGCVVR 163
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 12-77 2.49e-06

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: 43.77  E-value: 2.49e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518429266  12 VIDEGCEIGEGTKIwhfTHVMpnckIGKGCNLGQNVVISpEVILGDNVKVQNNVSIYTGVTCDNDV 77
Cdd:cd03356    1 LIGESTVIGENAII---KNSV----IGDNVRIGDGVTIT-NSILMDNVTIGANSVIVDSIIGDNAV 58
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 28-136 3.16e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 46.29  E-value: 3.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  28 FTHVMPNCKIGKGCNLGQNVVISPEVILGDNVKVQNNVSIYTGvtcdndVFLGPsmvftNVTnprsainrrdqyskthVG 107
Cdd:PRK00892 100 AAGIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAG------AVIGD-----GVK----------------IG 152

                         90       100
                 ....*....|....*....|....*....
gi 518429266 108 KGATIGANATIVCGHDIGPFAFIGAGSVV 136
Cdd:PRK00892 153 ADCRLHANVTIYHAVRIGNRVIIHSGAVI 181
PLN02296 PLN02296
carbonate dehydratase
 6-152 1.51e-05

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 43.96  E-value: 1.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266   6 FAHPTAVIDEGCEIGEGTKIWhFTHVM----PNCKIGKGCNLGQNVVIS-----------PEVIlGDNVKVQNNvSIYTG 70
Cdd:PLN02296  60 FVAPSASVIGDVQVGRGSSIW-YGCVLrgdvNSISVGSGTNIQDNSLVHvaktnlsgkvlPTII-GDNVTIGHS-AVLHG 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  71 VTCDNDVFlgpsmvftnvtnprsainrrdqyskthVGKGATIGANATIVCGhdigpfAFIGAGSVVTK--TVPAYALLVG 148
Cdd:PLN02296 137 CTVEDEAF---------------------------VGMGATLLDGVVVEKH------AMVAAGALVRQntRIPSGEVWAG 183


                 ....
gi 518429266 149 NPAK 152
Cdd:PLN02296 184 NPAK 187
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 6-145 2.36e-05

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: 42.61  E-value: 2.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266   6 FAHPTAV------IDEGCEIG--------EGTKIWhfthvmpnckIGKGCNLGQNVVI----SPEVILGDNVKVQNNVSI 67
Cdd:cd00710   10 YVHPTAVvigdviIGDNVFVGpgasiradEGTPII----------IGANVNIQDGVVIhaleGYSVWIGKNVSIAHGAIV 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518429266  68 YTGVTCDNDVFLG-PSMVFtnvtnprsainrrdqysKTHVGKGATIGANAtIVCGHDIGPFAFIGAGSVVTKTVPAYAL 145
Cdd:cd00710   80 HGPAYIGDNCFIGfRSVVF-----------------NAKVGDNCVIGHNA-VVDGVEIPPGRYVPAGAVITSQTQADAL 140
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 13-136 3.63e-05

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: 43.09  E-value: 3.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  13 IDEGCEIGEGTKIWHFTHVMPNCKIGKGCNLGQNVVISpevilgdNVKVQNNVSIytgvtcdndvflgpsmvftnvtnpr 92
Cdd:COG1207  263 IDGDVEIGRDVVIDPNVILEGKTVIGEGVVIGPNCTLK-------DSTIGDGVVI------------------------- 310

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 518429266  93 sainrrdQYSkthVGKGATIGANATIvcghdiGPFAFIGAGSVV 136
Cdd:COG1207  311 -------KYS---VIEDAVVGAGATV------GPFARLRPGTVL 338
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 19-75 4.86e-05

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: 40.25  E-value: 4.86e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 518429266  19 IGEGTKIWHFTHVMpNCKIGKGCNLGQNVVISPEVILgDNVKVQNNVSIYTGVTCDN 75
Cdd:cd05787    2 IGRGTSIGEGTTIK-NSVIGRNCKIGKNVVIDNSYIW-DDVTIEDGCTIHHSIVADG 56
PRK10191 PRK10191
putative acyl transferase; Provisional
 44-152 6.34e-05

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 41.41  E-value: 6.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  44 GQNVVISPEVILGDNVKVQNnvsiytGVTCDNdvfLGPsmvftnvtnprsainrrDQYSKTHVGKGATIGANATIVCGHD 123
Cdd:PRK10191  59 GYAVVINKNVVAGDDFTIRH------GVTIGN---RGA-----------------DNMACPHIGNGVELGANVIILGDIT 112

                         90       100
                 ....*....|....*....|....*....
gi 518429266 124 IGPFAFIGAGSVVTKTVPAYALLVGNPAK 152
Cdd:PRK10191 113 IGNNVTVGAGSVVLDSVPDNALVVGEKAR 141
lipid_A_lpxD TIGR01853
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD; This model describes LpxD, an ...
 19-92 6.46e-05

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD; This model describes LpxD, an enzyme for the biosynthesis of lipid A, a component oflipopolysaccharide (LPS) in the outer membrane outer leaflet of most Gram-negative bacteria. Some differences are found between lipid A of different species. This protein represents the third step from UDP-N-acetyl-D-glucosamine. The group added at this step generally is 14:0(3-OH) (myristate) but may vary; in Aquifex it appears to be 16:0(3-OH) (palmitate). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 273834 [Multi-domain]  Cd Length: 324  Bit Score: 42.28  E-value: 6.46e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518429266   19 IGEGTKIWHFTHVMPNCKIGKGCNLGQNVVISPEVILGDNVKVQNNVSIYTGVT-CDNDVFLGPSMVFTNVTNPR 92
Cdd:TIGR01853 220 IGEGTKIDNLVQIAHNCRIGENCIIVAQVGIAGSTKIGRNVIIGGQVGVAGHLEiGDNVTIGAKSGVTKSIPPPG 294
LbH_M1P_guanylylT_C cd05824
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 33-89 1.30e-04

Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Mannose-1-phosphate guanylyltransferase is also known as GDP-mannose pyrophosphorylase. It catalyzes the synthesis of GDP-mannose from GTP and mannose-1-phosphate, and is involved in the maintenance of cell wall integrity and glycosylation. Similar to ADP-glucose pyrophosphorylase, it contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain, presumably with 4 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: 100062 [Multi-domain]  Cd Length: 80  Bit Score: 39.06  E-value: 1.30e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 518429266  33 PNCKIGKGCNLGQNVVISPEVILGDNVKVQNNVsIYTGVTCDNDVFLGPSMVFTNVT 89
Cdd:cd05824    4 PSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCV-ILSNSTVRDHSWVKSSIVGWNST 59
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 17-156 1.61e-04

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 41.46  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  17 CEIGEGTKIWHFTHVmPNCKIGKGCNLGqnvvispevilGDNVKVQnnvsiYTGVTcdndvflgpsmvftnvtnprsain 96
Cdd:PRK14352 358 ATIGRGTKVPHLTYV-GDADIGEHSNIG-----------ASSVFVN-----YDGVN------------------------ 396

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518429266  97 rrdqYSKTHVGKGATIGANATIVCGHDIGPFAFIGAGSVVTKTVPAYALLV-GNPAKQI-GW 156
Cdd:PRK14352 397 ----KHRTTIGSHVRTGSDTMFVAPVTVGDGAYTGAGTVIREDVPPGALAVsEGPQRNIeGW 454
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 9-89 1.64e-04

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


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 40.06  E-value: 1.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266   9 PTAVIDEGCEIGEGTKIWHFTHVMPNCKIGKGCNLGQNVVI---------SPeVILGDNVKVQNNVSIYTGVTCDNDVFL 79
Cdd:cd03350   24 MPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVIggvleplqaTP-VIIEDDVFIGANCEVVEGVIVGKGAVL 102

                         90
                 ....*....|
gi 518429266  80 GPSMVFTNVT 89
Cdd:cd03350  103 AAGVVLTQST 112
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 12-64 1.70e-04

Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Glucose-1-phosphate adenylyltransferase is also known as ADP-glucose synthase or ADP-glucose pyrophosphorylase. It catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for regulation of storage polysaccharide accumulation in plants and bacteria. The enzyme is a homotetramer, with each subunit containing an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain with at 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The LbH domain is involved in cooperative allosteric regulation and oligomerization.


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 39.37  E-value: 1.70e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 518429266  12 VIDEGCEIGEGTKIWHfTHVMPNCKIGKGCNLgQNVVISPEVILGDNVKVQNN 64
Cdd:cd04651   30 VLFRGVRVGSGSVVED-SVIMPNVGIGRNAVI-RRAIIDKNVVIPDGVVIGGD 80
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
16-44 1.72e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 37.32  E-value: 1.72e-04
                          10        20
                  ....*....|....*....|....*....
gi 518429266   16 GCEIGEGTKIWHFTHVMPNCKIGKGCNLG 44
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIG 29
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 2-67 2.16e-04

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 38.38  E-value: 2.16e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518429266   2 ENKFFAHPTAVIDEGCEIGEGTKIWHFTHVM----PNCK----IGKGCNLGQNVVISPEVILGDNVKVQNNVSI 67
Cdd:cd00208    4 GEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGaatgPNEKnptiIGDNVEIGANAVIHGGVKIGDNAVIGAGAVV 77
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 12-61 2.23e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 41.01  E-value: 2.23e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 518429266  12 VIDEGCEIGEGTKIWHfTHVMPNCKIGKGCNLgQNVVISPEVILGDNVKV 61
Cdd:PRK05293 310 VLFQGVQVGEGSVVKD-SVIMPGAKIGENVVI-ERAIIGENAVIGDGVII 357
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 12-72 3.55e-04

eIF-2B gamma subunit, C-terminal 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 gamma subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH domain with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 37.94  E-value: 3.55e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518429266  12 VIDEGCEIGEGTKIwHFTHVMPNCKIGKGCNLgQNVVISPEVILGDNVKVQNNVsIYTGVT 72
Cdd:cd04652    1 LVGENTQVGEKTSI-KRSVIGANCKIGKRVKI-TNCVIMDNVTIEDGCTLENCI-IGNGAV 58
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 11-72 6.07e-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: 37.22  E-value: 6.07e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518429266  11 AVIDEGCEIGEGTKIWHfTHVMPNCKIGKGCNLgQNVVISPEVILGDNVKVQNNVSIYTGVT 72
Cdd:cd03356   17 SVIGDNVRIGDGVTITN-SILMDNVTIGANSVI-VDSIIGDNAVIGENVRVVNLCIIGDDVV 76
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 9-143 6.75e-04

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


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 38.13  E-value: 6.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266   9 PTAVIDEGCEIGEGTKIWHFTHVMPNCKIGKGCNLGQNVVISPEVILGDNVKVQNNVSIytgvtcdndvflgpsmvfTNV 88
Cdd:cd03350    6 PGAIIRDGAFIGPGAVLMMPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVI------------------GGV 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 518429266  89 TNPRSAinrrdqySKTHVGKGATIGANATIVCGHDIGPFAFIGAGSVVTKTVPAY 143
Cdd:cd03350   68 LEPLQA-------TPVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTQSTPIY 115
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 12-81 2.33e-03

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: 35.63  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  12 VIDEGCEIGEGTKIWHFThVMPNCKIGKGCNL-----------GQNVVISpEVILGDNVKVQNNVSIYTGVTCDNDVFLG 80
Cdd:cd05787    1 VIGRGTSIGEGTTIKNSV-IGRNCKIGKNVVIdnsyiwddvtiEDGCTIH-HSIVADGAVIGKGCTIPPGSLISFGVVIG 78


                 .
gi 518429266  81 P 81
Cdd:cd05787   79 D 79
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 106-151 2.43e-03

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 37.81  E-value: 2.43e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 518429266  106 VGKGATIGANATIVCGHDIGPFAFIGAGSVVTK--TVPAYALLVGNPA 151
Cdd:TIGR02353 648 IGDGATLGPGAIVLYGVVMGEGSVLGPDSLVMKgeEVPAHTRWRGNPA 695
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
36-68 3.65e-03

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 33.95  E-value: 3.65e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 518429266   36 KIGKGCNLGQNVVISpeVILGDNVKVQNNVSIY 68
Cdd:pfam14602   2 IIGDNCLIGANSGIG--VSLGDNCVVGAGVVIT 32
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 44-156 5.45e-03

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 36.93  E-value: 5.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266  44 GQNVVISPEVILGDNVKVQNNVSIYTG-----VTCDNDVFLGPSMVFTNVT-------NP----RSAINRRD-------- 99
Cdd:PRK09451 269 GRDVEIDTNVIIEGNVTLGNRVKIGAGcvlknCVIGDDCEISPYSVVEDANlgaactiGPfarlRPGAELAEgahvgnfv 348

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518429266 100 QYSKTHVGKG-----------ATIGAN-----ATIVCGHD--------------------------IGPFAFIGAGSVVT 137
Cdd:PRK09451 349 EMKKARLGKGskaghltylgdAEIGDNvnigaGTITCNYDgankfktiigddvfvgsdtqlvapvtVGKGATIGAGTTVT 428

                        170       180
                 ....*....|....*....|.
gi 518429266 138 KTVPAYALLVGN-PAKQI-GW 156
Cdd:PRK09451 429 RDVAENELVISRvPQRHIqGW 449
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
34-63 7.60e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 32.69  E-value: 7.60e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 518429266   34 NCKIGKGCNLGQNVVISPEVILGDNVKVQN 63
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
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.
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