NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1084692515|gb|OGP39012|]
View 

hypothetical protein A2X93_07215 [Deltaproteobacteria bacterium GWC2_56_8]

Protein Classification

serine O-acetyltransferase( domain architecture ID 11437200)

serine O-acetyltransferase (SAT) catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetyl-L-serine

CATH:  2.160.10.10
EC:  2.3.1.30
Gene Ontology:  GO:0009001|GO:0006535
PubMed:  15500694|11747907|15581568

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 34-189 8.29e-49

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: 156.40  E-value: 8.29e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  34 IVYSPGIWITFLYRIGRYLHlKAGENLFLRLLTvpynilyFVLSVFTGLNIPIEAVIGKGLYIGHWGGVTIHPQAVIGKN 113
Cdd:COG1045    26 LLCYPGFHALALHRLAHWLW-KRGLPLLARLLS-------ERARFLTGIDIHPGATIGRGFFIDHGTGVVIGETAVIGDN 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1084692515 114 LNLSQGVTIGESGRGDERGVPVIGDNVYIGPGAKVFGKIVIGNNVAIGANAVVNKSVPDNAVVGGIPAVILNYRGS 189
Cdd:COG1045    98 VTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVKRKGS 173
 
Name Accession Description Interval E-value
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 34-189 8.29e-49

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: 156.40  E-value: 8.29e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  34 IVYSPGIWITFLYRIGRYLHlKAGENLFLRLLTvpynilyFVLSVFTGLNIPIEAVIGKGLYIGHWGGVTIHPQAVIGKN 113
Cdd:COG1045    26 LLCYPGFHALALHRLAHWLW-KRGLPLLARLLS-------ERARFLTGIDIHPGATIGRGFFIDHGTGVVIGETAVIGDN 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1084692515 114 LNLSQGVTIGESGRGDERGVPVIGDNVYIGPGAKVFGKIVIGNNVAIGANAVVNKSVPDNAVVGGIPAVILNYRGS 189
Cdd:COG1045    98 VTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVKRKGS 173
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 80-180 4.68e-40

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: 131.79  E-value: 4.68e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  80 TGLNIPIEAVIGKGLYIGHWGGVTIHPQAVIGKNLNLSQGVTIGESGRGDERGVPVIGDNVYIGPGAKVFGKIVIGNNVA 159
Cdd:cd03354     1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                          90       100
                  ....*....|....*....|.
gi 1084692515 160 IGANAVVNKSVPDNAVVGGIP 180
Cdd:cd03354    81 IGANAVVTKDVPANSTVVGVP 101
cysE PRK11132
serine acetyltransferase; Provisional
 46-183 1.68e-19

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 83.21  E-value: 1.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  46 YRIGRYLHLKAGENLFLRLLTVpynilyfvLSVFTGLNIPIEAVIGKGLYIGHWGGVTIHPQAVIGKNLNLSQGVTIGES 125
Cdd:PRK11132  114 YRIGHWLWNQGRRALAIYLQNQ--------ISVAFQVDIHPAAKIGRGIMLDHATGIVIGETAVIENDVSILQSVTLGGT 185

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515 126 GR--GDERgvPVIGDNVYIGPGAKVFGKIVIGNNVAIGANAVVNKSVPDNAVVGGIPAVI 183
Cdd:PRK11132  186 GKtsGDRH--PKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARI 243
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 87-181 1.53e-14

sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff.


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 68.67  E-value: 1.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  87 EAVIGKGLYIGHwgGVTIHPQAVIGKNLNLSQGVTIGE----------------SGrgderGVpVIGDNVYIGPGAKVFG 150
Cdd:TIGR03570  99 SASIGEGTVIMA--GAVINPDVRIGDNVIINTGAIVEHdcvigdfvhiapgvtlSG-----GV-VIGEGVFIGAGATIIQ 170

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1084692515 151 KIVIGNNVAIGANAVVNKSVPDNAVVGGIPA 181
Cdd:TIGR03570 171 GVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
134-162 3.88e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 36.55  E-value: 3.88e-04
                          10        20
                  ....*....|....*....|....*....
gi 1084692515 134 PVIGDNVYIGPGAKVFGKIVIGNNVAIGA 162
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 34-189 8.29e-49

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: 156.40  E-value: 8.29e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  34 IVYSPGIWITFLYRIGRYLHlKAGENLFLRLLTvpynilyFVLSVFTGLNIPIEAVIGKGLYIGHWGGVTIHPQAVIGKN 113
Cdd:COG1045    26 LLCYPGFHALALHRLAHWLW-KRGLPLLARLLS-------ERARFLTGIDIHPGATIGRGFFIDHGTGVVIGETAVIGDN 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1084692515 114 LNLSQGVTIGESGRGDERGVPVIGDNVYIGPGAKVFGKIVIGNNVAIGANAVVNKSVPDNAVVGGIPAVILNYRGS 189
Cdd:COG1045    98 VTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVKRKGS 173
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 80-180 4.68e-40

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: 131.79  E-value: 4.68e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  80 TGLNIPIEAVIGKGLYIGHWGGVTIHPQAVIGKNLNLSQGVTIGESGRGDERGVPVIGDNVYIGPGAKVFGKIVIGNNVA 159
Cdd:cd03354     1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                          90       100
                  ....*....|....*....|.
gi 1084692515 160 IGANAVVNKSVPDNAVVGGIP 180
Cdd:cd03354    81 IGANAVVTKDVPANSTVVGVP 101
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
89-191 1.57e-19

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 80.30  E-value: 1.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  89 VIGKGLYIGHwgGVTIHPQA--VIGKNLNLSQGVTIGESG-------RGDERGVPV-IGDNVYIGPGAKVFGKIVIGNNV 158
Cdd:COG0110    29 TIGDNVYIGP--GVTIDDPGgiTIGDNVLIGPGVTILTGNhpiddpaTFPLRTGPVtIGDDVWIGAGATILPGVTIGDGA 106

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1084692515 159 AIGANAVVNKSVPDNAVVGGIPAVILNYRGSGD 191
Cdd:COG0110   107 VVGAGSVVTKDVPPYAIVAGNPARVIRKRDEEE 139
cysE PRK11132
serine acetyltransferase; Provisional
 46-183 1.68e-19

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 83.21  E-value: 1.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  46 YRIGRYLHLKAGENLFLRLLTVpynilyfvLSVFTGLNIPIEAVIGKGLYIGHWGGVTIHPQAVIGKNLNLSQGVTIGES 125
Cdd:PRK11132  114 YRIGHWLWNQGRRALAIYLQNQ--------ISVAFQVDIHPAAKIGRGIMLDHATGIVIGETAVIENDVSILQSVTLGGT 185

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515 126 GR--GDERgvPVIGDNVYIGPGAKVFGKIVIGNNVAIGANAVVNKSVPDNAVVGGIPAVI 183
Cdd:PRK11132  186 GKtsGDRH--PKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARI 243
PRK10191 PRK10191
putative acyl transferase; Provisional
 46-178 1.88e-19

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 80.32  E-value: 1.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  46 YRIGRYLHLKAGENLFLRLLTVPYNILY-FVLSVFTGLNIPIEAVIGKGLYIGHWGGVTIHPQAVIGKNLNLSQGVTIGE 124
Cdd:PRK10191    5 YRVAHFCSVWRKKNVLNNLWAAPLLVLYrIITECFFGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGVTIGN 84

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1084692515 125 SGrGDERGVPVIGDNVYIGPGAKVFGKIVIGNNVAIGANAVVNKSVPDNAVVGG 178
Cdd:PRK10191   85 RG-ADNMACPHIGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVG 137
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 89-184 2.72e-16

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: 70.95  E-value: 2.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  89 VIGKGLYIGHWGGVTIHPQAVIGKNLNLSQGVTI-------GESGRGDERGVP----VIGDNVYIGPGAKVFGKIVIGNN 157
Cdd:cd04647     3 SIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIydhnhdiDDPERPIEQGVTsapiVIGDDVWIGANVVILPGVTIGDG 82

                          90       100
                  ....*....|....*....|....*..
gi 1084692515 158 VAIGANAVVNKSVPDNAVVGGIPAVIL 184
Cdd:cd04647    83 AVVGAGSVVTKDVPPNSIVAGNPAKVI 109
PLN02694 PLN02694
serine O-acetyltransferase
 88-181 4.50e-16

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 74.29  E-value: 4.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  88 AVIGKGLYIGHWGGVTIHPQAVIGKNLNLSQGVTIGESGRGDERGVPVIGDNVYIGPGAKVFGKIVIGNNVAIGANAVVN 167
Cdd:PLN02694  167 AKIGKGILFDHATGVVIGETAVIGNNVSILHHVTLGGTGKACGDRHPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVL 246

                          90
                  ....*....|....
gi 1084692515 168 KSVPDNAVVGGIPA 181
Cdd:PLN02694  247 IDVPPRTTAVGNPA 260
PLN02739 PLN02739
serine acetyltransferase
 75-197 7.41e-16

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 74.30  E-value: 7.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  75 VLSVFtGLNIPIEAVIGKGLYIGHWGGVTIHPQAVIGKNLNLSQGVTIGESGR--GDERgvPVIGDNVYIGPGAKVFGKI 152
Cdd:PLN02739  200 VSEVF-GIDIHPAARIGKGILLDHGTGVVIGETAVIGDRVSILHGVTLGGTGKetGDRH--PKIGDGALLGACVTILGNI 276

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1084692515 153 VIGNNVAIGANAVVNKSVPDNAVVGGIPAVILNYRGSGDFVITGE 197
Cdd:PLN02739  277 SIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFVDEQDPSLTME 321
PLN02357 PLN02357
serine acetyltransferase
 88-184 1.75e-15

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 73.38  E-value: 1.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  88 AVIGKGLYIGHWGGVTIHPQAVIGKNLNLSQGVTIGESGR--GDERgvPVIGDNVYIGPGAKVFGKIVIGNNVAIGANAV 165
Cdd:PLN02357  233 AKIGQGILLDHATGVVIGETAVVGNNVSILHNVTLGGTGKqsGDRH--PKIGDGVLIGAGTCILGNITIGEGAKIGAGSV 310

                          90
                  ....*....|....*....
gi 1084692515 166 VNKSVPDNAVVGGIPAVIL 184
Cdd:PLN02357  311 VLKDVPPRTTAVGNPARLI 329
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 81-184 3.33e-15

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: 69.76  E-value: 3.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  81 GLNIpieaVIGKGLYIGHwgGVTI--HPQAVIGKNLNLSQGVTI---------GESGRGDERGVPV-IGDNVYIGPGAKV 148
Cdd:cd03357    60 GYNI----HIGDNFYANF--NCTIldVAPVTIGDNVLIGPNVQIytaghpldpEERNRGLEYAKPItIGDNVWIGGGVII 133

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1084692515 149 FGKIVIGNNVAIGANAVVNKSVPDNAVVGGIPAVIL 184
Cdd:cd03357   134 LPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 87-180 1.44e-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: 68.67  E-value: 1.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  87 EAVIGKGLYIGHwgGVTIHPQAVIGKNLNLSQGVTIGE----------------SGrgderGVpVIGDNVYIGPGAKVFG 150
Cdd:cd03360    96 SAVIGEGCVIMA--GAVINPDARIGDNVIINTGAVIGHdcvigdfvhiapgvvlSG-----GV-TIGEGAFIGAGATIIQ 167

                          90       100       110
                  ....*....|....*....|....*....|
gi 1084692515 151 KIVIGNNVAIGANAVVNKSVPDNAVVGGIP 180
Cdd:cd03360   168 GVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 87-181 1.53e-14

sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff.


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 68.67  E-value: 1.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  87 EAVIGKGLYIGHwgGVTIHPQAVIGKNLNLSQGVTIGE----------------SGrgderGVpVIGDNVYIGPGAKVFG 150
Cdd:TIGR03570  99 SASIGEGTVIMA--GAVINPDVRIGDNVIINTGAIVEHdcvigdfvhiapgvtlSG-----GV-VIGEGVFIGAGATIIQ 170

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1084692515 151 KIVIGNNVAIGANAVVNKSVPDNAVVGGIPA 181
Cdd:TIGR03570 171 GVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 110-184 9.22e-14

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 66.38  E-value: 9.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515 110 IGKNLNLSQGVTI---------GESGRGDERGVPV-IGDNVYIGPGAKVFGKIVIGNNVAIGANAVVNKSVPDNAVVGGI 179
Cdd:PRK10092   96 IGDNCMLAPGVHIytathpldpVARNSGAELGKPVtIGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGN 175


                  ....*
gi 1084692515 180 PAVIL 184
Cdd:PRK10092  176 PARII 180
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 89-187 5.98e-12

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: 60.64  E-value: 5.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  89 VIGKGLYIGHWGGVTIHPQAVIGKNLNLSQGVTIGESGR--------------------------GDERGVPVIGDNVYI 142
Cdd:cd03349     3 SVGDYSYGSGPDCDVGGDKLSIGKFCSIAPGVKIGLGGNhptdwvstypfyifggeweddakfddWPSKGDVIIGNDVWI 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1084692515 143 GPGAKVFGKIVIGNNVAIGANAVVNKSVPDNAVVGGIPAVILNYR 187
Cdd:cd03349    83 GHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRYR 127
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 19-187 7.58e-11

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 58.73  E-value: 7.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  19 LILMRRKRIGAILRLI--------VYSPGIWITFLYRIGRYLHLKAGENLF----LRLLTVPYNILYFVLSVFTGLNIPI 86
Cdd:PRK09677    1 LKLAKRYGLCGFIRLVrdvlltkvFYRNCRIIRFPFYIRNDGSINFGEGFTsgvgLRLDAFGRGKLFFGDNVQVNDYVHI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  87 EAV----IGKGLYIGHWGGVTIHPQAVIGKNLNLSQGvTIGESGRGDERGVPVIGDNVYIGPGAKVFGKIVIGNNVAIGA 162
Cdd:PRK09677   81 ACIesitIGRDTLIASKVFITDHNHGSFKHSDDFSSP-NLPPDMRTLESSAVVIGQRVWIGENVTILPGVSIGNGCIVGA 159

                         170       180
                  ....*....|....*....|....*
gi 1084692515 163 NAVVNKSVPDNAVVGGIPAVILNYR 187
Cdd:PRK09677  160 NSVVTKSIPENTVIAGNPAKIIKKY 184
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 88-166 3.31e-10

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: 58.11  E-value: 3.31e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1084692515  88 AVIGKGLYIGHwgGVTIHPQAVIGKNLNLSQGVTIGEsgrgderGVpVIGDNVYIGPGAKVFGKIVIGNNVAIGANAVV 166
Cdd:COG1044   109 AKIGEGVSIGP--FAVIGAGVVIGDGVVIGPGVVIGD-------GV-VIGDDCVLHPNVTIYERCVIGDRVIIHSGAVI 177
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 85-184 2.03e-09

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 55.01  E-value: 2.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  85 PIEAVIGKGLYIG-----HWGGVTIHPQAV-IGKNLNLSQGVTIGESG---------RGDERGVPV-IGDNVYIGPGAKV 148
Cdd:PRK09527   67 PVYFSYGSNIHIGrnfyaNFNLTIVDDYTVtIGDNVLIAPNVTLSVTGhpvhhelrkNGEMYSFPItIGNNVWIGSHVVI 146

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1084692515 149 FGKIVIGNNVAIGANAVVNKSVPDNAVVGGIPAVIL 184
Cdd:PRK09527  147 NPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVI 182
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 88-167 3.75e-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: 51.48  E-value: 3.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  88 AVIGKGLYIGHWggVTIHPQAVIGKNLNLSQGVTIGESGRGDERGVPVIGDNVYIGPGAKVFGKIVIGNNVAIGANAVVN 167
Cdd:cd00208     1 VFIGEGVKIHPK--AVIRGPVVIGDNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 136-184 3.92e-09

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 53.49  E-value: 3.92e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1084692515 136 IGDNVYIGPGAKVFGKIVIGNNVAIGANAVV--NKSVPDNAVVGGIPAVIL 184
Cdd:COG0663    91 IGDNVLIGMGAIVLDGAVIGDGSIVGAGALVteGKVVPPGSLVVGSPAKVV 141
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 88-166 6.36e-09

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 54.37  E-value: 6.36e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1084692515  88 AVIGKGLYIGHwgGVTIHPQAVIGKNLNLSQGVTIGesgrgdeRGVpVIGDNVYIGPGAKVFGKIVIGNNVAIGANAVV 166
Cdd:PRK00892  113 AKIGEGVSIGP--NAVIGAGVVIGDGVVIGAGAVIG-------DGV-KIGADCRLHANVTIYHAVRIGNRVIIHSGAVI 181
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 90-184 9.96e-09

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: 51.35  E-value: 9.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  90 IGKGLYIGhwGGVTIHPQAVIGKNLNLSQGVTIGEsgrgderGVpVIGDNVYIGPGA---------------KVFGKIVI 154
Cdd:cd03358     1 IGDNCIIG--TNVFIENDVKIGDNVKIQSNVSIYE-------GV-TIEDDVFIGPNVvftndlyprskiyrkWELKGTTV 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1084692515 155 GNNVAIGANA------------------VVNKSVPDNAVVGGIPAVIL 184
Cdd:cd03358    71 KRGASIGANAtilpgvtigeyalvgagaVVTKDVPPYALVVGNPARII 118
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 88-166 1.07e-08

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 52.80  E-value: 1.07e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1084692515  88 AVIGKGLYIGHwgGVTIHPQAVIGKNLNLSQGVTIGEsgrgderGVpVIGDNVYIGPGAKVFGKIVIGNNVAIGANAVV 166
Cdd:cd03352     2 AKIGENVSIGP--NAVIGEGVVIGDGVVIGPGVVIGD-------GV-VIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 135-182 1.20e-08

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 52.80  E-value: 1.20e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1084692515 135 VIGDNVYIGPGAKVFGKIVIGNNVAIGANAVVNKSVPDNAVVGGIPAV 182
Cdd:cd03352   152 TIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQ 199
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 88-182 2.10e-08

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: 52.71  E-value: 2.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  88 AVIGKGLYIGH----WGGVTIHPQAVIGKNLNLSQGVTIGESGRG---DERG----VP-----VIGDNV----------- 140
Cdd:COG1044   139 VVIGDGVVIGDdcvlHPNVTIYERCVIGDRVIIHSGAVIGADGFGfapDEDGgwvkIPqlgrvVIGDDVeiganttidrg 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515 141 -----YIGPGAK------------------------------------------VFGKIVIGNNVAIGANAVVNKSVPDN 173
Cdd:COG1044   219 algdtVIGDGTKidnlvqiahnvrigehtaiaaqvgiagstkigdnvviggqvgIAGHLTIGDGVIIGAQSGVTKSIPEG 298


                  ....*....
gi 1084692515 174 AVVGGIPAV 182
Cdd:COG1044   299 GVYSGSPAQ 307
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 89-181 5.38e-08

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: 50.10  E-value: 5.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  89 VIGKGLYIGHwgGVTIHpqavigknlnlsqGVTIGesgrgdergvpvigDNVYIGPGAKVFGKIVIGNNVAIGANAVV-- 166
Cdd:cd04645    62 IIGDNVTVGH--GAVLH-------------GCTIG--------------DNCLIGMGAIILDGAVIGKGSIVAAGSLVpp 112

                          90
                  ....*....|....*
gi 1084692515 167 NKSVPDNAVVGGIPA 181
Cdd:cd04645   113 GKVIPPGSLVAGSPA 127
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 88-166 6.43e-08

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: 51.56  E-value: 6.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  88 AVIGKGLYIGhwGGVTIHPQAVIGKNLNLSQGVTIGEsgrgderGVpVIGDNVYIGPGAKV----FG----------KI- 152
Cdd:COG1044   127 VVIGDGVVIG--PGVVIGDGVVIGDDCVLHPNVTIYE-------RC-VIGDRVIIHSGAVIgadgFGfapdedggwvKIp 196

                          90
                  ....*....|....*....
gi 1084692515 153 -----VIGNNVAIGANAVV 166
Cdd:COG1044   197 qlgrvVIGDDVEIGANTTI 215
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 104-177 8.61e-08

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: 51.17  E-value: 8.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515 104 IHPQAVIGKNLNLSQGVTIG-----ESGrgdergVpVIGDNVYIGPGAkvfgkiVIGNNVAIGANAVV--NKSVPDNAVV 176
Cdd:COG1044    99 IHPSAVIDPSAKIGEGVSIGpfaviGAG------V-VIGDGVVIGPGV------VIGDGVVIGDDCVLhpNVTIYERCVI 165


                  .
gi 1084692515 177 G 177
Cdd:COG1044   166 G 166
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 88-177 1.31e-07

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 49.71  E-value: 1.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  88 AVIGKGLYIGHwgGVTIHPQAVIGKNLNLSQGVTIGEsgrgderGVpVIGDNVYIGPGAKV------------------- 148
Cdd:cd03352    20 VVIGDGVVIGP--GVVIGDGVVIGDDCVIHPNVTIYE-------GC-IIGDRVIIHSGAVIgsdgfgfapdgggwvkipq 89

                          90       100
                  ....*....|....*....|....*....
gi 1084692515 149 FGKIVIGNNVAIGANAVVNKSVPDNAVVG 177
Cdd:cd03352    90 LGGVIIGDDVEIGANTTIDRGALGDTVIG 118
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 104-166 2.02e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 49.75  E-value: 2.02e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084692515 104 IHPQAVIGKNLNLSQGVTIGEsgrgderGVpVIGDNVYIGPGAKVFGKIVIGNNVAIGANAVV 166
Cdd:PRK00892  109 IDPSAKIGEGVSIGPNAVIGA-------GV-VIGDGVVIGAGAVIGDGVKIGADCRLHANVTI 163
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 88-177 2.31e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 49.75  E-value: 2.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  88 AVIGKGLYIGhwGGVTIHPQAVIGKNL------NLSQGVTIGESGRgdergvpvIGDNVYIGPGAKV----FG------- 150
Cdd:PRK00892  125 AVIGAGVVIG--DGVVIGAGAVIGDGVkigadcRLHANVTIYHAVR--------IGNRVIIHSGAVIgsdgFGfandrgg 194

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1084692515 151 --KI------VIGNNVAIGANAVVNKSVPDNAVVG 177
Cdd:PRK00892  195 wvKIpqlgrvIIGDDVEIGANTTIDRGALDDTVIG 229
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 90-184 8.67e-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: 45.67  E-value: 8.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  90 IGKGLYIGHwgGVTIHPQA--VIGKNLNLSQGVTIGeSGRGDERGVP--------VIGDNVYIGPGAKVFGKIVIGNNVA 159
Cdd:cd05825     6 IGDNSWIGE--GVWIYNLApvTIGSDACISQGAYLC-TGSHDYRSPAfplitapiVIGDGAWVAAEAFVGPGVTIGEGAV 82

                          90       100
                  ....*....|....*....|....*
gi 1084692515 160 IGANAVVNKSVPDNAVVGGIPAVIL 184
Cdd:cd05825    83 VGARSVVVRDLPAWTVYAGNPAVPV 107
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 88-176 1.03e-06

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 48.10  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  88 AVIGKGLYIGHwggVTIHPQAVIGKNLNLSQGvTIGESGRGDERGVPVIGDNVYIGPGAKVFGKIVIGNNVAIGANAVVN 167
Cdd:PRK09451  353 ARLGKGSKAGH---LTYLGDAEIGDNVNIGAG-TITCNYDGANKFKTIIGDDVFVGSDTQLVAPVTVGKGATIGAGTTVT 428


                  ....*....
gi 1084692515 168 KSVPDNAVV 176
Cdd:PRK09451  429 RDVAENELV 437
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 84-171 2.21e-06

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


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 45.45  E-value: 2.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  84 IPIEAVIGKGLYIGHWggVTIHPQAVIGKNLNLSQGVTIGESGRGDERGVPVIGDNVYIGPGAKVFGKIVIGNNVAIGAN 163
Cdd:cd03350    28 VNIGAYVDEGTMVDSW--ATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIEDDVFIGANCEVVEGVIVGKGAVLAAG 105


                  ....*...
gi 1084692515 164 AVVNKSVP 171
Cdd:cd03350   106 VVLTQSTP 113
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 100-176 4.43e-06

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


Pssm-ID: 100049 [Multi-domain]  Cd Length: 161  Bit Score: 44.90  E-value: 4.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515 100 GGVTIHPQAV---------IGKNLNLSQGVTIGESGRGDERGV---PV-IGDNVYIGPGAKVFGKIvIGNNVAIGANAVV 166
Cdd:cd03359    26 GKTIIQSDVIirgdlatvsIGRYCILSEGCVIRPPFKKFSKGVaffPLhIGDYVFIGENCVVNAAQ-IGSYVHIGKNCVI 104

                          90
                  ....*....|..
gi 1084692515 167 NK--SVPDNAVV 176
Cdd:cd03359   105 GRrcIIKDCVKI 116
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 108-176 6.70e-06

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 45.69  E-value: 6.70e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1084692515 108 AVIGKNLNLSQGvTIGESGRGDERGVPVIGDNVYIGPGAKVFGKIVIGNNVAIGANAVVNKSVPDNAVV 176
Cdd:PRK14360  366 ATLGEQVNIGAG-TITANYDGVKKHRTVIGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLA 433
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 108-187 7.33e-06

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: 45.11  E-value: 7.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515 108 AVIGKNLNLSQGVTIGesgrgderGV-------PV-IGDNVYIGPGAKVFGKIVIGNNVAIGANAVVNKS---------- 169
Cdd:COG2171   145 AQIGKNVHLSGGAGIG--------GVleplqaaPViIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLTAStkiydrvtge 216

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1084692515 170 -----VPDNAVV------------GGIPAVILNYR 187
Cdd:COG2171   217 vyygrVPAGSVVvpgslpgkdgdyGLYCAVIVKRR 251
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 108-175 1.40e-05

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 44.75  E-value: 1.40e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1084692515 108 AVIGKNLNLSQGvTIGESGRGDERGVPVIGDNVYIGPGAKVFGKIVIGNNVAIGANAVVNKSVPDNAV 175
Cdd:PRK14357  359 ATVGKNVNIGAG-TITCNYDGKKKNPTFIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSL 425
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 135-182 2.26e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 43.97  E-value: 2.26e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1084692515 135 VIGDNVYIGPGAKVFGKIVIGNNVAIGANAVVNKSVPD-NAVVGGIPAV 182
Cdd:PRK00892  263 KIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEpGEYSSGIPAQ 311
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 109-177 3.58e-05

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: 40.69  E-value: 3.58e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515 109 VIGKNLNLSQGVTIGESgrgdergvpVIGDNVYIGPGAKVFGKIvIGNNVAIGANAVVNKSV-PDNAVVG 177
Cdd:cd03356     1 LIGESTVIGENAIIKNS---------VIGDNVRIGDGVTITNSI-LMDNVTIGANSVIVDSIiGDNAVIG 60
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 88-175 3.72e-05

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 43.56  E-value: 3.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  88 AVIGKGLYIGHwggVTIHPQAVIGKNLNLSQGvTIGESGRGDERGVPVIGDNVYIGPGAKVFGKIVIGNNVAIGANAVVN 167
Cdd:PRK14356  357 AVLGKGAKANH---LTYLGDAEIGAGANIGAG-TITCNYDGVNKHRTVIGEGAFIGSNTALVAPVTIGDGALVGAGSVIT 432


                  ....*...
gi 1084692515 168 KSVPDNAV 175
Cdd:PRK14356  433 KDVPDGSL 440
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 87-170 5.75e-05

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: 39.92  E-value: 5.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  87 EAVIGKGLYIGHwggvtihpqAVIGKNLNLSQGVTIGESgrgdergvpVIGDNVYIGPGAKVFGKIvIGNNVAIGANA-V 165
Cdd:cd03356     5 STVIGENAIIKN---------SVIGDNVRIGDGVTITNS---------ILMDNVTIGANSVIVDSI-IGDNAVIGENVrV 65


                  ....*
gi 1084692515 166 VNKSV 170
Cdd:cd03356    66 VNLCI 70
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 104-180 6.15e-05

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: 42.31  E-value: 6.15e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1084692515 104 IHPQAVIGKNLNLSQGVTIGesgrgdergvP--VIGDNVYIGPGAKVFGKIVIGNNVAIGANAVVNksvpDNAVVGGIP 180
Cdd:COG1043     4 IHPTAIVDPGAKLGENVEIG----------PfcVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIF----PFASIGEEP 68
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 104-196 7.40e-05

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: 42.03  E-value: 7.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515 104 IHPQAVIGKNLNLSQGVTIGesgrgdergvP--VIGDNVYIGPGAKVFGKIVIGNNVAIGANAVVNksvpDNAVVGGIPA 181
Cdd:cd03351     2 IHPTAIVDPGAKIGENVEIG----------PfcVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIF----PFASIGEAPQ 67

                          90
                  ....*....|....*
gi 1084692515 182 vILNYRGSGDFVITG 196
Cdd:cd03351    68 -DLKYKGEPTRLEIG 81
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 86-187 9.07e-05

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


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 42.10  E-value: 9.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  86 IEAVIGKGLYIGHWggVTIHPQAVIGKNLNLSQGVTIGesgrgderGV-------PV-IGDNVYIGPGAKVFGKIVIGNN 157
Cdd:PRK11830  131 IGAYVDEGTMVDTW--ATVGSCAQIGKNVHLSGGVGIG--------GVleplqanPViIEDNCFIGARSEVVEGVIVEEG 200

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1084692515 158 VAIGANAVVNKS---------------VPDNAVV---------GGI---PAVILNYR 187
Cdd:PRK11830  201 SVLGMGVFLGQStkiydretgevhygrVPAGSVVvpgslpskdGGYslyCAVIVKKV 257
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 136-184 1.38e-04

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: 40.63  E-value: 1.38e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1084692515 136 IGDNVYIGPGAKVFGKIVIGNNVAIGANAVV--NKSVPDNAVVGGIPAVIL 184
Cdd:cd04650    81 VGNYVIVGMGAILLNGAKIGDHVIIGAGAVVtpGKEIPDYSLVLGVPAKVV 131
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 134-183 1.79e-04

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 40.40  E-value: 1.79e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1084692515 134 PVIGDNVYIGPGAKVFGKIVIGNNVAIGANAVV-----------NKSVPDNAVV---GGIPAVI 183
Cdd:COG0663    11 PQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLrgdvgpirigeGSNIQDGVVLhvdPGYPLTI 74
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 89-177 3.63e-04

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: 39.53  E-value: 3.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  89 VIGKGLYIGhwGGVTIH----PQAVIGKNLNLSQGVTIgesgRGDERGVPVIGDNVYIGPGAKVFGKIVIGNNVAIGANA 164
Cdd:cd00710    22 IIGDNVFVG--PGASIRadegTPIIIGANVNIQDGVVI----HALEGYSVWIGKNVSIAHGAIVHGPAYIGDNCFIGFRS 95

                          90
                  ....*....|....
gi 1084692515 165 VV-NKSVPDNAVVG 177
Cdd:cd00710    96 VVfNAKVGDNCVIG 109
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 102-177 3.77e-04

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: 39.71  E-value: 3.77e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1084692515 102 VTIHPQAVIGKNLNLSQGVTIgesgrgdeRGVPVIGDNVYIGPGAkVFGKIVIGNNVAIGANAVV-NKSVPDNAVVG 177
Cdd:cd03353    10 TYIDGDVEIGVDVVIDPGVIL--------EGKTVIGEDCVIGPNC-VIKDSTIGDGVVIKASSVIeGAVIGNGATVG 77
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
134-162 3.88e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 36.55  E-value: 3.88e-04
                          10        20
                  ....*....|....*....|....*....
gi 1084692515 134 PVIGDNVYIGPGAKVFGKIVIGNNVAIGA 162
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
PRK10502 PRK10502
putative acyl transferase; Provisional
 110-187 5.10e-04

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 39.16  E-value: 5.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515 110 IGKNLNLSQGVTI--G----ESGRGDERGVP-VIGDNVYIGPGAKVFGKIVIGNNVAIGANAVVNKSVPDNAVVGGIPAV 182
Cdd:PRK10502   94 IGAHCVISQKSYLctGshdySDPHFDLNTAPiVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAV 173


                  ....*
gi 1084692515 183 ILNYR 187
Cdd:PRK10502  174 PIRPR 178
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 88-174 5.45e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 40.11  E-value: 5.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  88 AVIGKGLYIGHwggVTIHPQAVIGKNLNLSQG-VTIGESGRGDERgvPVIGDNVYIGPGAKVFGKIVIGNNVAIGANAVV 166
Cdd:PRK14355  356 IVMGEGSKASH---LTYLGDATIGRNVNIGCGtITCNYDGVKKHR--TVIEDDVFVGSDVQFVAPVTVGRNSLIAAGTTV 430


                  ....*...
gi 1084692515 167 NKSVPDNA 174
Cdd:PRK14355  431 TKDVPPDS 438
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 101-177 8.52e-04

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 39.24  E-value: 8.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515 101 GVTIH-PQAV-IGKNLNLSQGVTI-------GESgrgdergvpVIGDNVYIGPGAkvfgkiVIgNNVAIGANAVVNKSVP 171
Cdd:COG1207   252 GVTIIdPATTyIDGDVEIGRDVVIdpnvileGKT---------VIGEGVVIGPNC------TL-KDSTIGDGVVIKYSVI 315


                  ....*.
gi 1084692515 172 DNAVVG 177
Cdd:COG1207   316 EDAVVG 321
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
104-180 1.51e-03

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 38.16  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515 104 IHPQAVIgknlnlsqgvtigesgrgdERGVpVIGDNVYIGPGAKVFGKIVIGNNVAIGANAVV---------NKSVPdNA 174
Cdd:PRK05289    5 IHPTAIV-------------------EPGA-KIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIdghttigknNRIFP-FA 63


                  ....*.
gi 1084692515 175 VVGGIP 180
Cdd:PRK05289   64 SIGEDP 69
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 104-196 1.93e-03

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: 37.16  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515 104 IHPQAVIGKNLNLSQGVTIGESG--------RGDERGVPV-----IGDNVYIGPGAKVfgKIVIGNNVAIGANAVVNKSV 170
Cdd:cd04650     3 ISPKAYVHPTSYVIGDVVIGELTsvwhyaviRGDNDSIYIgkysnVQENVSIHTDHGY--PTEIGDYVTIGHNAVVHGAK 80

                          90       100
                  ....*....|....*....|....*.
gi 1084692515 171 PDNAVVGGIPAVILNYRGSGDFVITG 196
Cdd:cd04650    81 VGNYVIVGMGAILLNGAKIGDHVIIG 106
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 134-177 2.01e-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: 37.22  E-value: 2.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1084692515 134 PVIGDNVYIGPGAKVFGKIVIGNNVAIGANAVVNKSVPDNAVVG 177
Cdd:cd00710     3 PVIDPSAYVHPTAVVIGDVIIGDNVFVGPGASIRADEGTPIIIG 46
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 135-176 2.23e-03

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 37.40  E-value: 2.23e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1084692515 135 VIGDNVYIGPGAKVFGKIVIGNNVAIGANAVVNKSVPDNAVV 176
Cdd:cd03353   146 VIGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGALA 187
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 104-182 2.66e-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: 36.96  E-value: 2.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515 104 IHPQAVIgknlnlsqgvtIGESgrgdergvpVIGDNVYIGPGAKV---FGKIVIGNnvaiGANavvnksVPDNAVVGGIP 180
Cdd:cd04745     9 VHPTAVL-----------IGDV---------IIGKNCYIGPHASLrgdFGRIVIRD----GAN------VQDNCVIHGFP 58


                  ..
gi 1084692515 181 AV 182
Cdd:cd04745    59 GQ 60
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 88-174 3.06e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 37.50  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  88 AVIGKGLYIGHwggVTIHPQAVIGKNLNLSQGvTIGESGRGDERGVPVIGDNVYIGPGAKVFGKIVIGNNVAIGANAVVN 167
Cdd:PRK14354  352 STIGEGTKVSH---LTYIGDAEVGENVNIGCG-TITVNYDGKNKFKTIIGDNAFIGCNSNLVAPVTVGDNAYIAAGSTIT 427


                  ....*..
gi 1084692515 168 KSVPDNA 174
Cdd:PRK14354  428 KDVPEDA 434
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 135-183 3.89e-03

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: 36.24  E-value: 3.89e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1084692515 135 VIGDNVYIGPGAKVFGKIVIGNNVAIGANAVV-----------NKSVPDNAVV---GGIPAVI 183
Cdd:cd04645     1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLrgdvnpirigeRTNIQDGSVLhvdPGYPTII 63
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 101-177 6.45e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 36.73  E-value: 6.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515 101 GVT--------IHPQAVIGKNLNLSQGVTIgesgrgdeRGVPVIGDNVYIGPGAKvfgkIV---IGNNVAIgANAVVNKS 169
Cdd:PRK14354  251 GVTiidpestyIDADVEIGSDTVIEPGVVI--------KGNTVIGEDCVIGPGSR----IVdstIGDGVTI-TNSVIEES 317


                  ....*....
gi 1084692515 170 -VPDNAVVG 177
Cdd:PRK14354  318 kVGDNVTVG 326
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 135-182 7.26e-03

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: 34.75  E-value: 7.26e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1084692515 135 VIGDNVYIGPGAKVFGKIVIGnNVAIGANAVVNKS-------VPDNAVVGGIPAV 182
Cdd:cd04651    30 VLFRGVRVGSGSVVEDSVIMP-NVGIGRNAVIRRAiidknvvIPDGVVIGGDPEE 83
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 7-181 7.79e-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: 36.65  E-value: 7.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515   7 LYMFLESDLGRYLILMRRKrigaILRLIVYSPG---IWITFLYRigRYLHLKAGENLFLRLLTVPYNILYFVLSVFTGLN 83
Cdd:TIGR02353 524 ALILMAVGVGAFLILVERK----WLVFGRLKPQehpLWSPFVWL--HELHWKLYESVAVPNFLRPFRGTPFLPAILRLLG 597

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  84 ipieAVIGKGLYI-GHWggVTIHPQAVIGKNLNLSQGVTIG----ESGRGDERGVpVIGDNVYIGPGAKVFGKIVIGNNV 158
Cdd:TIGR02353 598 ----VKIGRGVYIdGTD--LTERDLVTIGDDSTLNEGSVIQthlfEDRVMKSDTV-TIGDGATLGPGAIVLYGVVMGEGS 670

                         170       180
                  ....*....|....*....|....*
gi 1084692515 159 AIGANAVVNK--SVPDNAVVGGIPA 181
Cdd:TIGR02353 671 VLGPDSLVMKgeEVPAHTRWRGNPA 695
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 135-174 7.84e-03

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: 36.54  E-value: 7.84e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1084692515 135 VIGDNVYIG-------PgakvfgkIVIGNNVAIGANAVVNKSVPDNA 174
Cdd:COG1207   396 VIGDGAFIGsntnlvaP-------VTIGDGATIGAGSTITKDVPAGA 435
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 84-170 9.84e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 35.96  E-value: 9.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1084692515  84 IPIEAVIGKGLYIghWGGVTIHPQAVIGKNLNLSQGVTIGESGRGDerGVPV---------IGDNVYIGPGAKVFGKIVI 154
Cdd:PRK14354  262 IDADVEIGSDTVI--EPGVVIKGNTVIGEDCVIGPGSRIVDSTIGD--GVTItnsvieeskVGDNVTVGPFAHLRPGSVI 337

                          90
                  ....*....|....*..
gi 1084692515 155 GNNVAIGaNAV-VNKSV 170
Cdd:PRK14354  338 GEEVKIG-NFVeIKKST 353
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH