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Conserved domains on  [gi|1724806011|gb|QEE41088|]
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N-acetyltransferase [Methylobacterium sp. WL1]

Protein Classification

acyltransferase( domain architecture ID 10129729)

acyltransferase belonging to the transferase hexapeptide repeat family, catalyzes the transfer of an acyl group from an acyl-CoA to a substrate; similar to Helicobacter pullorum N-acetyltransferase

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 ...
 27-152 7.07e-52

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: 161.51  E-value: 7.07e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  27 IKTGSLIGPFVEIQRNSTIGPRCKISSHTFICEGVSIGAEVFVGHGVVFTNERYPEATNADgslkrdgDWELVETLVGDR 106
Cdd:cd03358     1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKIYR-------KWELKGTTVKRG 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1724806011 107 ASIGSNATIVAGITIGEGALVGAGAVVTRDVPPYAIVAGCPARVIG 152
Cdd:cd03358    74 ASIGANATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
 
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 ...
 27-152 7.07e-52

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: 161.51  E-value: 7.07e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  27 IKTGSLIGPFVEIQRNSTIGPRCKISSHTFICEGVSIGAEVFVGHGVVFTNERYPEATNADgslkrdgDWELVETLVGDR 106
Cdd:cd03358     1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKIYR-------KWELKGTTVKRG 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1724806011 107 ASIGSNATIVAGITIGEGALVGAGAVVTRDVPPYAIVAGCPARVIG 152
Cdd:cd03358    74 ASIGANATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
18-159 2.64e-35

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 120.36  E-value: 2.64e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  18 DLVNIYGCEIKTGSLIGPFVEIQ-RNSTIGPRCKISSHTFI--CEGVSIGAEVFVGHGVVFTNERYPEATNADGSLKRDG 94
Cdd:COG0110     2 KLLLLFGARIGDGVVIGPGVRIYgGNITIGDNVYIGPGVTIddPGGITIGDNVLIGPGVTILTGNHPIDDPATFPLRTGP 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1724806011  95 dwelveTLVGDRASIGSNATIVAGITIGEGALVGAGAVVTRDVPPYAIVAGCPARVIGDTRQKRA 159
Cdd:COG0110    82 ------VTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEEER 140
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 24-148 2.91e-19

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: 80.62  E-value: 2.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  24 GCEIKTGSLIGPFVEIQRNSTIGPRCKISSHTFICEGVSIGAEVFVGHGVVftnerypeatnadgslkrdgdwelvetlV 103
Cdd:TIGR03570 105 GTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVV----------------------------I 156

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1724806011 104 GDRASIGSNATIVAGITIGEGALVGAGAVVTRDVPPYAIVAGCPA 148
Cdd:TIGR03570 157 GEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 24-142 4.31e-19

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 83.34  E-value: 4.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  24 GCEIKTGSLIGPFVEIqRNSTIGPRCKISSHTFICEGVsIGAEVFVGHGVVFTNerYpeatnaDGSLKRdgdwelvETLV 103
Cdd:PRK14354  334 GSVIGEEVKIGNFVEI-KKSTIGEGTKVSHLTYIGDAE-VGENVNIGCGTITVN--Y------DGKNKF-------KTII 396

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1724806011 104 GDRASIGSNATIVAGITIGEGALVGAGAVVTRDVPPYAI 142
Cdd:PRK14354  397 GDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDAL 435
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
103-135 1.67e-03

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 34.72  E-value: 1.67e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1724806011 103 VGDRASIGSNATIvaGITIGEGALVGAGAVVTR 135
Cdd:pfam14602   3 IGDNCLIGANSGI--GVSLGDNCVVGAGVVITA 33
 
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 ...
 27-152 7.07e-52

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: 161.51  E-value: 7.07e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  27 IKTGSLIGPFVEIQRNSTIGPRCKISSHTFICEGVSIGAEVFVGHGVVFTNERYPEATNADgslkrdgDWELVETLVGDR 106
Cdd:cd03358     1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKIYR-------KWELKGTTVKRG 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1724806011 107 ASIGSNATIVAGITIGEGALVGAGAVVTRDVPPYAIVAGCPARVIG 152
Cdd:cd03358    74 ASIGANATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
18-159 2.64e-35

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 120.36  E-value: 2.64e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  18 DLVNIYGCEIKTGSLIGPFVEIQ-RNSTIGPRCKISSHTFI--CEGVSIGAEVFVGHGVVFTNERYPEATNADGSLKRDG 94
Cdd:COG0110     2 KLLLLFGARIGDGVVIGPGVRIYgGNITIGDNVYIGPGVTIddPGGITIGDNVLIGPGVTILTGNHPIDDPATFPLRTGP 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1724806011  95 dwelveTLVGDRASIGSNATIVAGITIGEGALVGAGAVVTRDVPPYAIVAGCPARVIGDTRQKRA 159
Cdd:COG0110    82 ------VTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEEER 140
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 37-151 6.46e-28

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: 100.22  E-value: 6.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  37 VEIQRNSTIGPRCKISSHtficEGVSIGAEVFVGHGVVFTNERYPEAtnaDGSLKRDGDWELVETLVGDRASIGSNATIV 116
Cdd:cd04647     2 ISIGDNVYIGPGCVISAG----GGITIGDNVLIGPNVTIYDHNHDID---DPERPIEQGVTSAPIVIGDDVWIGANVVIL 74

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1724806011 117 AGITIGEGALVGAGAVVTRDVPPYAIVAGCPARVI 151
Cdd:cd04647    75 PGVTIGDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 33-151 1.19e-25

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: 95.69  E-value: 1.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  33 IGPFVEIQRNSTIGPRckiSSHTFicegvsigaeVFVGHGVVFTNERYPEATNADGSLKRDGDwelveTLVGDRASIGSN 112
Cdd:cd03349    24 IGKFCSIAPGVKIGLG---GNHPT----------DWVSTYPFYIFGGEWEDDAKFDDWPSKGD-----VIIGNDVWIGHG 85

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1724806011 113 ATIVAGITIGEGALVGAGAVVTRDVPPYAIVAGCPARVI 151
Cdd:cd03349    86 ATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVI 124
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 3-167 2.74e-21

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: 89.32  E-value: 2.74e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011   3 ITDADIERDVGIFYPDlvnIYGCEIKTGSLIGP------------------FVEIqRNSTIGPRCKISSHTFIceG-VSI 63
Cdd:COG1207   299 LKDSTIGDGVVIKYSV---IEDAVVGAGATVGPfarlrpgtvlgegvkignFVEV-KNSTIGEGSKVNHLSYI--GdAEI 372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  64 GAEVFVGHGVVFTNerYpeatnaDGSLKRdgdwelvETLVGDRASIGSNATIVAGITIGEGALVGAGAVVTRDVPPYAIv 143
Cdd:COG1207   373 GEGVNIGAGTITCN--Y------DGVNKH-------RTVIGDGAFIGSNTNLVAPVTIGDGATIGAGSTITKDVPAGAL- 436

                         170       180
                  ....*....|....*....|....*
gi 1724806011 144 agcparVIGDTRQK-RARSQRPSRP 167
Cdd:COG1207   437 ------AIARARQRnIEGWVRPKKK 455
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 24-143 3.67e-21

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: 85.55  E-value: 3.67e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  24 GCEIKTGSLIGPFVEIqRNSTIGPRCKISSHTFIceG-VSIGAEVFVGHGVVFTNerYpeatnaDGSLKRdgdwelvETL 102
Cdd:cd03353    85 GTVLGEGVHIGNFVEI-KKSTIGEGSKANHLSYL--GdAEIGEGVNIGAGTITCN--Y------DGVNKH-------RTV 146

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1724806011 103 VGDRASIGSNATIVAGITIGEGALVGAGAVVTRDVPPYAIV 143
Cdd:cd03353   147 IGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGALA 187
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 58-151 1.01e-20

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: 83.63  E-value: 1.01e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  58 CEGVSIGAEVFVGHGVVFTNERYPeaTNADgslKRDGDWEL---VEtlVGDRASIGSNATIVAGITIGEGALVGAGAVVT 134
Cdd:cd03357    80 VAPVTIGDNVLIGPNVQIYTAGHP--LDPE---ERNRGLEYakpIT--IGDNVWIGGGVIILPGVTIGDNSVIGAGSVVT 152

                          90
                  ....*....|....*..
gi 1724806011 135 RDVPPYAIVAGCPARVI 151
Cdd:cd03357   153 KDIPANVVAAGNPARVI 169
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 24-148 2.91e-19

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: 80.62  E-value: 2.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  24 GCEIKTGSLIGPFVEIQRNSTIGPRCKISSHTFICEGVSIGAEVFVGHGVVftnerypeatnadgslkrdgdwelvetlV 103
Cdd:TIGR03570 105 GTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVV----------------------------I 156

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1724806011 104 GDRASIGSNATIVAGITIGEGALVGAGAVVTRDVPPYAIVAGCPA 148
Cdd:TIGR03570 157 GEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 24-142 4.31e-19

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 83.34  E-value: 4.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  24 GCEIKTGSLIGPFVEIqRNSTIGPRCKISSHTFICEGVsIGAEVFVGHGVVFTNerYpeatnaDGSLKRdgdwelvETLV 103
Cdd:PRK14354  334 GSVIGEEVKIGNFVEI-KKSTIGEGTKVSHLTYIGDAE-VGENVNIGCGTITVN--Y------DGKNKF-------KTII 396

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1724806011 104 GDRASIGSNATIVAGITIGEGALVGAGAVVTRDVPPYAI 142
Cdd:PRK14354  397 GDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDAL 435
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 37-147 1.08e-18

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: 76.32  E-value: 1.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  37 VEIQRNSTIGPRCKISSHTFIC--EGVSIGAEVFVGHGVVFtnerypeatnadGSLKRDGDWELVetLVGDRASIGSNAT 114
Cdd:cd03354     3 IDIHPGAKIGPGLFIDHGTGIVigETAVIGDNCTIYQGVTL------------GGKGKGGGKRHP--TIGDNVVIGAGAK 68

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1724806011 115 IVAGITIGEGALVGAGAVVTRDVPPYAIVAGCP 147
Cdd:cd03354    69 ILGNITIGDNVKIGANAVVTKDVPANSTVVGVP 101
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 37-157 3.77e-18

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: 77.05  E-value: 3.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  37 VEIQRNSTIGPRCKIsSHTFiceGVSIGAEVFVG------HGV------VFTNERYPeatnadgslkrdgdwelvetLVG 104
Cdd:COG1045    66 IDIHPGATIGRGFFI-DHGT---GVVIGETAVIGdnvtiyQGVtlggtgKEKGKRHP--------------------TIG 121

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1724806011 105 DRASIGSNATIVAGITIGEGALVGAGAVVTRDVPPYAIVAGCPARVIGDTRQK 157
Cdd:COG1045   122 DNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVKRKGSK 174
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 24-138 7.61e-18

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 79.77  E-value: 7.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  24 GCEIKTGSLIGPFVEIQRnSTIGPRCKISSHTFI--CEgvsIGAEVFVGHGVVftnerypeATNADGSLKRdgdwelvET 101
Cdd:PRK14356  339 GAVLEEGARVGNFVEMKK-AVLGKGAKANHLTYLgdAE---IGAGANIGAGTI--------TCNYDGVNKH-------RT 399

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1724806011 102 LVGDRASIGSNATIVAGITIGEGALVGAGAVVTRDVP 138
Cdd:PRK14356  400 VIGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVP 436
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 25-147 2.01e-17

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: 75.60  E-value: 2.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  25 CEIKTGSLIGPFVEIQRNSTIGPRCKISSHTFICEGVSIGAEVFVGHGVVFTnerypeatnadgslkrdGDwelveTLVG 104
Cdd:cd03360    97 AVIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLS-----------------GG-----VTIG 154

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1724806011 105 DRASIGSNATIVAGITIGEGALVGAGAVVTRDVPPYAIVAGCP 147
Cdd:cd03360   155 EGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 24-162 2.48e-17

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 78.27  E-value: 2.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  24 GCEIKTGSLIGPFVEIqRNSTIGPRCKISSHTFICEGVsIGAEVFVGHGVVftnerypeATNADGSLKRdgdwelvETLV 103
Cdd:PRK14357  324 GTVLKKSVKIGNFVEI-KKSTIGENTKAQHLTYLGDAT-VGKNVNIGAGTI--------TCNYDGKKKN-------PTFI 386

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1724806011 104 GDRASIGSNATIVAGITIGEGALVGAGAVVTRDVPPYAIVAGCPARVIGDTRQKRARSQ 162
Cdd:PRK14357  387 EDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQIVKEGWVLKKRKE 445
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 24-145 3.99e-17

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 77.59  E-value: 3.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  24 GCEIKTGSLIGPFVEIqRNSTIGPRCKISSHTFICEGvSIGAEVFVGHGVVFTNerYpeatnaDGSLKrdgdwelVETLV 103
Cdd:PRK14353  321 GAELGEGAKVGNFVEV-KNAKLGEGAKVNHLTYIGDA-TIGAGANIGAGTITCN--Y------DGFNK-------HRTEI 383

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1724806011 104 GDRASIGSNATIVAGITIGEGALVGAGAVVTRDVPPYAIVAG 145
Cdd:PRK14353  384 GAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALG 425
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 25-157 7.02e-16

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 74.19  E-value: 7.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  25 CEIKTGSLIGPFVEIqRNSTIGPRCKISSHTFICEGvSIGAEVFVGHGVVftnerypeATNADGSLKRdgdwelvETLVG 104
Cdd:PRK14360  332 AQIGSNCRIGNFVEI-KKSQLGEGSKVNHLSYIGDA-TLGEQVNIGAGTI--------TANYDGVKKH-------RTVIG 394

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1724806011 105 DRASIGSNATIVAGITIGEGALVGAGAVVTRDVPPYAIvagcparVIGDTRQK 157
Cdd:PRK14360  395 DRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSL-------AIARSRQV 440
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 26-151 1.53e-15

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


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 68.40  E-value: 1.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  26 EIKTGSLIGPFVEI--QRNSTIGPRCKISSHTFICEGvsigaevfvghgvvftNERYpeatnadgslkRDGDWELV--ET 101
Cdd:cd05825     5 TIGDNSWIGEGVWIynLAPVTIGSDACISQGAYLCTG----------------SHDY-----------RSPAFPLItaPI 57

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1724806011 102 LVGDRASIGSNATIVAGITIGEGALVGAGAVVTRDVPPYAIVAGCPARVI 151
Cdd:cd05825    58 VIGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 61-157 7.47e-15

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 69.26  E-value: 7.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  61 VSIGAEVFVGHGVVFTNERYPeatnADGSLKRDGDWELVETLVGDRASIGSNATIVAGITIGEGALVGAGAVVTRDVPPY 140
Cdd:PRK09527   96 VTIGDNVLIAPNVTLSVTGHP----VHHELRKNGEMYSFPITIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPN 171

                          90
                  ....*....|....*..
gi 1724806011 141 AIVAGCPARVIGDTRQK 157
Cdd:PRK09527  172 VVAAGVPCRVIREINDR 188
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 24-169 4.01e-14

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 69.20  E-value: 4.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  24 GCEIKTGSLIGPFVEIqRNSTIGPRCKISSHTFICEGVsIGAEVFVGHGVVFTNerYpeatnaDGSLKRdgdwelvETLV 103
Cdd:PRK14352  340 GTVLGEEGKLGAFVET-KNATIGRGTKVPHLTYVGDAD-IGEHSNIGASSVFVN--Y------DGVNKH-------RTTI 402

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1724806011 104 GDRASIGSNATIVAGITIGEGALVGAGAVVTRDVPPYAI-VAGCPARVIGDTRQKRarsqRPSRPAA 169
Cdd:PRK14352  403 GSHVRTGSDTMFVAPVTVGDGAYTGAGTVIREDVPPGALaVSEGPQRNIEGWVQRK----RPGTPAA 465
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 33-153 6.16e-14

Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 65.51  E-value: 6.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  33 IGPFVEIQRNSTIgprckissHTFICEGVSIGAEVFVGHGVVftnerypeatnadgslkrdgdweLVETLVGDRASIGSN 112
Cdd:cd04645    41 IGERTNIQDGSVL--------HVDPGYPTIIGDNVTVGHGAV-----------------------LHGCTIGDNCLIGMG 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1724806011 113 ATIVAGITIGEGALVGAGAVVT--RDVPPYAIVAGCPARVIGD 153
Cdd:cd04645    90 AIILDGAVIGKGSIVAAGSLVPpgKVIPPGSLVAGSPAKVVRE 132
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 45-151 3.28e-13

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 64.51  E-value: 3.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  45 IGPRCKISSHTFIC--EGVSIGAEVFVGHGVVFTNERYPEATNAD----GSLKRDgDWELVET--LVGDRASIGSNATIV 116
Cdd:PRK09677   68 FGDNVQVNDYVHIAciESITIGRDTLIASKVFITDHNHGSFKHSDdfssPNLPPD-MRTLESSavVIGQRVWIGENVTIL 146

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1724806011 117 AGITIGEGALVGAGAVVTRDVPPYAIVAGCPARVI 151
Cdd:PRK09677  147 PGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKII 181
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 33-153 4.41e-13

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 63.51  E-value: 4.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  33 IGPFVEIQRNSTIgprckissHTFICEGVSIGAEVFVGHGVVftnerypeatnadgslkrdgdwelvetL----VGDRAS 108
Cdd:COG0663    52 IGEGSNIQDGVVL--------HVDPGYPLTIGDDVTIGHGAI---------------------------LhgctIGDNVL 96

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1724806011 109 IGSNATIVAGITIGEGALVGAGAVVT--RDVPPYAIVAGCPARVIGD 153
Cdd:COG0663    97 IGMGAIVLDGAVIGDGSIVGAGALVTegKVVPPGSLVVGSPAKVVRE 143
cysE PRK11132
serine acetyltransferase; Provisional
 109-165 4.84e-13

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 65.10  E-value: 4.84e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1724806011 109 IGSNATIVAGITIGEGALVGAGAVVTRDVPPYAIVAGCPARVIGdtrqkRARSQRPS 165
Cdd:PRK11132  202 IGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVG-----KPESDKPS 253
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 57-151 1.21e-12

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 62.91  E-value: 1.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  57 ICEgVSIGAEVFVGHGV-VFTnerypeATNADGSLKRDGDWELVETL-VGDRASIGSNATIVAGITIGEGALVGAGAVVT 134
Cdd:PRK10092   91 VCP-IRIGDNCMLAPGVhIYT------ATHPLDPVARNSGAELGKPVtIGNNVWIGGRAVINPGVTIGDNVVVASGAVVT 163

                          90
                  ....*....|....*..
gi 1724806011 135 RDVPPYAIVAGCPARVI 151
Cdd:PRK10092  164 KDVPDNVVVGGNPARII 180
PLN02739 PLN02739
serine acetyltransferase
 60-152 4.64e-12

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 63.13  E-value: 4.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  60 GVSIGAEVFVGHGVVFTNerypeATNADGSLKRDGDwelVETLVGDRASIGSNATIVAGITIGEGALVGAGAVVTRDVPP 139
Cdd:PLN02739  225 GVVIGETAVIGDRVSILH-----GVTLGGTGKETGD---RHPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPS 296

                          90
                  ....*....|...
gi 1724806011 140 YAIVAGCPARVIG 152
Cdd:PLN02739  297 HSMVAGNPAKLIG 309
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 33-152 5.19e-12

Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane/envelope biogenesis]; Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 61.96  E-value: 5.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  33 IGPFVEIQRNSTIGPRCKISSHTFICEGVSIGAEVFVGHGVV---------FTNE-------------------RypeAT 84
Cdd:COG1043    22 IGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASigeepqdlkYKGEptrleigdnntirefvtihR---GT 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  85 NADGSLKRDGDWEL----------------------------VEtlVGDRASIGSNATIVAGITIGEGALVGAGAVVTRD 136
Cdd:COG1043    99 VQGGGVTRIGDDNLlmayvhvahdcvvgnnvilannatlaghVE--VGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKD 176

                         170
                  ....*....|....*.
gi 1724806011 137 VPPYAIVAGCPARVIG 152
Cdd:COG1043   177 VPPYVLAAGNPARLRG 192
PLN02694 PLN02694
serine O-acetyltransferase
 60-162 7.00e-12

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 61.97  E-value: 7.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  60 GVSIGAEVFVGHGVVFTNErypeaTNADGSLKRDGDwelVETLVGDRASIGSNATIVAGITIGEGALVGAGAVVTRDVPP 139
Cdd:PLN02694  180 GVVIGETAVIGNNVSILHH-----VTLGGTGKACGD---RHPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPP 251

                          90       100
                  ....*....|....*....|...
gi 1724806011 140 YAIVAGCPARVIGDtRQKRARSQ 162
Cdd:PLN02694  252 RTTAVGNPARLVGG-KEKPAKHE 273
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 33-152 7.75e-12

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: 61.68  E-value: 7.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  33 IGPFVEIQRNSTIGPRCKISSH------------TFICEGVSIGAE------------VFVGHGVVF----TNERypeAT 84
Cdd:cd03351    20 IGPFCVIGPNVEIGDGTVIGSHvvidgpttigknNRIFPFASIGEApqdlkykgeptrLEIGDNNTIrefvTIHR---GT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  85 NADGSLKRDGDWELV--------ETLVGDRASIGSNAT-----------IVAGIT-------IGEGALVGAGAVVTRDVP 138
Cdd:cd03351    97 AQGGGVTRIGNNNLLmayvhvahDCVIGNNVILANNATlaghveigdyaIIGGLSavhqfcrIGRHAMVGGGSGVVQDVP 176

                         170
                  ....*....|....
gi 1724806011 139 PYAIVAGCPARVIG 152
Cdd:cd03351   177 PYVIAAGNRARLRG 190
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 24-166 1.13e-11

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 61.97  E-value: 1.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  24 GCEIKTGSLIGPFVEIqRNSTIGPRCKISSHTFICEGvSIGAEVFVGHGVVftnerypeATNADGSLKrdgdwelVETLV 103
Cdd:PRK09451  335 GAELAEGAHVGNFVEM-KKARLGKGSKAGHLTYLGDA-EIGDNVNIGAGTI--------TCNYDGANK-------FKTII 397

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1724806011 104 GDRASIGSNATIVAGITIGEGALVGAGAVVTRDVppyaivaGCPARVIGDTRQKRARS-QRPSR 166
Cdd:PRK09451  398 GDDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDV-------AENELVISRVPQRHIQGwQRPVK 454
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 24-149 9.20e-11

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: 59.26  E-value: 9.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  24 GCEIKTGSLIGPFVEIQRNSTIGPRCKISSHTFICEGVSIGAEVFVGHGVVFtnerypeatNADG---SLKRDGDWELVE 100
Cdd:COG1044   126 GVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVIGDRVIIHSGAVI---------GADGfgfAPDEDGGWVKIP 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011 101 TL----VGDRASIGSNATI---------------------------------------VAG------------------- 118
Cdd:COG1044   197 QLgrvvIGDDVEIGANTTIdrgalgdtvigdgtkidnlvqiahnvrigehtaiaaqvgIAGstkigdnvviggqvgiagh 276

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1724806011 119 ITIGEGALVGAGAVVTRDVPPYAIVAGCPAR 149
Cdd:COG1044   277 LTIGDGVIIGAQSGVTKSIPEGGVYSGSPAQ 307
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
24-152 1.88e-10

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 57.80  E-value: 1.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  24 GCEIKTGSLIGPFVEIQRNSTIGPRCKISSHTFICE------GVSIGA------------EVFVGHGVVF----TNERyp 81
Cdd:PRK05289   20 NVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKnnrifpFASIGEdpqdlkykgeptRLVIGDNNTIrefvTINR-- 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  82 eATNADGSLKRDGD--WELVET------LVGDRASIGSNAT-----------IVAGIT-------IGEGALVGAGAVVTR 135
Cdd:PRK05289   98 -GTVQGGGVTRIGDnnLLMAYVhvahdcVVGNHVILANNATlaghvevgdyaIIGGLTavhqfvrIGAHAMVGGMSGVSQ 176

                         170
                  ....*....|....*..
gi 1724806011 136 DVPPYAIVAGCPARVIG 152
Cdd:PRK05289  177 DVPPYVLAEGNPARLRG 193
PLN02357 PLN02357
serine acetyltransferase
 103-165 2.41e-10

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 57.97  E-value: 2.41e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1724806011 103 VGDRASIGSNATIVAGITIGEGALVGAGAVVTRDVPPYAIVAGCPARVIGDTRQKRARSQRPS 165
Cdd:PLN02357  281 IGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLIGGKENPIKHDKIPS 343
PRK10502 PRK10502
putative acyl transferase; Provisional
 19-153 2.99e-10

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 56.11  E-value: 2.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  19 LVNIYGCEIKTGSLIGPFVEIqrnsTIGPRCKISSHTFICEGVSIG--AEVFVGHGVVFTNERYPEATNADGSlkrDGDW 96
Cdd:PRK10502   46 LLRLFGAKIGKGVVIRPSVRI----TYPWKLTIGDYAWIGDDVWLYnlGEITIGAHCVISQKSYLCTGSHDYS---DPHF 118

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1724806011  97 ELVET--LVGDRASIGSNATIVAGITIGEGALVGAGAVVTRDVPPYAIVAGCPARVIGD 153
Cdd:PRK10502  119 DLNTApiVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIRP 177
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 5-149 3.02e-10

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: 56.65  E-value: 3.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011   5 DADIERDVGIfYPDLVNIYGCEIKTGSLIGPFVEIQRNSTIGPRCKISSHTFICEGVSIGAEVFVGHGVVFTNERYpeat 84
Cdd:cd03352     1 SAKIGENVSI-GPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIGSDGF---- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  85 nadGSLKRDGDWELVETL----VGDRASIGSNATI---------------------------------------VAG--- 118
Cdd:cd03352    76 ---GFAPDGGGWVKIPQLggviIGDDVEIGANTTIdrgalgdtvigdgtkidnlvqiahnvrigencliaaqvgIAGstt 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1724806011 119 ----------------ITIGEGALVGAGAVVTRDVPPYAIVAGCPAR 149
Cdd:cd03352   153 igdnviiggqvgiaghLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQ 199
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 43-134 6.40e-10

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: 53.02  E-value: 6.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  43 STIGPRCKISSHTFICEGVSIGAEVFVGHGVVFTNERYPEatnadgslkrdgdwELVETLVGDRASIGSNATIVAGITIG 122
Cdd:cd00208     1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGPN--------------EKNPTIIGDNVEIGANAVIHGGVKIG 66

                          90
                  ....*....|..
gi 1724806011 123 EGALVGAGAVVT 134
Cdd:cd00208    67 DNAVIGAGAVVT 78
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 24-139 1.29e-09

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 55.91  E-value: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  24 GCEIKTGSLIGPFVEIQRnSTIGPRCKISSHTFICEGvSIGAEVFVGHGVVftnerypeATNADGSLKRdgdwelvETLV 103
Cdd:PRK14355  338 GTELSAHVKIGNFVETKK-IVMGEGSKASHLTYLGDA-TIGRNVNIGCGTI--------TCNYDGVKKH-------RTVI 400

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1724806011 104 GDRASIGSNATIVAGITIGEGALVGAGAVVTRDVPP 139
Cdd:PRK14355  401 EDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPP 436
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 28-152 2.38e-09

acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes LpxA, 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, but this protein represents the first step (from UDP-N-acetyl-D-glucosamine) and appears to be conserved in function. Proteins from this family contain many copies of the bacterial transferase hexapeptide repeat (pfam00132). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 54.57  E-value: 2.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  28 KTGSLIGPFVEIQRNSTI-------GPRCKISSHTFICEGVSIGAEVFVGHGVVFTNErypeATNADgslkrdgdwelvE 100
Cdd:TIGR01852  74 KTRLIIGDNNTIREFVTInrgtasgGGVTRIGNNNLLMAYSHIAHDCVVGNHVILANN----ATLAG------------H 137

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1724806011 101 TLVGDRASIGSNATIVAGITIGEGALVGAGAVVTRDVPPYAIVAGCPARVIG 152
Cdd:TIGR01852 138 VEVGDYAIIGGLVAVHQFVRIGRYAMIGGLSAVSKDVPPYCLAEGNRARLRG 189
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 33-153 9.51e-09

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: 51.83  E-value: 9.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  33 IGPFVEIQRNSTIGPRCKISSHTFICEGVSIGAEVFVGHGVVFtnerypEATNadgslkrdgdwelvetlVGDRASIGSN 112
Cdd:cd03359    45 IGRYCILSEGCVIRPPFKKFSKGVAFFPLHIGDYVFIGENCVV------NAAQ-----------------IGSYVHIGKN 101

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1724806011 113 ATIVAGITIGEGALVGAGAVVTRD--VPPYAIVAGCPARVIGD 153
Cdd:cd03359   102 CVIGRRCIIKDCVKILDGTVVPPDtvIPPYSVVSGRPARFIGE 144
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 26-152 5.89e-08

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 50.79  E-value: 5.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  26 EIKTGSLIGPFVEIQR------NSTIGPRCKISSHTFICEGVSIGAEVFVGHGVVFTNErypeatnadgslkrdgdwelV 99
Cdd:PRK12461   79 EIGDRNVIREGVTIHRgtkgggVTRIGNDNLLMAYSHVAHDCQIGNNVILVNGALLAGH--------------------V 138

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1724806011 100 EtlVGDRASIGSNATIVAGITIGEGALVGAGAVVTRDVPPYAIVAGCPARVIG 152
Cdd:PRK12461  139 T--VGDRAIISGNCLVHQFCRIGALAMMAGGSRISKDVPPYCMMAGHPTNVHG 189
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 33-151 9.30e-08

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: 49.11  E-value: 9.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  33 IGPFVEIQRNSTIgprckissHTFICEGVSIGAEVFVGHGVVFTNERypeatnadgslkrdgdwelvetlVGDRASIGSN 112
Cdd:cd04650    42 IGKYSNVQENVSI--------HTDHGYPTEIGDYVTIGHNAVVHGAK-----------------------VGNYVIVGMG 90

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1724806011 113 ATIVAGITIGEGALVGAGAVVT--RDVPPYAIVAGCPARVI 151
Cdd:cd04650    91 AILLNGAKIGDHVIIGAGAVVTpgKEIPDYSLVLGVPAKVV 131
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 3-142 1.65e-07

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 49.98  E-value: 1.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011   3 ITDADIERDVgIFYPDLVnIYGCEIKTGSLIGPFVEIQRNSTIGPRCKI----------------SSHTFICEGVSIGAE 66
Cdd:PRK14358  303 VTDSVLHEGA-VIKPHSV-LEGAEVGAGSDVGPFARLRPGTVLGEGVHIgnfvetknarldagvkAGHLAYLGDVTIGAE 380

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1724806011  67 VFVGHGVVftnerypeATNADGSLKRdgdwelvETLVGDRASIGSNATIVAGITIGEGALVGAGAVVTRDVPPYAI 142
Cdd:PRK14358  381 TNVGAGTI--------VANFDGVNKH-------QSKVGAGVFIGSNTTLIAPRVVGDAAFIAAGSAVHDDVPEGAM 441
PRK10191 PRK10191
putative acyl transferase; Provisional
 38-150 1.89e-07

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 47.96  E-value: 1.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  38 EIQRNSTIGPRCKISsHTF---ICEGVSIGAEVFVGHGVVFTNErypeatnadgslkrdGDWELVETLVGDRASIGSNAT 114
Cdd:PRK10191   43 EIQAAATIGRRFTIH-HGYavvINKNVVAGDDFTIRHGVTIGNR---------------GADNMACPHIGNGVELGANVI 106

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1724806011 115 IVAGITIGEGALVGAGAVVTRDVPPYAIVAGCPARV 150
Cdd:PRK10191  107 ILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKARV 142
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 45-148 3.65e-07

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 48.98  E-value: 3.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  45 IGPRCKISShTFICEG--VSIGAEVFVGHGVVFTNERYpeatnADGSLKRDGdwelveTLVGDRASIGSNATIVAGITIG 122
Cdd:TIGR02353 600 IGRGVYIDG-TDLTERdlVTIGDDSTLNEGSVIQTHLF-----EDRVMKSDT------VTIGDGATLGPGAIVLYGVVMG 667

                          90       100
                  ....*....|....*....|....*...
gi 1724806011 123 EGALVGAGAVVTR--DVPPYAIVAGCPA 148
Cdd:TIGR02353 668 EGSVLGPDSLVMKgeEVPAHTRWRGNPA 695
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 14-133 5.20e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 48.21  E-value: 5.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  14 IFYPDLVNIYGCEIKTGSLIGPFVEIQRNSTIGPRCKISSHTFICEGVSIGAEVFVGHGVVftnerypeatnadgslkrd 93
Cdd:PRK00892   90 LFDPPATPSPAAGIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVK------------------- 150

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1724806011  94 gdwelvetlVGDRASIGSNATIVAGITIGEGALVGAGAVV 133
Cdd:PRK00892  151 ---------IGADCRLHANVTIYHAVRIGNRVIIHSGAVI 181
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 33-133 9.98e-07

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: 47.32  E-value: 9.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  33 IGPFVEIQRNSTIGPRCKISSHTFICEGVSIGAEVFVGHGVVftnerypeatnadgslkrdgdwelvetlVGDRASIGSN 112
Cdd:COG1044   105 IDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVV----------------------------IGDDCVLHPN 156

                          90       100
                  ....*....|....*....|.
gi 1724806011 113 ATIVAGITIGEGALVGAGAVV 133
Cdd:COG1044   157 VTIYERCVIGDRVIIHSGAVI 177
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 24-134 2.46e-06

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: 45.27  E-value: 2.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  24 GCEIKTGSLIGPFVEIQRNSTIGPRCKISSHTFICEGVSIGAEVFVGHGVVFTNERYP----------------EATNAD 87
Cdd:cd05636    23 GAIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSIIMDGTKVPhlnyvgdsvlgenvnlGAGTIT 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1724806011  88 GSLKRDG-------DWELVET-------LVGDRASIGSNATIVAGITIGEGALVGAGAVVT 134
Cdd:cd05636   103 ANLRFDDkpvkvrlKGERVDTgrrklgaIIGDGVKTGINVSLNPGVKIGPGSWVYPGCVVR 163
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 6-148 2.50e-06

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


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 44.68  E-value: 2.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011   6 ADIERDVGIFYPDLVNIygceiktGSLIGPFVEIQRNSTIGPRCKISshtficEGVSIGAEVFVGhGVVftneRYPEATn 85
Cdd:cd03350    14 AFIGPGAVLMMPSYVNI-------GAYVDEGTMVDSWATVGSCAQIG------KNVHLSAGAVIG-GVL----EPLQAT- 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1724806011  86 adgslkrdgdwelvETLVGDRASIGSNATIVAGITIGEGALVGAGAVVTR---------------DVPPYAIV-AGCPA 148
Cdd:cd03350    75 --------------PVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTQstpiydretgeiyygRVPPGSVVvAGSLP 139
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 24-149 5.14e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 45.52  E-value: 5.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  24 GCEIKTGSLIGPFVEIQRNSTIGPRCKISSHTFICEGVSIGAEVFVGHGVV-------FTNERypeatnadgslkrdGDW 96
Cdd:PRK00892  130 GVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVigsdgfgFANDR--------------GGW 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  97 ELVETL----VGDRASIGSNATI---------------------------------------VAG--------------- 118
Cdd:PRK00892  196 VKIPQLgrviIGDDVEIGANTTIdrgalddtvigegvkidnlvqiahnvvigrhtaiaaqvgIAGstkigrycmiggqvg 275

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1724806011 119 ----ITIGEGALVGAGAVVTRDVPPY-AIVAGCPAR 149
Cdd:PRK00892  276 iaghLEIGDGVTITAMSGVTKSIPEPgEYSSGIPAQ 311
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 101-143 1.34e-05

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: 43.95  E-value: 1.34e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1724806011 101 TLVGDRASIGSNATIVAGITIGEGALVGAGAVVTR---------------DVPPYAIV 143
Cdd:COG2171   171 VIIEDNCFIGARSGVVEGVIVGEGAVLGAGVYLTAstkiydrvtgevyygRVPAGSVV 228
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 45-168 1.63e-05

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 43.97  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  45 IGPRCKISSHTFICEG-VSIGAEVFVGHGVVFTNERypeatnADGSLKRDGDWElvetlVGDRASIGSNATIVAGITIGE 123
Cdd:TIGR02353 115 IGKGVDIGSLPPVCTDlLTIGAGTIVRKEVMLLGYR------AERGRLHTGPVT-----LGRDAFIGTRSTLDIDTSIGD 183

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1724806011 124 GALVGAGAVVTRD--VPPYAIVAGCPARVIGDTRqkraRSQRPSRPA 168
Cdd:TIGR02353 184 GAQLGHGSALQGGqsIPDGERWHGSPAQKTGADY----RKVQPARPY 226
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 24-138 5.90e-05

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 42.28  E-value: 5.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  24 GCEIKTgSLIGPFVEIQRNSTIGPR---------CKISshtficEGVSIGAevfvghGVVftnerypeATNADGSLKRdg 94
Cdd:PRK14359  310 KSEIKN-THIGNFVETKNAKLNGVKaghlsylgdCEID------EGTNIGA------GTI--------TCNYDGKKKH-- 366

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1724806011  95 dwelvETLVGDRASIGSNATIVAGITIGEGALVGAGAVVTRDVP 138
Cdd:PRK14359  367 -----KTIIGKNVFIGSDTQLVAPVNIEDNVLIAAGSTVTKDVP 405
PLN02296 PLN02296
carbonate dehydratase
 23-149 9.03e-05

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 41.65  E-value: 9.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  23 YGC-------EIKTGSligpFVEIQRNSTIG-PRCKISSHTFiceGVSIGAEVFVGHGVVftnerypeatnadgslkrdg 94
Cdd:PLN02296   81 YGCvlrgdvnSISVGS----GTNIQDNSLVHvAKTNLSGKVL---PTIIGDNVTIGHSAV-------------------- 133

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1724806011  95 dweLVETLVGDRASIGSNATIVAGITIGEGALVGAGAVVTRD--VPPYAIVAGCPAR 149
Cdd:PLN02296  134 ---LHGCTVEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNtrIPSGEVWAGNPAK 187
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 103-151 1.08e-04

paaY-like: This group is composed by uncharacterized proteins with similarity to the protein product of the E. coli paaY gene, which is part of the paa gene cluster responsible for phenylacetic acid degradation. Proteins in this group are expected to adopt the left-handed parallel beta-helix (LbH) structure. They contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Similarity to gamma carbonic anhydrase and Ferripyochelin Binding Protein (FBP) may suggest metal binding capacity.


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 40.43  E-value: 1.08e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1724806011 103 VGDRASIGSNATIVAGITIGEGALVGAGAVVTR--DVPPYAIVAGCPARVI 151
Cdd:cd04745    81 IGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAgtVIPPRSLIAGSPAKVI 131
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 57-137 1.84e-04

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: 40.77  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  57 ICEGVSIGAEVFVGHGVVftnerypeatnadgslkrdgdwelvetlVGDRASIGSNATIVAGITIGEGALVGAGAVVTRD 136
Cdd:COG1044   111 IGEGVSIGPFAVIGAGVV----------------------------IGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYER 162


                  .
gi 1724806011 137 V 137
Cdd:COG1044   163 C 163
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 103-137 2.14e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 40.51  E-value: 2.14e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1724806011 103 VGDRASIGSNATIVAGITIGEGALVGAGAVVTRDV 137
Cdd:PRK00892  115 IGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGV 149
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 51-132 2.63e-04

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: 40.39  E-value: 2.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  51 ISSHTFICEGVSIGAEVFVGHGVVftnerypeatnadgslkrdgdwelvetlVGDRASIGSNATIVAGITIGEGALVGAG 130
Cdd:COG1044    99 IHPSAVIDPSAKIGEGVSIGPFAV----------------------------IGAGVVIGDGVVIGPGVVIGDGVVIGDD 150


                  ..
gi 1724806011 131 AV 132
Cdd:COG1044   151 CV 152
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 35-137 6.30e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 39.35  E-value: 6.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  35 PFVEIQRNSTIGPRCKISshtficEGVSIGAEVFVGHGVVftnerypeatnadgslkrdgdwelvetlVGDRASIGSNAT 114
Cdd:PRK00892   99 PAAGIHPSAVIDPSAKIG------EGVSIGPNAVIGAGVV----------------------------IGDGVVIGAGAV 144

                          90       100
                  ....*....|....*....|...
gi 1724806011 115 IVAGITIGEGALVGAGAVVTRDV 137
Cdd:PRK00892  145 IGDGVKIGADCRLHANVTIYHAV 167
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
103-135 1.67e-03

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 34.72  E-value: 1.67e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1724806011 103 VGDRASIGSNATIvaGITIGEGALVGAGAVVTR 135
Cdd:pfam14602   3 IGDNCLIGANSGI--GVSLGDNCVVGAGVVITA 33
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 24-129 2.65e-03

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: 35.30  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1724806011  24 GCEIKTGSLIGPFVeIQRNSTIGPRCKISsHTFICEGVSIGAEVfvghgvvftnerypeatnadgslkrdgdwELVETLV 103
Cdd:cd03356     5 STVIGENAIIKNSV-IGDNVRIGDGVTIT-NSILMDNVTIGANS-----------------------------VIVDSII 53

                          90       100
                  ....*....|....*....|....*.
gi 1724806011 104 GDRASIGSNATIVAGITIGEGALVGA 129
Cdd:cd03356    54 GDNAVIGENVRVVNLCIIGDDVVVED 79
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 61-128 5.56e-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: 5.56e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1724806011  61 VSIGAEVFVGHGVVFTNERYpeatnadgslkrDGDW-ELVETLVGDRASIGSNATIVAGITIGEGALVG 128
Cdd:TIGR02353 373 TDIGEETFIADGLLMGNARL------------SGGWfRLGRTRIGRRSFLGNSGYYPPGAKTGDNVLLG 429
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 101-143 6.68e-03

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


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 35.94  E-value: 6.68e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1724806011 101 TLVGDRASIGSNATIVAGITIGEGALVGAGAVVTR---------------DVPPYAIV 143
Cdd:PRK11830  177 VIIEDNCFIGARSEVVEGVIVEEGSVLGMGVFLGQstkiydretgevhygRVPAGSVV 234
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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