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Conserved domains on  [gi|515624707|ref|WP_017057307|]
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MULTISPECIES: DapH/DapD/GlmU-related protein [Vibrio]

Protein Classification

acyltransferase( domain architecture ID 11414744)

acyltransferase belonging to the transferase hexapeptide repeat family, catalyzes the transfer of an acyl group from an acyl-CoA to a substrate

CATH:  2.160.10.10
EC:  2.3.-.-
Gene Ontology:  GO:0046677|GO:0016746|GO:0120225
PubMed:  15500694
SCOP:  4002841

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
96-239 3.86e-41

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


:

Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 138.08  E-value: 3.86e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707  96 ISIGDNCRISGHTTFSGCSqpldsfkpplLSIGNNVDIGWQSTIAVGKRVIISDNVRIAGGAFLFGySGHPLDakrradG 175
Cdd:COG0110    9 ARIGDGVVIGPGVRIYGGN----------ITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILT-GNHPID------D 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515624707 176 EGDDPQQISDIILERDVWLGTNVTVKGGVTIGEGAVIAAGSVVIKNVPPFAIAAGNPARVVGQV 239
Cdd:COG0110   72 PATFPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKR 135
 
Name Accession Description Interval E-value
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
96-239 3.86e-41

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 138.08  E-value: 3.86e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707  96 ISIGDNCRISGHTTFSGCSqpldsfkpplLSIGNNVDIGWQSTIAVGKRVIISDNVRIAGGAFLFGySGHPLDakrradG 175
Cdd:COG0110    9 ARIGDGVVIGPGVRIYGGN----------ITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILT-GNHPID------D 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515624707 176 EGDDPQQISDIILERDVWLGTNVTVKGGVTIGEGAVIAAGSVVIKNVPPFAIAAGNPARVVGQV 239
Cdd:COG0110   72 PATFPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKR 135
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 125-236 1.18e-37

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: 127.96  E-value: 1.18e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 125 LSIGNNVDIGWQSTIAVGKRVIISDNVRIAGGAFLFGySGHPLDAKRRAdgeGDDPQQISDIILERDVWLGTNVTVKGGV 204
Cdd:cd04647    2 ISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYD-HNHDIDDPERP---IEQGVTSAPIVIGDDVWIGANVVILPGV 77

                         90       100       110
                 ....*....|....*....|....*....|..
gi 515624707 205 TIGEGAVIAAGSVVIKNVPPFAIAAGNPARVV 236
Cdd:cd04647   78 TIGDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 121-239 3.62e-19

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 82.74  E-value: 3.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 121 KPPL-LSIGNNVDIG------WQSTIAVGKRVIISDNVRIAGGAFLfGYSGHPLDAKRRADGEgddpQQISDIILERDVW 193
Cdd:PRK09527  65 EPPVyFSYGSNIHIGrnfyanFNLTIVDDYTVTIGDNVLIAPNVTL-SVTGHPVHHELRKNGE----MYSFPITIGNNVW 139

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 515624707 194 LGTNVTVKGGVTIGEGAVIAAGSVVIKNVPPFAIAAGNPARVVGQV 239
Cdd:PRK09527 140 IGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIREI 185
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 127-233 1.56e-16

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


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 75.61  E-value: 1.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707  127 IGNNVDIgWQSTIaVGKRVIISDNVRIAGGAFLFGYsghpldakrradgegddpqqisdIILERDVWLGTNVTVKGGVTI 206
Cdd:TIGR03570 120 IGDNVII-NTGAI-VEHDCVIGDFVHIAPGVTLSGG-----------------------VVIGEGVFIGAGATIIQGVTI 174

                          90       100
                  ....*....|....*....|....*..
gi 515624707  207 GEGAVIAAGSVVIKNVPPFAIAAGNPA 233
Cdd:TIGR03570 175 GAGAIVGAGAVVTKDIPDGGVVVGVPA 201
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
185-214 3.40e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 36.93  E-value: 3.40e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 515624707  185 DIILERDVWLGTNVTVKGGVTIGEGAVIAA 214
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
96-239 3.86e-41

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 138.08  E-value: 3.86e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707  96 ISIGDNCRISGHTTFSGCSqpldsfkpplLSIGNNVDIGWQSTIAVGKRVIISDNVRIAGGAFLFGySGHPLDakrradG 175
Cdd:COG0110    9 ARIGDGVVIGPGVRIYGGN----------ITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILT-GNHPID------D 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515624707 176 EGDDPQQISDIILERDVWLGTNVTVKGGVTIGEGAVIAAGSVVIKNVPPFAIAAGNPARVVGQV 239
Cdd:COG0110   72 PATFPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKR 135
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 125-236 1.18e-37

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: 127.96  E-value: 1.18e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 125 LSIGNNVDIGWQSTIAVGKRVIISDNVRIAGGAFLFGySGHPLDAKRRAdgeGDDPQQISDIILERDVWLGTNVTVKGGV 204
Cdd:cd04647    2 ISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYD-HNHDIDDPERP---IEQGVTSAPIVIGDDVWIGANVVILPGV 77

                         90       100       110
                 ....*....|....*....|....*....|..
gi 515624707 205 TIGEGAVIAAGSVVIKNVPPFAIAAGNPARVV 236
Cdd:cd04647   78 TIGDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 125-236 4.93e-31

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: 112.90  E-value: 4.93e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 125 LSIGNNVDIGWQSTIAVGKRVIISDNVRIAGGAFLFGySGHPLDAKRRADGEgddpqQISD-IILERDVWLGTNVTVKGG 203
Cdd:cd03357   63 IHIGDNFYANFNCTILDVAPVTIGDNVLIGPNVQIYT-AGHPLDPEERNRGL-----EYAKpITIGDNVWIGGGVIILPG 136

                         90       100       110
                 ....*....|....*....|....*....|...
gi 515624707 204 VTIGEGAVIAAGSVVIKNVPPFAIAAGNPARVV 236
Cdd:cd03357  137 VTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 141-238 9.64e-30

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: 108.79  E-value: 9.64e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 141 VGKRVIISDNVRIAGGAF--LFGYSGHPL---DAKRRADGEGDDPQQISDIILERDVWLGTNVTVKGGVTIGEGAVIAAG 215
Cdd:cd03349   24 IGKFCSIAPGVKIGLGGNhpTDWVSTYPFyifGGEWEDDAKFDDWPSKGDVIIGNDVWIGHGATILPGVTIGDGAVIAAG 103

                         90       100
                 ....*....|....*....|...
gi 515624707 216 SVVIKNVPPFAIAAGNPARVVGQ 238
Cdd:cd03349  104 AVVTKDVPPYAIVGGNPAKVIRY 126
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 127-237 9.45e-24

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: 92.56  E-value: 9.45e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 127 IGNNVDIGWQSTIavGKRVIISDNVRIAGGAFLFGYS--------GHPL----DAKRRADGEGDDPQQisDIILERDVWL 194
Cdd:cd03358    1 IGDNCIIGTNVFI--ENDVKIGDNVKIQSNVSIYEGVtieddvfiGPNVvftnDLYPRSKIYRKWELK--GTTVKRGASI 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 515624707 195 GTNVTVKGGVTIGEGAVIAAGSVVIKNVPPFAIAAGNPARVVG 237
Cdd:cd03358   77 GANATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 121-239 3.62e-19

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 82.74  E-value: 3.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 121 KPPL-LSIGNNVDIG------WQSTIAVGKRVIISDNVRIAGGAFLfGYSGHPLDAKRRADGEgddpQQISDIILERDVW 193
Cdd:PRK09527  65 EPPVyFSYGSNIHIGrnfyanFNLTIVDDYTVTIGDNVLIAPNVTL-SVTGHPVHHELRKNGE----MYSFPITIGNNVW 139

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 515624707 194 LGTNVTVKGGVTIGEGAVIAAGSVVIKNVPPFAIAAGNPARVVGQV 239
Cdd:PRK09527 140 IGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIREI 185
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 127-236 5.56e-19

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: 79.57  E-value: 5.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 127 IGNNVDIGWQSTIAVGKRVIISDNVRIAGGAFLFGYSGHPLDAKRradgegddpqqisdIILERDVWLGTNVTVKGGVTI 206
Cdd:cd05825   12 IGEGVWIYNLAPVTIGSDACISQGAYLCTGSHDYRSPAFPLITAP--------------IVIGDGAWVAAEAFVGPGVTI 77

                         90       100       110
                 ....*....|....*....|....*....|
gi 515624707 207 GEGAVIAAGSVVIKNVPPFAIAAGNPARVV 236
Cdd:cd05825   78 GEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 103-236 1.92e-18

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 80.69  E-value: 1.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 103 RISGHTTF-SGCSQPLDSFKPPLLSIGNNVDIGWQSTIAVGKRVIISDNVRIAGGAFL----FGYSGHPLDAKRRADGEG 177
Cdd:PRK09677  43 SINFGEGFtSGVGLRLDAFGRGKLFFGDNVQVNDYVHIACIESITIGRDTLIASKVFItdhnHGSFKHSDDFSSPNLPPD 122

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 515624707 178 DDPQQISDIILERDVWLGTNVTVKGGVTIGEGAVIAAGSVVIKNVPPFAIAAGNPARVV 236
Cdd:PRK09677 123 MRTLESSAVVIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKII 181
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 122-232 2.02e-17

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: 75.17  E-value: 2.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 122 PPLLSIGNNVDIGWQSTIAVGKRVIISDNVRIA-----GGAFLFGYSGHPldakrradgegddpqqisdiILERDVWLGT 196
Cdd:cd03354    6 HPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYqgvtlGGKGKGGGKRHP--------------------TIGDNVVIGA 65

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 515624707 197 NVTVKGGVTIGEGAVIAAGSVVIKNVPPFAIAAGNP 232
Cdd:cd03354   66 GAKILGNITIGDNVKIGANAVVTKDVPANSTVVGVP 101
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 147-239 2.13e-17

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 77.55  E-value: 2.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 147 ISDNVRIAGGAFLFGYSgHPLDAKRRADG-EGDDPQQISDiilerDVWLGTNVTVKGGVTIGEGAVIAAGSVVIKNVPPF 225
Cdd:PRK10092  96 IGDNCMLAPGVHIYTAT-HPLDPVARNSGaELGKPVTIGN-----NVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDN 169

                         90
                 ....*....|....
gi 515624707 226 AIAAGNPARVVGQV 239
Cdd:PRK10092 170 VVVGGNPARIIKKL 183
PRK10502 PRK10502
putative acyl transferase; Provisional
 122-238 7.22e-17

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 76.14  E-value: 7.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 122 PPLLSIGNNVDIG---WQSTIAvgkRVIISDNVRIAGGAFLFGYSgHplDAKRRADGegddpQQISDIILERDVWLGTNV 198
Cdd:PRK10502  69 PWKLTIGDYAWIGddvWLYNLG---EITIGAHCVISQKSYLCTGS-H--DYSDPHFD-----LNTAPIVIGEGCWLAADV 137

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 515624707 199 TVKGGVTIGEGAVIAAGSVVIKNVPPFAIAAGNPARVVGQ 238
Cdd:PRK10502 138 FVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIRP 177
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 127-233 1.56e-16

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


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 75.61  E-value: 1.56e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707  127 IGNNVDIgWQSTIaVGKRVIISDNVRIAGGAFLFGYsghpldakrradgegddpqqisdIILERDVWLGTNVTVKGGVTI 206
Cdd:TIGR03570 120 IGDNVII-NTGAI-VEHDCVIGDFVHIAPGVTLSGG-----------------------VVIGEGVFIGAGATIIQGVTI 174

                          90       100
                  ....*....|....*....|....*..
gi 515624707  207 GEGAVIAAGSVVIKNVPPFAIAAGNPA 233
Cdd:TIGR03570 175 GAGAIVGAGAVVTKDIPDGGVVVGVPA 201
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 187-238 2.18e-16

Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440667 [Multi-domain]  Cd Length: 174  Bit Score: 74.35  E-value: 2.18e-16
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 515624707 187 ILERDVWLGTNVTVKGGVTIGEGAVIAAGSVVIKNVPPFAIAAGNPARVVGQ 238
Cdd:COG1045  119 TIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVKR 170
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 127-232 3.08e-15

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: 71.75  E-value: 3.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 127 IGNNVDIgWQSTIaVGKRVIISDNVRIAGGAFLfgySGHpldakrradgegddpqqisdIILERDVWLGTNVTVKGGVTI 206
Cdd:cd03360  117 IGDNVII-NTGAV-IGHDCVIGDFVHIAPGVVL---SGG--------------------VTIGEGAFIGAGATIIQGVTI 171

                         90       100
                 ....*....|....*....|....*.
gi 515624707 207 GEGAVIAAGSVVIKNVPPFAIAAGNP 232
Cdd:cd03360  172 GAGAIIGAGAVVTKDVPDGSVVVGNP 197
PLN02739 PLN02739
serine acetyltransferase
 123-259 9.59e-13

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 66.98  E-value: 9.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 123 PLLSIGNNVDIGWQSTIAVGKRVIISDNVRIAGGAFLFGYSGHpldakrradgEGDDPQQISDIILerdvwLGTNVTVKG 202
Cdd:PLN02739 210 PAARIGKGILLDHGTGVVIGETAVIGDRVSILHGVTLGGTGKE----------TGDRHPKIGDGAL-----LGACVTILG 274

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 203 GVTIGEGAVIAAGSVVIKNVPPFAIAAGNPARVVGQVQSVK---AAKPDTAKSFENHRGD 259
Cdd:PLN02739 275 NISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFVDEQDpslTMEYDATREFFQNVAV 334
PLN02694 PLN02694
serine O-acetyltransferase
 123-237 1.03e-12

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 66.59  E-value: 1.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 123 PLLSIGNNVDIGWQSTIAVGKRVIISDNVRIAGGAFLFGysghpldakrRADGEGDDPQQISDIILerdvwLGTNVTVKG 202
Cdd:PLN02694 165 PAAKIGKGILFDHATGVVIGETAVIGNNVSILHHVTLGG----------TGKACGDRHPKIGDGVL-----IGAGATILG 229

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 515624707 203 GVTIGEGAVIAAGSVVIKNVPPFAIAAGNPARVVG 237
Cdd:PLN02694 230 NVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLVG 264
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 98-237 3.33e-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: 64.38  E-value: 3.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707  98 IGDNCRISGHTTFS-GCSQPLDsfkppLLSIGNNVDIGWQSTIA----VGKRVIISDNVRIAGgaflfgysgHpldakrr 172
Cdd:cd03351   80 IGDNNTIREFVTIHrGTAQGGG-----VTRIGNNNLLMAYVHVAhdcvIGNNVILANNATLAG---------H------- 138

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515624707 173 adgegddpqqisdIILERDVWLGTNVTVKGGVTIGEGAVIAAGSVVIKNVPPFAIAAGNPARVVG 237
Cdd:cd03351  139 -------------VEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARLRG 190
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 88-237 3.39e-12

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


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 64.65  E-value: 3.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707  88 PF-VSGPlQISIGDNCR------ISGHTT-------FSGCS---QPLD-SFK--PPLLSIGNNVDI-------------G 134
Cdd:COG1043   24 PFcVIGP-DVEIGDGTVigshvvIEGPTTigknnriFPFASigeEPQDlKYKgePTRLEIGDNNTIrefvtihrgtvqgG 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 135 WQSTIA----------------VGKRVIISDNVRIAGgaflfgysgHpldakrradgegddpqqisdIILERDVWLGTNV 198
Cdd:COG1043  103 GVTRIGddnllmayvhvahdcvVGNNVILANNATLAG---------H--------------------VEVGDHAIIGGLS 153

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 515624707 199 TVKGGVTIGEGAVIAAGSVVIKNVPPFAIAAGNPARVVG 237
Cdd:COG1043  154 AVHQFVRIGAHAMVGGGSGVVKDVPPYVLAAGNPARLRG 192
PLN02357 PLN02357
serine acetyltransferase
 123-237 1.52e-11

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 63.36  E-value: 1.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 123 PLLSIGNNVDIGWQSTIAVGKRVIISDNVRIAGGAFLFGysghpldakrRADGEGDDPQQISDIILerdvwLGTNVTVKG 202
Cdd:PLN02357 231 PGAKIGQGILLDHATGVVIGETAVVGNNVSILHNVTLGG----------TGKQSGDRHPKIGDGVL-----IGAGTCILG 295

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 515624707 203 GVTIGEGAVIAAGSVVIKNVPPFAIAAGNPARVVG 237
Cdd:PLN02357 296 NITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLIG 330
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 127-234 2.85e-11

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 61.27  E-value: 2.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 127 IGNNVDIGWQSTIA--------VGKRVIISD------NVRIAGGAFLFGYSGhpldakrradgegddpqqISD-IILERD 191
Cdd:cd03352   95 IGDDVEIGANTTIDrgalgdtvIGDGTKIDNlvqiahNVRIGENCLIAAQVG------------------IAGsTTIGDN 156

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 515624707 192 VWLGTNVTVKGGVTIGEGAVIAAGSVVIKNVPPFAIAAGNPAR 234
Cdd:cd03352  157 VIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQ 199
cysE PRK11132
serine acetyltransferase; Provisional
 139-245 3.42e-11

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 62.02  E-value: 3.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 139 IAVGKRVIISDNVRIAGGAFLFGY---SG--HPldaKRRadgEGddpqqisdiilerdVWLGTNVTVKGGVTIGEGAVIA 213
Cdd:PRK11132 162 IVIGETAVIENDVSILQSVTLGGTgktSGdrHP---KIR---EG--------------VMIGAGAKILGNIEVGRGAKIG 221

                         90       100       110
                 ....*....|....*....|....*....|..
gi 515624707 214 AGSVVIKNVPPFAIAAGNPARVVGQVQSVKAA 245
Cdd:PRK11132 222 AGSVVLQPVPPHTTAAGVPARIVGKPESDKPS 253
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 188-239 5.42e-09

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 53.88  E-value: 5.42e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 515624707 188 LERDVWLGTNVTVKGGVTIGEGAVIAAGSVVIKN--VPPFAIAAGNPARVVGQV 239
Cdd:COG0663   91 IGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGkvVPPGSLVVGSPAKVVREL 144
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
88-237 1.37e-08

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 53.95  E-value: 1.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707  88 PF-VSGPlQISIGDNCR------ISGHTT-------FSGCS---QPLD-SFK--PPLLSIGNNVDI-------------G 134
Cdd:PRK05289  25 PFcVIGP-NVVIGDGTVigshvvIDGHTTigknnriFPFASigeDPQDlKYKgePTRLVIGDNNTIrefvtinrgtvqgG 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 135 WQSTI----------------AVGKRVIISDNVRIAGgaflfgysgHpldakrradgegddpqqisdiilerdVWLGTNV 198
Cdd:PRK05289 104 GVTRIgdnnllmayvhvahdcVVGNHVILANNATLAG---------H--------------------------VEVGDYA 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 515624707 199 TVKGG------VTIGEGAVIAAGSVVIKNVPPFAIAAGNPARVVG 237
Cdd:PRK05289 149 IIGGLtavhqfVRIGAHAMVGGMSGVSQDVPPYVLAEGNPARLRG 193
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 127-239 3.90e-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: 51.26  E-value: 3.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 127 IGNNVDIGWQSTIAV--GKRVIISDNVRIAGGAFLFGysghpldakrradgegddpqqisdIILERDVWLGTNVTVKGGV 204
Cdd:cd04645   41 IGERTNIQDGSVLHVdpGYPTIIGDNVTVGHGAVLHG------------------------CTIGDNCLIGMGAIILDGA 96

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 515624707 205 TIGEGAVIAAGSVVIKN--VPPFAIAAGNPARVVGQV 239
Cdd:cd04645   97 VIGKGSIVAAGSLVPPGkvIPPGSLVAGSPAKVVREL 133
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 127-218 1.65e-07

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 47.63  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 127 IGNNVDIGWQSTIavGKRVIISDNVRIAGGAFLfgysghpldakrradGEGDDPQQISDIILERDVWLGTNVTVKGGVTI 206
Cdd:cd00208    3 IGEGVKIHPKAVI--RGPVVIGDNVNIGPGAVI---------------GAATGPNEKNPTIIGDNVEIGANAVIHGGVKI 65

                         90
                 ....*....|..
gi 515624707 207 GEGAVIAAGSVV 218
Cdd:cd00208   66 GDNAVIGAGAVV 77
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 127-236 4.73e-07

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 50.15  E-value: 4.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 127 IGNNVDIGwQSTIAVGKRV---------IISDNVRIAGGAFLFGYsghpldakrraDGEGDDPQQISDiilerDVWLGTN 197
Cdd:PRK14357 333 IGNFVEIK-KSTIGENTKAqhltylgdaTVGKNVNIGAGTITCNY-----------DGKKKNPTFIED-----GAFIGSN 395

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 515624707 198 VTVKGGVTIGEGAVIAAGSVVIKNVPPFAIAAGNPARVV 236
Cdd:PRK14357 396 SSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQIV 434
PRK10191 PRK10191
putative acyl transferase; Provisional
 133-235 1.12e-06

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 47.19  E-value: 1.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 133 IGWQSTIAVGKRVIISDNVrIAGGAFLFGysgHPLDAKRRAdgegddPQQISDIILERDVWLGTNVTVKGGVTIGEGAVI 212
Cdd:PRK10191  50 IGRRFTIHHGYAVVINKNV-VAGDDFTIR---HGVTIGNRG------ADNMACPHIGNGVELGANVIILGDITIGNNVTV 119

                         90       100
                 ....*....|....*....|...
gi 515624707 213 AAGSVVIKNVPPFAIAAGNPARV 235
Cdd:PRK10191 120 GAGSVVLDSVPDNALVVGEKARV 142
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 187-228 3.64e-06

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 47.52  E-value: 3.64e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 515624707 187 ILERDVWLGTNVTVKGGVTIGEGAVIAAGSVVIKNVPPFAIA 228
Cdd:PRK14354 395 IIGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDALA 436
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 103-237 3.80e-06

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: 47.82  E-value: 3.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707  103 RISGHTTFSGcsQPLDSFKPPLLS--IGNNVDIGwQSTIAVGKRVIISDNVRIAGGAFLFGYsghpldakrRADGegdDP 180
Cdd:TIGR02353  91 DAAPTVLLSG--SPLYSLYLRALGakIGKGVDIG-SLPPVCTDLLTIGAGTIVRKEVMLLGY---------RAER---GR 155

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 515624707  181 QQISDIILERDVWLGTNVTVKGGVTIGEGAVIAAGSVVIKN--VPPFAIAAGNPARVVG 237
Cdd:TIGR02353 156 LHTGPVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGSALQGGqsIPDGERWHGSPAQKTG 214
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 204-228 7.70e-06

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: 46.56  E-value: 7.70e-06
                         10        20
                 ....*....|....*....|....*
gi 515624707 204 VTIGEGAVIAAGSVVIKNVPPFAIA 228
Cdd:COG1207  413 VTIGDGATIGAGSTITKDVPAGALA 437
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 127-234 1.47e-05

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 45.39  E-value: 1.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 127 IGNNVDIGWQSTI---AVGKRVI-----------ISDNVRI------AGGAflfGYSGhpldakrradgegddpqqiSDI 186
Cdd:COG1044  203 IGDDVEIGANTTIdrgALGDTVIgdgtkidnlvqIAHNVRIgehtaiAAQV---GIAG-------------------STK 260

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 515624707 187 IlERDVWLGTNVTVKGGVTIGEGAVIAAGSVVIKNVPPFAIAAGNPAR 234
Cdd:COG1044  261 I-GDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSGSPAQ 307
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 92-237 1.53e-05

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 45.01  E-value: 1.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707  92 GPLQISIGDNCRISGHTTFSGCSQPldsfkppllsiGNNVDIG----WQSTIAVGKRVIISDNVRIAGGAFLFGYsghpl 167
Cdd:PRK12461  74 EESRLEIGDRNVIREGVTIHRGTKG-----------GGVTRIGndnlLMAYSHVAHDCQIGNNVILVNGALLAGH----- 137

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 168 dakrradgegddpqqisdIILERDVWLGTNVTVKGGVTIGEGAVIAAGSVVIKNVPPFAIAAGNPARVVG 237
Cdd:PRK12461 138 ------------------VTVGDRAIISGNCLVHQFCRIGALAMMAGGSRISKDVPPYCMMAGHPTNVHG 189
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 187-228 1.64e-05

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: 44.33  E-value: 1.64e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 515624707 187 ILERDVWLGTNVTVKGGVTIGEGAVIAAGSVVIKNVPPFAIA 228
Cdd:cd03353  146 VIGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGALA 187
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 141-230 1.77e-05

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: 43.52  E-value: 1.77e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 141 VGKRVIISDNVRIAGGAFLFGYSghpldakrradgegdDPQQISDIILERDVWLGTNVTVKGGVTIGEGAVIAAGSVVIK 220
Cdd:cd03350   46 VGSCAQIGKNVHLSAGAVIGGVL---------------EPLQATPVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTQ 110

                         90
                 ....*....|
gi 515624707 221 NVPPFAIAAG 230
Cdd:cd03350  111 STPIYDRETG 120
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 191-253 1.85e-05

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 45.24  E-value: 1.85e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515624707 191 DVWLGTNVTVKGGVTIGEGAVIAAGSVVIKNVPPFAIAAGNPARVVgqvqsvkaaKPDTAKSF 253
Cdd:PRK14353 386 GAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALGRARQET---------KPGWAKKL 439
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 127-218 8.06e-05

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: 42.40  E-value: 8.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 127 IGNNVDIGWQSTIavGKRVIISDNVRIAGGAFLfgysghpldakrradgeGDDpqqisdIILERDVWLGTNVTVKGGVTI 206
Cdd:cd03352    4 IGENVSIGPNAVI--GEGVVIGDGVVIGPGVVI-----------------GDG------VVIGDDCVIHPNVTIYEGCII 58

                         90
                 ....*....|..
gi 515624707 207 GEGAVIAAGSVV 218
Cdd:cd03352   59 GDRVIIHSGAVI 70
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 98-222 9.80e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 42.82  E-value: 9.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707  98 IGDNCRISGHTTfsgcsqpldsfkppllsIGNNVDIGWQSTIA----------VGKRVIISDNVRIagGAFLFGYSGhpl 167
Cdd:PRK00892 133 IGDGVVIGAGAV-----------------IGDGVKIGADCRLHanvtiyhavrIGNRVIIHSGAVI--GSDGFGFAN--- 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 168 dakrrADGEGDDPQQISDIILERDVWLGTNVTV-----------KG-----------GVTIGEGAVIA-----AGSVVI- 219
Cdd:PRK00892 191 -----DRGGWVKIPQLGRVIIGDDVEIGANTTIdrgalddtvigEGvkidnlvqiahNVVIGRHTAIAaqvgiAGSTKIg 265


                 ...
gi 515624707 220 KNV 222
Cdd:PRK00892 266 RYC 268
PLN02296 PLN02296
carbonate dehydratase
 125-234 1.44e-04

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 42.03  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 125 LSIGNNVDIGWQSTIAVGKR--------VIISDNVRIAGGAFLFGYSghpldakrradgegddpqqisdiiLERDVWLGT 196
Cdd:PLN02296  92 ISVGSGTNIQDNSLVHVAKTnlsgkvlpTIIGDNVTIGHSAVLHGCT------------------------VEDEAFVGM 147

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 515624707 197 NVTVKGGVTIGEGAVIAAGSVVIKN--VPPFAIAAGNPAR 234
Cdd:PLN02296 148 GATLLDGVVVEKHAMVAAGALVRQNtrIPSGEVWAGNPAK 187
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 192-230 1.58e-04

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 42.40  E-value: 1.58e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 515624707 192 VWLGTNVTVKGGVTIGEGAVIAAGSVVIKNVPP--FAIAAG 230
Cdd:PRK14356 405 AFIGSNTALVAPVTIGDGALVGAGSVITKDVPDgsLAIARG 445
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 95-159 1.94e-04

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 39.15  E-value: 1.94e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 515624707  95 QISIGDNCRISGHTTFSGCSQPLDSFKPpllSIGNNVDIGWQSTIavGKRVIISDNVRIAGGAFL 159
Cdd:cd00208   18 PVVIGDNVNIGPGAVIGAATGPNEKNPT---IIGDNVEIGANAVI--HGGVKIGDNAVIGAGAVV 77
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 187-228 2.02e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 42.04  E-value: 2.02e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 515624707 187 ILERDVWLGTNVTVKGGVTIGEGAVIAAGSVVIKNVPPFAIA 228
Cdd:PRK14355 399 VIEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPPDSLA 440
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
185-214 3.40e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 36.93  E-value: 3.40e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 515624707  185 DIILERDVWLGTNVTVKGGVTIGEGAVIAA 214
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 204-250 3.93e-04

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 41.46  E-value: 3.93e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 515624707 204 VTIGEGAVIAAGSVVIKNVPPFAIA-AGNPARVV-GQVQsvkAAKPDTA 250
Cdd:PRK14352 418 VTVGDGAYTGAGTVIREDVPPGALAvSEGPQRNIeGWVQ---RKRPGTP 463
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 98-222 3.94e-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: 41.16  E-value: 3.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707  98 IGDNCRIsghttFSGCSqpldsfkppllsIGNNVDIGWQSTIA----------VGKRVIISDNVRIagGAFLFGYSGHPl 167
Cdd:COG1044  129 IGDGVVI-----GPGVV------------IGDGVVIGDDCVLHpnvtiyercvIGDRVIIHSGAVI--GADGFGFAPDE- 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 168 dakrraDGEGDDPQQISDIILERDVWLGTNVTV-----------KG-----------GVTIGEGAVIA-----AGSVVI- 219
Cdd:COG1044  189 ------DGGWVKIPQLGRVVIGDDVEIGANTTIdrgalgdtvigDGtkidnlvqiahNVRIGEHTAIAaqvgiAGSTKIg 262


                 ...
gi 515624707 220 KNV 222
Cdd:COG1044  263 DNV 265
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 126-218 4.24e-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: 4.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 126 SIGNNVDIGWQSTIavGKRVIISDNVRIAGGAFLfgysghpldakrradgeGDDpqqisdIILERDVWLGTNVTVKGGVT 205
Cdd:COG1044  110 KIGEGVSIGPFAVI--GAGVVIGDGVVIGPGVVI-----------------GDG------VVIGDDCVLHPNVTIYERCV 164

                         90
                 ....*....|...
gi 515624707 206 IGEGAVIAAGSVV 218
Cdd:COG1044  165 IGDRVIIHSGAVI 177
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 98-239 4.33e-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: 39.66  E-value: 4.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707  98 IGDNCRISGHTTFSGcsqpldSFKPPLLSIGNNVDIGWQSTIAVGKRVIISDNVRIAGGAFLFGysghpldakrradgeg 177
Cdd:cd04745   21 IGKNCYIGPHASLRG------DFGRIVIRDGANVQDNCVIHGFPGQDTVLEENGHIGHGAILHG---------------- 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 515624707 178 ddpqqisdIILERDVWLGTNVTVKGGVTIGEGAVIAAGSVVIKN--VPPFAIAAGNPARVVGQV 239
Cdd:cd04745   79 --------CTIGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAGtvIPPRSLIAGSPAKVIREL 134
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 179-222 4.73e-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: 41.17  E-value: 4.73e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 515624707 179 DPQQI---SDIILERDVWLGTNVTVKGGVTIGEGAVIAAGSvVIKNV 222
Cdd:COG1207  257 DPATTyidGDVEIGRDVVIDPNVILEGKTVIGEGVVIGPNC-TLKDS 302
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 98-222 1.10e-03

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 40.01  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707  98 IGDNCRISGHTTFSG------CS-QPLDSFKP--PLLS---IGNNVDIGwQSTIAVGKRV---------IISDNVRIAGG 156
Cdd:PRK09451 303 IGDDCEISPYSVVEDanlgaaCTiGPFARLRPgaELAEgahVGNFVEMK-KARLGKGSKAghltylgdaEIGDNVNIGAG 381

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 515624707 157 AFLFGYsghpldakrraDGEGDDPQQISDiilerDVWLGTNVTVKGGVTIGEGAVIAAGSVVIKNV 222
Cdd:PRK09451 382 TITCNY-----------DGANKFKTIIGD-----DVFVGSDTQLVAPVTVGKGATIGAGTTVTRDV 431
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 127-234 1.28e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 39.35  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 127 IGNNVDIGWQSTI---AVGKRVI-----------ISDNVRI------AGGAflfGYSGhpldakrradgegddpqqiSDI 186
Cdd:PRK00892 206 IGDDVEIGANTTIdrgALDDTVIgegvkidnlvqIAHNVVIgrhtaiAAQV---GIAG-------------------STK 263

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 515624707 187 IlERDVWLGTNVTVKGGVTIGEGAVIAAGSVVIKNVPPF-AIAAGNPAR 234
Cdd:PRK00892 264 I-GRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEPgEYSSGIPAQ 311
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 192-239 1.46e-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: 38.32  E-value: 1.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 515624707 192 VWLGTNVTVKGGVTIGEGAVIAAGSVVIKN--VPPFAIAAGNPARVVGQV 239
Cdd:cd04650   85 VIVGMGAILLNGAKIGDHVIIGAGAVVTPGkeIPDYSLVLGVPAKVVRKL 134
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 138-239 3.47e-03

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: 37.19  E-value: 3.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 138 TIAVGKRVIISDNVRIAGgaflfgysghPLdaKRRADGEGDDPQQISD--IILERDV----WLGTNVTVKGGVTIGEGAV 211
Cdd:cd03359   42 TVSIGRYCILSEGCVIRP----------PF--KKFSKGVAFFPLHIGDyvFIGENCVvnaaQIGSYVHIGKNCVIGRRCI 109

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 515624707 212 IAAGSVVIKN--------VPPFAIAAGNPARVVGQV 239
Cdd:cd03359  110 IKDCVKILDGtvvppdtvIPPYSVVSGRPARFIGEL 145
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 182-233 3.48e-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: 38.58  E-value: 3.48e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 515624707  182 QISDIILERDVWLGTNVTVKGGVTIGEGAVIAAGSVVIK--NVPPFAIAAGNPA 233
Cdd:TIGR02353 642 KSDTVTIGDGATLGPGAIVLYGVVMGEGSVLGPDSLVMKgeEVPAHTRWRGNPA 695
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
186-218 4.01e-03

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 33.95  E-value: 4.01e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 515624707  186 IILERDVWLGTNVTVkgGVTIGEGAVIAAGSVV 218
Cdd:pfam14602   1 VIIGDNCLIGANSGI--GVSLGDNCVVGAGVVI 31
Acetyltransf_11 pfam13720
Udp N-acetylglucosamine O-acyltransferase; Domain 2; This is domain 2, or the C-terminal ...
 222-237 6.87e-03

Udp N-acetylglucosamine O-acyltransferase; Domain 2; This is domain 2, or the C-terminal domain, of Udp N-acetylglucosamine O-acyltransferase. This enzyme is a zinc-dependent enzyme that catalyzes the deacetylation of UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine to form UDP-3-O-(R-hydroxymyristoyl)glucosamine and acetate.


Pssm-ID: 463967 [Multi-domain]  Cd Length: 82  Bit Score: 34.74  E-value: 6.87e-03
                          10
                  ....*....|....*.
gi 515624707  222 VPPFAIAAGNPARVVG 237
Cdd:pfam13720   2 VPPYVLAAGNPARLRG 17
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 185-256 7.75e-03

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 37.15  E-value: 7.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515624707 185 DIILERDVWLGTNVTVKGGVTIGEGAVIAA-----GSVVIKN--VPPFA-------IAAGnpARvVGQVQSVKAAKPDT- 249
Cdd:PRK14353 268 DTVIGRDVVIEPNVVFGPGVTVASGAVIHAfshleGAHVGEGaeVGPYArlrpgaeLGEG--AK-VGNFVEVKNAKLGEg 344


                 ....*..
gi 515624707 250 AKSfeNH 256
Cdd:PRK14353 345 AKV--NH 349
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 188-222 8.33e-03

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: 36.92  E-value: 8.33e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 515624707 188 LERDVWLGTNVTVKGGVTIGEGAVIAAGSVVIKNV 222
Cdd:COG1044  111 IGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGV 145
 
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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