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Conserved domains on  [gi|502860062|ref|WP_013095038|]
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acyltransferase [Enterobacter cloacae]

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 ...
 30-148 3.15e-43

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: 138.79  E-value: 3.15e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  30 LGNGVFIGPFVEIQGNTRIGDESKIQSHTFICEYVTLGERCFIGHGVMFANDMFRdGKPNTDRNSWGRITVGNDVSIGSG 109
Cdd:cd03358    1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYP-RSKIYRKWELKGTTVKRGASIGAN 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 502860062 110 ATILA-VSICDGVVIGAGSVVTKSITEKGVYAGNPARLLR 148
Cdd:cd03358   80 ATILPgVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 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 ...
 30-148 3.15e-43

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: 138.79  E-value: 3.15e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  30 LGNGVFIGPFVEIQGNTRIGDESKIQSHTFICEYVTLGERCFIGHGVMFANDMFRdGKPNTDRNSWGRITVGNDVSIGSG 109
Cdd:cd03358    1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYP-RSKIYRKWELKGTTVKRGASIGAN 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 502860062 110 ATILA-VSICDGVVIGAGSVVTKSITEKGVYAGNPARLLR 148
Cdd:cd03358   80 ATILPgVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
25-150 3.25e-36

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 121.52  E-value: 3.25e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  25 LYDCVLGNGVFIGPFVEIQG-NTRIGDESKIQSHTFI--CEYVTLGERCFIGHGVMFANDMFRDGKPNTDRNSWGRITVG 101
Cdd:COG0110    6 LFGARIGDGVVIGPGVRIYGgNITIGDNVYIGPGVTIddPGGITIGDNVLIGPGVTILTGNHPIDDPATFPLRTGPVTIG 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 502860062 102 NDVSIGSGATILA-VSICDGVVIGAGSVVTKSITEKGVYAGNPARLLRRL 150
Cdd:COG0110   86 DDVWIGAGATILPgVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKR 135
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 27-144 1.40e-21

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: 85.62  E-value: 1.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062   27 DCVLGNGVFIGPFVEIQGNTRIGDeskiqsHTFICEYVTLGERCFIGHGVMFAndmfrdgkPNTDRNswGRITVGNDVSI 106
Cdd:TIGR03570  99 SASIGEGTVIMAGAVINPDVRIGD------NVIINTGAIVEHDCVIGDFVHIA--------PGVTLS--GGVVIGEGVFI 162

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 502860062  107 GSGATIL-AVSICDGVVIGAGSVVTKSITEKGVYAGNPA 144
Cdd:TIGR03570 163 GAGATIIqGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 27-148 2.50e-16

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 74.02  E-value: 2.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  27 DCVLGNGVFIGPFVEIQGNTRIGDESKIQSHTFICEYVTLGERCFIGHGVMFANDmFRDGK-----PN-----------T 90
Cdd:PRK00892 112 SAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHA-VRIGNrviihSGavigsdgfgfaN 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  91 DRNSW------GRITVGNDVSIGSGATI---------------------------------------LA----------- 114
Cdd:PRK00892 191 DRGGWvkipqlGRVIIGDDVEIGANTTIdrgalddtvigegvkidnlvqiahnvvigrhtaiaaqvgIAgstkigrycmi 270

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 502860062 115 ---------VSICDGVVIGAGSVVTKSITEKGVY-AGNPARLLR 148
Cdd:PRK00892 271 ggqvgiaghLEIGDGVTITAMSGVTKSIPEPGEYsSGIPAQPNK 314
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
27-56 6.14e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.39  E-value: 6.14e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 502860062   27 DCVLGNGVFIGPFVEIQGNTRIGDESKIQS 56
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
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 ...
 30-148 3.15e-43

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: 138.79  E-value: 3.15e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  30 LGNGVFIGPFVEIQGNTRIGDESKIQSHTFICEYVTLGERCFIGHGVMFANDMFRdGKPNTDRNSWGRITVGNDVSIGSG 109
Cdd:cd03358    1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYP-RSKIYRKWELKGTTVKRGASIGAN 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 502860062 110 ATILA-VSICDGVVIGAGSVVTKSITEKGVYAGNPARLLR 148
Cdd:cd03358   80 ATILPgVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
25-150 3.25e-36

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 121.52  E-value: 3.25e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  25 LYDCVLGNGVFIGPFVEIQG-NTRIGDESKIQSHTFI--CEYVTLGERCFIGHGVMFANDMFRDGKPNTDRNSWGRITVG 101
Cdd:COG0110    6 LFGARIGDGVVIGPGVRIYGgNITIGDNVYIGPGVTIddPGGITIGDNVLIGPGVTILTGNHPIDDPATFPLRTGPVTIG 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 502860062 102 NDVSIGSGATILA-VSICDGVVIGAGSVVTKSITEKGVYAGNPARLLRRL 150
Cdd:COG0110   86 DDVWIGAGATILPgVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKR 135
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 45-147 1.13e-23

Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 88.67  E-value: 1.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  45 NTRIGDESKIQSHTFIC--EYVTLGERCFIGHGVMFAN---DMFRDGKPNTDRNSWGRITVGNDVSIGSGATILA-VSIC 118
Cdd:cd04647    1 NISIGDNVYIGPGCVISagGGITIGDNVLIGPNVTIYDhnhDIDDPERPIEQGVTSAPIVIGDDVWIGANVVILPgVTIG 80

                         90       100
                 ....*....|....*....|....*....
gi 502860062 119 DGVVIGAGSVVTKSITEKGVYAGNPARLL 147
Cdd:cd04647   81 DGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 30-147 6.47e-22

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: 85.94  E-value: 6.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  30 LGNGVFIGP--FVEIQGNTRIGDeskiqsHTFI--------CEYVTLGERCFIGHGVMFA-----------NDMFRDGKP 88
Cdd:cd03357   45 VGENVYIEPpfHCDYGYNIHIGD------NFYAnfnctildVAPVTIGDNVLIGPNVQIYtaghpldpeerNRGLEYAKP 118

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  89 ntdrnswgrITVGNDVSIGSGATILA-VSICDGVVIGAGSVVTKSITEKGVYAGNPARLL 147
Cdd:cd03357  119 ---------ITIGDNVWIGGGVIILPgVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 27-144 1.40e-21

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: 85.62  E-value: 1.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062   27 DCVLGNGVFIGPFVEIQGNTRIGDeskiqsHTFICEYVTLGERCFIGHGVMFAndmfrdgkPNTDRNswGRITVGNDVSI 106
Cdd:TIGR03570  99 SASIGEGTVIMAGAVINPDVRIGD------NVIINTGAIVEHDCVIGDFVHIA--------PGVTLS--GGVVIGEGVFI 162

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 502860062  107 GSGATIL-AVSICDGVVIGAGSVVTKSITEKGVYAGNPA 144
Cdd:TIGR03570 163 GAGATIIqGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 10-150 4.81e-20

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: 83.91  E-value: 4.81e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  10 NVTCGENVTLYEpcnlyDCVLGNGVFIGPFVEIQGNTRIGDESKIQSHTFICEYVTLGERCFIGHGVM-------FANDm 82
Cdd:COG1044  114 GVSIGPFAVIGA-----GVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVIGDRVIIHSGAVigadgfgFAPD- 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  83 fRDGKpntdrnsW------GRITVGNDVSIGSGATI-------------------------------------------- 112
Cdd:COG1044  188 -EDGG-------WvkipqlGRVVIGDDVEIGANTTIdrgalgdtvigdgtkidnlvqiahnvrigehtaiaaqvgiagst 259

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502860062 113 -------LA--------VSICDGVVIGAGSVVTKSITEKGVYAGNPAR----------LLRRL 150
Cdd:COG1044  260 kigdnvvIGgqvgiaghLTIGDGVIIGAQSGVTKSIPEGGVYSGSPAQphrewlrnaaALRRL 322
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 45-148 6.64e-20

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: 79.90  E-value: 6.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  45 NTRIGDESKIQSHTFIC--EYVTLGERCFIGHGV---MFAN------------DMFRDGKPNTDRNSW---GRITVGNDV 104
Cdd:cd03349    1 NISVGDYSYGSGPDCDVggDKLSIGKFCSIAPGVkigLGGNhptdwvstypfyIFGGEWEDDAKFDDWpskGDVIIGNDV 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 502860062 105 SIGSGATILA-VSICDGVVIGAGSVVTKSITEKGVYAGNPARLLR 148
Cdd:cd03349   81 WIGHGATILPgVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIR 125
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 27-143 1.58e-19

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: 80.22  E-value: 1.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  27 DCVLGNGVFIGPFVEIQGNTRIGDeskiqsHTFICEYVTLGERCFIGHGVMFAndmfrdgkPNTDRNswGRITVGNDVSI 106
Cdd:cd03360   96 SAVIGEGCVIMAGAVINPDARIGD------NVIINTGAVIGHDCVIGDFVHIA--------PGVVLS--GGVTIGEGAFI 159

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 502860062 107 GSGATIL-AVSICDGVVIGAGSVVTKSITEKGVYAGNP 143
Cdd:cd03360  160 GAGATIIqGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 27-150 5.72e-17

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 73.14  E-value: 5.72e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  27 DCVLGNGVFIGPFVEIQGNT---RIGDESKIQS----HTFICEYVTLGERCFIGHGVMfandmfrdgkpntdrnswgrI- 98
Cdd:COG0663   28 DVTIGEDVSVWPGAVLRGDVgpiRIGEGSNIQDgvvlHVDPGYPLTIGDDVTIGHGAI--------------------Lh 87

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 502860062  99 --TVGNDVSIGSGATIL--AVsICDGVVIGAGSVVT--KSITEKGVYAGNPARLLRRL 150
Cdd:COG0663   88 gcTIGDNVLIGMGAIVLdgAV-IGDGSIVGAGALVTegKVVPPGSLVVGSPAKVVREL 144
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 9-131 2.04e-16

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: 74.68  E-value: 2.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062   9 RNVTCGENVTLYEpCNLYDCVLGNGVFIGP------------------FVEIQgNTRIGDESKIQSHTficeYV---TLG 67
Cdd:COG1207  300 KDSTIGDGVVIKY-SVIEDAVVGAGATVGPfarlrpgtvlgegvkignFVEVK-NSTIGEGSKVNHLS----YIgdaEIG 373

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502860062  68 ERCFIGHGVMFANdmfRDGKpntdrNSWgRITVGNDVSIGSGATILA-VSICDGVVIGAGSVVTK 131
Cdd:COG1207  374 EGVNIGAGTITCN---YDGV-----NKH-RTVIGDGAFIGSNTNLVApVTIGDGATIGAGSTITK 429
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 27-148 2.50e-16

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 74.02  E-value: 2.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  27 DCVLGNGVFIGPFVEIQGNTRIGDESKIQSHTFICEYVTLGERCFIGHGVMFANDmFRDGK-----PN-----------T 90
Cdd:PRK00892 112 SAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHA-VRIGNrviihSGavigsdgfgfaN 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  91 DRNSW------GRITVGNDVSIGSGATI---------------------------------------LA----------- 114
Cdd:PRK00892 191 DRGGWvkipqlGRVIIGDDVEIGANTTIdrgalddtvigegvkidnlvqiahnvvigrhtaiaaqvgIAgstkigrycmi 270

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 502860062 115 ---------VSICDGVVIGAGSVVTKSITEKGVY-AGNPARLLR 148
Cdd:PRK00892 271 ggqvgiaghLEIGDGVTITAMSGVTKSIPEPGEYsSGIPAQPNK 314
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 9-136 9.84e-16

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: 70.14  E-value: 9.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062   9 RNVTCGENVTLYEPCNLYDCVLGNGVFIGP------------------FVEIQgNTRIGDESKIQSHTFICEyVTLGERC 70
Cdd:cd03353   49 KDSTIGDGVVIKASSVIEGAVIGNGATVGPfahlrpgtvlgegvhignFVEIK-KSTIGEGSKANHLSYLGD-AEIGEGV 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502860062  71 FIGHGVMFANdmfRDGKpntdrNSWgRITVGNDVSIGSGATILA-VSICDGVVIGAGSVVTKSITEK 136
Cdd:cd03353  127 NIGAGTITCN---YDGV-----NKH-RTVIGDNVFIGSNSQLVApVTIGDGATIAAGSTITKDVPPG 184
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 27-135 1.30e-15

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 72.56  E-value: 1.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  27 DCVLGNGVFIGPFVEIQGNTrIGDESKIqSH-TFICEyVTLGERCFIGHGVMFANdmfRDGKpntdrNSWgRITVGNDVS 105
Cdd:PRK14354 334 GSVIGEEVKIGNFVEIKKST-IGEGTKV-SHlTYIGD-AEVGENVNIGCGTITVN---YDGK-----NKF-KTIIGDNAF 401

                         90       100       110
                 ....*....|....*....|....*....|.
gi 502860062 106 IGSGATILA-VSICDGVVIGAGSVVTKSITE 135
Cdd:PRK14354 402 IGCNSNLVApVTVGDNAYIAAGSTITKDVPE 432
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 31-149 1.63e-15

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: 69.34  E-value: 1.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  31 GNGVFIGPFVEIqgntriGDESKIqshtficeY--VTLGERcfighgvmfandmfrdGKPNTDRnswgRITVGNDVSIGS 108
Cdd:COG1045   83 GTGVVIGETAVI------GDNVTI--------YqgVTLGGT----------------GKEKGKR----HPTIGDNVVIGA 128

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 502860062 109 GATIL-AVSICDGVVIGAGSVVTKSITEKGVYAGNPARLLRR 149
Cdd:COG1045  129 GAKILgPITIGDNAKIGANSVVLKDVPPGSTVVGVPARIVKR 170
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 9-149 5.36e-15

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: 68.59  E-value: 5.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062   9 RNVTCGENVTLYEPCNLYD-------CVLGN-------------------GVFIGPFVEIQ----------GNTRIGDES 52
Cdd:cd03352   42 DDCVIHPNVTIYEGCIIGDrviihsgAVIGSdgfgfapdgggwvkipqlgGVIIGDDVEIGanttidrgalGDTVIGDGT 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  53 KIQSHTFICEYVTLGERCFIGHGVMFAndmfrdgkpntdrnswGRITVGNDVSIGSGATILA-VSICDGVVIGAGSVVTK 131
Cdd:cd03352  122 KIDNLVQIAHNVRIGENCLIAAQVGIA----------------GSTTIGDNVIIGGQVGIAGhLTIGDGVVIGAGSGVTS 185

                        170
                 ....*....|....*...
gi 502860062 132 SITEKGVYAGNPARLLRR 149
Cdd:cd03352  186 IVPPGEYVSGTPAQPHRE 203
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 40-143 1.32e-14

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


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 65.15  E-value: 1.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  40 VEIQGNTRIGDESKIQSHTFIC--EYVTLGERCFIGHGVMFANDMFRDGKpntdrnswGRITVGNDVSIGSGATIL-AVS 116
Cdd:cd03354    3 IDIHPGAKIGPGLFIDHGTGIVigETAVIGDNCTIYQGVTLGGKGKGGGK--------RHPTIGDNVVIGAGAKILgNIT 74

                         90       100
                 ....*....|....*....|....*..
gi 502860062 117 ICDGVVIGAGSVVTKSITEKGVYAGNP 143
Cdd:cd03354   75 IGDNVKIGANAVVTKDVPANSTVVGVP 101
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 45-147 1.76e-11

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: 57.23  E-value: 1.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  45 NTRIGDESKIQSHTFI--CEYVTLGERCFIGHGVM-------FANDMFR-DGKPntdrnswgrITVGNDVSIGSGATIL- 113
Cdd:cd05825    3 NLTIGDNSWIGEGVWIynLAPVTIGSDACISQGAYlctgshdYRSPAFPlITAP---------IVIGDGAWVAAEAFVGp 73

                         90       100       110
                 ....*....|....*....|....*....|....
gi 502860062 114 AVSICDGVVIGAGSVVTKSITEKGVYAGNPARLL 147
Cdd:cd05825   74 GVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 34-148 2.18e-11

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 58.73  E-value: 2.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  34 VFIGPFVEIQGNTRIGDESKIQShtfiCEYVTLGERCFIGHGVMFANDMFRDGKPNTDRNS-------WG----RITVGN 102
Cdd:PRK09677  60 AFGRGKLFFGDNVQVNDYVHIAC----IESITIGRDTLIASKVFITDHNHGSFKHSDDFSSpnlppdmRTlessAVVIGQ 135

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 502860062 103 DVSIGSGATIL-AVSICDGVVIGAGSVVTKSITEKGVYAGNPARLLR 148
Cdd:PRK09677 136 RVWIGENVTILpGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIK 182
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 10-135 1.11e-10

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 58.11  E-value: 1.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  10 NVTCGENVTLYEPCNLYDCVLGNGVFIGP-----------------------------------FVEIQgNTRIGDESKI 54
Cdd:PRK09451 283 NVTLGNRVKIGAGCVLKNCVIGDDCEISPysvvedanlgaactigpfarlrpgaelaegahvgnFVEMK-KARLGKGSKA 361

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  55 QSHTFICEyVTLGERCFIGHGVMFANdmfRDGKpntdrNSWGRItVGNDVSIGSGATILA-VSICDGVVIGAGSVVTKSI 133
Cdd:PRK09451 362 GHLTYLGD-AEIGDNVNIGAGTITCN---YDGA-----NKFKTI-IGDDVFVGSDTQLVApVTVGKGATIGAGTTVTRDV 431


                 ..
gi 502860062 134 TE 135
Cdd:PRK09451 432 AE 433
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 60-150 1.20e-10

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 56.75  E-value: 1.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  60 ICEyVTLGERCFIGHGVmfanDMFRDGKP--NTDRNSwGR-----ITVGNDVSIGSGATI-LAVSICDGVVIGAGSVVTK 131
Cdd:PRK10092  91 VCP-IRIGDNCMLAPGV----HIYTATHPldPVARNS-GAelgkpVTIGNNVWIGGRAVInPGVTIGDNVVVASGAVVTK 164

                         90
                 ....*....|....*....
gi 502860062 132 SITEKGVYAGNPARLLRRL 150
Cdd:PRK10092 165 DVPDNVVVGGNPARIIKKL 183
PRK10502 PRK10502
putative acyl transferase; Provisional
 31-148 2.49e-10

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 55.73  E-value: 2.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  31 GNGVFIGP--------FVEIQGNTRIGDESKIQShtfiCEYVTLGERCFIGHGVMFANDMFRDGKPNTDRNSwGRITVGN 102
Cdd:PRK10502  55 GKGVVIRPsvritypwKLTIGDYAWIGDDVWLYN----LGEITIGAHCVISQKSYLCTGSHDYSDPHFDLNT-APIVIGE 129

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 502860062 103 DVSIGSGATI-LAVSICDGVVIGAGSVVTKSITEKGVYAGNPARLLR 148
Cdd:PRK10502 130 GCWLAADVFVaPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIR 176
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 12-150 2.70e-10

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 56.17  E-value: 2.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  12 TCGENVTLYEPCNLydcVLGNGVFIGPFVEIQGNTRIGDE--SKIQSHTFICEYVTLGercFIGHGVMFANDMfrdgkpN 89
Cdd:PRK09527  57 TVGENAWVEPPVYF---SYGSNIHIGRNFYANFNLTIVDDytVTIGDNVLIAPNVTLS---VTGHPVHHELRK------N 124

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502860062  90 TDRNSWgRITVGNDVSIGSGATI-LAVSICDGVVIGAGSVVTKSITEKGVYAGNPARLLRRL 150
Cdd:PRK09527 125 GEMYSF-PITIGNNVWIGSHVVInPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIREI 185
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 29-133 8.15e-10

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 55.64  E-value: 8.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  29 VLGNGVFIGPFVEIQgNTRIGDESKIQSHTFICEyVTLGERCFIGHGVMFANdmfRDG--KpntdrnswGRITVGNDVSI 106
Cdd:PRK14353 323 ELGEGAKVGNFVEVK-NAKLGEGAKVNHLTYIGD-ATIGAGANIGAGTITCN---YDGfnK--------HRTEIGAGAFI 389

                         90       100
                 ....*....|....*....|....*...
gi 502860062 107 GSGATILA-VSICDGVVIGAGSVVTKSI 133
Cdd:PRK14353 390 GSNSALVApVTIGDGAYIASGSVITEDV 417
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 29-150 2.99e-09

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: 52.41  E-value: 2.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  29 VLGNGVFIGPFVEIQGNTRIGDESKIQSHTFI---CEYVTLGERCFIGHGVMFANDmfrDGKPntdrnswgrITVGNDVS 105
Cdd:cd04645    1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLrgdVNPIRIGERTNIQDGSVLHVD---PGYP---------TIIGDNVT 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502860062 106 IGSGATILAVSICDGVVIG------------------AGSVVT--KSITEKGVYAGNPARLLRRL 150
Cdd:cd04645   69 VGHGAVLHGCTIGDNCLIGmgaiildgavigkgsivaAGSLVPpgKVIPPGSLVAGSPAKVVREL 133
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 10-131 8.14e-09

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 53.01  E-value: 8.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  10 NVTCGENVT-LYEpcNLYDCVLGNGVFIGP------------------FVEIQgNTRIGDESKIQSHTFICEyVTLGERC 70
Cdd:PRK14360 297 NSQIGENVTvLYS--VVSDSQIGDGVKIGPyahlrpeaqigsncrignFVEIK-KSQLGEGSKVNHLSYIGD-ATLGEQV 372

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502860062  71 FIGHGVMFANdmfRDGKPNTdrnswgRITVGNDVSIGSGATILA-VSICDGVVIGAGSVVTK 131
Cdd:PRK14360 373 NIGAGTITAN---YDGVKKH------RTVIGDRSKTGANSVLVApITLGEDVTVAAGSTITK 425
PLN02694 PLN02694
serine O-acetyltransferase
 64-147 8.61e-09

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 52.72  E-value: 8.61e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  64 VTLGERCFIGHGVMFAN--DMFRDGKPNTDRNSwgriTVGNDVSIGSGATILA-VSICDGVVIGAGSVVTKSITEKGVYA 140
Cdd:PLN02694 181 VVIGETAVIGNNVSILHhvTLGGTGKACGDRHP----KIGDGVLIGAGATILGnVKIGEGAKIGAGSVVLIDVPPRTTAV 256


                 ....*..
gi 502860062 141 GNPARLL 147
Cdd:PLN02694 257 GNPARLV 263
PLN02739 PLN02739
serine acetyltransferase
 40-148 9.22e-09

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 52.73  E-value: 9.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  40 VEIQGNTRIGDESKIQSHT--FICEYVTLGERCFIGHGVMFANDmfrdGKPNTDRNSwgriTVGNDVSIGSGATILA-VS 116
Cdd:PLN02739 206 IDIHPAARIGKGILLDHGTgvVIGETAVIGDRVSILHGVTLGGT----GKETGDRHP----KIGDGALLGACVTILGnIS 277

                         90       100       110
                 ....*....|....*....|....*....|..
gi 502860062 117 ICDGVVIGAGSVVTKSITEKGVYAGNPARLLR 148
Cdd:PLN02739 278 IGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIG 309
PLN02357 PLN02357
serine acetyltransferase
 64-147 9.37e-09

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 52.58  E-value: 9.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  64 VTLGERCFIG------HGVMFANDmfrdGKPNTDRNSwgriTVGNDVSIGSGATILA-VSICDGVVIGAGSVVTKSITEK 136
Cdd:PLN02357 247 VVIGETAVVGnnvsilHNVTLGGT----GKQSGDRHP----KIGDGVLIGAGTCILGnITIGEGAKIGAGSVVLKDVPPR 318

                         90
                 ....*....|.
gi 502860062 137 GVYAGNPARLL 147
Cdd:PLN02357 319 TTAVGNPARLI 329
PLN02296 PLN02296
carbonate dehydratase
 10-150 9.74e-08

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 49.35  E-value: 9.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  10 NVTCGENVTLYepcnlYDCVLGNGVfigpfveiqGNTRIGDESKIQSHTFI----------CEYVTLGERCFIGHG-VMF 78
Cdd:PLN02296  70 DVQVGRGSSIW-----YGCVLRGDV---------NSISVGSGTNIQDNSLVhvaktnlsgkVLPTIIGDNVTIGHSaVLH 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  79 AndmfrdgkpntdrnswgrITVGNDVSIGSGATILavsicDGVVI------GAGSVVTKS--ITEKGVYAGNPARLLRRL 150
Cdd:PLN02296 136 G------------------CTVEDEAFVGMGATLL-----DGVVVekhamvAAGALVRQNtrIPSGEVWAGNPAKFLRKL 192
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 29-76 1.08e-07

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: 49.25  E-value: 1.08e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 502860062  29 VLGNGVFIGPFVEIQGNTRIGDESKIQSHTFICEYVTLGERCFIGHGV 76
Cdd:COG1043   15 KLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFA 62
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 28-136 1.21e-07

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 49.34  E-value: 1.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  28 CVLGNGVFIGPFVEIQgNTRIGDESKIQSHTFI--CEyvtLGERCFIGHGVMFANdmfRDGKpNTDRNswgriTVGNDVS 105
Cdd:PRK14356 340 AVLEEGARVGNFVEMK-KAVLGKGAKANHLTYLgdAE---IGAGANIGAGTITCN---YDGV-NKHRT-----VIGEGAF 406

                         90       100       110
                 ....*....|....*....|....*....|..
gi 502860062 106 IGSGATILA-VSICDGVVIGAGSVVTKSITEK 136
Cdd:PRK14356 407 IGSNTALVApVTIGDGALVGAGSVITKDVPDG 438
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 27-131 1.28e-07

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 49.55  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  27 DCVLGNGVFIGPFVEIQGNTRIGDESKIQshTFI---------------CEYV---TLGERCFIGHGVMFANdmfRDGkp 88
Cdd:PRK14352 322 ESEIGAGATVGPFTYLRPGTVLGEEGKLG--AFVetknatigrgtkvphLTYVgdaDIGEHSNIGASSVFVN---YDG-- 394

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 502860062  89 nTDRNswgRITVGNDVSIGSGATILA-VSICDGVVIGAGSVVTK 131
Cdd:PRK14352 395 -VNKH---RTTIGSHVRTGSDTMFVApVTVGDGAYTGAGTVIRE 434
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 29-135 1.82e-07

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 48.99  E-value: 1.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  29 VLGNGVFIGPFVEIQgNTRIGDESKIQSHTFICEyVTLGERCFIGHGVMFANdmfRDGKPNTdrnswgRITVGNDVSIGS 108
Cdd:PRK14357 326 VLKKSVKIGNFVEIK-KSTIGENTKAQHLTYLGD-ATVGKNVNIGAGTITCN---YDGKKKN------PTFIEDGAFIGS 394

                         90       100
                 ....*....|....*....|....*...
gi 502860062 109 GATILA-VSICDGVVIGAGSVVTKSITE 135
Cdd:PRK14357 395 NSSLVApVRIGKGALIGAGSVITEDVPP 422
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 29-75 2.13e-07

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: 48.58  E-value: 2.13e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 502860062  29 VLGNGVFIGPFVEIQGNTRIGDESKIQSHTFICEYVTLGERCFIGHG 75
Cdd:cd03351   13 KIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPF 59
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
29-76 2.38e-07

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 48.17  E-value: 2.38e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 502860062  29 VLGNGVFIGPFVEIQGNTRIGDESKIQSHTFICEYVTLGERCFIGHGV 76
Cdd:PRK05289  16 KIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFA 63
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 46-144 1.88e-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: 46.28  E-value: 1.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062   46 TRIGDESKIQSHTFIC-EYVTLGERCFIGHGVMFANDMFRDGKPNTdrnswGRITVGNDVSIGSGATILA-VSICDGVVI 123
Cdd:TIGR02353 113 AKIGKGVDIGSLPPVCtDLLTIGAGTIVRKEVMLLGYRAERGRLHT-----GPVTLGRDAFIGTRSTLDIdTSIGDGAQL 187

                          90       100
                  ....*....|....*....|...
gi 502860062  124 GAGSVVT--KSITEKGVYAGNPA 144
Cdd:TIGR02353 188 GHGSALQggQSIPDGERWHGSPA 210
cysE PRK11132
serine acetyltransferase; Provisional
 48-149 4.51e-06

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 44.69  E-value: 4.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  48 IGDESKIQSHTFICEYVTLGercfighGVmfandmfrdGKPNTDRNSwgRITVGndVSIGSGATILA-VSICDGVVIGAG 126
Cdd:PRK11132 164 IGETAVIENDVSILQSVTLG-------GT---------GKTSGDRHP--KIREG--VMIGAGAKILGnIEVGRGAKIGAG 223

                         90       100
                 ....*....|....*....|...
gi 502860062 127 SVVTKSITEKGVYAGNPARLLRR 149
Cdd:PRK11132 224 SVVLQPVPPHTTAAGVPARIVGK 246
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 28-129 4.88e-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: 43.73  E-value: 4.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  28 CVLGNGVFIGPFVEIQgNTRIGDESKIQSHTFICEYVtLGERCFIGHGVMFANDMF---------RDGKPNTDRNSWGRI 98
Cdd:cd05636   54 TVLGDGCVVGNSVEVK-NSIIMDGTKVPHLNYVGDSV-LGENVNLGAGTITANLRFddkpvkvrlKGERVDTGRRKLGAI 131

                         90       100       110
                 ....*....|....*....|....*....|.
gi 502860062  99 tVGNDVSIGSGATILAvsicdGVVIGAGSVV 129
Cdd:cd05636  132 -IGDGVKTGINVSLNP-----GVKIGPGSWV 156
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 27-149 9.78e-06

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: 43.47  E-value: 9.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  27 DCVLGNGVFIGPFVEIQGNTRIGDESKI----------Q--------------SHTFICEYVTL-------------GER 69
Cdd:COG1043   31 DVEIGDGTVIGSHVVIEGPTTIGKNNRIfpfasigeepQdlkykgeptrleigDNNTIREFVTIhrgtvqgggvtriGDD 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  70 CF------------IGHGVMFANdmfrdgkpntdrNSW--GRITVGNDVSIGSGATILA-VSICDGVVIGAGSVVTKSIT 134
Cdd:COG1043  111 NLlmayvhvahdcvVGNNVILAN------------NATlaGHVEVGDHAIIGGLSAVHQfVRIGAHAMVGGGSGVVKDVP 178

                        170       180
                 ....*....|....*....|..
gi 502860062 135 EKGVYAGNPARL-------LRR 149
Cdd:COG1043  179 PYVLAAGNPARLrglnlvgLKR 200
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 17-129 1.36e-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: 42.79  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  17 VTLYEPCNLY---DCVLGNGVFIGPFVEIQGNTRIGDEskiqshtficeyvtlgerCFIGHGVMFandmfrdgkpntdrn 93
Cdd:cd03353    2 VTLIDPETTYidgDVEIGVDVVIDPGVILEGKTVIGED------------------CVIGPNCVI--------------- 48

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 502860062  94 swgritvgNDVSIGSGATILAVSICDGVVIGAGSVV 129
Cdd:cd03353   49 --------KDSTIGDGVVIKASSVIEGAVIGNGATV 76
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 29-135 1.64e-05

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 43.43  E-value: 1.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  29 VLGNGVFIGPFVEIQgNTRIgDESKIQSHTFICEYVTLGERCFIGHGVMFANdmfRDGKpNTDRNswgriTVGNDVSIGS 108
Cdd:PRK14358 342 VLGEGVHIGNFVETK-NARL-DAGVKAGHLAYLGDVTIGAETNVGAGTIVAN---FDGV-NKHQS-----KVGAGVFIGS 410

                         90       100
                 ....*....|....*....|....*...
gi 502860062 109 GATILAVSIC-DGVVIGAGSVVTKSITE 135
Cdd:PRK14358 411 NTTLIAPRVVgDAAFIAAGSAVHDDVPE 438
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 34-130 1.96e-05

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 40.70  E-value: 1.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  34 VFIGPFVEIQGNTRIGDESKIqshtficeyvtlGERCFIGHGVMFANDMFRDGKpntdrnswGRITVGNDVSIGSGATIL 113
Cdd:cd00208    1 VFIGEGVKIHPKAVIRGPVVI------------GDNVNIGPGAVIGAATGPNEK--------NPTIIGDNVEIGANAVIH 60

                         90
                 ....*....|....*...
gi 502860062 114 A-VSICDGVVIGAGSVVT 130
Cdd:cd00208   61 GgVKIGDNAVIGAGAVVT 78
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 58-146 2.60e-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: 42.02  E-value: 2.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  58 TFICEYVTLGERCFIGHGVMFAndmfrdgkpntdrnswGRITVGNDVSIGSGATILAVSICDGVVIGAGSVVTKSITEKG 137
Cdd:cd03353   10 TYIDGDVEIGVDVVIDPGVILE----------------GKTVIGEDCVIGPNCVIKDSTIGDGVVIKASSVIEGAVIGNG 73


                 ....*....
gi 502860062 138 VYAGNPARL 146
Cdd:cd03353   74 ATVGPFAHL 82
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 27-150 3.13e-05

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: 41.58  E-value: 3.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  27 DCVLGNGVFIGPFVEIQGN---TRIGDESKIQS----HTFICEYVTLGERCFIGHGVMFANdmfrdgkpntdrnswgrIT 99
Cdd:cd04745   18 DVIIGKNCYIGPHASLRGDfgrIVIRDGANVQDncviHGFPGQDTVLEENGHIGHGAILHG-----------------CT 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 502860062 100 VGNDVSIGSGATILavsicDGVVIGAGSVVTKSITEKGVY--------AGNPARLLRRL 150
Cdd:cd04745   81 IGRNALVGMNAVVM-----DGAVIGEESIVGAMAFVKAGTvipprsliAGSPAKVIREL 134
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 27-149 4.00e-05

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


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 42.03  E-value: 4.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  27 DCVLGNGVFIGPFVEIQGNTRIGDESKIQSH------------------------TFICEYVTL-------------GER 69
Cdd:cd03351   29 NVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFasigeapqdlkykgeptrleigdnNTIREFVTIhrgtaqgggvtriGNN 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  70 CF------------IGHGVMFANdmfrdgkpntdrNSW--GRITVGNDVSIGSGATILA-VSICDGVVIGAGSVVTKSIT 134
Cdd:cd03351  109 NLlmayvhvahdcvIGNNVILAN------------NATlaGHVEIGDYAIIGGLSAVHQfCRIGRHAMVGGGSGVVQDVP 176

                        170       180
                 ....*....|....*....|..
gi 502860062 135 EKGVYAGNPARL-------LRR 149
Cdd:cd03351  177 PYVIAAGNRARLrglnlvgLKR 198
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 15-114 5.05e-05

Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix (LbH) domain: Proteins in this family show simlarity to glucose-1-phosphate adenylyltransferases in that they contain N-terminal catalytic domains that resemble a dinucleotide-binding Rossmann fold and C-terminal LbH fold domains. Members in this family are predicted to be glucose-1-phosphate thymidylyltransferases, which are involved in the dTDP-L-rhamnose biosynthetic pathway. Glucose-1-phosphate thymidylyltransferase catalyzes the synthesis of deoxy-thymidine di-phosphate (dTDP)-L-rhamnose, an important component of the cell wall of many microorganisms. The C-terminal LbH domain contains multiple turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 41.03  E-value: 5.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  15 ENVTLYEPCnlydcVLGNGVFIGPFVEIQGNTRIGDESKIQSHTFICEYVTLGERCFIGHGVMFANDMFRDGKPNTDRNS 94
Cdd:cd05636   10 EGVTIKGPV-----WIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSIIMDGTKVPHLNY 84

                         90       100
                 ....*....|....*....|
gi 502860062  95 WGRITVGNDVSIGSGaTILA 114
Cdd:cd05636   85 VGDSVLGENVNLGAG-TITA 103
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 27-129 7.69e-05

Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three distinct groups of carbonic anhydrases - alpha, beta and gamma - which show no significant sequence identity or structural similarity. Gamma CAs are homotrimeric enzymes, with each subunit containing a left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 40.69  E-value: 7.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  27 DCVLGNGVFIGPFVEIQGNT----RIGDESKIQS----HTFICEYVTLGERCFIGHGVMFAndmfrdgkpntdrnswGRI 98
Cdd:cd00710   20 DVIIGDNVFVGPGASIRADEgtpiIIGANVNIQDgvviHALEGYSVWIGKNVSIAHGAIVH----------------GPA 83

                         90       100       110
                 ....*....|....*....|....*....|.
gi 502860062  99 TVGNDVSIGSGATILAVSICDGVVIGAGSVV 129
Cdd:cd00710   84 YIGDNCFIGFRSVVFNAKVGDNCVIGHNAVV 114
PRK10191 PRK10191
putative acyl transferase; Provisional
 41-146 8.97e-05

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 40.26  E-value: 8.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  41 EIQGNTRIGDESKIQsHTF---ICEYVTLGERCFIGHGVMFANdmfrdgkpnTDRNSWGRITVGNDVSIGSGATILA-VS 116
Cdd:PRK10191  43 EIQAAATIGRRFTIH-HGYavvINKNVVAGDDFTIRHGVTIGN---------RGADNMACPHIGNGVELGANVIILGdIT 112

                         90       100       110
                 ....*....|....*....|....*....|
gi 502860062 117 ICDGVVIGAGSVVTKSITEKGVYAGNPARL 146
Cdd:PRK10191 113 IGNNVTVGAGSVVLDSVPDNALVVGEKARV 142
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 36-140 1.04e-04

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 41.13  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  36 IGPFVEIQGNTRIGDESKIQSHTFICEyvtLGERCFIGHGVMFANdmfRDGKPNTdrnswgRITVGNDVSIGSGATILA- 114
Cdd:PRK14359 318 IGNFVETKNAKLNGVKAGHLSYLGDCE---IDEGTNIGAGTITCN---YDGKKKH------KTIIGKNVFIGSDTQLVAp 385

                         90       100
                 ....*....|....*....|....*.
gi 502860062 115 VSICDGVVIGAGSVVTKSItEKGVYA 140
Cdd:PRK14359 386 VNIEDNVLIAAGSTVTKDV-PKGSLA 410
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
27-149 2.46e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 39.70  E-value: 2.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  27 DCVLGNGVFIGPFVEIQGNTRIGDESKIQSH------------------------TFICEYVTL-------------GER 69
Cdd:PRK05289  32 NVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFasigedpqdlkykgeptrlvigdnNTIREFVTInrgtvqgggvtriGDN 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502860062  70 CF------------IGHGVMFANdmfrdgkpntdrNSW--GRITVGNDVSIGSGATILA-VSICDGVVIGAGSVVTKSIT 134
Cdd:PRK05289 112 NLlmayvhvahdcvVGNHVILAN------------NATlaGHVEVGDYAIIGGLTAVHQfVRIGAHAMVGGMSGVSQDVP 179

                        170       180
                 ....*....|....*....|..
gi 502860062 135 EKGVYAGNPARL-------LRR 149
Cdd:PRK05289 180 PYVLAEGNPARLrglnlvgLKR 201
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
27-56 6.14e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.39  E-value: 6.14e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 502860062   27 DCVLGNGVFIGPFVEIQGNTRIGDESKIQS 56
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 98-138 6.81e-04

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 38.81  E-value: 6.81e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 502860062  98 ITVGNDVSIGSGATILAVS-ICDGVVIGAGSVVTKSITEKGV 138
Cdd:PRK14358 271 VTLGRDVTIEPGVLLRGQTrVADGVTIGAYSVVTDSVLHEGA 312
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 30-72 1.00e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 37.69  E-value: 1.00e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 502860062  30 LGNGVFIGPFVEIQGNTRIGDESKIQSHTFICEYVTLGERCFI 72
Cdd:PRK12461  14 LGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKI 56
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 9-60 2.06e-03

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: 35.49  E-value: 2.06e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 502860062   9 RNVTCGENVTL---YEPCNLYDCVLGNGVFIGPFVEIQGNTRIGDESKIQSHTFI 60
Cdd:cd03354   33 DNCTIYQGVTLggkGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVKIGANAVV 87
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 99-129 2.28e-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: 2.28e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 502860062  99 TVGNDVSIGSGATILA-VSICDGVVIGAGSVV 129
Cdd:COG1044  110 KIGEGVSIGPFAVIGAgVVIGDGVVIGPGVVI 141
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 96-146 5.89e-03

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 35.77  E-value: 5.89e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 502860062  96 GRITVGNDVSIGSGATILAVSICDGVVIgAGSVVTKSITEKGVYAGNPARL 146
Cdd:COG1207  283 GKTVIGEGVVIGPNCTLKDSTIGDGVVI-KYSVIEDAVVGAGATVGPFARL 332
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 64-128 6.57e-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: 35.76  E-value: 6.57e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502860062  64 VTLGERCFIGHGVmfandmfrdgkpntdrnswgriTVGNDVSIGSGATILA-VSICDGVVIGAGSV 128
Cdd:COG1044  109 AKIGEGVSIGPFA----------------------VIGAGVVIGDGVVIGPgVVIGDGVVIGDDCV 152
 
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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