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Conserved domains on  [gi|527036111|ref|WP_020882853|]
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MULTISPECIES: acyltransferase [Enterobacter]

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 ...
 31-149 8.12e-42

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: 135.32  E-value: 8.12e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  31 LGDNVFIGPFVEIQANSHIGADSKIQSHTFICEYVTVGERCFIGHGVMFANDMFRdGKPNADRRSWGHIRVGNDVSIGSG 110
Cdd:cd03358    1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYP-RSKIYRKWELKGTTVKRGASIGAN 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 527036111 111 ATILA-VSICDGAVIGAGSVVTKSITEKGVYAGNPARLLR 149
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 ...
 31-149 8.12e-42

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: 135.32  E-value: 8.12e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  31 LGDNVFIGPFVEIQANSHIGADSKIQSHTFICEYVTVGERCFIGHGVMFANDMFRdGKPNADRRSWGHIRVGNDVSIGSG 110
Cdd:cd03358    1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYP-RSKIYRKWELKGTTVKRGASIGAN 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 527036111 111 ATILA-VSICDGAVIGAGSVVTKSITEKGVYAGNPARLLR 149
Cdd:cd03358   80 ATILPgVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
26-151 7.71e-36

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 120.75  E-value: 7.71e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  26 LYECSLGDNVFIGPFVEIQ-ANSHIGADSKIQSHTFI--CEYVTVGERCFIGHGVMFANDMFRDGKPNADRRSWGHIRVG 102
Cdd:COG0110    6 LFGARIGDGVVIGPGVRIYgGNITIGDNVYIGPGVTIddPGGITIGDNVLIGPGVTILTGNHPIDDPATFPLRTGPVTIG 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 527036111 103 NDVSIGSGATILA-VSICDGAVIGAGSVVTKSITEKGVYAGNPARLLRRL 151
Cdd:COG0110   86 DDVWIGAGATILPgVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKR 135
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 28-145 1.84e-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: 1.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111   28 ECSLGDNVFIGPFVEIQANSHIGAdskiqsHTFICEYVTVGERCFIGHGVMFAndmfrdgkPNADRRswGHIRVGNDVSI 107
Cdd:TIGR03570  99 SASIGEGTVIMAGAVINPDVRIGD------NVIINTGAIVEHDCVIGDFVHIA--------PGVTLS--GGVVIGEGVFI 162

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 527036111  108 GSGATIL-AVSICDGAVIGAGSVVTKSITEKGVYAGNPA 145
Cdd:TIGR03570 163 GAGATIIqGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 31-149 1.20e-14

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 69.40  E-value: 1.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  31 LGDNVFIGPFVEIQANSHIGADSKIQSHTFICEYVTVGERCFIGHGVMFANDmFRDGK-----PNA-----------DRR 94
Cdd:PRK00892 115 IGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHA-VRIGNrviihSGAvigsdgfgfanDRG 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  95 SWGHI------RVGNDVSIGSGATI---------------------------------------LA-------------- 115
Cdd:PRK00892 194 GWVKIpqlgrvIIGDDVEIGANTTIdrgalddtvigegvkidnlvqiahnvvigrhtaiaaqvgIAgstkigrycmiggq 273

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 527036111 116 ------VSICDGAVIGAGSVVTKSITEKGVY-AGNPARLLR 149
Cdd:PRK00892 274 vgiaghLEIGDGVTITAMSGVTKSIPEPGEYsSGIPAQPNK 314
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
99-132 4.06e-03

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 33.18  E-value: 4.06e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 527036111   99 IRVGNDVSIGSGATIlAVSICDGAVIGAGSVVTK 132
Cdd:pfam14602   1 VIIGDNCLIGANSGI-GVSLGDNCVVGAGVVITA 33
 
Name Accession Description Interval E-value
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 31-149 8.12e-42

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: 135.32  E-value: 8.12e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  31 LGDNVFIGPFVEIQANSHIGADSKIQSHTFICEYVTVGERCFIGHGVMFANDMFRdGKPNADRRSWGHIRVGNDVSIGSG 110
Cdd:cd03358    1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYP-RSKIYRKWELKGTTVKRGASIGAN 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 527036111 111 ATILA-VSICDGAVIGAGSVVTKSITEKGVYAGNPARLLR 149
Cdd:cd03358   80 ATILPgVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
26-151 7.71e-36

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 120.75  E-value: 7.71e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  26 LYECSLGDNVFIGPFVEIQ-ANSHIGADSKIQSHTFI--CEYVTVGERCFIGHGVMFANDMFRDGKPNADRRSWGHIRVG 102
Cdd:COG0110    6 LFGARIGDGVVIGPGVRIYgGNITIGDNVYIGPGVTIddPGGITIGDNVLIGPGVTILTGNHPIDDPATFPLRTGPVTIG 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 527036111 103 NDVSIGSGATILA-VSICDGAVIGAGSVVTKSITEKGVYAGNPARLLRRL 151
Cdd:COG0110   86 DDVWIGAGATILPgVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKR 135
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 30-148 1.52e-24

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: 90.98  E-value: 1.52e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  30 SLGDNVFIGPFVEIQANSHIgadskiqshtficeyvTVGERCFIGHGVMFAN---DMFRDGKPNADRRSWGHIRVGNDVS 106
Cdd:cd04647    3 SIGDNVYIGPGCVISAGGGI----------------TIGDNVLIGPNVTIYDhnhDIDDPERPIEQGVTSAPIVIGDDVW 66

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 527036111 107 IGSGATILA-VSICDGAVIGAGSVVTKSITEKGVYAGNPARLL 148
Cdd:cd04647   67 IGANVVILPgVTIGDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 2-148 2.21e-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: 87.09  E-value: 2.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111   2 PEQRQAAIRHVV--CGENVVIYEPANlyeCSLGDNVFIGPFVEIQANShigadskiqshTFI-CEYVTVGERCFIGHGVM 78
Cdd:cd03357   31 AEERRELLKELFgsVGENVYIEPPFH---CDYGYNIHIGDNFYANFNC-----------TILdVAPVTIGDNVLIGPNVQ 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  79 FA-----------NDMFRDGKPnadrrswghIRVGNDVSIGSGATILA-VSICDGAVIGAGSVVTKSITEKGVYAGNPAR 146
Cdd:cd03357   97 IYtaghpldpeerNRGLEYAKP---------ITIGDNVWIGGGVIILPgVTIGDNSVIGAGSVVTKDIPANVVAAGNPAR 167


                 ..
gi 527036111 147 LL 148
Cdd:cd03357  168 VI 169
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 25-149 9.36e-22

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: 84.90  E-value: 9.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  25 NLYECSLG-DNVFIGPFVEIQANSHIGADSkiqSHTFicEYVTvgercfigHGVMFANDMFRDGKPN-ADRRSWGHIRVG 102
Cdd:cd03349   11 SGPDCDVGgDKLSIGKFCSIAPGVKIGLGG---NHPT--DWVS--------TYPFYIFGGEWEDDAKfDDWPSKGDVIIG 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 527036111 103 NDVSIGSGATILA-VSICDGAVIGAGSVVTKSITEKGVYAGNPARLLR 149
Cdd:cd03349   78 NDVWIGHGATILPgVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIR 125
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 28-145 1.84e-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: 1.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111   28 ECSLGDNVFIGPFVEIQANSHIGAdskiqsHTFICEYVTVGERCFIGHGVMFAndmfrdgkPNADRRswGHIRVGNDVSI 107
Cdd:TIGR03570  99 SASIGEGTVIMAGAVINPDVRIGD------NVIINTGAIVEHDCVIGDFVHIA--------PGVTLS--GGVVIGEGVFI 162

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 527036111  108 GSGATIL-AVSICDGAVIGAGSVVTKSITEKGVYAGNPA 145
Cdd:TIGR03570 163 GAGATIIqGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 11-151 2.56e-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: 84.68  E-value: 2.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  11 HVVCGENVVIyepanlyecslGDNVFIGPFVEIQANSHIGADSKIQSHTFICEYVTVGERCFIGHGVM-------FANDm 83
Cdd:COG1044  120 FAVIGAGVVI-----------GDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVIGDRVIIHSGAVigadgfgFAPD- 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  84 fRDGKpnadrrsW------GHIRVGNDVSIGSGATI-------------------------------------------- 113
Cdd:COG1044  188 -EDGG-------WvkipqlGRVVIGDDVEIGANTTIdrgalgdtvigdgtkidnlvqiahnvrigehtaiaaqvgiagst 259

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 527036111 114 -------LA--------VSICDGAVIGAGSVVTKSITEKGVYAGNPAR----------LLRRL 151
Cdd:COG1044  260 kigdnvvIGgqvgiaghLTIGDGVIIGAQSGVTKSIPEGGVYSGSPAQphrewlrnaaALRRL 322
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 28-144 2.87e-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: 79.84  E-value: 2.87e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  28 ECSLGDNVFIGPFVEIQANSHIGADSKIQSHTFICEYVTVGERCFIGHGVMFAndmfrdgkpnadrrswGHIRVGNDVSI 107
Cdd:cd03360   96 SAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLS----------------GGVTIGEGAFI 159

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 527036111 108 GSGATIL-AVSICDGAVIGAGSVVTKSITEKGVYAGNP 144
Cdd:cd03360  160 GAGATIIqGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 31-132 1.13e-15

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: 72.75  E-value: 1.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  31 LGDNVFIGPFVEIQaNSHIGADSKIQSHTficeYV---TVGERCFIGHGVMFANdmfRDGKpnadRRSwgHIRVGNDVSI 107
Cdd:COG1207  338 LGEGVKIGNFVEVK-NSTIGEGSKVNHLS----YIgdaEIGEGVNIGAGTITCN---YDGV----NKH--RTVIGDGAFI 403

                         90       100
                 ....*....|....*....|....*.
gi 527036111 108 GSGATILA-VSICDGAVIGAGSVVTK 132
Cdd:COG1207  404 GSNTNLVApVTIGDGATIGAGSTITK 429
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 41-144 1.18e-15

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: 67.85  E-value: 1.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  41 VEIQANSHIGADSKIQSHTFIC--EYVTVGERCFIGHGVMFANDMFRDGKpnadrrswGHIRVGNDVSIGSGATIL-AVS 117
Cdd:cd03354    3 IDIHPGAKIGPGLFIDHGTGIVigETAVIGDNCTIYQGVTLGGKGKGGGK--------RHPTIGDNVVIGAGAKILgNIT 74

                         90       100
                 ....*....|....*....|....*..
gi 527036111 118 ICDGAVIGAGSVVTKSITEKGVYAGNP 144
Cdd:cd03354   75 IGDNVKIGANAVVTKDVPANSTVVGVP 101
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 10-150 1.11e-14

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: 67.82  E-value: 1.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  10 RHVVCGENVVIYEPAnlyecSLGDNVFIGPFVEIQANSHIGADSKIQSHTFICEYVTVGERCFIGHGVMFANDMFRDGKp 89
Cdd:cd03352    6 ENVSIGPNAVIGEGV-----VIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIGSDGFGFAP- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  90 naDRRSW------GHIRVGNDVSIGSGATI---------------------------------LA--------------- 115
Cdd:cd03352   80 --DGGGWvkipqlGGVIIGDDVEIGANTTIdrgalgdtvigdgtkidnlvqiahnvrigenclIAaqvgiagsttigdnv 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 527036111 116 -----------VSICDGAVIGAGSVVTKSITEKGVYAGNPARLLRR 150
Cdd:cd03352  158 iiggqvgiaghLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQPHRE 203
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 61-150 1.16e-14

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: 67.03  E-value: 1.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  61 ICEYVTVGERCFIGHGVMFANDMFRDGKpnadrrswGHIRVGNDVSIGSGATIL-AVSICDGAVIGAGSVVTKSITEKGV 139
Cdd:COG1045   88 IGETAVIGDNVTIYQGVTLGGTGKEKGK--------RHPTIGDNVVIGAGAKILgPITIGDNAKIGANSVVLKDVPPGST 159

                         90
                 ....*....|.
gi 527036111 140 YAGNPARLLRR 150
Cdd:COG1045  160 VVGVPARIVKR 170
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 31-149 1.20e-14

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 69.40  E-value: 1.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  31 LGDNVFIGPFVEIQANSHIGADSKIQSHTFICEYVTVGERCFIGHGVMFANDmFRDGK-----PNA-----------DRR 94
Cdd:PRK00892 115 IGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHA-VRIGNrviihSGAvigsdgfgfanDRG 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  95 SWGHI------RVGNDVSIGSGATI---------------------------------------LA-------------- 115
Cdd:PRK00892 194 GWVKIpqlgrvIIGDDVEIGANTTIdrgalddtvigegvkidnlvqiahnvvigrhtaiaaqvgIAgstkigrycmiggq 273

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 527036111 116 ------VSICDGAVIGAGSVVTKSITEKGVY-AGNPARLLR 149
Cdd:PRK00892 274 vgiaghLEIGDGVTITAMSGVTKSIPEPGEYsSGIPAQPNK 314
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 9-137 2.62e-14

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: 66.67  E-value: 2.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111   9 IRHVVCGENVVIYEPANLYECSLGDNVFIGP------------------FVEIQaNSHIGADSKIQSHTFICEyVTVGER 70
Cdd:cd03353   48 IKDSTIGDGVVIKASSVIEGAVIGNGATVGPfahlrpgtvlgegvhignFVEIK-KSTIGEGSKANHLSYLGD-AEIGEG 125

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527036111  71 CFIGHGVMFANdmfRDGKpnADRRSwghiRVGNDVSIGSGATILA-VSICDGAVIGAGSVVTKSITEK 137
Cdd:cd03353  126 VNIGAGTITCN---YDGV--NKHRT----VIGDNVFIGSNSQLVApVTIGDGATIAAGSTITKDVPPG 184
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 31-151 3.79e-14

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 65.82  E-value: 3.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  31 LGDNVFIGPFVEIQANSH---IGADSKIQS----HTFICEYVTVGERCFIGHGVMFandmfrdgkpnadrrswgH-IRVG 102
Cdd:COG0663   31 IGEDVSVWPGAVLRGDVGpirIGEGSNIQDgvvlHVDPGYPLTIGDDVTIGHGAIL------------------HgCTIG 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 527036111 103 NDVSIGSGATILavsicDGAVIG------AGSVVT--KSITEKGVYAGNPARLLRRL 151
Cdd:COG0663   93 DNVLIGMGAIVL-----DGAVIGdgsivgAGALVTegKVVPPGSLVVGSPAKVVREL 144
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 23-148 4.44e-14

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: 63.78  E-value: 4.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  23 PANLyecSLGDNVFIGPFVEI--QANSHIGADSKIQSHTFICEyvtvgercfighgvmfANDMFRDGKPNADRRSwghIR 100
Cdd:cd05825    1 PWNL---TIGDNSWIGEGVWIynLAPVTIGSDACISQGAYLCT----------------GSHDYRSPAFPLITAP---IV 58

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 527036111 101 VGNDVSIGSGATIL-AVSICDGAVIGAGSVVTKSITEKGVYAGNPARLL 148
Cdd:cd05825   59 IGDGAWVAAEAFVGpGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 9-136 6.16e-13

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 64.85  E-value: 6.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111   9 IRHVVCGENVVIyEPANLYECSLGDNVFIGP------------------FVEIQaNSHIGADSKIqSH-TFICEyVTVGE 69
Cdd:PRK14354 298 IVDSTIGDGVTI-TNSVIEESKVGDNVTVGPfahlrpgsvigeevkignFVEIK-KSTIGEGTKV-SHlTYIGD-AEVGE 373

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 527036111  70 RCFIGHGVMFANdmfRDGKPNAdrrswgHIRVGNDVSIGSGATILA-VSICDGAVIGAGSVVTKSITE 136
Cdd:PRK14354 374 NVNIGCGTITVN---YDGKNKF------KTIIGDNAFIGCNSNLVApVTVGDNAYIAAGSTITKDVPE 432
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 30-149 1.56e-12

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 61.82  E-value: 1.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  30 SLGDNVFIGPFVEIQANSH--IGADSKIQSHTFICEYvtvgercfiGHGVMFANDMFRDGKPNADRRSWGH--IRVGNDV 105
Cdd:PRK09677  67 FFGDNVQVNDYVHIACIESitIGRDTLIASKVFITDH---------NHGSFKHSDDFSSPNLPPDMRTLESsaVVIGQRV 137

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 527036111 106 SIGSGATIL-AVSICDGAVIGAGSVVTKSITEKGVYAGNPARLLR 149
Cdd:PRK09677 138 WIGENVTILpGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIK 182
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 3-151 1.24e-11

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 59.63  E-value: 1.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111   3 EQRQAAIRHVV--CGENVVIYEPANLyecSLGDNVFIGPfvEIQANSHIgadskiqshTFICEY-VTVGERCFI------ 73
Cdd:PRK09527  45 EKRESLIKEMFatVGENAWVEPPVYF---SYGSNIHIGR--NFYANFNL---------TIVDDYtVTIGDNVLIapnvtl 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  74 ---GHGVMFANDMfrdgkpNADRRSWGhIRVGNDVSIGSGATI-LAVSICDGAVIGAGSVVTKSITEKGVYAGNPARLLR 149
Cdd:PRK09527 111 svtGHPVHHELRK------NGEMYSFP-ITIGNNVWIGSHVVInPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIR 183


                 ..
gi 527036111 150 RL 151
Cdd:PRK09527 184 EI 185
PLN02694 PLN02694
serine O-acetyltransferase
 65-148 2.62e-11

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 59.66  E-value: 2.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  65 VTVGERCFIGHGVMFAN--DMFRDGKPNADRrswgHIRVGNDVSIGSGATILA-VSICDGAVIGAGSVVTKSITEKGVYA 141
Cdd:PLN02694 181 VVIGETAVIGNNVSILHhvTLGGTGKACGDR----HPKIGDGVLIGAGATILGnVKIGEGAKIGAGSVVLIDVPPRTTAV 256


                 ....*..
gi 527036111 142 GNPARLL 148
Cdd:PLN02694 257 GNPARLV 263
PLN02357 PLN02357
serine acetyltransferase
 61-148 3.49e-11

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 59.51  E-value: 3.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  61 ICEYVTVGERCFIGHGVMFANDmfrdGKPNADRrswgHIRVGNDVSIGSGATILA-VSICDGAVIGAGSVVTKSITEKGV 139
Cdd:PLN02357 249 IGETAVVGNNVSILHNVTLGGT----GKQSGDR----HPKIGDGVLIGAGTCILGnITIGEGAKIGAGSVVLKDVPPRTT 320


                 ....*....
gi 527036111 140 YAGNPARLL 148
Cdd:PLN02357 321 AVGNPARLI 329
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 3-151 4.04e-11

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 57.90  E-value: 4.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111   3 EQRQAAIRHVVCGENVVIYEPAnlYECSLGDNVFIGpfveiqANSHIGADSKIQShtfICEyVTVGERCFIGHGVmfanD 82
Cdd:PRK10092  44 TLRQQILADLFGQVTEAYIEPT--FRCDYGYNIFLG------NNFYANFDCVMLD---VCP-IRIGDNCMLAPGV----H 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527036111  83 MFRDGKP-NADRRSWGH-----IRVGNDVSIGSGATI-LAVSICDGAVIGAGSVVTKSITEKGVYAGNPARLLRRL 151
Cdd:PRK10092 108 IYTATHPlDPVARNSGAelgkpVTIGNNVWIGGRAVInPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARIIKKL 183
PRK10502 PRK10502
putative acyl transferase; Provisional
 15-149 9.18e-11

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 56.88  E-value: 9.18e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  15 GENVVIYEPANL---YECSLGDNVFIGPFVEIQ--ANSHIGADSKIQSHTFICEyvtvgercfighgvmfANDMFRDgkP 89
Cdd:PRK10502  55 GKGVVIRPSVRItypWKLTIGDYAWIGDDVWLYnlGEITIGAHCVISQKSYLCT----------------GSHDYSD--P 116

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527036111  90 NADRRSwGHIRVGNDVSIGSGATI-LAVSICDGAVIGAGSVVTKSITEKGVYAGNPARLLR 149
Cdd:PRK10502 117 HFDLNT-APIVIGEGCWLAADVFVaPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIR 176
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 30-134 9.71e-11

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 58.33  E-value: 9.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  30 SLGDNVFIGPFVEIQaNSHIGADSKIQSHTFICEyVTVGERCFIGHGVMFAN-DMFRDGKpnadrrswghIRVGNDVSIG 108
Cdd:PRK14353 323 ELGEGAKVGNFVEVK-NAKLGEGAKVNHLTYIGD-ATIGAGANIGAGTITCNyDGFNKHR----------TEIGAGAFIG 390

                         90       100
                 ....*....|....*....|....*..
gi 527036111 109 SGATILA-VSICDGAVIGAGSVVTKSI 134
Cdd:PRK14353 391 SNSALVApVTIGDGAYIASGSVITEDV 417
PLN02739 PLN02739
serine acetyltransferase
 61-149 1.76e-10

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 57.74  E-value: 1.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  61 ICEYVTVGERCFIGHGVMFANDmfrdGKPNADRrswgHIRVGNDVSIGSGATILA-VSICDGAVIGAGSVVTKSITEKGV 139
Cdd:PLN02739 228 IGETAVIGDRVSILHGVTLGGT----GKETGDR----HPKIGDGALLGACVTILGnISIGAGAMVAAGSLVLKDVPSHSM 299

                         90
                 ....*....|
gi 527036111 140 YAGNPARLLR 149
Cdd:PLN02739 300 VAGNPAKLIG 309
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 9-136 7.81e-10

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 55.80  E-value: 7.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111   9 IRHVVCGENVVI-----YEPANLYE-CSLG------------DNVFIGPFVEIQaNSHIGADSKIQSHTFICEyVTVGER 70
Cdd:PRK09451 298 LKNCVIGDDCEIspysvVEDANLGAaCTIGpfarlrpgaelaEGAHVGNFVEMK-KARLGKGSKAGHLTYLGD-AEIGDN 375

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 527036111  71 CFIGHGVMFANdmfRDGkpnADRRSwghIRVGNDVSIGSGATILA-VSICDGAVIGAGSVVTKSITE 136
Cdd:PRK09451 376 VNIGAGTITCN---YDG---ANKFK---TIIGDDVFVGSDTQLVApVTVGKGATIGAGTTVTRDVAE 433
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 31-132 1.66e-09

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 54.94  E-value: 1.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  31 LGDNVFIGPFVEIQaNSHIGADSKIQSHTficeYV---TVGERCFIGHGVMFANdmfRDGKpnadrrSWGHIRVGNDVSI 107
Cdd:PRK14352 343 LGEEGKLGAFVETK-NATIGRGTKVPHLT----YVgdaDIGEHSNIGASSVFVN---YDGV------NKHRTTIGSHVRT 408

                         90       100
                 ....*....|....*....|....*.
gi 527036111 108 GSGATILA-VSICDGAVIGAGSVVTK 132
Cdd:PRK14352 409 GSDTMFVApVTVGDGAYTGAGTVIRE 434
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 31-136 8.11e-09

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 52.84  E-value: 8.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  31 LGDNVFIGPFVEIQaNSHIGADSKIQSHTFICEyVTVGERCFIGHGVMFANdmfRDGKpnadRRSWGHIrvGNDVSIGSG 110
Cdd:PRK14357 327 LKKSVKIGNFVEIK-KSTIGENTKAQHLTYLGD-ATVGKNVNIGAGTITCN---YDGK----KKNPTFI--EDGAFIGSN 395

                         90       100
                 ....*....|....*....|....*..
gi 527036111 111 ATILA-VSICDGAVIGAGSVVTKSITE 136
Cdd:PRK14357 396 SSLVApVRIGKGALIGAGSVITEDVPP 422
cysE PRK11132
serine acetyltransferase; Provisional
 87-150 1.52e-07

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 48.92  E-value: 1.52e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527036111  87 GKPNADRrswgHIRVGNDVSIGSGATILA-VSICDGAVIGAGSVVTKSITEKGVYAGNPARLLRR 150
Cdd:PRK11132 186 GKTSGDR----HPKIREGVMIGAGAKILGnIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVGK 246
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 30-151 1.76e-07

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: 47.41  E-value: 1.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  30 SLGDNVFIGPFVEIQANSHIGADSKIQSHTFI---CEYVTVGERCFIGHGVMFANDmfrDGKPnadrrswghIRVGNDVS 106
Cdd:cd04645    1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLrgdVNPIRIGERTNIQDGSVLHVD---PGYP---------TIIGDNVT 68

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 527036111 107 -----------------IGSGATIL--AVsICDGAVIGAGSVVT--KSITEKGVYAGNPARLLRRL 151
Cdd:cd04645   69 vghgavlhgctigdnclIGMGAIILdgAV-IGKGSIVAAGSLVPpgKVIPPGSLVAGSPAKVVREL 133
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 31-77 2.17e-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: 48.48  E-value: 2.17e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 527036111  31 LGDNVFIGPFVEIQANSHIGADSKIQSHTFICEYVTVGERCFIGHGV 77
Cdd:COG1043   16 LGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFA 62
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 49-145 2.42e-07

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 48.59  E-value: 2.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111   49 IGADSKIQSHTFIC-EYVTVGERCFIGHGVMFANdmfrdGKPNADRRSWGHIRVGNDVSIGSGATILA-VSICDGAVIGA 126
Cdd:TIGR02353 115 IGKGVDIGSLPPVCtDLLTIGAGTIVRKEVMLLG-----YRAERGRLHTGPVTLGRDAFIGTRSTLDIdTSIGDGAQLGH 189

                          90       100
                  ....*....|....*....|.
gi 527036111  127 GSVVT--KSITEKGVYAGNPA 145
Cdd:TIGR02353 190 GSALQggQSIPDGERWHGSPA 210
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 31-76 2.43e-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: 48.20  E-value: 2.43e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 527036111  31 LGDNVFIGPFVEIQANSHIGADSKIQSHTFICEYVTVGERCFIGHG 76
Cdd:cd03351   14 IGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPF 59
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 6-132 2.82e-07

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 48.39  E-value: 2.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111   6 QAAIRHVVCGENVVIYEPANLY-ECSLGDNVFIGPFVEIQaNSHIGADSKIQSHTFICEyVTVGERCFIGHGVMFANdmf 84
Cdd:PRK14360 308 YSVVSDSQIGDGVKIGPYAHLRpEAQIGSNCRIGNFVEIK-KSQLGEGSKVNHLSYIGD-ATLGEQVNIGAGTITAN--- 382

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 527036111  85 RDGKpNADRrswghIRVGNDVSIGSGATILA-VSICDGAVIGAGSVVTK 132
Cdd:PRK14360 383 YDGV-KKHR-----TVIGDRSKTGANSVLVApITLGEDVTVAAGSTITK 425
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 12-130 3.15e-07

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: 47.24  E-value: 3.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  12 VVCGeNVVIyepanlyecslGDNVFIGPFVEIQANS----HIGADSKIQS----HTFICEYVTVGERCFIGHGVMFAndm 83
Cdd:cd00710   16 VVIG-DVII-----------GDNVFVGPGASIRADEgtpiIIGANVNIQDgvviHALEGYSVWIGKNVSIAHGAIVH--- 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 527036111  84 frdgkpnadrrswGHIRVGNDVSIGSGATILAVSICDGAVIGAGSVV 130
Cdd:cd00710   81 -------------GPAYIGDNCFIGFRSVVFNAKVGDNCVIGHNAVV 114
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 33-151 6.56e-07

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: 46.02  E-value: 6.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  33 DNVFIGPFVEIQANSHIGADSKIQshTFICEYVTVGERCFIgHGVmfandmfrdgkpnadrrswghiRVGNDVSIGSGAT 112
Cdd:cd04650   38 DSIYIGKYSNVQENVSIHTDHGYP--TEIGDYVTIGHNAVV-HGA----------------------KVGNYVIVGMGAI 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 527036111 113 IL-AVSICDGAVIGAGSVVT--KSITEKGVYAGNPARLLRRL 151
Cdd:cd04650   93 LLnGAKIGDHVIIGAGAVVTpgKEIPDYSLVLGVPAKVVRKL 134
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
31-77 9.96e-07

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 46.63  E-value: 9.96e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 527036111  31 LGDNVFIGPFVEIQANSHIGADSKIQSHTFICEYVTVGERCFIGHGV 77
Cdd:PRK05289  17 IGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFA 63
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 33-130 1.11e-06

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: 45.87  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  33 DNVFIGPFVEIqanshiGADSKIQSHTFICEYVTVGERCFIGHGVMFandmfrdgkpnadrrswghirvgNDVSIGSGAT 112
Cdd:cd03353    8 ETTYIDGDVEI------GVDVVIDPGVILEGKTVIGEDCVIGPNCVI-----------------------KDSTIGDGVV 58

                         90
                 ....*....|....*...
gi 527036111 113 ILAVSICDGAVIGAGSVV 130
Cdd:cd03353   59 IKASSVIEGAVIGNGATV 76
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 29-137 3.87e-06

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 45.10  E-value: 3.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  29 CSLGDNVFIGPFVEIQaNSHIGADSKIQSHTFI--CEyvtVGERCFIGHGVMFANdmfRDGKPNAdrrswgHIRVGNDVS 106
Cdd:PRK14356 340 AVLEEGARVGNFVEMK-KAVLGKGAKANHLTYLgdAE---IGAGANIGAGTITCN---YDGVNKH------RTVIGEGAF 406

                         90       100       110
                 ....*....|....*....|....*....|..
gi 527036111 107 IGSGATILA-VSICDGAVIGAGSVVTKSITEK 137
Cdd:PRK14356 407 IGSNTALVApVTIGDGALVGAGSVITKDVPDG 438
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 59-147 2.36e-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: 42.41  E-value: 2.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  59 TFICEYVTVGERCFIGHGVMFAndmfrdgkpnadrrswGHIRVGNDVSIGSGATILAVSICDGAVIGAGSVVTKSITEKG 138
Cdd:cd03353   10 TYIDGDVEIGVDVVIDPGVILE----------------GKTVIGEDCVIGPNCVIKDSTIGDGVVIKASSVIEGAVIGNG 73


                 ....*....
gi 527036111 139 VYAGNPARL 147
Cdd:cd03353   74 ATVGPFAHL 82
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 29-130 3.06e-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: 41.80  E-value: 3.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  29 CSLGDNVFIGPFVEIQaNSHIGADSKIQSHTFICEYVtVGERCFIGHGVMFANDMF---------RDGKPNADRRSWGHI 99
Cdd:cd05636   54 TVLGDGCVVGNSVEVK-NSIIMDGTKVPHLNYVGDSV-LGENVNLGAGTITANLRFddkpvkvrlKGERVDTGRRKLGAI 131

                         90       100       110
                 ....*....|....*....|....*....|.
gi 527036111 100 rVGNDVSIGSGatilaVSICDGAVIGAGSVV 130
Cdd:cd05636  132 -IGDGVKTGIN-----VSLNPGVKIGPGSWV 156
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 12-147 3.74e-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: 3.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  12 VVCGENVVIyepanlyecslGDNVFIGPFVEIQANSHIGADSKIQSH------------------------TFICEYVT- 66
Cdd:cd03351   24 CVIGPNVEI-----------GDGTVIGSHVVIDGPTTIGKNNRIFPFasigeapqdlkykgeptrleigdnNTIREFVTi 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  67 ------------VGERCF------------IGHGVMFANdmfrdgkpNADRRswGHIRVGNDVSIGSGATILA-VSICDG 121
Cdd:cd03351   93 hrgtaqgggvtrIGNNNLlmayvhvahdcvIGNNVILAN--------NATLA--GHVEIGDYAIIGGLSAVHQfCRIGRH 162

                        170       180
                 ....*....|....*....|....*.
gi 527036111 122 AVIGAGSVVTKSITEKGVYAGNPARL 147
Cdd:cd03351  163 AMVGGGSGVVQDVPPYVIAAGNRARL 188
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 31-136 4.92e-05

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 41.89  E-value: 4.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  31 LGDNVFIGPFVEIQaNSHIGADSKIQSHTFICEyVTVGERCFIGHGVMFANdmfrdgkpnADRRSWGHIRVGNDVSIGSG 110
Cdd:PRK14358 343 LGEGVHIGNFVETK-NARLDAGVKAGHLAYLGD-VTIGAETNVGAGTIVAN---------FDGVNKHQSKVGAGVFIGSN 411

                         90       100
                 ....*....|....*....|....*..
gi 527036111 111 ATILAVSIC-DGAVIGAGSVVTKSITE 136
Cdd:PRK14358 412 TTLIAPRVVgDAAFIAAGSAVHDDVPE 438
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 46-130 7.46e-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: 40.85  E-value: 7.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  46 NSHIGADSKIQSHTFICEYVTVGERCFIGHGVmfandmfrdgkpnadrrswghiRVGNDVSIGSGATILA-VSICDGAVI 124
Cdd:cd03352    1 SAKIGENVSIGPNAVIGEGVVIGDGVVIGPGV----------------------VIGDGVVIGDDCVIHPnVTIYEGCII 58


                 ....*.
gi 527036111 125 GAGSVV 130
Cdd:cd03352   59 GDRVII 64
PRK10191 PRK10191
putative acyl transferase; Provisional
 42-147 1.02e-04

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 39.87  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  42 EIQANSHIGADSKIQsHTF---ICEYVTVGERCFIGHGVMFANDmfrdgkpNADRRSWGHIrvGNDVSIGSGATILA-VS 117
Cdd:PRK10191  43 EIQAAATIGRRFTIH-HGYavvINKNVVAGDDFTIRHGVTIGNR-------GADNMACPHI--GNGVELGANVIILGdIT 112

                         90       100       110
                 ....*....|....*....|....*....|
gi 527036111 118 ICDGAVIGAGSVVTKSITEKGVYAGNPARL 147
Cdd:PRK10191 113 IGNNVTVGAGSVVLDSVPDNALVVGEKARV 142
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 31-73 1.07e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 40.78  E-value: 1.07e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 527036111  31 LGDNVFIGPFVEIQANSHIGADSKIQSHTFICEYVTVGERCFI 73
Cdd:PRK12461  14 LGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKI 56
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 25-145 4.05e-04

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: 39.35  E-value: 4.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111   25 NLYECSLGDNVFIGPF-------VEIQANSHIGADSKIQSH-----TFICEYVTVGERCfighgvmfandmfrdgkpnad 92
Cdd:TIGR02353 594 RLLGVKIGRGVYIDGTdlterdlVTIGDDSTLNEGSVIQTHlfedrVMKSDTVTIGDGA--------------------- 652

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 527036111   93 rrswghirvgndvSIGSGATIL-AVSICDGAVIGAGSVVTK--SITEKGVYAGNPA 145
Cdd:TIGR02353 653 -------------TLGPGAIVLyGVVMGEGSVLGPDSLVMKgeEVPAHTRWRGNPA 695
PLN02296 PLN02296
carbonate dehydratase
 101-151 4.14e-04

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 38.95  E-value: 4.14e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 527036111 101 VGNDVSIGSGATILAVSICD------------------GAVIGAGSVVTKS--ITEKGVYAGNPARLLRRL 151
Cdd:PLN02296 122 IGDNVTIGHSAVLHGCTVEDeafvgmgatlldgvvvekHAMVAAGALVRQNtrIPSGEVWAGNPAKFLRKL 192
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 34-141 4.57e-04

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 39.20  E-value: 4.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  34 NVFIGPFVEIQANSHIGADSKIQSHTFICEyvtVGERCFIGHGVMFANdmfRDGKpnADRRSwghiRVGNDVSIGSGATI 113
Cdd:PRK14359 315 NTHIGNFVETKNAKLNGVKAGHLSYLGDCE---IDEGTNIGAGTITCN---YDGK--KKHKT----IIGKNVFIGSDTQL 382

                         90       100
                 ....*....|....*....|....*....
gi 527036111 114 LA-VSICDGAVIGAGSVVTKSItEKGVYA 141
Cdd:PRK14359 383 VApVNIEDNVLIAAGSTVTKDV-PKGSLA 410
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
13-150 9.82e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 37.77  E-value: 9.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  13 VCGENVVIyepanlyecslGDNVFIGPFVEIQANSHIGADSKI----------Q-------------------------- 56
Cdd:PRK05289  28 VIGPNVVI-----------GDGTVIGSHVVIDGHTTIGKNNRIfpfasigedpQdlkykgeptrlvigdnntirefvtin 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  57 -------------SHTFICEYVTVGERCFIGHGVMFANdmfrdgkpN---AdrrswGHIRVGNDVSIGSGATILA-VSIC 119
Cdd:PRK05289  97 rgtvqgggvtrigDNNLLMAYVHVAHDCVVGNHVILAN--------NatlA-----GHVEVGDYAIIGGLTAVHQfVRIG 163

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 527036111 120 DGAVIGAGSVVTKSITEKGVYAGNPARL-------LRR 150
Cdd:PRK05289 164 AHAMVGGMSGVSQDVPPYVLAEGNPARLrglnlvgLKR 201
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 31-131 1.76e-03

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: 35.30  E-value: 1.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  31 LGDNVFIGPFVEIQANSHIgadskiqshtficeyvtvGERCFIGHGVMFANDMFRDGKpnadrrswGHIRVGNDVSIGSG 110
Cdd:cd00208    3 IGEGVKIHPKAVIRGPVVI------------------GDNVNIGPGAVIGAATGPNEK--------NPTIIGDNVEIGAN 56

                         90       100
                 ....*....|....*....|..
gi 527036111 111 ATILA-VSICDGAVIGAGSVVT 131
Cdd:cd00208   57 AVIHGgVKIGDNAVIGAGAVVT 78
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 31-151 2.67e-03

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


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 36.19  E-value: 2.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  31 LGDNVFIGPFVEIQANSH---IGADSKIQS----HTFICEYVTVGERCFIGHGVMFandmfrdgkpnadrrswgH-IRVG 102
Cdd:cd04745   21 IGKNCYIGPHASLRGDFGrivIRDGANVQDncviHGFPGQDTVLEENGHIGHGAIL------------------HgCTIG 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 527036111 103 NDVSIGSGATILavsicDGAVIGAGSVVTKSITEKGVY--------AGNPARLLRRL 151
Cdd:cd04745   83 RNALVGMNAVVM-----DGAVIGEESIVGAMAFVKAGTvipprsliAGSPAKVIREL 134
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 100-130 3.02e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 36.66  E-value: 3.02e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 527036111 100 RVGNDVSIGSGATILA-VSICDGAVIGAGSVV 130
Cdd:PRK00892 114 KIGEGVSIGPNAVIGAgVVIGDGVVIGAGAVI 145
Hexapep_2 pfam14602
Hexapeptide repeat of succinyl-transferase;
99-132 4.06e-03

Hexapeptide repeat of succinyl-transferase;


Pssm-ID: 434064 [Multi-domain]  Cd Length: 33  Bit Score: 33.18  E-value: 4.06e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 527036111   99 IRVGNDVSIGSGATIlAVSICDGAVIGAGSVVTK 132
Cdd:pfam14602   1 VIIGDNCLIGANSGI-GVSLGDNCVVGAGVVITA 33
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 10-77 5.60e-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: 35.27  E-value: 5.60e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 527036111  10 RHVVCGENVVIYEPANLYECS-------LGDNVFIGPFVEIQAnshigadSKIQSHTFICEYVTVGERCFIGHGV 77
Cdd:cd03359   47 RYCILSEGCVIRPPFKKFSKGvaffplhIGDYVFIGENCVVNA-------AQIGSYVHIGKNCVIGRRCIIKDCV 114
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 16-125 5.98e-03

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 35.67  E-value: 5.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 527036111  16 ENVVIYEPANlyeCSLGDNVFIGPFVEIQANSHIGADSKIQSH------TFIcEYVTVGERCFIGHGVMFandmfrdgkp 89
Cdd:PRK14360 247 AGVTFIDPAS---CTISETVELGPDVIIEPQTHLRGNTVIGSGcrigpgSLI-ENSQIGENVTVLYSVVS---------- 312

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 527036111  90 nadrrswgHIRVGNDVSIGSGATIL-AVSICDGAVIG 125
Cdd:PRK14360 313 --------DSQIGDGVKIGPYAHLRpEAQIGSNCRIG 341
PLN02472 PLN02472
uncharacterized protein
 98-151 6.67e-03

uncharacterized protein


Pssm-ID: 215263 [Multi-domain]  Cd Length: 246  Bit Score: 35.71  E-value: 6.67e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 527036111  98 HIRVGNDVSIGSGATILAVSICDGAVIGA------GSVV-TKSITEKG-------------VYAGNPARLLRRL 151
Cdd:PLN02472 126 ETLIDRYVTIGAYSLLRSCTIEPECIIGQhsilmeGSLVeTHSILEAGsvlppgrriptgeLWAGNPARFVRTL 199
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
29-57 6.80e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 32.69  E-value: 6.80e-03
                          10        20
                  ....*....|....*....|....*....
gi 527036111   29 CSLGDNVFIGPFVEIQANSHIGADSKIQS 57
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 100-130 9.87e-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: 34.99  E-value: 9.87e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 527036111 100 RVGNDVSIGSGATILA-VSICDGAVIGAGSVV 130
Cdd:COG1044  110 KIGEGVSIGPFAVIGAgVVIGDGVVIGPGVVI 141
 
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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