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Conserved domains on  [gi|535274496|gb|EQU17713|]
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hypothetical protein G853_04959 [Escherichia coli HVH 201 (4-4459431)]

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 ...
 32-148 1.29e-41

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: 134.55  E-value: 1.29e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  32 DNVFVGPFVEIQKGCVIGSGSRIQSHTFICENVTLGENCFIGHNVTFANDLFrSGAPDPSPDNWISITLGDSVTVGSGAI 111
Cdd:cd03358    3 DNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLY-PRSKIYRKWELKGTTVKRGASIGANAT 81

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 535274496 112 ILS-PYICSGAVIGAGSVVVKPIENKGIYAGNPARLLR 148
Cdd:cd03358   82 ILPgVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 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 ...
 32-148 1.29e-41

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: 134.55  E-value: 1.29e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  32 DNVFVGPFVEIQKGCVIGSGSRIQSHTFICENVTLGENCFIGHNVTFANDLFrSGAPDPSPDNWISITLGDSVTVGSGAI 111
Cdd:cd03358    3 DNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLY-PRSKIYRKWELKGTTVKRGASIGANAT 81

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 535274496 112 ILS-PYICSGAVIGAGSVVVKPIENKGIYAGNPARLLR 148
Cdd:cd03358   82 ILPgVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
25-148 4.82e-25

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 93.01  E-value: 4.82e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  25 IYECELRDNVFVGPFVEIQKGCV-IGSGSRIQSHTFI--CENVTLGENCFIGHNVTFANDLFRSGAPDPSPDNWISITLG 101
Cdd:COG0110    6 LFGARIGDGVVIGPGVRIYGGNItIGDNVYIGPGVTIddPGGITIGDNVLIGPGVTILTGNHPIDDPATFPLRTGPVTIG 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 535274496 102 DSVTVGSGAIILsP--YICSGAVIGAGSVVVKPIENKGIYAGNPARLLR 148
Cdd:COG0110   86 DDVWIGAGATIL-PgvTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIR 133
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 34-144 1.75e-15

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: 69.83  E-value: 1.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496   34 VFVGPFVEIQKGCVIGSGSRIQS------HTFICENVTLGENCFIGHNVTFANDLFRSGApdpspdnwisITLGDSVTVG 107
Cdd:TIGR03570  94 AIVSPSASIGEGTVIMAGAVINPdvrigdNVIINTGAIVEHDCVIGDFVHIAPGVTLSGG----------VVIGEGVFIG 163

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 535274496  108 SGAIILsPY--ICSGAVIGAGSVVVKPIENKGIYAGNPA 144
Cdd:TIGR03570 164 AGATII-QGvtIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 32-125 8.19e-13

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 64.00  E-value: 8.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  32 DNVFVGPFVEIQKGCVIGSGSRIQSHTFICENVTLGENCFIGHNVtfandlfrsgapdpspdnwisiTLGDSVTVGSGAI 111
Cdd:PRK00892 117 EGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANV----------------------TIYHAVRIGNRVI 174

                         90
                 ....*....|....
gi 535274496 112 ILspyicSGAVIGA 125
Cdd:PRK00892 175 IH-----SGAVIGS 183
 
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 ...
 32-148 1.29e-41

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: 134.55  E-value: 1.29e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  32 DNVFVGPFVEIQKGCVIGSGSRIQSHTFICENVTLGENCFIGHNVTFANDLFrSGAPDPSPDNWISITLGDSVTVGSGAI 111
Cdd:cd03358    3 DNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLY-PRSKIYRKWELKGTTVKRGASIGANAT 81

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 535274496 112 ILS-PYICSGAVIGAGSVVVKPIENKGIYAGNPARLLR 148
Cdd:cd03358   82 ILPgVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
25-148 4.82e-25

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 93.01  E-value: 4.82e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  25 IYECELRDNVFVGPFVEIQKGCV-IGSGSRIQSHTFI--CENVTLGENCFIGHNVTFANDLFRSGAPDPSPDNWISITLG 101
Cdd:COG0110    6 LFGARIGDGVVIGPGVRIYGGNItIGDNVYIGPGVTIddPGGITIGDNVLIGPGVTILTGNHPIDDPATFPLRTGPVTIG 85

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 535274496 102 DSVTVGSGAIILsP--YICSGAVIGAGSVVVKPIENKGIYAGNPARLLR 148
Cdd:COG0110   86 DDVWIGAGATIL-PgvTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIR 133
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 40-147 3.29e-17

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: 72.10  E-value: 3.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  40 VEIQKGCVIGSGSRIQSHtficENVTLGENCFIGHNVTFANDLFRSGAPDPSPDNWIS---ITLGDSVTVGSGAIILSP- 115
Cdd:cd04647    2 ISIGDNVYIGPGCVISAG----GGITIGDNVLIGPNVTIYDHNHDIDDPERPIEQGVTsapIVIGDDVWIGANVVILPGv 77

                         90       100       110
                 ....*....|....*....|....*....|..
gi 535274496 116 YICSGAVIGAGSVVVKPIENKGIYAGNPARLL 147
Cdd:cd04647   78 TIGDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 34-144 1.75e-15

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: 69.83  E-value: 1.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496   34 VFVGPFVEIQKGCVIGSGSRIQS------HTFICENVTLGENCFIGHNVTFANDLFRSGApdpspdnwisITLGDSVTVG 107
Cdd:TIGR03570  94 AIVSPSASIGEGTVIMAGAVINPdvrigdNVIINTGAIVEHDCVIGDFVHIAPGVTLSGG----------VVIGEGVFIG 163

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 535274496  108 SGAIILsPY--ICSGAVIGAGSVVVKPIENKGIYAGNPA 144
Cdd:TIGR03570 164 AGATII-QGvtIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 32-145 2.13e-15

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: 71.20  E-value: 2.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  32 DNVFVGPFVEIQKGCVIGSGSRIQSHTFICENVTLGENCFIGHNVTFAND-------LFRSG----------APDPSpDN 94
Cdd:COG1044  113 EGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERcvigdrvIIHSGavigadgfgfAPDED-GG 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  95 WISI-----------------------TLGD-----------------------------------SVTVGSGAII---- 112
Cdd:COG1044  192 WVKIpqlgrvvigddveiganttidrgALGDtvigdgtkidnlvqiahnvrigehtaiaaqvgiagSTKIGDNVVIggqv 271

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 535274496 113 -----LSpyICSGAVIGAGSVVVKPIENKGIYAGNPAR 145
Cdd:COG1044  272 giaghLT--IGDGVIIGAQSGVTKSIPEGGVYSGSPAQ 307
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 34-143 1.36e-14

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 67.51  E-value: 1.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  34 VFVGPFVEIQKGCVIGSGSRIQSHTFICENV------TLGENCFIGHNVTFANDLFRSGapdpspdnwiSITLGDSVTVG 107
Cdd:cd03360   91 AVVSPSAVIGEGCVIMAGAVINPDARIGDNViintgaVIGHDCVIGDFVHIAPGVVLSG----------GVTIGEGAFIG 160

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 535274496 108 SGAIILSPY-ICSGAVIGAGSVVVKPIENKGIYAGNP 143
Cdd:cd03360  161 AGATIIQGVtIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 40-143 7.23e-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: 63.23  E-value: 7.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  40 VEIQKGCVIGSGSRIQSHTF--ICENVTLGENCFIGHNVTFANDLFRSGAPDPspdnwisiTLGDSVTVGSGAIILSP-Y 116
Cdd:cd03354    3 IDIHPGAKIGPGLFIDHGTGivIGETAVIGDNCTIYQGVTLGGKGKGGGKRHP--------TIGDNVVIGAGAKILGNiT 74

                         90       100
                 ....*....|....*....|....*..
gi 535274496 117 ICSGAVIGAGSVVVKPIENKGIYAGNP 143
Cdd:cd03354   75 IGDNVKIGANAVVTKDVPANSTVVGVP 101
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 32-125 8.19e-13

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 64.00  E-value: 8.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  32 DNVFVGPFVEIQKGCVIGSGSRIQSHTFICENVTLGENCFIGHNVtfandlfrsgapdpspdnwisiTLGDSVTVGSGAI 111
Cdd:PRK00892 117 EGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANV----------------------TIYHAVRIGNRVI 174

                         90
                 ....*....|....
gi 535274496 112 ILspyicSGAVIGA 125
Cdd:PRK00892 175 IH-----SGAVIGS 183
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 40-148 1.08e-12

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: 62.02  E-value: 1.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  40 VEIQKGCVIGSGSRIQsHTF---ICENVTLGENCFIGHNVTFANDLFRSGAPDPspdnwisiTLGDSVTVGSGAIILSP- 115
Cdd:COG1045   66 IDIHPGATIGRGFFID-HGTgvvIGETAVIGDNVTIYQGVTLGGTGKEKGKRHP--------TIGDNVVIGAGAKILGPi 136

                         90       100       110
                 ....*....|....*....|....*....|...
gi 535274496 116 YICSGAVIGAGSVVVKPIENKGIYAGNPARLLR 148
Cdd:COG1045  137 TIGDNAKIGANSVVLKDVPPGSTVVGVPARIVK 169
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 46-148 1.27e-12

Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of a large number of microbial enzymes that catalyze the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. Members of this class of enzymes include Enterococcus faecium streptogramin A acetyltransferase and Pseudomonas aeruginosa chloramphenicol acetyltransferase. They contain repeated copies of a six-residue hexapeptide repeat sequence motif (X-[STAV]-X-[LIV]-[GAED]-X) and adopt a left-handed parallel beta helix (LbH) structure. The active enzyme is a trimer with CoA and substrate binding sites at the interface of two separate LbH subunits. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients.


Pssm-ID: 100040 [Multi-domain]  Cd Length: 145  Bit Score: 61.02  E-value: 1.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  46 CVIGSGSRIQSHTFIC--ENVTLGENCFIGHNVTF---------------ANDLFRSGAPDPSPDNWIS---ITLGDSVT 105
Cdd:cd03349    2 ISVGDYSYGSGPDCDVggDKLSIGKFCSIAPGVKIglggnhptdwvstypFYIFGGEWEDDAKFDDWPSkgdVIIGNDVW 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 535274496 106 VGSGAIILSPY-ICSGAVIGAGSVVVKPIENKGIYAGNPARLLR 148
Cdd:cd03349   82 IGHGATILPGVtIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIR 125
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 14-147 1.91e-12

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: 61.28  E-value: 1.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  14 GTNVRIVKPVNiyeCELRDNVFVGPFVEIQKGCVIGSGSRIqshtficenvTLGENCFIGHNVTFA-----------NDL 82
Cdd:cd03357   46 GENVYIEPPFH---CDYGYNIHIGDNFYANFNCTILDVAPV----------TIGDNVLIGPNVQIYtaghpldpeerNRG 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 535274496  83 FRSGAPdpspdnwisITLGDSVTVGSGAIILsP--YICSGAVIGAGSVVVKPIENKGIYAGNPARLL 147
Cdd:cd03357  113 LEYAKP---------ITIGDNVWIGGGVIIL-PgvTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 32-125 1.45e-11

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 59.34  E-value: 1.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  32 DNVFVGPFVEIQKGCVIGSGSRIQSHTFICENVTLGENCFIGHNVtfandlfrsgapdpspdnwisiTLGDSVTVGSGAI 111
Cdd:cd03352    6 ENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNV----------------------TIYEGCIIGDRVI 63

                         90
                 ....*....|....
gi 535274496 112 ILspyicSGAVIGA 125
Cdd:cd03352   64 IH-----SGAVIGS 72
PLN02357 PLN02357
serine acetyltransferase
 40-147 2.47e-11

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 59.90  E-value: 2.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  40 VEIQKGCVIGSGSRIQSHT--FICENVTLGENCFIGHNVTFANDLFRSGAPDPSpdnwisitLGDSVTVGSGAIILSPY- 116
Cdd:PLN02357 227 VDIHPGAKIGQGILLDHATgvVIGETAVVGNNVSILHNVTLGGTGKQSGDRHPK--------IGDGVLIGAGTCILGNIt 298

                         90       100       110
                 ....*....|....*....|....*....|.
gi 535274496 117 ICSGAVIGAGSVVVKPIENKGIYAGNPARLL 147
Cdd:PLN02357 299 IGEGAKIGAGSVVLKDVPPRTTAVGNPARLI 329
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 11-150 1.46e-10

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: 55.88  E-value: 1.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  11 VIYGtNVRIVKPVNI-YECELR---DNVFVGPFVEIQKGCVIgsgsriqsHTFICENVTLGENCFIGHNVTFAndlfrsG 86
Cdd:cd04645   13 TVIG-DVTLGEGSSVwFGAVLRgdvNPIRIGERTNIQDGSVL--------HVDPGYPTIIGDNVTVGHGAVLH------G 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 535274496  87 ApdpspdnwisiTLGDSVTVGSGAIILS-PYICSGAVIGAGSVVV--KPIENKGIYAGNPARLLRIL 150
Cdd:cd04645   78 C-----------TIGDNCLIGMGAIILDgAVIGKGSIVAAGSLVPpgKVIPPGSLVAGSPAKVVREL 133
PLN02694 PLN02694
serine O-acetyltransferase
 40-147 2.99e-10

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 56.96  E-value: 2.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  40 VEIQKGCVIGSGSRIQSHTficeNVTLGENCFIGHNVTFANDLFRSGAPDPSPDNWISItlGDSVTVGSGAIILSPY-IC 118
Cdd:PLN02694 161 VDIHPAAKIGKGILFDHAT----GVVIGETAVIGNNVSILHHVTLGGTGKACGDRHPKI--GDGVLIGAGATILGNVkIG 234

                         90       100
                 ....*....|....*....|....*....
gi 535274496 119 SGAVIGAGSVVVKPIENKGIYAGNPARLL 147
Cdd:PLN02694 235 EGAKIGAGSVVLIDVPPRTTAVGNPARLV 263
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 6-145 7.92e-09

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 53.11  E-value: 7.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496   6 CAVRDVIYGTNVrIVKPVNIYE-------C------------ELRDNVFVGPFVEIQKGCvIGSGSRIQSHTFIcENVTL 66
Cdd:PRK09451 296 CVLKNCVIGDDC-EISPYSVVEdanlgaaCtigpfarlrpgaELAEGAHVGNFVEMKKAR-LGKGSKAGHLTYL-GDAEI 372

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  67 GENCFIGHNVTFANdlfRSGApdpspdNWISITLGDSVTVGSGAIILSPY-ICSGAVIGAGSVVVKPI-ENKGIYAGNPA 144
Cdd:PRK09451 373 GDNVNIGAGTITCN---YDGA------NKFKTIIGDDVFVGSDTQLVAPVtVGKGATIGAGTTVTRDVaENELVISRVPQ 443


                 .
gi 535274496 145 R 145
Cdd:PRK09451 444 R 444
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 10-112 1.24e-08

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 51.25  E-value: 1.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  10 DVIYGTNVRIVKPVNIYE-CELRDNVFVGPFVEIQKGCVIGSGSRIQSHTFICENVTLGENCFIGHNVTFANDLFrsgAP 88
Cdd:cd03352    1 SAKIGENVSIGPNAVIGEgVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIGSDGF---GF 77

                         90       100       110
                 ....*....|....*....|....*....|
gi 535274496  89 DPSPDNWISI------TLGDSVTVGSGAII 112
Cdd:cd03352   78 APDGGGWVKIpqlggvIIGDDVEIGANTTI 107
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 64-148 5.10e-08

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 50.00  E-value: 5.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  64 VTLGENCFIGHNVTFA-------NDLFRSGAPDPSPdnwisITLGDSVTVGSgAIILSPYICSG--AVIGAGSVVVKPIE 134
Cdd:PRK09527  96 VTIGDNVLIAPNVTLSvtghpvhHELRKNGEMYSFP-----ITIGNNVWIGS-HVVINPGVTIGdnSVIGAGSVVTKDIP 169

                         90
                 ....*....|....
gi 535274496 135 NKGIYAGNPARLLR 148
Cdd:PRK09527 170 PNVVAAGVPCRVIR 183
PLN02739 PLN02739
serine acetyltransferase
 36-150 6.07e-08

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 50.42  E-value: 6.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  36 VGPFVEIQKGCVIGSGSRIqshtFICENVTLGENCFIGHNVTFANDLFRSGAPDPSpdnwisitLGDSVTVGSGAIILSP 115
Cdd:PLN02739 208 IHPAARIGKGILLDHGTGV----VIGETAVIGDRVSILHGVTLGGTGKETGDRHPK--------IGDGALLGACVTILGN 275

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 535274496 116 Y-ICSGAVIGAGSVVVKPIENKGIYAGNPARLLRIL 150
Cdd:PLN02739 276 IsIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFV 311
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 29-77 7.09e-08

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: 49.63  E-value: 7.09e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 535274496  29 ELRDNVFVGPFVEIQKGCVIGSGSRIQSHTFICENVTLGENCFIGHNVT 77
Cdd:COG1043   15 KLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFAS 63
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 27-136 2.03e-07

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: 47.80  E-value: 2.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  27 ECELRDNVFVGPFVEIqKGCVIGSGSRIQSHTFIcENVTLGENCFIGHNVTFAN----DLFRSgapdpspdnwisiTLGD 102
Cdd:cd03353   85 GTVLGEGVHIGNFVEI-KKSTIGEGSKANHLSYL-GDAEIGEGVNIGAGTITCNydgvNKHRT-------------VIGD 149

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 535274496 103 SVTVGSGAIILSPY-ICSGAVIGAGSVVVKPIENK 136
Cdd:cd03353  150 NVFIGSNSQLVAPVtIGDGATIAAGSTITKDVPPG 184
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 29-147 2.55e-07

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


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 46.06  E-value: 2.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  29 ELRDNVFVGPFVEI--QKGCVIGSGSRIQSHTFICENvtlgencfiGHNvtFANDLFRSGAPdpspdnwiSITLGDSVTV 106
Cdd:cd05825    5 TIGDNSWIGEGVWIynLAPVTIGSDACISQGAYLCTG---------SHD--YRSPAFPLITA--------PIVIGDGAWV 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 535274496 107 GSGAIILsP--YICSGAVIGAGSVVVKPIENKGIYAGNPARLL 147
Cdd:cd05825   66 AAEAFVG-PgvTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
39-146 3.12e-07

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 47.79  E-value: 3.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  39 FVEIQKGCVIGSG-SRIQSHTFICENVTLGENCFIGHNVTFANdlfrsgapdpspdnwiSITLGDSVTVGSGAII--LSP 115
Cdd:PRK05289  92 FVTINRGTVQGGGvTRIGDNNLLMAYVHVAHDCVVGNHVILAN----------------NATLAGHVEVGDYAIIggLTA 155

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 535274496 116 -----YICSGAVIGAGSVVVKPIENKGIYAGNPARL 146
Cdd:PRK05289 156 vhqfvRIGAHAMVGGMSGVSQDVPPYVLAEGNPARL 191
PLN02296 PLN02296
carbonate dehydratase
 33-150 3.51e-07

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 47.81  E-value: 3.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  33 NVFVGPFVEIQKGCV---------IGSGSRIQSH----------------TFICENVTLGENCFIgHNVTFANDLFrsga 87
Cdd:PLN02296  70 DVQVGRGSSIWYGCVlrgdvnsisVGSGTNIQDNslvhvaktnlsgkvlpTIIGDNVTIGHSAVL-HGCTVEDEAF---- 144

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 535274496  88 pdpspdnwisitlgdsvtVGSGAIILS-PYICSGAVIGAGSVVVKP--IENKGIYAGNPARLLRIL 150
Cdd:PLN02296 145 ------------------VGMGATLLDgVVVEKHAMVAAGALVRQNtrIPSGEVWAGNPAKFLRKL 192
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 14-141 5.86e-07

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 47.62  E-value: 5.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  14 GTNVRIVKPVnIYECELRDNVFVGPFVEIQKGCVIGSGSRIQSHTFIcENVTLGENCFIGHnVTFANDlfrsgapdpspd 93
Cdd:PRK14360 301 GENVTVLYSV-VSDSQIGDGVKIGPYAHLRPEAQIGSNCRIGNFVEI-KKSQLGEGSKVNH-LSYIGD------------ 365

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  94 nwisITLGDSVTVGSGAIILSpY---------ICSGAVIGAGSVVVKPI---ENKGIYAG 141
Cdd:PRK14360 366 ----ATLGEQVNIGAGTITAN-YdgvkkhrtvIGDRSKTGANSVLVAPItlgEDVTVAAG 420
PRK10502 PRK10502
putative acyl transferase; Provisional
 42-148 5.99e-07

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 46.48  E-value: 5.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  42 IQKGCVIGSGSRIQ--------SHTFICENV--------TLGENCFIGHNVTFAndlfrSGAPDPSPDNW----ISITLG 101
Cdd:PRK10502  54 IGKGVVIRPSVRITypwkltigDYAWIGDDVwlynlgeiTIGAHCVISQKSYLC-----TGSHDYSDPHFdlntAPIVIG 128

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 535274496 102 DSVTVGSGAIIlSP--YICSGAVIGAGSVVVKPIENKGIYAGNPARLLR 148
Cdd:PRK10502 129 EGCWLAADVFV-APgvTIGSGAVVGARSSVFKSLPANTICRGNPAVPIR 176
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 29-77 9.03e-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: 46.66  E-value: 9.03e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 535274496  29 ELRDNVFVGPFVEIQKGCVIGSGSRIQSHTFICENVTLGENCFIGHNVT 77
Cdd:cd03351   13 KIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFAS 61
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
29-72 1.74e-06

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 45.86  E-value: 1.74e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 535274496  29 ELRDNVFVGPFVEIQKGCVIGSGSRIQSHTFICENVTLGENCFI 72
Cdd:PRK05289  16 KIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRI 59
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 30-149 9.59e-06

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 43.33  E-value: 9.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  30 LRDNVFVGPFVEIQKGCVIGSGSRIQShtfiCENVTLGENCFIG---------HNVTFANDLFRSGA--PDPSPDNWISI 98
Cdd:PRK09677  56 LRLDAFGRGKLFFGDNVQVNDYVHIAC----IESITIGRDTLIAskvfitdhnHGSFKHSDDFSSPNlpPDMRTLESSAV 131

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 535274496  99 TLGDSVTVGSGAIIL-SPYICSGAVIGAGSVVVKPIENKGIYAGNPARLLRI 149
Cdd:PRK09677 132 VIGQRVWIGENVTILpGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKK 183
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 8-133 1.19e-05

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 43.60  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496   8 VRDVIYGTNVRIVKPvniyECE---LRDNVFVGPFVEIQKGCVIGSGSRIQSHTFIcENVTLGENCFIGHnVTFANDlfr 84
Cdd:PRK14357 288 IVDCEIGNNVKIIRS----ECEksvIEDDVSVGPFSRLREGTVLKKSVKIGNFVEI-KKSTIGENTKAQH-LTYLGD--- 358

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 535274496  85 sgapdpspdnwisITLGDSVTVGSGAIILS--------PYICSGAVIGAGSVVVKPI 133
Cdd:PRK14357 359 -------------ATVGKNVNIGAGTITCNydgkkknpTFIEDGAFIGSNSSLVAPV 402
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 27-131 1.99e-05

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: 43.09  E-value: 1.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  27 ECELRDNVFVGPFVEIqKGCVIGSGSRIQSHTFIcENVTLGENCFIGHNVTFAN----DLFRSgapdpspdnwisiTLGD 102
Cdd:COG1207  335 GTVLGEGVKIGNFVEV-KNSTIGEGSKVNHLSYI-GDAEIGEGVNIGAGTITCNydgvNKHRT-------------VIGD 399

                         90       100       110
                 ....*....|....*....|....*....|
gi 535274496 103 SVTVGSGAIILSPY-ICSGAVIGAGSVVVK 131
Cdd:COG1207  400 GAFIGSNTNLVAPVtIGDGATIGAGSTITK 429
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 29-134 2.51e-05

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 42.93  E-value: 2.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  29 ELRDNVFVGPFVEIQKGcVIGSGSRIQSHTFIcENVTLGENCFIGHNVTFAN-DLFrsgapdpspdNWISITLGDSVTVG 107
Cdd:PRK14353 323 ELGEGAKVGNFVEVKNA-KLGEGAKVNHLTYI-GDATIGAGANIGAGTITCNyDGF----------NKHRTEIGAGAFIG 390

                         90       100
                 ....*....|....*....|....*...
gi 535274496 108 SGAIILSPY-ICSGAVIGAGSVVVKPIE 134
Cdd:PRK14353 391 SNSALVAPVtIGDGAYIASGSVITEDVP 418
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 47-129 2.54e-05

eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 40.25  E-value: 2.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  47 VIGSGSRIQSHTFIcENVTLGENCFIGHNVTFANDLfrsgapdpspdnwisitLGDSVTVGSGAIILSPYICSGAVIGAG 126
Cdd:cd05787    1 VIGRGTSIGEGTTI-KNSVIGRNCKIGKNVVIDNSY-----------------IWDDVTIEDGCTIHHSIVADGAVIGKG 62


                 ...
gi 535274496 127 SVV 129
Cdd:cd05787   63 CTI 65
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 26-150 2.72e-05

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 42.11  E-value: 2.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  26 YECELRDNVFVGPFVEIQKGCVIGSgsriqshtfICEnVTLGENCFIG---HNVTFANDL----FRSGAPDPSPdnwisI 98
Cdd:PRK10092  66 FRCDYGYNIFLGNNFYANFDCVMLD---------VCP-IRIGDNCMLApgvHIYTATHPLdpvaRNSGAELGKP-----V 130

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 535274496  99 TLGDSVTVGSGAIIlSPYICSG--AVIGAGSVVVKPIENKGIYAGNPARLLRIL 150
Cdd:PRK10092 131 TIGNNVWIGGRAVI-NPGVTIGdnVVVASGAVVTKDVPDNVVVGGNPARIIKKL 183
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 45-144 4.81e-05

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 42.05  E-value: 4.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496   45 GCVIGSGSRIQShTFICEN--VTLGENCFIGHNVTFANDLFRSGAPDPSpdnwiSITLGDSVTVGSGAIIL-SPYICSGA 121
Cdd:TIGR02353 597 GVKIGRGVYIDG-TDLTERdlVTIGDDSTLNEGSVIQTHLFEDRVMKSD-----TVTIGDGATLGPGAIVLyGVVMGEGS 670

                          90       100
                  ....*....|....*....|....*
gi 535274496  122 VIGAGSVVVK--PIENKGIYAGNPA 144
Cdd:TIGR02353 671 VLGPDSLVMKgeEVPAHTRWRGNPA 695
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 40-129 4.84e-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: 39.54  E-value: 4.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  40 VEIQKGCVIGSGSRIQSHTFICENVTLGENCFIgHNVTFANDLFrsgapdpspdnwiSITLGDSVTVGSGAIILSP-YIC 118
Cdd:cd00208    1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVI-GAATGPNEKN-------------PTIIGDNVEIGANAVIHGGvKIG 66

                         90
                 ....*....|.
gi 535274496 119 SGAVIGAGSVV 129
Cdd:cd00208   67 DNAVIGAGAVV 77
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 10-148 5.68e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 41.66  E-value: 5.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  10 DVIYGTNVRIVKPVNIYE-CELRDNVFVGPFVEIQKGCVIGSGSRIQShtficeNVTLGENCFIGHNVT----------- 77
Cdd:PRK00892 112 SAKIGEGVSIGPNAVIGAgVVIGDGVVIGAGAVIGDGVKIGADCRLHA------NVTIYHAVRIGNRVIihsgavigsdg 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  78 --FANDlfrSGAPDPSP-----------------------------------DNWISI---------------------- 98
Cdd:PRK00892 186 fgFAND---RGGWVKIPqlgrviigddveiganttidrgalddtvigegvkiDNLVQIahnvvigrhtaiaaqvgiagst 262

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 535274496  99 TLGDSVTVGSGAII---LSpyICSGAVIGAGSVVVKPIENKGIY-AGNPARLLR 148
Cdd:PRK00892 263 KIGRYCMIGGQVGIaghLE--IGDGVTITAMSGVTKSIPEPGEYsSGIPAQPNK 314
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 8-131 5.69e-05

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 41.74  E-value: 5.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496   8 VRDVIYGTNVRIVKPVnIYECELRDNVFVGP------------------FVEIqKGCVIGSGSRIqSH-TFIcENVTLGE 68
Cdd:PRK14354 298 IVDSTIGDGVTITNSV-IEESKVGDNVTVGPfahlrpgsvigeevkignFVEI-KKSTIGEGTKV-SHlTYI-GDAEVGE 373

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 535274496  69 NCFIGHNVTFAN----DLFRSgapdpspdnwisiTLGDSVTVGSGAIILSPY-ICSGAVIGAGSVVVK 131
Cdd:PRK14354 374 NVNIGCGTITVNydgkNKFKT-------------IIGDNAFIGCNSNLVAPVtVGDNAYIAAGSTITK 428
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 63-148 7.85e-05

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 40.40  E-value: 7.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  63 NVTLGENCFIGHNVTFANDLfrsgapdpspdNWISI--------------------TLGDSVTVGSGAIILSPYI----- 117
Cdd:COG0663   28 DVTIGEDVSVWPGAVLRGDV-----------GPIRIgegsniqdgvvlhvdpgyplTIGDDVTIGHGAILHGCTIgdnvl 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 535274496 118 -------CSGAVIGAGSVV-----VKP---IENKGIYAGNPARLLR 148
Cdd:COG0663   97 igmgaivLDGAVIGDGSIVgagalVTEgkvVPPGSLVVGSPAKVVR 142
cysE PRK11132
serine acetyltransferase; Provisional
 45-146 8.90e-05

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 40.84  E-value: 8.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  45 GCVIGSGSRIQSHTFICENVTLGencfighnvtfandlfrsGAPDPSPDNWISITLGdsVTVGSGAIILSPY-ICSGAVI 123
Cdd:PRK11132 161 GIVIGETAVIENDVSILQSVTLG------------------GTGKTSGDRHPKIREG--VMIGAGAKILGNIeVGRGAKI 220

                         90       100
                 ....*....|....*....|...
gi 535274496 124 GAGSVVVKPIENKGIYAGNPARL 146
Cdd:PRK11132 221 GAGSVVLQPVPPHTTAAGVPARI 243
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 32-126 1.78e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 40.20  E-value: 1.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  32 DNVFVGPFVEIQKGCVIGSGSRIQSHTFICENVTLG-----ENCFIGHNVTFANDLFrsgapdpspdnwISITLGDSVTV 106
Cdd:PRK14354 258 ESTYIDADVEIGSDTVIEPGVVIKGNTVIGEDCVIGpgsriVDSTIGDGVTITNSVI------------EESKVGDNVTV 325

                         90       100
                 ....*....|....*....|
gi 535274496 107 GSGAiilspYICSGAVIGAG 126
Cdd:PRK14354 326 GPFA-----HLRPGSVIGEE 340
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 27-76 1.94e-04

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 40.30  E-value: 1.94e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 535274496  27 ECELRDNVFVGPFVEIQKGCVIGSGSRIQSHTFIcENVTLGENCFIGHNV 76
Cdd:PRK14360 262 TVELGPDVIIEPQTHLRGNTVIGSGCRIGPGSLI-ENSQIGENVTVLYSV 310
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 32-129 3.36e-04

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 38.94  E-value: 3.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  32 DNVFVGPFVEIQKGCVIGSGSRIQSHTFICENVTLGENCFIGhnvtfandlfrsgapdpspdnwisitlgdSVTVGSGAI 111
Cdd:cd03353    8 ETTYIDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIK-----------------------------DSTIGDGVV 58

                         90
                 ....*....|....*...
gi 535274496 112 ILSPYICSGAVIGAGSVV 129
Cdd:cd03353   59 IKASSVIEGAVIGNGATV 76
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 29-72 5.39e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 38.85  E-value: 5.39e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 535274496  29 ELRDNVFVGPFVEIQKGCVIGSGSRIQSHTFICENVTLGENCFI 72
Cdd:PRK12461  13 KLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKI 56
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 31-130 1.49e-03

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


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 36.59  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  31 RDNVFVGP--------FVEIqkGCVIGSGSRIQSHTFICENVTLGENCFIGHNVTFANDLfrsgapdpSPDNWISITLGD 102
Cdd:cd03350   11 RDGAFIGPgavlmmpsYVNI--GAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVIGGVL--------EPLQATPVIIED 80

                         90       100
                 ....*....|....*....|....*....
gi 535274496 103 SVTVGSGAIILSPYIC-SGAVIGAGSVVV 130
Cdd:cd03350   81 DVFIGANCEVVEGVIVgKGAVLAAGVVLT 109
PRK10191 PRK10191
putative acyl transferase; Provisional
 41-146 1.49e-03

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 36.79  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  41 EIQKGCVIGSGSRIQsHTF---ICENVTLGENCFIGHNVTFANDlfrsgapdpSPDNWISITLGDSVTVGSGAIILSPY- 116
Cdd:PRK10191  43 EIQAAATIGRRFTIH-HGYavvINKNVVAGDDFTIRHGVTIGNR---------GADNMACPHIGNGVELGANVIILGDIt 112

                         90       100       110
                 ....*....|....*....|....*....|
gi 535274496 117 ICSGAVIGAGSVVVKPIENKGIYAGNPARL 146
Cdd:PRK10191 113 IGNNVTVGAGSVVLDSVPDNALVVGEKARV 142
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 32-150 1.97e-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: 36.58  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  32 DNVFVGPFVEIQ---KGCVIGSGSRIQS----HTFICENVTLGENCFIGHNVTFandlfrSGApdpspdnwisiTLGDSV 104
Cdd:cd04745   23 KNCYIGPHASLRgdfGRIVIRDGANVQDncviHGFPGQDTVLEENGHIGHGAIL------HGC-----------TIGRNA 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 535274496 105 TVGSGAIILspyicSGAVIGAGSVV-----VKP---IENKGIYAGNPARLLRIL 150
Cdd:cd04745   86 LVGMNAVVM-----DGAVIGEESIVgamafVKAgtvIPPRSLIAGSPAKVIREL 134
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 28-136 3.23e-03

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 36.63  E-value: 3.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  28 CELRDNVFVGPFVEIQKG----------------CVIGSGSRIQSHTFIC----EN---VTLGENCFIGHNVTFAndlfr 84
Cdd:PRK14356 340 AVLEEGARVGNFVEMKKAvlgkgakanhltylgdAEIGAGANIGAGTITCnydgVNkhrTVIGEGAFIGSNTALV----- 414

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 535274496  85 sgAPdpspdnwisitlgdsVTVGSGAIIlspyicsgaviGAGSVVVKPIENK 136
Cdd:PRK14356 415 --AP---------------VTIGDGALV-----------GAGSVITKDVPDG 438
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 47-130 3.67e-03

Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 34.52  E-value: 3.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  47 VIGSGSRIQSHTFIcENVTLGENCFIGHNVTFANdlfrsgapdpspdnwiSItLGDSVTVGSGAIILSPYICSGAVIGAG 126
Cdd:cd03356    1 LIGESTVIGENAII-KNSVIGDNVRIGDGVTITN----------------SI-LMDNVTIGANSVIVDSIIGDNAVIGEN 62


                 ....
gi 535274496 127 SVVV 130
Cdd:cd03356   63 VRVV 66
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 17-129 3.81e-03

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 36.54  E-value: 3.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  17 VRIVKPvniyecelrDNVFVGPFVEIQKGCVIGSGSRIQSHTFICENVTLGENCFIghnvtfandlfrsgapdpspdnwi 96
Cdd:COG1207  253 VTIIDP---------ATTYIDGDVEIGRDVVIDPNVILEGKTVIGEGVVIGPNCTL------------------------ 299

                         90       100       110
                 ....*....|....*....|....*....|...
gi 535274496  97 sitlgDSVTVGSGAIILSPYIcSGAVIGAGSVV 129
Cdd:COG1207  300 -----KDSTIGDGVVIKYSVI-EDAVVGAGATV 326
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 4-73 6.97e-03

Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 33.75  E-value: 6.97e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496   4 MECAVRDVIYGTNVRIVKPVNIYECELRDNVFVGPFVEIqKGCVIGSGSRIQSHTFICENVTLGENCFIG 73
Cdd:cd03356   10 ENAIIKNSVIGDNVRIGDGVTITNSILMDNVTIGANSVI-VDSIIGDNAVIGENVRVVNLCIIGDDVVVE 78
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 36-75 7.40e-03

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: 34.87  E-value: 7.40e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 535274496  36 VGPFVEIQKGCVIGSGSRIQSHTFICENVTLGENCFIGHN 75
Cdd:cd05636    8 VEEGVTIKGPVWIGEGAIVRSGAYIEGPVIIGKGCEIGPN 47
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 16-112 7.40e-03

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: 34.87  E-value: 7.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535274496  16 NVRIVKPVNIYEcelrdNVFVGPFVEIQKGCVIGSGSRIQSHTFICENVTLGENCFIGHNVTFANDLFRSGAPDPSPdNW 95
Cdd:cd05636   11 GVTIKGPVWIGE-----GAIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSIIMDGTKVPHL-NY 84

                         90
                 ....*....|....*....
gi 535274496  96 I--SItLGDSVTVGSGAII 112
Cdd:cd05636   85 VgdSV-LGENVNLGAGTIT 102
 
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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