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Conserved domains on  [gi|1120757468|gb|APP07902|]
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dTDP-6-deoxy-3,4-keto-hexulose isomerase [Vibrio harveyi]

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 ...
 39-156 1.31e-63

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: 190.79  E-value: 1.31e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  39 IGSNCNICAHTLIENDVVIGDDVTIKSGVYVWDGITIEDGAFIGPSVVFSNDKYPRSKVYP-EKFMRTLVQRGASIGANA 117
Cdd:cd03358     1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKIYRkWELKGTTVKRGASIGANA 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1120757468 118 TILPGITIGERSMVGAGAVVTKDVPSKAIVMGNPAKVVG 156
Cdd:cd03358    81 TILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 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 ...
 39-156 1.31e-63

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: 190.79  E-value: 1.31e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  39 IGSNCNICAHTLIENDVVIGDDVTIKSGVYVWDGITIEDGAFIGPSVVFSNDKYPRSKVYP-EKFMRTLVQRGASIGANA 117
Cdd:cd03358     1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKIYRkWELKGTTVKRGASIGANA 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1120757468 118 TILPGITIGERSMVGAGAVVTKDVPSKAIVMGNPAKVVG 156
Cdd:cd03358    81 TILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
36-158 1.94e-37

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 124.98  E-value: 1.94e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  36 NAVIGSNCNICAHTLIE-NDVVIGDDVTIKSGVYVWD--GITIEDGAFIGPSVVFSNDKYPRSKV--YPEKFMRTLVQRG 110
Cdd:COG0110     8 GARIGDGVVIGPGVRIYgGNITIGDNVYIGPGVTIDDpgGITIGDNVLIGPGVTILTGNHPIDDPatFPLRTGPVTIGDD 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1120757468 111 ASIGANATILPGITIGERSMVGAGAVVTKDVPSKAIVMGNPAKVVGYV 158
Cdd:COG0110    88 VWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKR 135
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 31-152 1.71e-25

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: 96.41  E-value: 1.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  31 SIIFANAVIGSNCNICAHTLIENDVVIGDDVTIKSGVYVWDGITIEDGAFIGPSVVFSNDkyprskvypekfmrTLVQRG 110
Cdd:TIGR03570  94 AIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGG--------------VVIGEG 159

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1120757468 111 ASIGANATILPGITIGERSMVGAGAVVTKDVPSKAIVMGNPA 152
Cdd:TIGR03570 160 VFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
PLN02739 PLN02739
serine acetyltransferase
 55-158 2.65e-15

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 71.61  E-value: 2.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  55 VVIGDDVTIKSGVYVWDGITIedgafiGPSVVFSNDKYPRskvypekfmrtlVQRGASIGANATILPGITIGERSMVGAG 134
Cdd:PLN02739  226 VVIGETAVIGDRVSILHGVTL------GGTGKETGDRHPK------------IGDGALLGACVTILGNISIGAGAMVAAG 287

                          90       100
                  ....*....|....*....|....
gi 1120757468 135 AVVTKDVPSKAIVMGNPAKVVGYV 158
Cdd:PLN02739  288 SLVLKDVPSHSMVAGNPAKLIGFV 311
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
54-83 2.88e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.85  E-value: 2.88e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1120757468  54 DVVIGDDVTIKSGVYVWDGITIEDGAFIGP 83
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 39-156 1.31e-63

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: 190.79  E-value: 1.31e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  39 IGSNCNICAHTLIENDVVIGDDVTIKSGVYVWDGITIEDGAFIGPSVVFSNDKYPRSKVYP-EKFMRTLVQRGASIGANA 117
Cdd:cd03358     1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTNDLYPRSKIYRkWELKGTTVKRGASIGANA 80

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1120757468 118 TILPGITIGERSMVGAGAVVTKDVPSKAIVMGNPAKVVG 156
Cdd:cd03358    81 TILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
36-158 1.94e-37

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 124.98  E-value: 1.94e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  36 NAVIGSNCNICAHTLIE-NDVVIGDDVTIKSGVYVWD--GITIEDGAFIGPSVVFSNDKYPRSKV--YPEKFMRTLVQRG 110
Cdd:COG0110     8 GARIGDGVVIGPGVRIYgGNITIGDNVYIGPGVTIDDpgGITIGDNVLIGPGVTILTGNHPIDDPatFPLRTGPVTIGDD 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1120757468 111 ASIGANATILPGITIGERSMVGAGAVVTKDVPSKAIVMGNPAKVVGYV 158
Cdd:COG0110    88 VWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKR 135
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 54-155 2.20e-26

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: 95.99  E-value: 2.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  54 DVVIGDDVTIKSGVYVWD--GITIEDGAFIGPSVVFSN-----DKYPRSKVYPEKFMRTLVQRGASIGANATILPGITIG 126
Cdd:cd04647     1 NISIGDNVYIGPGCVISAggGITIGDNVLIGPNVTIYDhnhdiDDPERPIEQGVTSAPIVIGDDVWIGANVVILPGVTIG 80

                          90       100
                  ....*....|....*....|....*....
gi 1120757468 127 ERSMVGAGAVVTKDVPSKAIVMGNPAKVV 155
Cdd:cd04647    81 DGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 31-151 4.37e-26

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: 97.56  E-value: 4.37e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  31 SIIFANAVIGSNCNICAHTLIENDVVIGDDVTIKSGVYVWDGITIEDGAFIGPSVVFSNDkyprskvypekfmrTLVQRG 110
Cdd:cd03360    91 AVVSPSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGG--------------VTIGEG 156

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1120757468 111 ASIGANATILPGITIGERSMVGAGAVVTKDVPSKAIVMGNP 151
Cdd:cd03360   157 AFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 31-152 1.71e-25

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: 96.41  E-value: 1.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  31 SIIFANAVIGSNCNICAHTLIENDVVIGDDVTIKSGVYVWDGITIEDGAFIGPSVVFSNDkyprskvypekfmrTLVQRG 110
Cdd:TIGR03570  94 AIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGG--------------VVIGEG 159

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1120757468 111 ASIGANATILPGITIGERSMVGAGAVVTKDVPSKAIVMGNPA 152
Cdd:TIGR03570 160 VFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 57-155 5.94e-23

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: 88.63  E-value: 5.94e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  57 IGDDVTIKSGVYVWDG--ITIEDGAFIGPSVVFSNDKYPrskVYPEKfMRTLVQRGAS--------IGANATILPGITIG 126
Cdd:cd03357    65 IGDNFYANFNCTILDVapVTIGDNVLIGPNVQIYTAGHP---LDPEE-RNRGLEYAKPitigdnvwIGGGVIILPGVTIG 140

                          90       100
                  ....*....|....*....|....*....
gi 1120757468 127 ERSMVGAGAVVTKDVPSKAIVMGNPAKVV 155
Cdd:cd03357   141 DNSVIGAGSVVTKDIPANVVAAGNPARVI 169
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 3-155 1.12e-19

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 80.46  E-value: 1.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468   3 QLGQNMFIHELS----DVKsnaIGEDTRVWQFSII---FANAVIGSNCNI----CAHTLIENDVVIGDDVTIKSGVYVwD 71
Cdd:COG0663    12 QIHPSAFVAPTAvvigDVT---IGEDVSVWPGAVLrgdVGPIRIGEGSNIqdgvVLHVDPGYPLTIGDDVTIGHGAIL-H 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  72 GITIEDGAFIGpsvvfsndkyprskvypekfMrtlvqrgasigaNATILPGITIGERSMVGAGAVVT--KDVPSKAIVMG 149
Cdd:COG0663    88 GCTIGDNVLIG--------------------M------------GAIVLDGAVIGDGSIVGAGALVTegKVVPPGSLVVG 135


                  ....*.
gi 1120757468 150 NPAKVV 155
Cdd:COG0663   136 SPAKVV 141
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 113-157 9.42e-19

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: 77.20  E-value: 9.42e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1120757468 113 IGANATILPGITIGERSMVGAGAVVTKDVPSKAIVMGNPAKVVGY 157
Cdd:cd03349    82 IGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRY 126
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 55-156 2.65e-18

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


Pssm-ID: 440667 [Multi-domain]  Cd Length: 174  Bit Score: 77.05  E-value: 2.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  55 VVIGDDVTIKSGVyvwdgiTIedgafiGPSVVFSNDKYPRskvypekfmrtlVQRGASIGANATILPGITIGERSMVGAG 134
Cdd:COG1045    92 AVIGDNVTIYQGV------TL------GGTGKEKGKRHPT------------IGDNVVIGAGAKILGPITIGDNAKIGAN 147

                          90       100
                  ....*....|....*....|..
gi 1120757468 135 AVVTKDVPSKAIVMGNPAKVVG 156
Cdd:COG1045   148 SVVLKDVPPGSTVVGVPARIVK 169
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 3-155 3.37e-18

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: 75.91  E-value: 3.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468   3 QLGQNMFIHELSDVKSNA-IGEDTRVWQFSII---FANAVIGSNCNI----CAHTLIENDVVIGDDVTIKSGVYVwDGIT 74
Cdd:cd04645     1 EIDPSAFIAPNATVIGDVtLGEGSSVWFGAVLrgdVNPIRIGERTNIqdgsVLHVDPGYPTIIGDNVTVGHGAVL-HGCT 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  75 IEDGAFIGPsvvfsndkyprskvypekfmrtlvqrgasigaNATILPGITIGERSMVGAGAVVT--KDVPSKAIVMGNPA 152
Cdd:cd04645    80 IGDNCLIGM--------------------------------GAIILDGAVIGKGSIVAAGSLVPpgKVIPPGSLVAGSPA 127


                  ...
gi 1120757468 153 KVV 155
Cdd:cd04645   128 KVV 130
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 39-155 2.31e-16

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: 69.94  E-value: 2.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  39 IGSNCNICAHTLIEN--DVVIGDDVTIKSGVYVWDG---ITIEDGAFIGPSVVfsndkyprskvypekfmrtlVQRGASI 113
Cdd:cd05825     6 IGDNSWIGEGVWIYNlaPVTIGSDACISQGAYLCTGshdYRSPAFPLITAPIV--------------------IGDGAWV 65

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1120757468 114 GANATILPGITIGERSMVGAGAVVTKDVPSKAIVMGNPAKVV 155
Cdd:cd05825    66 AAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 55-151 2.08e-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: 67.47  E-value: 2.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  55 VVIGDDVTIKSGVYVWDGITIedgafiGPSVVFSNDKYPRskvypekfmrtlVQRGASIGANATILPGITIGERSMVGAG 134
Cdd:cd03354    23 IVIGETAVIGDNCTIYQGVTL------GGKGKGGGKRHPT------------IGDNVVIGAGAKILGNITIGDNVKIGAN 84

                          90
                  ....*....|....*..
gi 1120757468 135 AVVTKDVPSKAIVMGNP 151
Cdd:cd03354    85 AVVTKDVPANSTVVGVP 101
PLN02739 PLN02739
serine acetyltransferase
 55-158 2.65e-15

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 71.61  E-value: 2.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  55 VVIGDDVTIKSGVYVWDGITIedgafiGPSVVFSNDKYPRskvypekfmrtlVQRGASIGANATILPGITIGERSMVGAG 134
Cdd:PLN02739  226 VVIGETAVIGDRVSILHGVTL------GGTGKETGDRHPK------------IGDGALLGACVTILGNISIGAGAMVAAG 287

                          90       100
                  ....*....|....*....|....
gi 1120757468 135 AVVTKDVPSKAIVMGNPAKVVGYV 158
Cdd:PLN02739  288 SLVLKDVPSHSMVAGNPAKLIGFV 311
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 18-153 7.03e-15

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 68.59  E-value: 7.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  18 SNAIGEDTRVWQFSIIFANAVIGSNCNICAHTLIENDVVIGDDVTIKSGVYVWDGITIEDGAFIGPSVV-----FSNDKY 92
Cdd:cd03352     1 SAKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVigsdgFGFAPD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  93 PRSKVYPEKFMRTLVQRGASIGANATI----------------------------------------------------- 119
Cdd:cd03352    81 GGGWVKIPQLGGVIIGDDVEIGANTTIdrgalgdtvigdgtkidnlvqiahnvrigencliaaqvgiagsttigdnviig 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1120757468 120 -----LPGITIGERSMVGAGAVVTKDVPSKAIVMGNPAK 153
Cdd:cd03352   161 gqvgiAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQ 199
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 33-155 1.08e-13

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 65.28  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  33 IFANAVI--GSNCNI--CAHTLIENDVVIGDDVTIKSGVYvwdgITIEDGAFIGPSVVFSNDKYPRSKvYPEKFMRTLVQ 108
Cdd:PRK09677   60 AFGRGKLffGDNVQVndYVHIACIESITIGRDTLIASKVF----ITDHNHGSFKHSDDFSSPNLPPDM-RTLESSAVVIG 134

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1120757468 109 RGASIGANATILPGITIGERSMVGAGAVVTKDVPSKAIVMGNPAKVV 155
Cdd:PRK09677  135 QRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKII 181
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 10-153 1.64e-13

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: 66.19  E-value: 1.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  10 IHELSDVKSNA-IGEDTRVWQFSIIFANAVIGSNCNICAHTLIENDVVIGDDVTIKSGVYVWDGITIEDGAFIGPSVV-- 86
Cdd:COG1044    99 IHPSAVIDPSAkIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVIGDRVIIHSGAVig 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  87 -----FSNDkyprskvyPEKFMRTLVQRGA-------SIGANATI----------------------------------- 119
Cdd:COG1044   179 adgfgFAPD--------EDGGWVKIPQLGRvvigddvEIGANTTIdrgalgdtvigdgtkidnlvqiahnvrigehtaia 250

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1120757468 120 ----------------LPG-------ITIGERSMVGAGAVVTKDVPSKAIVMGNPAK 153
Cdd:COG1044   251 aqvgiagstkigdnvvIGGqvgiaghLTIGDGVIIGAQSGVTKSIPEGGVYSGSPAQ 307
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 21-149 1.80e-13

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: 64.75  E-value: 1.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  21 IGEDTRVWQFSIIFANAVIGSNCNICAHTLIEnDVVIGDDVTIKSGVYVwDGITIEDGAFIGP-------SVVFSNDKY- 92
Cdd:cd03353    18 IGVDVVIDPGVILEGKTVIGEDCVIGPNCVIK-DSTIGDGVVIKASSVI-EGAVIGNGATVGPfahlrpgTVLGEGVHIg 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  93 -----------PRSKV----Y-----------------------PEKFmRTLVQRGASIGANATILPGITIGERSMVGAG 134
Cdd:cd03353    96 nfveikkstigEGSKAnhlsYlgdaeigegvnigagtitcnydgVNKH-RTVIGDNVFIGSNSQLVAPVTIGDGATIAAG 174

                         170
                  ....*....|....*
gi 1120757468 135 AVVTKDVPSKAIVMG 149
Cdd:cd03353   175 STITKDVPPGALAIA 189
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 55-155 5.31e-13

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 63.29  E-value: 5.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  55 VVIGDDVTIKSGVYVW------DGITIEDGAFIGPSVVFSNDKYprskvypekfmrtlvqrgasIGANATILPGITIGER 128
Cdd:PRK10092   94 IRIGDNCMLAPGVHIYtathplDPVARNSGAELGKPVTIGNNVW--------------------IGGRAVINPGVTIGDN 153

                          90       100
                  ....*....|....*....|....*..
gi 1120757468 129 SMVGAGAVVTKDVPSKAIVMGNPAKVV 155
Cdd:PRK10092  154 VVVASGAVVTKDVPDNVVVGGNPARII 180
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 21-149 2.80e-12

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: 63.12  E-value: 2.80e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  21 IGEDTRVWQFSIIFANAVIGSNCNICAHTLIEnDVVIGDDVTIKSGVYvwDGITIEDGAFIGP-------SVVFSNDKY- 92
Cdd:COG1207   269 IGRDVVIDPNVILEGKTVIGEGVVIGPNCTLK-DSTIGDGVVIKYSVI--EDAVVGAGATVGPfarlrpgTVLGEGVKIg 345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  93 -----------PRSKV----Y-----------------------PEKFmRTLVQRGASIGANATILPGITIGERSMVGAG 134
Cdd:COG1207   346 nfvevknstigEGSKVnhlsYigdaeigegvnigagtitcnydgVNKH-RTVIGDGAFIGSNTNLVAPVTIGDGATIGAG 424

                         170
                  ....*....|....*
gi 1120757468 135 AVVTKDVPSKAIVMG 149
Cdd:COG1207   425 STITKDVPAGALAIA 439
PLN02694 PLN02694
serine O-acetyltransferase
 55-156 3.97e-12

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 62.35  E-value: 3.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  55 VVIGDDVTIKSGVYVWDGITIedgafiGPSVVFSNDKYPRskvypekfmrtlVQRGASIGANATILPGITIGERSMVGAG 134
Cdd:PLN02694  181 VVIGETAVIGNNVSILHHVTL------GGTGKACGDRHPK------------IGDGVLIGAGATILGNVKIGEGAKIGAG 242

                          90       100
                  ....*....|....*....|..
gi 1120757468 135 AVVTKDVPSKAIVMGNPAKVVG 156
Cdd:PLN02694  243 SVVLIDVPPRTTAVGNPARLVG 264
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 7-146 1.04e-11

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 61.39  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468   7 NMFIHelSDVKsnaIGEDTRVWQFSIIFANAVIGSNCNICAHTLIEnDVVIGDDVTIKSGV----------------YVW 70
Cdd:PRK14354  259 STYID--ADVE---IGSDTVIEPGVVIKGNTVIGEDCVIGPGSRIV-DSTIGDGVTITNSVieeskvgdnvtvgpfaHLR 332

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  71 DGITIEDGAFIG------PSVVFSNDKYPR----------SKV----------YP--EKFmRTLVQRGASIGANATILPG 122
Cdd:PRK14354  333 PGSVIGEEVKIGnfveikKSTIGEGTKVSHltyigdaevgENVnigcgtitvnYDgkNKF-KTIIGDNAFIGCNSNLVAP 411

                         170       180
                  ....*....|....*....|....
gi 1120757468 123 ITIGERSMVGAGAVVTKDVPSKAI 146
Cdd:PRK14354  412 VTVGDNAYIAAGSTITKDVPEDAL 435
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 40-155 1.12e-11

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 60.02  E-value: 1.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  40 GSNCNICAHTLIENDVVIGDDVTIksgvyvwdgiTIEDGAFIGPSVVFSNDKYP---RSKVYPEKF-MRTLVQRGASIGA 115
Cdd:PRK09527   73 GSNIHIGRNFYANFNLTIVDDYTV----------TIGDNVLIAPNVTLSVTGHPvhhELRKNGEMYsFPITIGNNVWIGS 142

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1120757468 116 NATILPGITIGERSMVGAGAVVTKDVPSKAIVMGNPAKVV 155
Cdd:PRK09527  143 HVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVI 182
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 10-149 2.58e-11

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 60.51  E-value: 2.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  10 IHELSDVKSNAIGEDTRVWQFSIIfANAVIGSNCNICAH------TLIENDVVIGDDVTIKSGV-----------YVWDG 72
Cdd:PRK14356  296 IHSHCWLRDAVVSSGATIHSFSHL-EGAEVGDGCSVGPYarlrpgAVLEEGARVGNFVEMKKAVlgkgakanhltYLGDA 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  73 ItIEDGAFIGPSVVFSN----DKYprskvypekfmRTLVQRGASIGANATILPGITIGERSMVGAGAVVTKDVPSKAIVM 148
Cdd:PRK14356  375 E-IGAGANIGAGTITCNydgvNKH-----------RTVIGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSLAI 442


                  .
gi 1120757468 149 G 149
Cdd:PRK14356  443 A 443
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 55-138 2.74e-11

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: 56.10  E-value: 2.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  55 VVIGDDVTIKSGVYVWDGITIEDGAFIGPSVVFSNDKYPRSKVYPEkfmrtlVQRGASIGANATILPGITIGERSMVGAG 134
Cdd:cd00208     1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGPNEKNPTI------IGDNVEIGANAVIHGGVKIGDNAVIGAG 74


                  ....
gi 1120757468 135 AVVT 138
Cdd:cd00208    75 AVVT 78
PRK10502 PRK10502
putative acyl transferase; Provisional
 57-155 4.15e-11

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 58.04  E-value: 4.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  57 IGDDVTIKSGV---YVWDgITIEDGAFIGPSVVF--------------SNDKY-------PRSKVYPEKFMRTLVQRGAS 112
Cdd:PRK10502   54 IGKGVVIRPSVritYPWK-LTIGDYAWIGDDVWLynlgeitigahcviSQKSYlctgshdYSDPHFDLNTAPIVIGEGCW 132

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1120757468 113 IGANATILPGITIGERSMVGAGAVVTKDVPSKAIVMGNPAKVV 155
Cdd:PRK10502  133 LAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPI 175
PLN02357 PLN02357
serine acetyltransferase
 55-156 5.33e-11

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 59.51  E-value: 5.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  55 VVIGDDVTIKSGVYVWDGITIedgafiGPSVVFSNDKYPRskvypekfmrtlVQRGASIGANATILPGITIGERSMVGAG 134
Cdd:PLN02357  247 VVIGETAVVGNNVSILHNVTL------GGTGKQSGDRHPK------------IGDGVLIGAGTCILGNITIGEGAKIGAG 308

                          90       100
                  ....*....|....*....|..
gi 1120757468 135 AVVTKDVPSKAIVMGNPAKVVG 156
Cdd:PLN02357  309 SVVLKDVPPRTTAVGNPARLIG 330
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 8-156 3.08e-10

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: 56.57  E-value: 3.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468   8 MFIHELSDVKSNA-IGEDTRVWQFSIIFANAVIGSNCNICAHTLIEND------------------------------VV 56
Cdd:COG1043     2 AMIHPTAIVDPGAkLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPttigknnrifpfasigeepqdlkykgeptrLE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  57 IGDD------VTIKSGVYVWDGIT-IEDGAF------------IGPSVVFSNDKyprskvypekfmrTL-----VQRGAS 112
Cdd:COG1043    82 IGDNntirefVTIHRGTVQGGGVTrIGDDNLlmayvhvahdcvVGNNVILANNA-------------TLaghveVGDHAI 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1120757468 113 IGANATILPGITIGERSMVGAGAVVTKDVPSKAIVMGNPAKVVG 156
Cdd:COG1043   149 IGGLSAVHQFVRIGAHAMVGGGSGVVKDVPPYVLAAGNPARLRG 192
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-155 3.19e-10

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 57.25  E-value: 3.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468   3 QLGQNMFIHElSDVKSNAIGEDTRVWQFSIIFANAVIGSNCNICAHTLIENDVvIGDDVTIKSGVYVWDGiTIEDGAFIG 82
Cdd:PRK14360  299 QIGENVTVLY-SVVSDSQIGDGVKIGPYAHLRPEAQIGSNCRIGNFVEIKKSQ-LGEGSKVNHLSYIGDA-TLGEQVNIG 375

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1120757468  83 PSVVFSNdkYPRSKVYpekfmRTLVQRGASIGANATILPGITIGERSMVGAGAVVTKDVPSKAIVMGNPAKVV 155
Cdd:PRK14360  376 AGTITAN--YDGVKKH-----RTVIGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLAIARSRQVI 441
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 38-156 9.08e-10

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: 55.52  E-value: 9.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  38 VIGSNCNICAHTLIENDVVIGDDVTIKSGVYVWDGITIEDGAFigpsvvfsndkyprskvypekfmrtlvqrgasIGANA 117
Cdd:cd03351   104 RIGNNNLLMAYVHVAHDCVIGNNVILANNATLAGHVEIGDYAI--------------------------------IGGLS 151

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1120757468 118 TILPGITIGERSMVGAGAVVTKDVPSKAIVMGNPAKVVG 156
Cdd:cd03351   152 AVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARLRG 190
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 32-126 9.91e-10

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 55.53  E-value: 9.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  32 IIFANAVIGSNCNICAHTLIENDVVIGDDVTIKSGVYVWDGITIEDGAFIGPSVVfsndkyprskvypekfmrtlVQRGA 111
Cdd:PRK00892  108 VIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVT--------------------IYHAV 167

                          90
                  ....*....|....*
gi 1120757468 112 SIGANATILPGITIG 126
Cdd:PRK00892  168 RIGNRVIIHSGAVIG 182
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 3-156 3.04e-09

acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes LpxA, an enzyme for the biosynthesis of lipid A, a component oflipopolysaccharide (LPS) in the outer membrane outer leaflet of most Gram-negative bacteria. Some differences are found between lipid A of different species, but this protein represents the first step (from UDP-N-acetyl-D-glucosamine) and appears to be conserved in function. Proteins from this family contain many copies of the bacterial transferase hexapeptide repeat (pfam00132). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 53.80  E-value: 3.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468   3 QLGQNMFIHELSDVKSNA-IGEDTRVWQFSIIFANAVIGSNCNICAHTLIEND------------VVIGDDVTIKSGVYV 69
Cdd:TIGR01852  12 EIGENVEIGPFCIVGPGVkIGDGVELKSHVVILGHTTIGEGTRIFPGAVIGGVpqdlkykgektrLIIGDNNTIREFVTI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  70 WDGITIEDGA-------------------FIGPSVVFSNDKyprskvypekfmrTL---VQRG--ASIGANATILPGITI 125
Cdd:TIGR01852  92 NRGTASGGGVtrignnnllmayshiahdcVVGNHVILANNA-------------TLaghVEVGdyAIIGGLVAVHQFVRI 158

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1120757468 126 GERSMVGAGAVVTKDVPSKAIVMGNPAKVVG 156
Cdd:TIGR01852 159 GRYAMIGGLSAVSKDVPPYCLAEGNRARLRG 189
cysE PRK11132
serine acetyltransferase; Provisional
 51-156 3.43e-09

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 53.93  E-value: 3.43e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  51 IENDVVIGDDVTIksgvyvwDGITIEDGafigpsvvfsnDKYPRskvypekfmrtlVQRGASIGANATILPGITIGERSM 130
Cdd:PRK11132  170 IENDVSILQSVTL-------GGTGKTSG-----------DRHPK------------IREGVMIGAGAKILGNIEVGRGAK 219

                          90       100
                  ....*....|....*....|....*.
gi 1120757468 131 VGAGAVVTKDVPSKAIVMGNPAKVVG 156
Cdd:PRK11132  220 IGAGSVVLQPVPPHTTAAGVPARIVG 245
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 10-119 4.68e-09

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 53.60  E-value: 4.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  10 IHELSDVKSNA-IGEDTRVWQFSIIFANAVIGSNCNICAHTLIENDVVIGDDVTIKSGVYVWDGITIEDGAFIGPSVV-- 86
Cdd:PRK00892  103 IHPSAVIDPSAkIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVig 182

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1120757468  87 -----FSNDKYPRSKVypEKFMRTLVQRGASIGANATI 119
Cdd:PRK00892  183 sdgfgFANDRGGWVKI--PQLGRVIIGDDVEIGANTTI 218
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
6-156 6.52e-09

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 52.79  E-value: 6.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468   6 QNMFIHELSDVKSNA-IGEDTRVWQFSIIFANAVIGSNCNICAHTLIENDVVIGDD------------------------ 60
Cdd:PRK05289    1 MMAKIHPTAIVEPGAkIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNnrifpfasigedpqdlkykgeptr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  61 ------------VTIKSGVYVWDGIT-IEDGAF------------IGPSVVFSNdkyprskvypekfmrtlvqrGASIG- 114
Cdd:PRK05289   81 lvigdnntirefVTINRGTVQGGGVTrIGDNNLlmayvhvahdcvVGNHVILAN--------------------NATLAg 140

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1120757468 115 ----ANATILPGIT-------IGERSMVGAGAVVTKDVPSKAIVMGNPAKVVG 156
Cdd:PRK05289  141 hvevGDYAIIGGLTavhqfvrIGAHAMVGGMSGVSQDVPPYVLAEGNPARLRG 193
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 3-155 9.20e-09

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: 51.42  E-value: 9.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468   3 QLGQNMFIHELSDVKSNA-IGEDTRVWQFSIIFAN---AVIGSNCNICAHTLIEND----VVIGDDVTIKSGVYVwdgit 74
Cdd:cd04650     2 RISPKAYVHPTSYVIGDVvIGELTSVWHYAVIRGDndsIYIGKYSNVQENVSIHTDhgypTEIGDYVTIGHNAVV----- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  75 ieDGAFIGPSVVfsndkyprskvypekfmrtlvqrgasIGANATILPGITIGERSMVGAGAVVT--KDVPSKAIVMGNPA 152
Cdd:cd04650    77 --HGAKVGNYVI--------------------------VGMGAILLNGAKIGDHVIIGAGAVVTpgKEIPDYSLVLGVPA 128


                  ...
gi 1120757468 153 KVV 155
Cdd:cd04650   129 KVV 131
PLN02296 PLN02296
carbonate dehydratase
 21-153 1.20e-08

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 52.43  E-value: 1.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  21 IGEDTRVWQFSIIF--ANAV-IGSNCNICAHTLIE----------NDVVIGDDVTIKSGVyVWDGITIEDGAFIGpsvvf 87
Cdd:PLN02296   73 VGRGSSIWYGCVLRgdVNSIsVGSGTNIQDNSLVHvaktnlsgkvLPTIIGDNVTIGHSA-VLHGCTVEDEAFVG----- 146

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1120757468  88 sndkyprskvypekfmrtlvqrgasigANATILPGITIGERSMVGAGAVVTKD--VPSKAIVMGNPAK 153
Cdd:PLN02296  147 ---------------------------MGATLLDGVVVEKHAMVAAGALVRQNtrIPSGEVWAGNPAK 187
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 9-155 2.42e-08

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 51.69  E-value: 2.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468   9 FIHelSDVKsnaIGEDTRVWQFSIIFANAVIGSNCNI---------------------CAHTLIENDVVIGDDVTIKSGV 67
Cdd:PRK14357  251 YIH--YDVE---IGMDTIIYPMTFIEGKTRIGEDCEIgpmtrivdceignnvkiirseCEKSVIEDDVSVGPFSRLREGT 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  68 YVWDGITIEDGAFIGPSVVFSNDK--------------------------YPRSKVYPekfmrTLVQRGASIGANATILP 121
Cdd:PRK14357  326 VLKKSVKIGNFVEIKKSTIGENTKaqhltylgdatvgknvnigagtitcnYDGKKKNP-----TFIEDGAFIGSNSSLVA 400

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1120757468 122 GITIGERSMVGAGAVVTKDVPSKAIVMGNPAKVV 155
Cdd:PRK14357  401 PVRIGKGALIGAGSVITEDVPPYSLALGRARQIV 434
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 37-149 3.30e-08

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 51.40  E-value: 3.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  37 AVIGSNCNICAH------TLIENDVVIGDDVTIKSGV-----------YVWDGiTIEDGAFIGPSVVFSN----DKYprs 95
Cdd:PRK14353  304 AHVGEGAEVGPYarlrpgAELGEGAKVGNFVEVKNAKlgegakvnhltYIGDA-TIGAGANIGAGTITCNydgfNKH--- 379

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1120757468  96 kvypekfmRTLVQRGASIGANATILPGITIGERSMVGAGAVVTKDVPSKAIVMG 149
Cdd:PRK14353  380 --------RTEIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALG 425
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 55-155 1.17e-07

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: 48.52  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  55 VVIGDdVTIKSGVYV---------WDGITIEDGAFIGPSVVFS--NDKYPRSKVYPEKFMRTLVQ-----RGASIGANAT 118
Cdd:cd04745    14 VLIGD-VIIGKNCYIgphaslrgdFGRIVIRDGANVQDNCVIHgfPGQDTVLEENGHIGHGAILHgctigRNALVGMNAV 92

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1120757468 119 ILPGITIGERSMVGAGAVVTK--DVPSKAIVMGNPAKVV 155
Cdd:cd04745    93 VMDGAVIGEESIVGAMAFVKAgtVIPPRSLIAGSPAKVI 131
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 3-138 2.49e-07

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: 47.58  E-value: 2.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468   3 QLGQNMFIHELSDVKSNAIGEDTrvwqfSIIFANAVIGSNCNICAHTLIENDVVIGDDVTIKSGVyVWDGITIEDGAFIG 82
Cdd:cd05636    13 TIKGPVWIGEGAIVRSGAYIEGP-----VIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSI-IMDGTKVPHLNYVG 86

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1120757468  83 PSVV--------------FSNDKYPRSKVYPEKFMRT-------LVQRGASIGANATILPGITIGERSMVGAGAVVT 138
Cdd:cd05636    87 DSVLgenvnlgagtitanLRFDDKPVKVRLKGERVDTgrrklgaIIGDGVKTGINVSLNPGVKIGPGSWVYPGCVVR 163
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 39-152 2.73e-07

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 48.98  E-value: 2.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  39 IGSNCNICAHTLIENDVV-IGDDVTIKSGVyVWDGITIEDGAFigpsvvfsndkyprskvypeKFMRTLVQRGASIGANA 117
Cdd:TIGR02353 600 IGRGVYIDGTDLTERDLVtIGDDSTLNEGS-VIQTHLFEDRVM--------------------KSDTVTIGDGATLGPGA 658

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1120757468 118 TILPGITIGERSMVGAGAVVTK--DVPSKAIVMGNPA 152
Cdd:TIGR02353 659 IVLYGVVMGEGSVLGPDSLVMKgeEVPAHTRWRGNPA 695
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 32-126 2.76e-07

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: 45.65  E-value: 2.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  32 IIFANAVIGSNCNIcAHTLIENDVVIGDDVTIKsGVYVWDGITIEDGAFIGPSVVFSndkyprskvypekfmrtlvqrGA 111
Cdd:cd05787     1 VIGRGTSIGEGTTI-KNSVIGRNCKIGKNVVID-NSYIWDDVTIEDGCTIHHSIVAD---------------------GA 57

                          90
                  ....*....|....*
gi 1120757468 112 SIGANATILPGITIG 126
Cdd:cd05787    58 VIGKGCTIPPGSLIS 72
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 10-156 2.88e-07

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 48.48  E-value: 2.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  10 IHELSDVKSNA-IGEDTRVWQFSIIFANAVIGSNCNICAHTLIENDVVIGDDVTIKSGVYVWD----------------- 71
Cdd:PRK12461    2 IHPTAVIDPSAkLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGDepqdftykgeesrleig 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  72 -------GITIEDGAFIGPSVVFSNDKYprskvypekFM-------------RTLVQRGASIGANAT-----ILPGIT-- 124
Cdd:PRK12461   82 drnvireGVTIHRGTKGGGVTRIGNDNL---------LMayshvahdcqignNVILVNGALLAGHVTvgdraIISGNClv 152

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1120757468 125 -----IGERSMVGAGAVVTKDVPSKAIVMGNPAKVVG 156
Cdd:PRK12461  153 hqfcrIGALAMMAGGSRISKDVPPYCMMAGHPTNVHG 189
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 21-155 3.19e-07

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 48.59  E-value: 3.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  21 IGEDTRVWQFSIIFANAVIGSNCNICAHTLIEnDVVIGDDVTIKSGVyVWDGITIEDGAFIGPSVVFSNDKYPRSKVYPE 100
Cdd:PRK14355  271 IGRDTTIYPGVCISGDTRIGEGCTIEQGVVIK-GCRIGDDVTVKAGS-VLEDSVVGDDVAIGPMAHLRPGTELSAHVKIG 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468 101 KFMRT-------------LVQRG-ASIGANATILPG-------------------------------ITIGERSMVGAGA 135
Cdd:PRK14355  349 NFVETkkivmgegskashLTYLGdATIGRNVNIGCGtitcnydgvkkhrtvieddvfvgsdvqfvapVTVGRNSLIAAGT 428

                         170       180
                  ....*....|....*....|
gi 1120757468 136 VVTKDVPSKAIVMGNPAKVV 155
Cdd:PRK14355  429 TVTKDVPPDSLAIARSPQVN 448
PRK10191 PRK10191
putative acyl transferase; Provisional
 50-154 1.19e-06

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 45.65  E-value: 1.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  50 LIENDVVIGDDVTIKSGVYVwdgitiedgafigpsvvfsNDKYPRSKVYPekfmrtLVQRGASIGANATILPGITIGERS 129
Cdd:PRK10191   63 VINKNVVAGDDFTIRHGVTI-------------------GNRGADNMACP------HIGNGVELGANVIILGDITIGNNV 117

                          90       100
                  ....*....|....*....|....*
gi 1120757468 130 MVGAGAVVTKDVPSKAIVMGNPAKV 154
Cdd:PRK10191  118 TVGAGSVVLDSVPDNALVVGEKARV 142
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 47-137 1.70e-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: 45.49  E-value: 1.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  47 AHTLIENDVVIGDDVTIKSGVYVWDGITIEDGAFIGPSVVFSNdkyprskvypekfmrtlvqrgASIGANATILPGiTIG 126
Cdd:cd03353     8 ETTYIDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIKD---------------------STIGDGVVIKAS-SVI 65

                          90
                  ....*....|.
gi 1120757468 127 ERSMVGAGAVV 137
Cdd:cd03353    66 EGAVIGNGATV 76
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 47-137 3.27e-06

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 45.40  E-value: 3.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  47 AHTLIENDVVIGDDVTIKSGVYVWDGITIEDGAFIGPSVVFSNdkyprskvypekfmrtlvqrgASIGANATILPgiTIG 126
Cdd:COG1207   259 ATTYIDGDVEIGRDVVIDPNVILEGKTVIGEGVVIGPNCTLKD---------------------STIGDGVVIKY--SVI 315

                          90
                  ....*....|.
gi 1120757468 127 ERSMVGAGAVV 137
Cdd:COG1207   316 EDAVVGAGATV 326
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 47-136 1.08e-05

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 44.16  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  47 AHTLIENDVVIGDDVTIKSGVYVWDGITIEDGAFIGP-----------------SVVFSNDKYPRSKVYPEKFMR--TLV 107
Cdd:PRK14352  264 ATTWIDVDVTIGRDVVIHPGTQLLGRTTIGEDAVVGPdttltdvtvgegasvvrTHGSESEIGAGATVGPFTYLRpgTVL 343

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1120757468 108 QRGASIGA-----NATI-----LPGIT------IGERSMVGAGAV 136
Cdd:PRK14352  344 GEEGKLGAfvetkNATIgrgtkVPHLTyvgdadIGEHSNIGASSV 388
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 21-86 4.68e-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: 4.68e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1120757468  21 IGEDTRVWQFSIIFANAVIGSNCNICAHTLI--------ENDVVIGDDVTIKSGVYVWDGITIEDGAFIGPSVV 86
Cdd:cd00208     3 IGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIgaatgpneKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAV 76
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 18-77 8.47e-05

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: 39.15  E-value: 8.47e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  18 SNAIGEDTRVWQfSIIFANAVIGSNCNIcAHTLIENDVVIGDDVTIKSGVYVWDGITIED 77
Cdd:cd03356    22 NVRIGDGVTITN-SILMDNVTIGANSVI-VDSIIGDNAVIGENVRVVNLCIIGDDVVVED 79
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 75-141 9.01e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 41.28  E-value: 9.01e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1120757468  75 IEDGAFIGPSVVFSNdkyprskvypekfmrtlvqrGASIGANATILPGITIGERSMVGAGAVVTKDV 141
Cdd:PRK00892  103 IHPSAVIDPSAKIGE--------------------GVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGV 149
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 57-156 1.15e-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: 41.27  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  57 IGDDVTIKSGV-YVWDGITIEDGAFIGPSVVFSNDKYPRSKVypeKFMRTLVQRGASIGANATILPGITIGERSMVGAGA 135
Cdd:TIGR02353 115 IGKGVDIGSLPpVCTDLLTIGAGTIVRKEVMLLGYRAERGRL---HTGPVTLGRDAFIGTRSTLDIDTSIGDGAQLGHGS 191

                          90       100
                  ....*....|....*....|...
gi 1120757468 136 VVTKD--VPSKAIVMGNPAKVVG 156
Cdd:TIGR02353 192 ALQGGqsIPDGERWHGSPAQKTG 214
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 68-159 1.54e-04

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 40.69  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  68 YVWDGiTIEDGAFIGPSVVFSNdkyprskvYP-EKFMRTLVQRGASIGANATILPGITIGERSMVGAGAVVTKDVPSKAI 146
Cdd:PRK14352  371 YVGDA-DIGEHSNIGASSVFVN--------YDgVNKHRTTIGSHVRTGSDTMFVAPVTVGDGAYTGAGTVIREDVPPGAL 441

                          90
                  ....*....|....*
gi 1120757468 147 -VMGNPAKVV-GYVA 159
Cdd:PRK14352  442 aVSEGPQRNIeGWVQ 456
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 51-141 1.65e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 40.51  E-value: 1.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  51 IENDVVIGDDVTIKSGVYvwdgitIEDGAFIGPSVVfsndkyprskvypekfmrtlvqrgasIGANATILPGITIGERSM 130
Cdd:PRK00892  109 IDPSAKIGEGVSIGPNAV------IGAGVVIGDGVV--------------------------IGAGAVIGDGVKIGADCR 156

                          90
                  ....*....|.
gi 1120757468 131 VGAGAVVTKDV 141
Cdd:PRK00892  157 LHANVTIYHAV 167
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 21-86 1.89e-04

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: 37.99  E-value: 1.89e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1120757468  21 IGEDTRVWQFSIIfANAVIGSNCNICAHTLIEN-----DVVIGDDVTIKSGVYVW-----DGITIEDGAFIGPSVV 86
Cdd:cd03356     2 IGESTVIGENAII-KNSVIGDNVRIGDGVTITNsilmdNVTIGANSVIVDSIIGDnavigENVRVVNLCIIGDDVV 76
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 106-155 2.10e-04

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 39.79  E-value: 2.10e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1120757468 106 LVQRGASIGANATILPGITIGERSMVGAGAVVTKDV--PSKAIVMGNPAKVV 155
Cdd:PRK13627   90 VIGRDALVGMNSVIMDGAVIGEESIVAAMSFVKAGFqgEKRQLLMGTPARAV 141
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 21-66 2.22e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 40.24  E-value: 2.22e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1120757468  21 IGEDTRVWQfSIIFANAVIGSNCNIcAHTLIENDVVIGDDVTIKSG 66
Cdd:PRK05293  317 VGEGSVVKD-SVIMPGAKIGENVVI-ERAIIGENAVIGDGVIIGGG 360
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 50-132 2.62e-04

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 39.96  E-value: 2.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  50 LIENDVVIGDDVTIKSGVYVWDGITIEDGAFIGP-SVVFSNDKYPRSKVYPEKFMRTL-VQRGASIGANATILPGITIGE 127
Cdd:PRK14358  266 LIEDTVTLGRDVTIEPGVLLRGQTRVADGVTIGAySVVTDSVLHEGAVIKPHSVLEGAeVGAGSDVGPFARLRPGTVLGE 345


                  ....*
gi 1120757468 128 RSMVG 132
Cdd:PRK14358  346 GVHIG 350
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 3-139 3.83e-04

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: 38.76  E-value: 3.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468   3 QLGQNMFIHELSDVKSNA-IGEDTRVWQFSIIFANA----VIGSNCNI----CAHTLIENDVVIGDDVTIKSGVYVWDGI 73
Cdd:cd00710     4 VIDPSAYVHPTAVVIGDViIGDNVFVGPGASIRADEgtpiIIGANVNIqdgvVIHALEGYSVWIGKNVSIAHGAIVHGPA 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1120757468  74 TIEDGAFIG-PSVVFSndkyprskvypekfmrTLVQRGASIGANATILpGITIGERSMVGAGAVVTK 139
Cdd:cd00710    84 YIGDNCFIGfRSVVFN----------------AKVGDNCVIGHNAVVD-GVEIPPGRYVPAGAVITS 133
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 31-127 7.57e-04

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: 38.57  E-value: 7.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  31 SIIFANAVIGSNCNICAHTLIENDVVIGDDVTIKSGVYVwDGITiedgafigpsvvfsndkyprskvypekfmrtlvqrg 110
Cdd:cd03351     6 AIVDPGAKIGENVEIGPFCVIGPNVEIGDGTVIGSHVVI-DGPT------------------------------------ 48

                          90
                  ....*....|....*..
gi 1120757468 111 aSIGANATILPGITIGE 127
Cdd:cd03351    49 -TIGKNNRIFPFASIGE 64
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 4-77 9.84e-04

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: 36.02  E-value: 9.84e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1120757468   4 LGQNMFIHELSDVKSNAIGEDTR-----VWQFSIIFANAVIGSNCNIcAHTLIENDVVIGDDVTIKSGVYVWDGITIED 77
Cdd:cd05787     2 IGRGTSIGEGTTIKNSVIGRNCKigknvVIDNSYIWDDVTIEDGCTI-HHSIVADGAVIGKGCTIPPGSLISFGVVIGD 79
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 16-75 1.17e-03

Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 38.13  E-value: 1.17e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1120757468  16 VKSNAIGEDtrvwqfSIIFANAVIGSNCNIcAHTLIENDVVIGDDVTIKSG-------VYVWDGITI 75
Cdd:COG0448   312 VESGAVVEN------SVIMPGVVIGEGAVI-ENAIIDKNVVIPPGVVIGEDpeedrkrFTVSSGIVV 371
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 44-142 1.32e-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: 36.97  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  44 NICAHTLIENDVVIGDDVTIKS------GVYVWDGITIEDGAFIGP------SVVFSNDKYPRSKVYPEKFMRTLVQRGA 111
Cdd:cd03350     3 RVPPGAIIRDGAFIGPGAVLMMpsyvniGAYVDEGTMVDSWATVGScaqigkNVHLSAGAVIGGVLEPLQATPVIIEDDV 82

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1120757468 112 SIGANATILPGITIGERSMVGAGAVVTKDVP 142
Cdd:cd03350    83 FIGANCEVVEGVIVGKGAVLAAGVVLTQSTP 113
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 21-88 1.54e-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: 1.54e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1120757468  21 IGEDTRVWQFSIIFANAVIGSNCNICAHTLIE--------NDVVIGDDVTIKSGVYVWDGITIEDGAFIGPSVVFS 88
Cdd:cd03350    34 VDEGTMVDSWATVGSCAQIGKNVHLSAGAVIGgvleplqaTPVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLT 109
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
54-83 2.88e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.85  E-value: 2.88e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1120757468  54 DVVIGDDVTIKSGVYVWDGITIEDGAFIGP 83
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 37-98 3.06e-03

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


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 36.71  E-value: 3.06e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  37 AVIGSNCNICAHTLIE--------NDVVIGDDVTIKSGVYVWDGITIEDGAFIGPSVVFSndkyPRSKVY 98
Cdd:PRK11830  151 AQIGKNVHLSGGVGIGgvleplqaNPVIIEDNCFIGARSEVVEGVIVEEGSVLGMGVFLG----QSTKIY 216
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 47-153 3.26e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 37.03  E-value: 3.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1120757468  47 AHTLIENDVVIGDDVTIKSGVYVWDGITIEDGAFIGPSVVFSNDKY-PRSKVYPEKFMR-TLVQRGASIGANATILPGIT 124
Cdd:PRK14355  261 ETTYIDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVIKGCRIgDDVTVKAGSVLEdSVVGDDVAIGPMAHLRPGTE 340

                          90       100
                  ....*....|....*....|....*....
gi 1120757468 125 IGERSMVGagavvtKDVPSKAIVMGNPAK 153
Cdd:PRK14355  341 LSAHVKIG------NFVETKKIVMGEGSK 363
 
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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