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Conserved domains on  [gi|2551177256|ref|WP_302369142|]
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serine O-acetyltransferase [Bacteroides clarus]

Protein Classification

serine O-acetyltransferase( domain architecture ID 11437200)

serine O-acetyltransferase (SAT) catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetyl-L-serine

CATH:  2.160.10.10
EC:  2.3.1.30
Gene Ontology:  GO:0009001|GO:0006535
PubMed:  15500694|11747907|15581568
SCOP:  4001889

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 1-93 7.08e-39

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: 127.51  E-value: 7.08e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256   1 MFPHYSCIVINGAAIIGDNCTIYHSVTIGSVRGPKG-GVPRIGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIPDNS 79
Cdd:COG1045    79 FIDHGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGkRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGS 158

                          90
                  ....*....|....
gi 2551177256  80 VVVGIPGKVISKEG 93
Cdd:COG1045   159 TVVGVPARIVKRKG 172
 
Name Accession Description Interval E-value
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 1-93 7.08e-39

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: 127.51  E-value: 7.08e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256   1 MFPHYSCIVINGAAIIGDNCTIYHSVTIGSVRGPKG-GVPRIGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIPDNS 79
Cdd:COG1045    79 FIDHGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGkRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGS 158

                          90
                  ....*....|....
gi 2551177256  80 VVVGIPGKVISKEG 93
Cdd:COG1045   159 TVVGVPARIVKRKG 172
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 1-85 2.57e-31

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: 105.99  E-value: 2.57e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256   1 MFPHYSCIVINGAAIIGDNCTIYHSVTIGSVRGPKG-GVPRIGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIPDNS 79
Cdd:cd03354    16 FIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGkRHPTIGDNVVIGAGAKILGNITIGDNVKIGANAVVTKDVPANS 95


                  ....*.
gi 2551177256  80 VVVGIP 85
Cdd:cd03354    96 TVVGVP 101
PLN02694 PLN02694
serine O-acetyltransferase
 1-105 6.73e-20

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 81.61  E-value: 6.73e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256   1 MFPHYSCIVINGAAIIGDNCTIYHSVTIGSVrGPKGG--VPRIGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIPDN 78
Cdd:PLN02694  174 LFDHATGVVIGETAVIGNNVSILHHVTLGGT-GKACGdrHPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPR 252

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2551177256  79 SVVVGIPGKVIS------------KEGLEHTKYYSKNYD 105
Cdd:PLN02694  253 TTAVGNPARLVGgkekpakheecpGESMDHTSFISEWSD 291
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 9-85 7.47e-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: 66.75  E-value: 7.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256   9 VINGAAI------IGDNCTIYHSVTIGsvrgpkGGVpRIGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIPDNSVVV 82
Cdd:TIGR03570 125 IINTGAIvehdcvIGDFVHIAPGVTLS------GGV-VIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVV 197


                  ...
gi 2551177256  83 GIP 85
Cdd:TIGR03570 198 GVP 200
Fucokinase pfam07959
L-fucokinase; In the salvage pathway of GDP-L-fucose, free cytosolic fucose is phosphorylated ...
 9-85 8.07e-04

L-fucokinase; In the salvage pathway of GDP-L-fucose, free cytosolic fucose is phosphorylated by L-fucokinase to form L-fucose-L-phosphate, which is then further converted to GDP-L-fucose in the reaction catalyzed by GDP-L-fucose pyrophosphorylase.


Pssm-ID: 462323  Cd Length: 405  Bit Score: 36.86  E-value: 8.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256   9 VINGAAIIGDNCTIYHSVtigsvrgpkggvprIGNNVVIASGAkVIGNVTIGNNVMIGSGSIVV----------TDIPDN 78
Cdd:pfam07959 262 VIANARQLKAGASVINSV--------------LEPGVSVGPGS-VIEYCHLGGPVSIGSGCILSgldlssslarLELPDD 326


                  ....*..
gi 2551177256  79 SVVVGIP 85
Cdd:pfam07959 327 TFLHTLP 333
 
Name Accession Description Interval E-value
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 1-93 7.08e-39

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: 127.51  E-value: 7.08e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256   1 MFPHYSCIVINGAAIIGDNCTIYHSVTIGSVRGPKG-GVPRIGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIPDNS 79
Cdd:COG1045    79 FIDHGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGkRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGS 158

                          90
                  ....*....|....
gi 2551177256  80 VVVGIPGKVISKEG 93
Cdd:COG1045   159 TVVGVPARIVKRKG 172
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 1-85 2.57e-31

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: 105.99  E-value: 2.57e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256   1 MFPHYSCIVINGAAIIGDNCTIYHSVTIGSVRGPKG-GVPRIGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIPDNS 79
Cdd:cd03354    16 FIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGkRHPTIGDNVVIGAGAKILGNITIGDNVKIGANAVVTKDVPANS 95


                  ....*.
gi 2551177256  80 VVVGIP 85
Cdd:cd03354    96 TVVGVP 101
PLN02694 PLN02694
serine O-acetyltransferase
 1-105 6.73e-20

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 81.61  E-value: 6.73e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256   1 MFPHYSCIVINGAAIIGDNCTIYHSVTIGSVrGPKGG--VPRIGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIPDN 78
Cdd:PLN02694  174 LFDHATGVVIGETAVIGNNVSILHHVTLGGT-GKACGdrHPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPR 252

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2551177256  79 SVVVGIPGKVIS------------KEGLEHTKYYSKNYD 105
Cdd:PLN02694  253 TTAVGNPARLVGgkekpakheecpGESMDHTSFISEWSD 291
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 5-89 2.35e-18

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: 75.15  E-value: 2.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256   5 YSCIVINGAAI-IGDNC---------TIYHSVTIGS-VRGPKGGVP-RIGNNVVIASGAKVIGNVTIGNNVMIGSGSIVV 72
Cdd:cd03357    73 FNCTILDVAPVtIGDNVligpnvqiyTAGHPLDPEErNRGLEYAKPiTIGDNVWIGGGVIILPGVTIGDNSVIGAGSVVT 152

                          90
                  ....*....|....*..
gi 2551177256  73 TDIPDNSVVVGIPGKVI 89
Cdd:cd03357   153 KDIPANVVAAGNPARVI 169
cysE PRK11132
serine acetyltransferase; Provisional
 1-91 2.02e-17

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 74.73  E-value: 2.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256   1 MFPHYSCIVINGAAIIGDNCTIYHSVTIGSVrGPKGG--VPRIGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIPDN 78
Cdd:PRK11132  155 MLDHATGIVIGETAVIENDVSILQSVTLGGT-GKTSGdrHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPH 233

                          90
                  ....*....|...
gi 2551177256  79 SVVVGIPGKVISK 91
Cdd:PRK11132  234 TTAAGVPARIVGK 246
PLN02357 PLN02357
serine acetyltransferase
 1-89 2.15e-17

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 75.30  E-value: 2.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256   1 MFPHYSCIVINGAAIIGDNCTIYHSVTIGSVRGPKGGV-PRIGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIPDNS 79
Cdd:PLN02357  240 LLDHATGVVIGETAVVGNNVSILHNVTLGGTGKQSGDRhPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRT 319

                          90
                  ....*....|
gi 2551177256  80 VVVGIPGKVI 89
Cdd:PLN02357  320 TAVGNPARLI 329
PRK10191 PRK10191
putative acyl transferase; Provisional
 4-88 2.34e-17

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 71.84  E-value: 2.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256   4 HYSCIVINGAAIIGDNCTIYHSVTIGSVRGPKGGVPRIGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIPDNSVVVG 83
Cdd:PRK10191   58 HGYAVVINKNVVAGDDFTIRHGVTIGNRGADNMACPHIGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVG 137


                  ....*
gi 2551177256  84 IPGKV 88
Cdd:PRK10191  138 EKARV 142
PLN02739 PLN02739
serine acetyltransferase
 1-89 1.52e-16

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 73.15  E-value: 1.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256   1 MFPHYSCIVINGAAIIGDNCTIYHSVTIGSVRGPKGGV-PRIGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIPDNS 79
Cdd:PLN02739  219 LLDHGTGVVIGETAVIGDRVSILHGVTLGGTGKETGDRhPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHS 298

                          90
                  ....*....|
gi 2551177256  80 VVVGIPGKVI 89
Cdd:PLN02739  299 MVAGNPAKLI 308
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
4-91 2.52e-16

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 69.13  E-value: 2.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256   4 HYSCIVINGAAIIGDNCTIYHSVTIG---------SVRGPKGGVPRIGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTD 74
Cdd:COG0110    38 PGVTIDDPGGITIGDNVLIGPGVTILtgnhpiddpATFPLRTGPVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKD 117

                          90
                  ....*....|....*..
gi 2551177256  75 IPDNSVVVGIPGKVISK 91
Cdd:COG0110   118 VPPYAIVAGNPARVIRK 134
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 9-85 7.47e-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: 66.75  E-value: 7.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256   9 VINGAAI------IGDNCTIYHSVTIGsvrgpkGGVpRIGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIPDNSVVV 82
Cdd:TIGR03570 125 IINTGAIvehdcvIGDFVHIAPGVTLS------GGV-VIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVV 197


                  ...
gi 2551177256  83 GIP 85
Cdd:TIGR03570 198 GVP 200
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 15-85 3.65e-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: 64.81  E-value: 3.65e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2551177256  15 IIGDNCTIYHSVTIGsvrgpkGGVpRIGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIPDNSVVVGIP 85
Cdd:cd03360   134 VIGDFVHIAPGVVLS------GGV-TIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 2-91 1.03e-13

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 63.29  E-value: 1.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256   2 FPHYSCIVINGAAI-IGDNCTIYHSVTIGSVRGPKGGVPR-----------IGNNVVIASGAKVIGNVTIGNNVMIGSGS 69
Cdd:PRK10092   81 YANFDCVMLDVCPIrIGDNCMLAPGVHIYTATHPLDPVARnsgaelgkpvtIGNNVWIGGRAVINPGVTIGDNVVVASGA 160

                          90       100
                  ....*....|....*....|..
gi 2551177256  70 IVVTDIPDNSVVVGIPGKVISK 91
Cdd:PRK10092  161 VVTKDVPDNVVVGGNPARIIKK 182
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 4-89 1.07e-13

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: 61.32  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256   4 HYSCIVINGAAIIGDNCTIYHSVTI------------GSVRGPKGGVPRIGNNVVIASGAKVIGNVTIGNNVMIGSGSIV 71
Cdd:cd04647    12 PGCVISAGGGITIGDNVLIGPNVTIydhnhdiddperPIEQGVTSAPIVIGDDVWIGANVVILPGVTIGDGAVVGAGSVV 91

                          90
                  ....*....|....*...
gi 2551177256  72 VTDIPDNSVVVGIPGKVI 89
Cdd:cd04647    92 TKDVPPNSIVAGNPAKVI 109
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 15-104 2.72e-13

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 61.97  E-value: 2.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256  15 IIGDNCTIYHSVTI-GSvrgpkggvpRIGNNVVIASGAKVIGNVTIGNNVMIGSGSIVV--TDIPDNSVVVGIPGKVI-- 89
Cdd:COG0663    73 TIGDDVTIGHGAILhGC---------TIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTegKVVPPGSLVVGSPAKVVre 143

                          90
                  ....*....|....*.
gi 2551177256  90 -SKEGLEHTKYYSKNY 104
Cdd:COG0663   144 lTEEEIAFLRESAENY 159
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 8-104 1.04e-12

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 61.17  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256   8 IVINGAAIIGDNCTIYHSVTIGSVRGPKGGVPR-----------IGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIP 76
Cdd:PRK09527   90 IVDDYTVTIGDNVLIAPNVTLSVTGHPVHHELRkngemysfpitIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIP 169

                          90       100
                  ....*....|....*....|....*...
gi 2551177256  77 DNSVVVGIPGKVISKEGLEHTKYYSKNY 104
Cdd:PRK09527  170 PNVVAAGVPCRVIREINDRDKQYYFKDY 197
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 15-104 3.17e-12

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: 58.58  E-value: 3.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256  15 IIGDNCTIYHSVTIGSVRgpkggvprIGNNVVIASGAKVIGNVTIGNNVMIGSGSIVV--TDIPDNSVVVGIPGKVI--- 89
Cdd:cd04645    62 IIGDNVTVGHGAVLHGCT--------IGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPpgKVIPPGSLVAGSPAKVVrel 133

                          90
                  ....*....|....*
gi 2551177256  90 SKEGLEHTKYYSKNY 104
Cdd:cd04645   134 TDEEIAELRESAEHY 148
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 15-89 3.96e-12

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: 57.90  E-value: 3.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256  15 IIGDNCTIYHSVTIGSVRGPKGGVPR--------IGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIPDNSVVVGIPG 86
Cdd:cd03358    36 TIEDDVFIGPNVVFTNDLYPRSKIYRkwelkgttVKRGASIGANATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPA 115


                  ...
gi 2551177256  87 KVI 89
Cdd:cd03358   116 RII 118
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 15-85 1.36e-10

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: 56.18  E-value: 1.36e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2551177256  15 IIGDNCTIYHSVTI-GSVRgpkggvprIGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIPDNSVVVGIP 85
Cdd:COG1044   242 RIGEHTAIAAQVGIaGSTK--------IGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSGSP 305
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 16-103 1.28e-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: 52.19  E-value: 1.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256  16 IGDNCTIYHSVTIGSVRgpkggvprIGNNVVIASGAKVIGNVTIGNNVMIGSGSIVV--TDIPDNSVVVGIPGKVISKEG 93
Cdd:cd04650    64 IGDYVTIGHNAVVHGAK--------VGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTpgKEIPDYSLVLGVPAKVVRKLT 135

                          90
                  ....*....|
gi 2551177256  94 LEHTKYYSKN 103
Cdd:cd04650   136 EEEIEWIKKN 145
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 41-89 1.90e-09

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: 51.39  E-value: 1.90e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2551177256  41 IGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIPDNSVVVGIPGKVI 89
Cdd:cd03349    76 IGNDVWIGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVI 124
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 30-95 1.09e-08

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 50.26  E-value: 1.09e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2551177256  30 SVRGPKGGVPRIGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIPDNSVVVGIPGKVISKEGLE 95
Cdd:PRK09677  122 DMRTLESSAVVIGQRVWIGENVTILPGVSIGNGCIVGANSVVTKSIPENTVIAGNPAKIIKKYNHE 187
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 15-95 2.65e-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: 2.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256  15 IIGDNCTIYHSVTI--GSVRGpkGGVPRIG------------------NNVVIASGAKVIGNVTIGNNV----------- 63
Cdd:COG1043    81 EIGDNNTIREFVTIhrGTVQG--GGVTRIGddnllmayvhvahdcvvgNNVILANNATLAGHVEVGDHAiigglsavhqf 158

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2551177256  64 -------MIGSGSIVVTDIPDNSVVVGIPGKV--ISKEGLE 95
Cdd:COG1043   159 vrigahaMVGGGSGVVKDVPPYVLAAGNPARLrgLNLVGLK 199
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 15-87 2.90e-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: 48.94  E-value: 2.90e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2551177256  15 IIGDNCTIYHSVTI-GSVRgpkggvprIGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIPDNSVVVGIPGK 87
Cdd:cd03352   134 RIGENCLIAAQVGIaGSTT--------IGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQ 199
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 15-96 8.82e-08

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


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 48.20  E-value: 8.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256  15 IIGDNCTIYHSVTI--GSVRGpkGGVPRIG------------------NNVVIASGAKVIGNVTIGNNV----------- 63
Cdd:cd03351    79 EIGDNNTIREFVTIhrGTAQG--GGVTRIGnnnllmayvhvahdcvigNNVILANNATLAGHVEIGDYAiigglsavhqf 156

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2551177256  64 -------MIGSGSIVVTDIPDNSVVVGIPGKV--ISKEGLEH 96
Cdd:cd03351   157 crigrhaMVGGGSGVVQDVPPYVIAAGNRARLrgLNLVGLKR 198
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 9-71 1.02e-07

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: 48.09  E-value: 1.02e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2551177256   9 VINGAAIIGDNCTIYHSVTIGSvrgpkgGVpRIGNNVVIASGAKVIGNVTIGNNVMIGSGSIV 71
Cdd:COG1044   122 VIGAGVVIGDGVVIGPGVVIGD------GV-VIGDDCVLHPNVTIYERCVIGDRVIIHSGAVI 177
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
15-94 1.09e-07

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 47.79  E-value: 1.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256  15 IIGDNCTIYHSVTI--GSVRGpkGGVPRIG------------------NNVVIASGAKVIGNVTIGNNV----------- 63
Cdd:PRK05289   82 VIGDNNTIREFVTInrGTVQG--GGVTRIGdnnllmayvhvahdcvvgNHVILANNATLAGHVEVGDYAiiggltavhqf 159

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2551177256  64 -------MIGSGSIVVTDIPDNSVVVGIPGKV--ISKEGL 94
Cdd:PRK05289  160 vrigahaMVGGMSGVSQDVPPYVLAEGNPARLrgLNLVGL 199
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 7-72 1.75e-07

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: 47.33  E-value: 1.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256   7 CIVINgaAIIGDNCTIYHSVTIGSVRGP----------------KGGVpRIGN-----NVVIASGAKV-----IGNVTIG 60
Cdd:COG1207   297 CTLKD--STIGDGVVIKYSVIEDAVVGAgatvgpfarlrpgtvlGEGV-KIGNfvevkNSTIGEGSKVnhlsyIGDAEIG 373

                          90
                  ....*....|..
gi 2551177256  61 NNVMIGSGSIVV 72
Cdd:COG1207   374 EGVNIGAGTITC 385
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 9-71 1.96e-07

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: 47.32  E-value: 1.96e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2551177256   9 VINGAAIIGDNCTIYHSVTIGSvrgpkgGVpRIGNNVVIASGAkVIG-NVTIGNNVMIGSGSIV 71
Cdd:COG1044   104 VIDPSAKIGEGVSIGPFAVIGA------GV-VIGDGVVIGPGV-VIGdGVVIGDDCVLHPNVTI 159
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 15-85 2.14e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 47.06  E-value: 2.14e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2551177256  15 IIGDNCTIYHSVTI-GSVRgpkggvprIGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIPDNSVVV-GIP 85
Cdd:PRK00892  245 VIGRHTAIAAQVGIaGSTK--------IGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEPGEYSsGIP 309
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 9-71 9.13e-07

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 43.01  E-value: 9.13e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2551177256   9 VINGAAIIGDNCTIYHSVTIGSVRGPKGGVP-RIGNNVVIASGAKVIGNVTIGNNVMIGSGSIV 71
Cdd:cd00208    14 VIRGPVVIGDNVNIGPGAVIGAATGPNEKNPtIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVV 77
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 40-93 1.13e-06

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 45.24  E-value: 1.13e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2551177256  40 RIGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIPDNSVVVGiPGKVISKEG 93
Cdd:PRK14353  382 EIGAGAFIGSNSALVAPVTIGDGAYIASGSVITEDVPDDALALG-RARQETKPG 434
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 14-69 1.30e-06

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 45.01  E-value: 1.30e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2551177256  14 AIIGDNCTIYHSVTIGSvrgpkgGVpRIGNNVVIASGA------------------KV--IGNVTIGNNVMIGSGS 69
Cdd:COG1044   145 VVIGDDCVLHPNVTIYE------RC-VIGDRVIIHSGAvigadgfgfapdedggwvKIpqLGRVVIGDDVEIGANT 213
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 9-89 1.70e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 44.74  E-value: 1.70e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256   9 VINGAAIIGDNCTIYHSVTIGSvrgpkgGVpRIGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTD----IPDNSVVVGI 84
Cdd:PRK00892  126 VIGAGVVIGDGVVIGAGAVIGD------GV-KIGADCRLHANVTIYHAVRIGNRVIIHSGAVIGSDgfgfANDRGGWVKI 198


                  ....*..
gi 2551177256  85 P--GKVI 89
Cdd:PRK00892  199 PqlGRVI 205
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 13-69 2.35e-06

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: 44.17  E-value: 2.35e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2551177256  13 AAIIGDNCTIYHSVTIGSVRGPKGGVPRIGNNVVIASGAKVIGNVTIGNNVMIGSGS 69
Cdd:TIGR01852  76 RLIIGDNNTIREFVTINRGTASGGGVTRIGNNNLLMAYSHIAHDCVVGNHVILANNA 132
PRK10502 PRK10502
putative acyl transferase; Provisional
 40-89 3.11e-06

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 43.40  E-value: 3.11e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2551177256  40 RIGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIPDNSVVVGIPGKVI 89
Cdd:PRK10502  126 VIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPI 175
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 9-69 3.42e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 43.59  E-value: 3.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256   9 VINGAAIIGDNCTIYHSVTIGSvrgpkgGVpRIGNNVVIASGAKV-------------------IGNVTIGNNVMIGSGS 69
Cdd:PRK00892  144 VIGDGVKIGADCRLHANVTIYH------AV-RIGNRVIIHSGAVIgsdgfgfandrggwvkipqLGRVIIGDDVEIGANT 216
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 40-89 5.57e-06

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: 41.44  E-value: 5.57e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2551177256  40 RIGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIPDNSVVVGIPGKVI 89
Cdd:cd05825    58 VIGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 12-82 6.19e-06

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 43.09  E-value: 6.19e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2551177256  12 GAAIIGDNCTIYHSVTIGSVRGPKGGVPRIGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIPDNSVVV 82
Cdd:PRK09451  368 GDAEIGDNVNIGAGTITCNYDGANKFKTIIGDDVFVGSDTQLVAPVTVGKGATIGAGTTVTRDVAENELVI 438
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 8-89 1.34e-05

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


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 41.20  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256   8 IVINGAAIIGDNCTIYHSVTIGSVRGPKGGV--------PRIGNNVVIASGAKVIGNVTIGNNVMIGSGSIVV--TDIPD 77
Cdd:cd04745    40 IVIRDGANVQDNCVIHGFPGQDTVLEENGHIghgailhgCTIGRNALVGMNAVVMDGAVIGEESIVGAMAFVKagTVIPP 119

                          90
                  ....*....|..
gi 2551177256  78 NSVVVGIPGKVI 89
Cdd:cd04745   120 RSLIAGSPAKVI 131
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 14-71 1.53e-05

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 41.62  E-value: 1.53e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2551177256  14 AIIGDNCTIYHSVTIGSvrgpkgGVpRIGNNVVIASGAKVIGNVTIGNNVMIGSGSIV 71
Cdd:cd03352    20 VVIGDGVVIGPGVVIGD------GV-VIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 41-83 2.88e-05

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 41.25  E-value: 2.88e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2551177256  41 IGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIPDNSVVVG 83
Cdd:PRK14356  401 IGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDGSLAIA 443
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 41-82 3.66e-05

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 40.74  E-value: 3.66e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2551177256  41 IGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIPDNSVVV 82
Cdd:PRK14359  370 IGKNVFIGSDTQLVAPVNIEDNVLIAAGSTVTKDVPKGSLAI 411
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 31-81 4.12e-05

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 40.01  E-value: 4.12e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2551177256  31 VRGPKGGVPRIGNNVVIASGAKVIGNVTIGNNVMIG--------SGSIVV---TDIPDNSVV 81
Cdd:COG0663     3 IYSFDGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWpgavlrgdVGPIRIgegSNIQDGVVL 64
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 41-83 5.27e-05

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 40.10  E-value: 5.27e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2551177256  41 IGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIPDNSVVVG 83
Cdd:cd03353   147 IGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGALAIA 189
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 41-93 6.56e-05

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: 6.56e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2551177256  41 IGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIPDNSVVVGIPGKVIsKEG 93
Cdd:PRK14360  393 IGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNSLAIARSRQVI-KEN 444
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 10-68 1.58e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 38.97  E-value: 1.58e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2551177256  10 INGAAIIGDNCTIYHSVTIG--SVRGPkgGVpRIGNNVVIASGAkVIG-NVTIGNNVMIGSG 68
Cdd:PRK00892  103 IHPSAVIDPSAKIGEGVSIGpnAVIGA--GV-VIGDGVVIGAGA-VIGdGVKIGADCRLHAN 160
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 15-71 2.69e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 38.08  E-value: 2.69e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2551177256  15 IIGDNCTIYHSVTIGsvRGPK-GGVPRIG------------------NNVVIASGAKVIGNVTIGNNVMIGSGSIV 71
Cdd:PRK12461   79 EIGDRNVIREGVTIH--RGTKgGGVTRIGndnllmayshvahdcqigNNVILVNGALLAGHVTVGDRAIISGNCLV 152
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 10-83 2.76e-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: 38.17  E-value: 2.76e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2551177256  10 INGAAIIGDNCTIYHSVTIgsvrgpKGGVpRIGNNVVIASGAkVIGNVTIGNNVMIGSGSIVVTDIPDNSVVVG 83
Cdd:cd03353    12 IDGDVEIGVDVVIDPGVIL------EGKT-VIGEDCVIGPNC-VIKDSTIGDGVVIKASSVIEGAVIGNGATVG 77
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 10-83 2.76e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 38.19  E-value: 2.76e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2551177256  10 INGAAIIGDNCTIYHSVTIGsvrgpkgGVPRIGNNVVIASGAkVIGNVTIGNNVMIGSGSIVVTDIPDNSVVVG 83
Cdd:PRK14355  265 IDRGVVIGRDTTIYPGVCIS-------GDTRIGEGCTIEQGV-VIKGCRIGDDVTVKAGSVLEDSVVGDDVAIG 330
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 12-93 4.04e-04

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 37.82  E-value: 4.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256  12 GAAIIGDNCTIYHSVTIGSVRGPKGGVPRIGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIPDNSVVVGIPGKVIsK 91
Cdd:PRK14357  357 GDATVGKNVNIGAGTITCNYDGKKKNPTFIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPPYSLALGRARQIV-K 435


                  ..
gi 2551177256  92 EG 93
Cdd:PRK14357  436 EG 437
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 4-83 4.30e-04

Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p27 is part of the pointed-end subcomplex in dynactin that also includes p25, p26, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain the imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100052 [Multi-domain]  Cd Length: 164  Bit Score: 37.30  E-value: 4.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256   4 HYSCIVINGAA--IIGDNCTIYHSVTIGSvRGPKGGV---------------------PRIGNNVVIASGAKVIGNVTIG 60
Cdd:cd04646    27 HPRATIIAEAGpiIIGENNIIEEQVTIVN-KKPKDPAepkpmiigsnnvfevgckceaLKIGNNNVFESKSFVGKNVIIT 105

                          90       100
                  ....*....|....*....|....*
gi 2551177256  61 NNVMIGSGSIVVTD--IPDNSVVVG 83
Cdd:cd04646   106 DGCIIGAGCKLPSSeiLPENTVIYG 130
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 14-72 4.58e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 37.89  E-value: 4.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256  14 AIIGDNCTIYHSVTIGSVRG------------PK---GGVPRIGNNV-----VIASGAKV-----IGNVTIGNNVMIGSG 68
Cdd:PRK14354  301 STIGDGVTITNSVIEESKVGdnvtvgpfahlrPGsviGEEVKIGNFVeikksTIGEGTKVshltyIGDAEVGENVNIGCG 380


                  ....
gi 2551177256  69 SIVV 72
Cdd:PRK14354  381 TITV 384
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 9-71 4.60e-04

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: 37.69  E-value: 4.60e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2551177256   9 VINGAAIIGDNCTIYHSVTIGsvrgpkGGVpRIGNNVVIASGAKVIGNVTIGNNVMIGSGSIV 71
Cdd:COG1043     9 IVDPGAKLGENVEIGPFCVIG------PDV-EIGDGTVIGSHVVIEGPTTIGKNNRIFPFASI 64
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 5-71 5.28e-04

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: 37.39  E-value: 5.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256   5 YSCIVINGAAIIGDNCTIYHSVTIGSvrgpkgGVpRIGNNVVIASGAKV-------------------IGNVTIGNNVMI 65
Cdd:cd03352    29 GPGVVIGDGVVIGDDCVIHPNVTIYE------GC-IIGDRVIIHSGAVIgsdgfgfapdgggwvkipqLGGVIIGDDVEI 101


                  ....*.
gi 2551177256  66 GSGSIV 71
Cdd:cd03352   102 GANTTI 107
PLN02296 PLN02296
carbonate dehydratase
 38-89 5.88e-04

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 37.41  E-value: 5.88e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2551177256  38 VPRIGNNVVIASGAKVIGNVTIG---------------NNVMIGSGsivvTDIPDNSVV----VGIPGKVI 89
Cdd:PLN02296   52 APVVDKDAFVAPSASVIGDVQVGrgssiwygcvlrgdvNSISVGSG----TNIQDNSLVhvakTNLSGKVL 118
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 15-81 7.39e-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: 36.83  E-value: 7.39e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2551177256  15 IIGDNCTIYHSVTIGSVrgpKGGVPRIGNNVVIASGAKVIGNVTIGNNVMIGSGSIVV-TDIPDNSVV 81
Cdd:cd00710    44 IIGANVNIQDGVVIHAL---EGYSVWIGKNVSIAHGAIVHGPAYIGDNCFIGFRSVVFnAKVGDNCVI 108
Fucokinase pfam07959
L-fucokinase; In the salvage pathway of GDP-L-fucose, free cytosolic fucose is phosphorylated ...
 9-85 8.07e-04

L-fucokinase; In the salvage pathway of GDP-L-fucose, free cytosolic fucose is phosphorylated by L-fucokinase to form L-fucose-L-phosphate, which is then further converted to GDP-L-fucose in the reaction catalyzed by GDP-L-fucose pyrophosphorylase.


Pssm-ID: 462323  Cd Length: 405  Bit Score: 36.86  E-value: 8.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256   9 VINGAAIIGDNCTIYHSVtigsvrgpkggvprIGNNVVIASGAkVIGNVTIGNNVMIGSGSIVV----------TDIPDN 78
Cdd:pfam07959 262 VIANARQLKAGASVINSV--------------LEPGVSVGPGS-VIEYCHLGGPVSIGSGCILSgldlssslarLELPDD 326


                  ....*..
gi 2551177256  79 SVVVGIP 85
Cdd:pfam07959 327 TFLHTLP 333
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 14-70 9.21e-04

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 36.83  E-value: 9.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256  14 AIIGDNCTIYHSV----TIGS-VR-GPK---------GGVPRIGN-----NVVIASGAKV-----IGNVTIGNNVMIGSG 68
Cdd:PRK14360  298 SQIGENVTVLYSVvsdsQIGDgVKiGPYahlrpeaqiGSNCRIGNfveikKSQLGEGSKVnhlsyIGDATLGEQVNIGAG 377


                  ..
gi 2551177256  69 SI 70
Cdd:PRK14360  378 TI 379
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 41-93 9.40e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 36.73  E-value: 9.40e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2551177256  41 IGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIPDNSVVVGiPGKVISKEG 93
Cdd:PRK14354  396 IGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPEDALAIA-RARQVNKEG 447
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 41-82 1.00e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 36.65  E-value: 1.00e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2551177256  41 IGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIPDNSVVV 82
Cdd:PRK14355  400 IEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPPDSLAI 441
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 3-104 1.11e-03

Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p25 is part of the pointed-end subcomplex in dynactin that also includes p26, p27, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100049 [Multi-domain]  Cd Length: 161  Bit Score: 36.04  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256   3 PHYSCIVINGAAIIGDNCTIYHSvtigsvrgpkggvpRIGNNVVIASGAkVIGN-VTIGNNVMIGSGSIVVTD--IPDNS 79
Cdd:cd03359    68 VAFFPLHIGDYVFIGENCVVNAA--------------QIGSYVHIGKNC-VIGRrCIIKDCVKILDGTVVPPDtvIPPYS 132

                          90       100
                  ....*....|....*....|....*
gi 2551177256  80 VVVGIPGKVISKEGlEHTKYYSKNY 104
Cdd:cd03359   133 VVSGRPARFIGELP-ECTQELMEEE 156
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 22-71 1.25e-03

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 36.65  E-value: 1.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2551177256  22 IYHSVTIGSVRGPKGGVPRIGNNVVIASGAKV-----------IGNVTIGNNVMIGSGSIV 71
Cdd:TIGR02353 115 IGKGVDIGSLPPVCTDLLTIGAGTIVRKEVMLlgyraergrlhTGPVTLGRDAFIGTRSTL 175
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-66 1.55e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 36.26  E-value: 1.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2551177256   5 YSCIVINGAAIIGDNCTIYHSVTIGSVrgpkggvpRIGNNVVIASGAkVIGNVTIGNNVMIG 66
Cdd:PRK14355  278 YPGVCISGDTRIGEGCTIEQGVVIKGC--------RIGDDVTVKAGS-VLEDSVVGDDVAIG 330
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 6-76 1.79e-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: 35.43  E-value: 1.79e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2551177256   6 SCIVINGAAIIGDNCTIYHSVTIGSVRGPKGGVPR-IGNNVVIASGAKVIGNVTIGNNVMIGSGSIVVTDIP 76
Cdd:cd03350    42 SWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPViIEDDVFIGANCEVVEGVIVGKGAVLAAGVVLTQSTP 113
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 9-71 2.12e-03

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: 35.49  E-value: 2.12e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2551177256   9 VINGAAIIGDNCTIYHSVTIGSvrgpkgGVpRIGNNVVIASGAKVIGNVTIGNNVMIGSGSIV 71
Cdd:cd03351     7 IVDPGAKIGENVEIGPFCVIGP------NV-EIGDGTVIGSHVVIDGPTTIGKNNRIFPFASI 62
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
39-67 2.46e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 32.69  E-value: 2.46e-03
                          10        20
                  ....*....|....*....|....*....
gi 2551177256  39 PRIGNNVVIASGAKVIGNVTIGNNVMIGS 67
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
14-71 3.34e-03

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 35.07  E-value: 3.34e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256  14 AIIGDNCTIYHSVTIG--SVRGPKGgvpRIGNNVVIASGAKVIGNVTIGNNVMIGSGSIV 71
Cdd:PRK05289    9 AIVEPGAKIGENVEIGpfCVIGPNV---VIGDGTVIGSHVVIDGHTTIGKNNRIFPFASI 65
PLN02296 PLN02296
carbonate dehydratase
 14-103 4.35e-03

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 34.72  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256  14 AIIGDNCTIYHSVTIGSVrgpkggvpRIGNNVVIASGAKVIGNVTIGNNVMIGSGSIVV--TDIPDNSVVVGIPGKVISK 91
Cdd:PLN02296  120 TIIGDNVTIGHSAVLHGC--------TVEDEAFVGMGATLLDGVVVEKHAMVAAGALVRqnTRIPSGEVWAGNPAKFLRK 191

                          90
                  ....*....|..
gi 2551177256  92 EGLEHTKYYSKN 103
Cdd:PLN02296  192 LTEEEIAFISQS 203
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 42-81 4.99e-03

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 34.62  E-value: 4.99e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2551177256  42 GNNVVIASGAKVIGNVTIGNNVMIGSGSIVV-TDIPDNSVV 81
Cdd:PRK09451  269 GRDVEIDTNVIIEGNVTLGNRVKIGAGCVLKnCVIGDDCEI 309
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 40-71 5.05e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 34.73  E-value: 5.05e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2551177256  40 RIGNNVVIASGAkVIG-NVTIGNNVMIGSGSIV 71
Cdd:PRK00892  114 KIGEGVSIGPNA-VIGaGVVIGDGVVIGAGAVI 145
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 5-72 7.45e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 34.34  E-value: 7.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2551177256   5 YSCIVINGAAIIGDNCTIYHSVTIGS------------VRGP-KGGVpRIGNNVVI---------ASGAKVIGN------ 56
Cdd:PRK00892  158 HANVTIYHAVRIGNRVIIHSGAVIGSdgfgfandrggwVKIPqLGRV-IIGDDVEIganttidrgALDDTVIGEgvkidn 236

                          90
                  ....*....|....*..
gi 2551177256  57 -VTIGNNVMIGSGSIVV 72
Cdd:PRK00892  237 lVQIAHNVVIGRHTAIA 253
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 40-81 7.47e-03

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: 33.92  E-value: 7.47e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2551177256  40 RIGNNVVIASGAKVIGNVTIGNNVMIGSGS--------IVV---TDIPDNSVV 81
Cdd:cd04645     1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAvlrgdvnpIRIgerTNIQDGSVL 53
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 14-71 8.10e-03

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: 33.92  E-value: 8.10e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2551177256  14 AIIGDNCTIYHSVTIGSvrgpkgGVpRIGNNVVIASGakvignVTIGNNVMIGSGSIV 71
Cdd:cd03352     2 AKIGENVSIGPNAVIGE------GV-VIGDGVVIGPG------VVIGDGVVIGDDCVI 46
 
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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