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Conserved domains on  [gi|1277025298|gb|PIQ34809|]
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serine O-acetyltransferase [Zetaproteobacteria bacterium CG17_big_fil_post_rev_8_21_14_2_50_50_13]

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 ...
 10-180 9.38e-106

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: 303.16  E-value: 9.38e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  10 LIKLIKEDVACVFERDPAARTIVEVLLTYPGVHALILQRVANRLWHRQWRLTARFISFVTRALTNVDIHPGATIGRRFFI 89
Cdd:COG1045     1 MLKALREDIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHPGATIGRGFFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  90 DHGACVVIGETAEIGRDVTLYHGVTLGGTSWNKGKRHPTLEDGVMVGAGAKILGPITVHANARVGANSVVIGDVPAGCTV 169
Cdd:COG1045    81 DHGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTV 160

                         170
                  ....*....|.
gi 1277025298 170 VGIPGKVVQVK 180
Cdd:COG1045   161 VGVPARIVKRK 171
 
Name Accession Description Interval E-value
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 10-180 9.38e-106

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: 303.16  E-value: 9.38e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  10 LIKLIKEDVACVFERDPAARTIVEVLLTYPGVHALILQRVANRLWHRQWRLTARFISFVTRALTNVDIHPGATIGRRFFI 89
Cdd:COG1045     1 MLKALREDIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHPGATIGRGFFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  90 DHGACVVIGETAEIGRDVTLYHGVTLGGTSWNKGKRHPTLEDGVMVGAGAKILGPITVHANARVGANSVVIGDVPAGCTV 169
Cdd:COG1045    81 DHGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTV 160

                         170
                  ....*....|.
gi 1277025298 170 VGIPGKVVQVK 180
Cdd:COG1045   161 VGVPARIVKRK 171
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 14-175 2.23e-89

serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 261.46  E-value: 2.23e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  14 IKEDVACVFERDPAARTIVEVLLTYPGVHALILQRVANRLWHRQWRLTARFISFVTRALTNVDIHPGATIGRRFFIDHGA 93
Cdd:TIGR01172   1 IREDIRAVRERDPAARSYLEVLLYYPGFHALWAYRFAHFLWKRGFKFLARLLSNFIRVLTGVDIHPGARIGRGVFIDHGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  94 CVVIGETAEIGRDVTLYHGVTLGGTSWNKGKRHPTLEDGVMVGAGAKILGPITVHANARVGANSVVIGDVPAGCTVVGIP 173
Cdd:TIGR01172  81 GVVIGETAVIGDDVTIYHGVTLGGTGKEKGKRHPTIGEGVMIGAGAKVLGNIEVGENAKIGANSVVLKDVPPGATVVGVP 160


                  ..
gi 1277025298 174 GK 175
Cdd:TIGR01172 161 AR 162
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 73-173 2.18e-51

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: 162.61  E-value: 2.18e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  73 TNVDIHPGATIGRRFFIDHGACVVIGETAEIGRDVTLYHGVTLGGTSWNKGKRHPTLEDGVMVGAGAKILGPITVHANAR 152
Cdd:cd03354     1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                          90       100
                  ....*....|....*....|.
gi 1277025298 153 VGANSVVIGDVPAGCTVVGIP 173
Cdd:cd03354    81 IGANAVVTKDVPANSTVVGVP 101
cysE PRK11132
serine acetyltransferase; Provisional
 17-197 4.43e-47

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 157.55  E-value: 4.43e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  17 DVACVFERDPAARTIVEVLLTYPGVHALILQRVANRLWHRQWRLTARFISFVTRALTNVDIHPGATIGRRFFIDHGACVV 96
Cdd:PRK11132   84 DIQAVRTRDPAVDKYSTPLLYLKGFHALQAYRIGHWLWNQGRRALAIYLQNQISVAFQVDIHPAAKIGRGIMLDHATGIV 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  97 IGETAEIGRDVTLYHGVTLGGTSWNKGKRHPTLEDGVMVGAGAKILGPITVHANARVGANSVVIGDVPAGCTVVGIPGKV 176
Cdd:PRK11132  164 IGETAVIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARI 243

                         170       180
                  ....*....|....*....|.
gi 1277025298 177 VQVKSAGHPNqfgIDLDHHLI 197
Cdd:PRK11132  244 VGKPESDKPS---MDMDQHFN 261
SATase_N pfam06426
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 9-44 3.57e-03

Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a sequence that is conserved in plants and bacteria.


Pssm-ID: 461909 [Multi-domain]  Cd Length: 104  Bit Score: 35.90  E-value: 3.57e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1277025298   9 SLIKLIKEDVACVFERDPAARTIVEVLLTYPGVHAL 44
Cdd:pfam06426  68 EIVEAARADLQAVYERDPACDRYLTPLLYFKGFHAL 103
SATase_N smart00971
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 9-44 9.84e-03

Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a sequence that is conserved in plants.and bacteria.


Pssm-ID: 198039 [Multi-domain]  Cd Length: 105  Bit Score: 34.82  E-value: 9.84e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1277025298    9 SLIKLIKEDVACVFERDPAARTIVEVLLTYPGVHAL 44
Cdd:smart00971  68 EIVEAAAADIQAVYDRDPACDRYLTPLLYFKGFHAL 103
 
Name Accession Description Interval E-value
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 10-180 9.38e-106

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: 303.16  E-value: 9.38e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  10 LIKLIKEDVACVFERDPAARTIVEVLLTYPGVHALILQRVANRLWHRQWRLTARFISFVTRALTNVDIHPGATIGRRFFI 89
Cdd:COG1045     1 MLKALREDIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHPGATIGRGFFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  90 DHGACVVIGETAEIGRDVTLYHGVTLGGTSWNKGKRHPTLEDGVMVGAGAKILGPITVHANARVGANSVVIGDVPAGCTV 169
Cdd:COG1045    81 DHGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTV 160

                         170
                  ....*....|.
gi 1277025298 170 VGIPGKVVQVK 180
Cdd:COG1045   161 VGVPARIVKRK 171
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 14-175 2.23e-89

serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 261.46  E-value: 2.23e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  14 IKEDVACVFERDPAARTIVEVLLTYPGVHALILQRVANRLWHRQWRLTARFISFVTRALTNVDIHPGATIGRRFFIDHGA 93
Cdd:TIGR01172   1 IREDIRAVRERDPAARSYLEVLLYYPGFHALWAYRFAHFLWKRGFKFLARLLSNFIRVLTGVDIHPGARIGRGVFIDHGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  94 CVVIGETAEIGRDVTLYHGVTLGGTSWNKGKRHPTLEDGVMVGAGAKILGPITVHANARVGANSVVIGDVPAGCTVVGIP 173
Cdd:TIGR01172  81 GVVIGETAVIGDDVTIYHGVTLGGTGKEKGKRHPTIGEGVMIGAGAKVLGNIEVGENAKIGANSVVLKDVPPGATVVGVP 160


                  ..
gi 1277025298 174 GK 175
Cdd:TIGR01172 161 AR 162
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 73-173 2.18e-51

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: 162.61  E-value: 2.18e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  73 TNVDIHPGATIGRRFFIDHGACVVIGETAEIGRDVTLYHGVTLGGTSWNKGKRHPTLEDGVMVGAGAKILGPITVHANAR 152
Cdd:cd03354     1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                          90       100
                  ....*....|....*....|.
gi 1277025298 153 VGANSVVIGDVPAGCTVVGIP 173
Cdd:cd03354    81 IGANAVVTKDVPANSTVVGVP 101
cysE PRK11132
serine acetyltransferase; Provisional
 17-197 4.43e-47

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 157.55  E-value: 4.43e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  17 DVACVFERDPAARTIVEVLLTYPGVHALILQRVANRLWHRQWRLTARFISFVTRALTNVDIHPGATIGRRFFIDHGACVV 96
Cdd:PRK11132   84 DIQAVRTRDPAVDKYSTPLLYLKGFHALQAYRIGHWLWNQGRRALAIYLQNQISVAFQVDIHPAAKIGRGIMLDHATGIV 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  97 IGETAEIGRDVTLYHGVTLGGTSWNKGKRHPTLEDGVMVGAGAKILGPITVHANARVGANSVVIGDVPAGCTVVGIPGKV 176
Cdd:PRK11132  164 IGETAVIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARI 243

                         170       180
                  ....*....|....*....|.
gi 1277025298 177 VQVKSAGHPNqfgIDLDHHLI 197
Cdd:PRK11132  244 VGKPESDKPS---MDMDQHFN 261
PLN02357 PLN02357
serine acetyltransferase
 7-177 2.34e-44

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 152.73  E-value: 2.34e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298   7 NLSLIKLIKEDVACVFERDPAARTIVEVLLTYPGVHALILQRVANRLWHRQWRLTARFISFVTRALTNVDIHPGATIGRR 86
Cdd:PLN02357  159 SPEIIESVKQDLRAVKERDPACISYVHCFLNFKGFLACQAHRIAHKLWTQGRKILALLIQNRVSEAFAVDIHPGAKIGQG 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  87 FFIDHGACVVIGETAEIGRDVTLYHGVTLGGTSWNKGKRHPTLEDGVMVGAGAKILGPITVHANARVGANSVVIGDVPAG 166
Cdd:PLN02357  239 ILLDHATGVVIGETAVVGNNVSILHNVTLGGTGKQSGDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPR 318

                         170
                  ....*....|.
gi 1277025298 167 CTVVGIPGKVV 177
Cdd:PLN02357  319 TTAVGNPARLI 329
PLN02694 PLN02694
serine O-acetyltransferase
 24-194 6.30e-43

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 147.48  E-value: 6.30e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  24 RDPAARTIVEVLLTYPGVHALILQRVANRLWHRQWRLTARFISFVTRALTNVDIHPGATIGRRFFIDHGACVVIGETAEI 103
Cdd:PLN02694  110 RDPACVSFSHCLLNYKGFLACQAHRVAHKLWTQSRRPLALALHSRISDVFAVDIHPAAKIGKGILFDHATGVVIGETAVI 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298 104 GRDVTLYHGVTLGGTSWNKGKRHPTLEDGVMVGAGAKILGPITVHANARVGANSVVIGDVPAGCTVVGIPGKVV--QVKS 181
Cdd:PLN02694  190 GNNVSILHHVTLGGTGKACGDRHPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLVggKEKP 269

                         170
                  ....*....|...
gi 1277025298 182 AGHPNQFGIDLDH 194
Cdd:PLN02694  270 AKHEECPGESMDH 282
PLN02739 PLN02739
serine acetyltransferase
 14-186 7.76e-42

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 146.33  E-value: 7.76e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  14 IKEDVACVFERDPAARTIVEVLLTYPGVHALILQRVANRLWHRQWRLTARFISFVTRALTNVDIHPGATIGRRFFIDHGA 93
Cdd:PLN02739  145 IRLDVQAFKDRDPACLSYSSAILHLKGYLALQAYRVAHKLWKQGRKLLALALQSRVSEVFGIDIHPAARIGKGILLDHGT 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  94 CVVIGETAEIGRDVTLYHGVTLGGTSWNKGKRHPTLEDGVMVGAGAKILGPITVHANARVGANSVVIGDVPAGCTVVGIP 173
Cdd:PLN02739  225 GVVIGETAVIGDRVSILHGVTLGGTGKETGDRHPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNP 304

                         170
                  ....*....|...
gi 1277025298 174 GKVVQVKSAGHPN 186
Cdd:PLN02739  305 AKLIGFVDEQDPS 317
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
66-177 7.95e-21

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 85.31  E-value: 7.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  66 SFVTRALTNVDIHPGATIGRRFFIDHGACVVIGETAEIGRDVTLY---HGVTLGGTSWNKGKrHPTLEDGVMVGAGAKIL 142
Cdd:COG0110    19 PGVRIYGGNITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILtgnHPIDDPATFPLRTG-PVTIGDDVWIGAGATIL 97

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1277025298 143 GPITVHANARVGANSVVIGDVPAGCTVVGIPGKVV 177
Cdd:COG0110    98 PGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVI 132
PRK10191 PRK10191
putative acyl transferase; Provisional
 47-180 8.67e-19

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 79.93  E-value: 8.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  47 QRVANRLWHRQWRLTARFIsfvTRALTNVDIHPGATIGRRFFIDHGACVVIGETAEIGRDVTLYHGVTLGgtswNKGKRH 126
Cdd:PRK10191   17 KNVLNNLWAAPLLVLYRII---TECFFGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGVTIG----NRGADN 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1277025298 127 ---PTLEDGVMVGAGAKILGPITVHANARVGANSVVIGDVPAGCTVVGIPGKVVQVK 180
Cdd:PRK10191   90 macPHIGNGVELGANVIILGDITIGNNVTVGAGSVVLDSVPDNALVVGEKARVKVIK 146
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 77-173 2.40e-16

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: 74.84  E-value: 2.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  77 IHPGATIGRRFFIDHGAcvVIGETAEIGRDVTLYHGVTLGGtswnkgkrHPTLEDGVMVGAGAKILGPITVHANARVGAN 156
Cdd:TIGR03570 114 INPDVRIGDNVIINTGA--IVEHDCVIGDFVHIAPGVTLSG--------GVVIGEGVFIGAGATIIQGVTIGAGAIVGAG 183

                          90
                  ....*....|....*..
gi 1277025298 157 SVVIGDVPAGCTVVGIP 173
Cdd:TIGR03570 184 AVVTKDIPDGGVVVGVP 200
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 82-177 2.85e-16

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


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 72.10  E-value: 2.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  82 TIGRRFFIDHGACVVIGETAEIGRDVTLYHGVTL----------GGTSWNKGKRHP-TLEDGVMVGAGAKILGPITVHAN 150
Cdd:cd04647     3 SIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIydhnhdiddpERPIEQGVTSAPiVIGDDVWIGANVVILPGVTIGDG 82

                          90       100
                  ....*....|....*....|....*..
gi 1277025298 151 ARVGANSVVIGDVPAGCTVVGIPGKVV 177
Cdd:cd04647    83 AVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 77-173 1.32e-15

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: 72.90  E-value: 1.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  77 IHPGATIGRRFFIDHGAcvVIGETAEIGRDVTLYHGVTLGGTSwnkgkrhpTLEDGVMVGAGAKILGPITVHANARVGAN 156
Cdd:cd03360   111 INPDARIGDNVIINTGA--VIGHDCVIGDFVHIAPGVVLSGGV--------TIGEGAFIGAGATIIQGVTIGAGAIIGAG 180

                          90
                  ....*....|....*..
gi 1277025298 157 SVVIGDVPAGCTVVGIP 173
Cdd:cd03360   181 AVVTKDVPDGSVVVGNP 197
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 73-177 7.26e-15

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: 68.68  E-value: 7.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  73 TNVDIHPGATIGRRFFIDHGacVVIGETAEIGRDVTLYHGVTL------GGTSWNKGK-RHPTLEDGVMVGAGAKILGPI 145
Cdd:cd03358     9 TNVFIENDVKIGDNVKIQSN--VSIYEGVTIEDDVFIGPNVVFtndlypRSKIYRKWElKGTTVKRGASIGANATILPGV 86

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1277025298 146 TVHANARVGANSVVIGDVPAGCTVVGIPGKVV 177
Cdd:cd03358    87 TIGEYALVGAGAVVTKDVPPYALVVGNPARII 118
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 81-159 8.00e-13

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: 62.27  E-value: 8.00e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1277025298  81 ATIGRRFFIDHGAcvVIGETAEIGRDVTLYHGVTLGGTSWNKGKRHPTLEDGVMVGAGAKILGPITVHANARVGANSVV 159
Cdd:cd00208     1 VFIGEGVKIHPKA--VIRGPVVIGDNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVV 77
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 82-177 2.49e-12

Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively at the C6 position of the nonreducing end glucosyl moiety. GAT specifically acetylates galactopyranosides. Furthermore, MAT shows higher affinity toward artificial substrates containing an alkyl or hydrophobic chain as well as a glucosyl unit. Active MAT and GAT are homotrimers, with each subunit consisting of an N-terminal alpha-helical region and a C-terminal left-handed parallel alpha-helix (LbH) subdomain with 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100047 [Multi-domain]  Cd Length: 169  Bit Score: 63.21  E-value: 2.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  82 TIGRRFFIDHGAC------VVIGETAEIGRDVTLY---HGV--TLGGTSWNKGKrhP-TLEDGVMVGAGAKILGPITVHA 149
Cdd:cd03357    64 HIGDNFYANFNCTildvapVTIGDNVLIGPNVQIYtagHPLdpEERNRGLEYAK--PiTIGDNVWIGGGVIILPGVTIGD 141

                          90       100
                  ....*....|....*....|....*...
gi 1277025298 150 NARVGANSVVIGDVPAGCTVVGIPGKVV 177
Cdd:cd03357   142 NSVIGAGSVVTKDIPANVVAAGNPARVI 169
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 77-177 4.67e-09

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 54.26  E-value: 4.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  77 IHPGAT------IGRRFFIDHGACV-------VIGE----------------TAEIGRDVTLYHGVTLGGtswnkgkrhP 127
Cdd:COG0663    19 VAPTAVvigdvtIGEDVSVWPGAVLrgdvgpiRIGEgsniqdgvvlhvdpgyPLTIGDDVTIGHGAILHG---------C 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1277025298 128 TLEDGVMVGAGAKILGPITVHANARVGANSVVIGD--VPAGCTVVGIPGKVV 177
Cdd:COG0663    90 TIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGkvVPPGSLVVGSPAKVV 141
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 80-170 5.32e-09

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: 53.54  E-value: 5.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  80 GATIGRRFFIDHGAcvVIGETAEIGRDVTLYHGVTLGGTSWNKGKRHPTLEDGVMVGAGAKILGPITVHANARVGANSVV 159
Cdd:cd03350    31 GAYVDEGTMVDSWA--TVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVL 108

                          90       100
                  ....*....|....*....|....*.
gi 1277025298 160 I---------------GDVPAGCTVV 170
Cdd:cd03350   109 TqstpiydretgeiyyGRVPPGSVVV 134
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 77-161 4.39e-08

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: 53.10  E-value: 4.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  77 IHPGATIGRRFFIdhGACVVIGETAEIGRDVTLYHGVTLGgtswnkgkrhptleDGVMVGAGAkILGP-ITVHANARVGA 155
Cdd:COG1044   105 IDPSAKIGEGVSI--GPFAVIGAGVVIGDGVVIGPGVVIG--------------DGVVIGDDC-VLHPnVTIYERCVIGD 167

                          90
                  ....*....|.
gi 1277025298 156 N-----SVVIG 161
Cdd:COG1044   168 RviihsGAVIG 178
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 82-177 5.12e-08

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: 50.87  E-value: 5.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  82 TIGRRFFIDHGACVVIGETA--EIGRDVTLYHGVTLGGTswnkgkrhpTLEDGVMVGAGAKILGPITVHANARVGANSVV 159
Cdd:cd04645    40 RIGERTNIQDGSVLHVDPGYptIIGDNVTVGHGAVLHGC---------TIGDNCLIGMGAIILDGAVIGKGSIVAAGSLV 110

                          90       100
                  ....*....|....*....|
gi 1277025298 160 IGD--VPAGCTVVGIPGKVV 177
Cdd:cd04645   111 PPGkvIPPGSLVAGSPAKVV 130
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 74-177 1.22e-07

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


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 48.76  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  74 NVDIHPGATIGRRFFIDHGACVVIGetaeigRDVTLYHGVTL--GGTSWNKG----KRHP-TLEDGVMVGAGAKILGPIT 146
Cdd:cd05825     3 NLTIGDNSWIGEGVWIYNLAPVTIG------SDACISQGAYLctGSHDYRSPafplITAPiVIGDGAWVAAEAFVGPGVT 76

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1277025298 147 VHANARVGANSVVIGDVPAGCTVVGIPGKVV 177
Cdd:cd05825    77 IGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 82-177 2.91e-07

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: 48.69  E-value: 2.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  82 TIGRRFFIDHGACVVIGETAEIGRDVTLYHGVTLGGT---------------SWNKG-----------KRHPTLEDGVMV 135
Cdd:cd03349     3 SVGDYSYGSGPDCDVGGDKLSIGKFCSIAPGVKIGLGgnhptdwvstypfyiFGGEWeddakfddwpsKGDVIIGNDVWI 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1277025298 136 GAGAKILGPITVHANARVGANSVVIGDVPAGCTVVGIPGKVV 177
Cdd:cd03349    83 GHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVI 124
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 74-175 3.59e-06

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: 46.25  E-value: 3.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  74 NVDIHPGATIGRRFF----IDHGAC----VVIGETAEIGRDVTLYHGVTLGGTSwnkgkrhpTLEDGVMVGAGAKILGPI 145
Cdd:cd03352    98 DVEIGANTTIDRGALgdtvIGDGTKidnlVQIAHNVRIGENCLIAAQVGIAGST--------TIGDNVIIGGQVGIAGHL 169

                          90       100       110
                  ....*....|....*....|....*....|
gi 1277025298 146 TVHANARVGANSVVIGDVPAGCTVVGIPGK 175
Cdd:cd03352   170 TIGDGVVIGAGSGVTSIVPPGEYVSGTPAQ 199
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 128-173 8.40e-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: 46.16  E-value: 8.40e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1277025298 128 TLEDGVMVGAGAKILGPITVHANARVGANSVVIGDVPAGCTVVGIP 173
Cdd:COG1044   260 KIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSGSP 305
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 77-161 1.00e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 45.90  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  77 IHPGATIGRRFFIDHGAcvVIGETAEIGRDVTLYHGVTLGgtswnkgkrhptleDGVMVGAGAKILGPITVHANARVGAN 156
Cdd:PRK00892  109 IDPSAKIGEGVSIGPNA--VIGAGVVIGDGVVIGAGAVIG--------------DGVKIGADCRLHANVTIYHAVRIGNR 172

                          90
                  ....*....|
gi 1277025298 157 -----SVVIG 161
Cdd:PRK00892  173 viihsGAVIG 182
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 101-180 1.01e-05

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 46.17  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298 101 AEIGRDVTL--------YHGVtlggtswNKgkrHPT-LEDGVMVGAGAKILGPITVHANARVGANSVVIGDVPAGCTVVG 171
Cdd:COG1207   370 AEIGEGVNIgagtitcnYDGV-------NK---HRTvIGDGAFIGSNTNLVAPVTIGDGATIGAGSTITKDVPAGALAIA 439

                          90
                  ....*....|....*
gi 1277025298 172 ------IPGKVVQVK 180
Cdd:COG1207   440 rarqrnIEGWVRPKK 454
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 83-178 1.01e-05

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 44.99  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  83 IGRRFFIDHGACVVIGETAEIGRDVTLYHGVTLGGTSwnkgkrHP----------------TLEDGVMVGAGAKILGPIT 146
Cdd:PRK09527   78 IGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTG------HPvhhelrkngemysfpiTIGNNVWIGSHVVINPGVT 151

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1277025298 147 VHANARVGANSVVIGDVPAGCTVVGIPGKVVQ 178
Cdd:PRK09527  152 IGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIR 183
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 74-169 1.20e-05

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: 45.39  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  74 NVDIHPGATIGRRFFIdhGACVVIGETAEIGRDVTLYHGVTLGgtswnkgkrhptleDGVMVGAGAkilgpiTVHANARV 153
Cdd:COG1044   120 FAVIGAGVVIGDGVVI--GPGVVIGDGVVIGDDCVLHPNVTIY--------------ERCVIGDRV------IIHSGAVI 177

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1277025298 154 GAN-------------------SVVIGD---VPAGCTV 169
Cdd:COG1044   178 GADgfgfapdedggwvkipqlgRVVIGDdveIGANTTI 215
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 97-171 2.28e-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: 43.95  E-value: 2.28e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1277025298  97 IGETAEIGRDVTLYHGVTLGGTSwnkgkrhpTLEDGVMVGAGAkILGPITVHANARVGANSVVIGDVPAGCTVVG 171
Cdd:cd03353    12 IDGDVEIGVDVVIDPGVILEGKT--------VIGEDCVIGPNC-VIKDSTIGDGVVIKASSVIEGAVIGNGATVG 77
PRK10502 PRK10502
putative acyl transferase; Provisional
 74-177 2.54e-05

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 43.78  E-value: 2.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  74 NVDIHPGATIGRRFFIDHGACVVIGETA--------EIGRDVTLYHGVTLGGTSWNKGKRH------P-TLEDGVMVGAG 138
Cdd:PRK10502   57 GVVIRPSVRITYPWKLTIGDYAWIGDDVwlynlgeiTIGAHCVISQKSYLCTGSHDYSDPHfdlntaPiVIGEGCWLAAD 136

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1277025298 139 AkILGP-ITVHANARVGANSVVIGDVPAGCTVVGIPGKVV 177
Cdd:PRK10502  137 V-FVAPgVTIGSGAVVGARSSVFKSLPANTICRGNPAVPI 175
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 101-166 3.23e-05

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 44.35  E-value: 3.23e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1277025298 101 AEIGRDVTL--------YHGVtlggtswnkgKRHPTL-EDGVMVGAGAKILGPITVHANARVGANSVVIGDVPAG 166
Cdd:PRK14355  373 ATIGRNVNIgcgtitcnYDGV----------KKHRTViEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPPD 437
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 101-171 4.34e-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: 43.18  E-value: 4.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298 101 AEIGRDVTL--------YHGVtlggtswNKgkrHPT-LEDGVMVGAGAKILGPITVHANARVGANSVVIGDVPAGCTVVG 171
Cdd:cd03353   120 AEIGEGVNIgagtitcnYDGV-------NK---HRTvIGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPGALAIA 189
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 74-169 4.98e-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: 43.17  E-value: 4.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  74 NVDIHPGATIGRRFFIdhGACVVIGETAEIGRDVTLYHGVTLGgtswnkgkrhptleDGVMVGAGAkilgpiTVHANARV 153
Cdd:cd03352    13 NAVIGEGVVIGDGVVI--GPGVVIGDGVVIGDDCVIHPNVTIY--------------EGCIIGDRV------IIHSGAVI 70

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1277025298 154 GAN------------------SVVIGD---VPAGCTV 169
Cdd:cd03352    71 GSDgfgfapdgggwvkipqlgGVIIGDdveIGANTTI 107
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 65-171 5.24e-05

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


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 43.97  E-value: 5.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  65 ISFVTRALtnvdihpGATIGRRFFIdHGACVVIGETAEIGRDVTLYHGVTLGGTSWNKGKRHptledgvmvgagakiLGP 144
Cdd:TIGR02353 104 YSLYLRAL-------GAKIGKGVDI-GSLPPVCTDLLTIGAGTIVRKEVMLLGYRAERGRLH---------------TGP 160

                          90       100
                  ....*....|....*....|....*..
gi 1277025298 145 ITVHANARVGANSVVIGDvpagcTVVG 171
Cdd:TIGR02353 161 VTLGRDAFIGTRSTLDID-----TSIG 182
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 74-184 1.17e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 42.43  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  74 NVDIHPGATIGRRFFIdhGACVVIGETAEIGRD------VTLYHGVTLG----------------GTSWNKGKRHP---- 127
Cdd:PRK00892  124 NAVIGAGVVIGDGVVI--GAGAVIGDGVKIGADcrlhanVTIYHAVRIGnrviihsgavigsdgfGFANDRGGWVKipql 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298 128 ---TLEDGVMVGAGAKI----LGPITVHA------------NARVGANSVVIGDVP-AGCTVVG----IPGkvvQVKSAG 183
Cdd:PRK00892  202 grvIIGDDVEIGANTTIdrgaLDDTVIGEgvkidnlvqiahNVVIGRHTAIAAQVGiAGSTKIGrycmIGG---QVGIAG 278


                  .
gi 1277025298 184 H 184
Cdd:PRK00892  279 H 279
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 81-170 1.84e-04

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 42.23  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  81 ATIGRRFFIDHGACV---VIGETAEIG-RDVTL-YHGVTlggtswnkgKRHPTLEDGVMVGAGAKILGPITVHANARVGA 155
Cdd:PRK14352  358 ATIGRGTKVPHLTYVgdaDIGEHSNIGaSSVFVnYDGVN---------KHRTTIGSHVRTGSDTMFVAPVTVGDGAYTGA 428

                          90
                  ....*....|....*
gi 1277025298 156 NSVVIGDVPAGCTVV 170
Cdd:PRK14352  429 GTVIREDVPPGALAV 443
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 97-166 2.90e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 41.74  E-value: 2.90e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277025298  97 IGEtAEIGRDVTL--------YHGvtlggtswnKGKRHPTLEDGVMVGAGAKILGPITVHANARVGANSVVIGDVPAG 166
Cdd:PRK14354  366 IGD-AEVGENVNIgcgtitvnYDG---------KNKFKTIIGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPED 433
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 77-162 4.46e-04

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: 40.77  E-value: 4.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  77 IHPGAtigrrffidhgacvVIGETAEIGRDVTLYHGVTLGgtswnkgkrhptleDGVMVGAGAKIlgpitvHANARVGAN 156
Cdd:COG1044    99 IHPSA--------------VIDPSAKIGEGVSIGPFAVIG--------------AGVVIGDGVVI------GPGVVIGDG 144


                  ....*.
gi 1277025298 157 sVVIGD 162
Cdd:COG1044   145 -VVIGD 149
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 81-161 4.75e-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: 40.08  E-value: 4.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  81 ATIGRRFFIDHGacVVIGETAEIGRDVTLYHGVTLGgtswnkgkrhptleDGVMVGAGAKILGPITVHANARVGANSV-- 158
Cdd:cd03352     2 AKIGENVSIGPN--AVIGEGVVIGDGVVIGPGVVIG--------------DGVVIGDDCVIHPNVTIYEGCIIGDRVIih 65


                  ....*.
gi 1277025298 159 ---VIG 161
Cdd:cd03352    66 sgaVIG 71
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 40-179 5.03e-04

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 39.86  E-value: 5.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  40 GVHALILQRVANRLWHRQWRL--------TARFISFVTRALTNVDIHPGA-TIGRRFFID--------HGACVvigETAE 102
Cdd:PRK09677   11 GFIRLVRDVLLTKVFYRNCRIirfpfyirNDGSINFGEGFTSGVGLRLDAfGRGKLFFGDnvqvndyvHIACI---ESIT 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298 103 IGRDVTLY---------HGVTLGGTSWNKGKRHP---TLE-------DGVMVGAGAKILGPITVHANARVGANSVVIGDV 163
Cdd:PRK09677   88 IGRDTLIAskvfitdhnHGSFKHSDDFSSPNLPPdmrTLEssavvigQRVWIGENVTILPGVSIGNGCIVGANSVVTKSI 167

                         170
                  ....*....|....*.
gi 1277025298 164 PAGCTVVGIPGKVVQV 179
Cdd:PRK09677  168 PENTVIAGNPAKIIKK 183
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 101-165 5.14e-04

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 40.90  E-value: 5.14e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277025298 101 AEIGRDVTLYHGVTLggTSWNKGKRHPT-LEDGVMVGAGAKILGPITVHANARVGANSVVIGDVPA 165
Cdd:PRK14357  359 ATVGKNVNIGAGTIT--CNYDGKKKNPTfIEDGAFIGSNSSLVAPVRIGKGALIGAGSVITEDVPP 422
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 97-169 1.07e-03

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 40.01  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  97 IGETAEIGRDVTLYHGVTLGGTSwnkgkrhpTLEDGVMVGAGAKIlgpitvhANARVGANSVV---------IGDvpaGC 167
Cdd:COG1207   263 IDGDVEIGRDVVIDPNVILEGKT--------VIGEGVVIGPNCTL-------KDSTIGDGVVIkysviedavVGA---GA 324


                  ..
gi 1277025298 168 TV 169
Cdd:COG1207   325 TV 326
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 103-177 1.45e-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: 38.95  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298 103 IGRDVTLYHGVTLGGtswnkgkrHPTLEDGVMVGAGAkilgpiTVHANARVGAN------SVVIGDVPAGCTVVGIPGKV 176
Cdd:cd03351   123 IGNNVILANNATLAG--------HVEIGDYAIIGGLS------AVHQFCRIGRHamvgggSGVVQDVPPYVIAAGNRARL 188


                  .
gi 1277025298 177 V 177
Cdd:cd03351   189 R 189
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 122-166 1.58e-03

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 39.32  E-value: 1.58e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1277025298 122 KGKRHPTLEDGVMVGAGAKILGPITVHANARVGANSVVIGDVPAG 166
Cdd:PRK14356  394 VNKHRTVIGEGAFIGSNTALVAPVTIGDGALVGAGSVITKDVPDG 438
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 90-178 1.64e-03

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: 37.93  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  90 DHGACVVIGETAEIGRDVTLyHGVTLGgtswnkgkrhptleDGVMVGAGAKILGPITVHANARVGANSVVI--GDVPAGC 167
Cdd:cd04650    57 DHGYPTEIGDYVTIGHNAVV-HGAKVG--------------NYVIVGMGAILLNGAKIGDHVIIGAGAVVTpgKEIPDYS 121

                          90
                  ....*....|.
gi 1277025298 168 TVVGIPGKVVQ 178
Cdd:cd04650   122 LVLGVPAKVVR 132
PLN02296 PLN02296
carbonate dehydratase
 103-175 2.57e-03

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 38.18  E-value: 2.57e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1277025298 103 IGRDVTLYHGVTLGGTswnkgkrhpTLEDGVMVGAGAKILGPITVHANARVGANSVVIGD--VPAGCTVVGIPGK 175
Cdd:PLN02296  122 IGDNVTIGHSAVLHGC---------TVEDEAFVGMGATLLDGVVVEKHAMVAAGALVRQNtrIPSGEVWAGNPAK 187
SATase_N pfam06426
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 9-44 3.57e-03

Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a sequence that is conserved in plants and bacteria.


Pssm-ID: 461909 [Multi-domain]  Cd Length: 104  Bit Score: 35.90  E-value: 3.57e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1277025298   9 SLIKLIKEDVACVFERDPAARTIVEVLLTYPGVHAL 44
Cdd:pfam06426  68 EIVEAARADLQAVYERDPACDRYLTPLLYFKGFHAL 103
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 64-173 5.41e-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: 37.81  E-value: 5.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  64 FISFVTRALtnvdihpGATIGRRFFIDhGACVVIGETAEIGRDVTLYHGVTLGGTSWNKG---KRHPTLEDGVMVGAGAK 140
Cdd:TIGR02353 588 FLPAILRLL-------GVKIGRGVYID-GTDLTERDLVTIGDDSTLNEGSVIQTHLFEDRvmkSDTVTIGDGATLGPGAI 659

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1277025298 141 ILGPITVHANARVGANSVVI-GD-VPAGCTVVGIP 173
Cdd:TIGR02353 660 VLYGVVMGEGSVLGPDSLVMkGEeVPAHTRWRGNP 694
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 77-177 5.97e-03

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


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 36.19  E-value: 5.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  77 IHPGA------TIGRRFFIDHGAC-------VVIGETAEI----------GRDVTLY------HGVTLGGTswnkgkrhp 127
Cdd:cd04745     9 VHPTAvligdvIIGKNCYIGPHASlrgdfgrIVIRDGANVqdncvihgfpGQDTVLEenghigHGAILHGC--------- 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1277025298 128 TLEDGVMVGAGAKILGPITVHANARVGANSVVIG--DVPAGCTVVGIPGKVV 177
Cdd:cd04745    80 TIGRNALVGMNAVVMDGAVIGEESIVGAMAFVKAgtVIPPRSLIAGSPAKVI 131
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 97-171 7.63e-03

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 37.21  E-value: 7.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  97 IGEtAEIGRDVTL--------YHGVtlggtswnkgKRHPT-LEDGVMVGAGAKILGPITVHANARVGANSVVIGDVPAGC 167
Cdd:PRK14360  363 IGD-ATLGEQVNIgagtitanYDGV----------KKHRTvIGDRSKTGANSVLVAPITLGEDVTVAAGSTITKDVPDNS 431


                  ....
gi 1277025298 168 TVVG 171
Cdd:PRK14360  432 LAIA 435
SATase_N smart00971
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 9-44 9.84e-03

Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a sequence that is conserved in plants.and bacteria.


Pssm-ID: 198039 [Multi-domain]  Cd Length: 105  Bit Score: 34.82  E-value: 9.84e-03
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 1277025298    9 SLIKLIKEDVACVFERDPAARTIVEVLLTYPGVHAL 44
Cdd:smart00971  68 EIVEAAAADIQAVYDRDPACDRYLTPLLYFKGFHAL 103
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 73-142 9.93e-03

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 34.15  E-value: 9.93e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277025298  73 TNVDIHPGATIGRRFFIDHGACVVIGETAEIGRDVTLYHGVTLGgtswnkgkrhptleDGVMVGAGAKIL 142
Cdd:cd00208    23 DNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGANAVIHGGVKIG--------------DNAVIGAGAVVT 78
 
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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