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Conserved domains on  [gi|1251371426|gb|PDE58473|]
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serine O-acetyltransferase [Listeria monocytogenes]

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 ...
 1-172 4.17e-88

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: 256.55  E-value: 4.17e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426   1 MPTRLKEDIATIIKNDPATKSFFDAFLTNPGLHALWWHRVANFFYRHKMVLFGKVLSQNARFWTNIEIHPGATIGRRLFI 80
Cdd:COG1045     1 MLKALREDIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHPGATIGRGFFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  81 DHGAGIVIGETAEIGDDVTIFHGVTLGGTGKDCGKRHPTVGDGALVSAGAKVLGPVEIGAGARIGAGAVVLKDVPPGATV 160
Cdd:COG1045    81 DHGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTV 160

                         170
                  ....*....|..
gi 1251371426 161 VGIPAKVVRLNG 172
Cdd:COG1045   161 VGVPARIVKRKG 172
 
Name Accession Description Interval E-value
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 1-172 4.17e-88

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: 256.55  E-value: 4.17e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426   1 MPTRLKEDIATIIKNDPATKSFFDAFLTNPGLHALWWHRVANFFYRHKMVLFGKVLSQNARFWTNIEIHPGATIGRRLFI 80
Cdd:COG1045     1 MLKALREDIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHPGATIGRGFFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  81 DHGAGIVIGETAEIGDDVTIFHGVTLGGTGKDCGKRHPTVGDGALVSAGAKVLGPVEIGAGARIGAGAVVLKDVPPGATV 160
Cdd:COG1045    81 DHGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTV 160

                         170
                  ....*....|..
gi 1251371426 161 VGIPAKVVRLNG 172
Cdd:COG1045   161 VGVPARIVKRKG 172
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 5-166 4.62e-75

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


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 223.32  E-value: 4.62e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426   5 LKEDIATIIKNDPATKSFFDAFLTNPGLHALWWHRVANFFYRHKMVLFGKVLSQNARFWTNIEIHPGATIGRRLFIDHGA 84
Cdd:TIGR01172   1 IREDIRAVRERDPAARSYLEVLLYYPGFHALWAYRFAHFLWKRGFKFLARLLSNFIRVLTGVDIHPGARIGRGVFIDHGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  85 GIVIGETAEIGDDVTIFHGVTLGGTGKDCGKRHPTVGDGALVSAGAKVLGPVEIGAGARIGAGAVVLKDVPPGATVVGIP 164
Cdd:TIGR01172  81 GVVIGETAVIGDDVTIYHGVTLGGTGKEKGKRHPTIGEGVMIGAGAKVLGNIEVGENAKIGANSVVLKDVPPGATVVGVP 160


                  ..
gi 1251371426 165 AK 166
Cdd:TIGR01172 161 AR 162
cysE PRK11132
serine acetyltransferase; Provisional
 8-168 1.81e-43

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 146.38  E-value: 1.81e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426   8 DIATIIKNDPATKSFFDAFLTNPGLHALWWHRVANFFYRHKMVLFGKVLSQNARFWTNIEIHPGATIGRRLFIDHGAGIV 87
Cdd:PRK11132   84 DIQAVRTRDPAVDKYSTPLLYLKGFHALQAYRIGHWLWNQGRRALAIYLQNQISVAFQVDIHPAAKIGRGIMLDHATGIV 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  88 IGETAEIGDDVTIFHGVTLGGTGKDCGKRHPTVGDGALVSAGAKVLGPVEIGAGARIGAGAVVLKDVPPGATVVGIPAKV 167
Cdd:PRK11132  164 IGETAVIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARI 243


                  .
gi 1251371426 168 V 168
Cdd:PRK11132  244 V 244
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 64-164 8.49e-43

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: 139.11  E-value: 8.49e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  64 TNIEIHPGATIGRRLFIDHGAGIVIGETAEIGDDVTIFHGVTLGGTGKDCGKRHPTVGDGALVSAGAKVLGPVEIGAGAR 143
Cdd:cd03354     1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                          90       100
                  ....*....|....*....|.
gi 1251371426 144 IGAGAVVLKDVPPGATVVGIP 164
Cdd:cd03354    81 IGANAVVTKDVPANSTVVGVP 101
 
Name Accession Description Interval E-value
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 1-172 4.17e-88

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: 256.55  E-value: 4.17e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426   1 MPTRLKEDIATIIKNDPATKSFFDAFLTNPGLHALWWHRVANFFYRHKMVLFGKVLSQNARFWTNIEIHPGATIGRRLFI 80
Cdd:COG1045     1 MLKALREDIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHPGATIGRGFFI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  81 DHGAGIVIGETAEIGDDVTIFHGVTLGGTGKDCGKRHPTVGDGALVSAGAKVLGPVEIGAGARIGAGAVVLKDVPPGATV 160
Cdd:COG1045    81 DHGTGVVIGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTV 160

                         170
                  ....*....|..
gi 1251371426 161 VGIPAKVVRLNG 172
Cdd:COG1045   161 VGVPARIVKRKG 172
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 5-166 4.62e-75

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


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 223.32  E-value: 4.62e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426   5 LKEDIATIIKNDPATKSFFDAFLTNPGLHALWWHRVANFFYRHKMVLFGKVLSQNARFWTNIEIHPGATIGRRLFIDHGA 84
Cdd:TIGR01172   1 IREDIRAVRERDPAARSYLEVLLYYPGFHALWAYRFAHFLWKRGFKFLARLLSNFIRVLTGVDIHPGARIGRGVFIDHGT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  85 GIVIGETAEIGDDVTIFHGVTLGGTGKDCGKRHPTVGDGALVSAGAKVLGPVEIGAGARIGAGAVVLKDVPPGATVVGIP 164
Cdd:TIGR01172  81 GVVIGETAVIGDDVTIYHGVTLGGTGKEKGKRHPTIGEGVMIGAGAKVLGNIEVGENAKIGANSVVLKDVPPGATVVGVP 160


                  ..
gi 1251371426 165 AK 166
Cdd:TIGR01172 161 AR 162
cysE PRK11132
serine acetyltransferase; Provisional
 8-168 1.81e-43

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 146.38  E-value: 1.81e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426   8 DIATIIKNDPATKSFFDAFLTNPGLHALWWHRVANFFYRHKMVLFGKVLSQNARFWTNIEIHPGATIGRRLFIDHGAGIV 87
Cdd:PRK11132   84 DIQAVRTRDPAVDKYSTPLLYLKGFHALQAYRIGHWLWNQGRRALAIYLQNQISVAFQVDIHPAAKIGRGIMLDHATGIV 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  88 IGETAEIGDDVTIFHGVTLGGTGKDCGKRHPTVGDGALVSAGAKVLGPVEIGAGARIGAGAVVLKDVPPGATVVGIPAKV 167
Cdd:PRK11132  164 IGETAVIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARI 243


                  .
gi 1251371426 168 V 168
Cdd:PRK11132  244 V 244
PLN02739 PLN02739
serine acetyltransferase
 3-170 6.91e-43

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 147.10  E-value: 6.91e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426   3 TRLKEDIATIIKNDPATKSFFDAFLTNPGLHALWWHRVANFFYRHKMVLFGKVLSQNARFWTNIEIHPGATIGRRLFIDH 82
Cdd:PLN02739  143 SSIRLDVQAFKDRDPACLSYSSAILHLKGYLALQAYRVAHKLWKQGRKLLALALQSRVSEVFGIDIHPAARIGKGILLDH 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  83 GAGIVIGETAEIGDDVTIFHGVTLGGTGKDCGKRHPTVGDGALVSAGAKVLGPVEIGAGARIGAGAVVLKDVPPGATVVG 162
Cdd:PLN02739  223 GTGVVIGETAVIGDRVSILHGVTLGGTGKETGDRHPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAG 302


                  ....*...
gi 1251371426 163 IPAKVVRL 170
Cdd:PLN02739  303 NPAKLIGF 310
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 64-164 8.49e-43

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: 139.11  E-value: 8.49e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  64 TNIEIHPGATIGRRLFIDHGAGIVIGETAEIGDDVTIFHGVTLGGTGKDCGKRHPTVGDGALVSAGAKVLGPVEIGAGAR 143
Cdd:cd03354     1 TGIDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVK 80

                          90       100
                  ....*....|....*....|.
gi 1251371426 144 IGAGAVVLKDVPPGATVVGIP 164
Cdd:cd03354    81 IGANAVVTKDVPANSTVVGVP 101
PLN02357 PLN02357
serine acetyltransferase
 5-168 1.30e-41

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 143.87  E-value: 1.30e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426   5 LKEDIATIIKNDPATKSFFDAFLTNPGLHALWWHRVANFFYRHKMVLFGKVLSQNARFWTNIEIHPGATIGRRLFIDHGA 84
Cdd:PLN02357  166 VKQDLRAVKERDPACISYVHCFLNFKGFLACQAHRIAHKLWTQGRKILALLIQNRVSEAFAVDIHPGAKIGQGILLDHAT 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  85 GIVIGETAEIGDDVTIFHGVTLGGTGKDCGKRHPTVGDGALVSAGAKVLGPVEIGAGARIGAGAVVLKDVPPGATVVGIP 164
Cdd:PLN02357  246 GVVIGETAVVGNNVSILHNVTLGGTGKQSGDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNP 325


                  ....
gi 1251371426 165 AKVV 168
Cdd:PLN02357  326 ARLI 329
PLN02694 PLN02694
serine O-acetyltransferase
 16-168 7.95e-40

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 137.47  E-value: 7.95e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  16 DPATKSFFDAFLTNPGLHALWWHRVANFFYRHKMVLFGKVLSQNARFWTNIEIHPGATIGRRLFIDHGAGIVIGETAEIG 95
Cdd:PLN02694  111 DPACVSFSHCLLNYKGFLACQAHRVAHKLWTQSRRPLALALHSRISDVFAVDIHPAAKIGKGILFDHATGVVIGETAVIG 190

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1251371426  96 DDVTIFHGVTLGGTGKDCGKRHPTVGDGALVSAGAKVLGPVEIGAGARIGAGAVVLKDVPPGATVVGIPAKVV 168
Cdd:PLN02694  191 NNVSILHHVTLGGTGKACGDRHPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLV 263
PRK10191 PRK10191
putative acyl transferase; Provisional
 67-167 1.29e-14

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 67.99  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  67 EIHPGATIGRRLFIDHGAGIVIGETAEIGDDVTIFHGVTLGGTGKD---CgkrhPTVGDGALVSAGAKVLGPVEIGAGAR 143
Cdd:PRK10191   43 EIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGVTIGNRGADnmaC----PHIGNGVELGANVIILGDITIGNNVT 118

                          90       100
                  ....*....|....*....|....
gi 1251371426 144 IGAGAVVLKDVPPGATVVGIPAKV 167
Cdd:PRK10191  119 VGAGSVVLDSVPDNALVVGEKARV 142
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
48-169 2.43e-13

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 64.12  E-value: 2.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  48 KMVLFGKVLSQNARFWTNIEIHPG-ATIGRRLFIDHGAGIVIGETAEIGDDVTIFHGVTLGGTG-------KDCGKRHP- 118
Cdd:COG0110     3 LLLLFGARIGDGVVIGPGVRIYGGnITIGDNVYIGPGVTIDDPGGITIGDNVLIGPGVTILTGNhpiddpaTFPLRTGPv 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1251371426 119 ------------------TVGDGALVSAGAkvlgpveigagarigagaVVLKDVPPGATVVGIPAKVVR 169
Cdd:COG0110    83 tigddvwigagatilpgvTIGDGAVVGAGS------------------VVTKDVPPYAIVAGNPARVIR 133
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 64-169 3.54e-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: 60.59  E-value: 3.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  64 TNIEIHPGATIGRRLFIDHGAgiVIGETAEIGDDVTIFHGVTL------GGTGKDCGK-RHPTVGDGALVSAGAKVLGPV 136
Cdd:cd03358     9 TNVFIENDVKIGDNVKIQSNV--SIYEGVTIEDDVFIGPNVVFtndlypRSKIYRKWElKGTTVKRGASIGANATILPGV 86

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1251371426 137 EIGAGARIGAGAVVLKDVPPGATVVGIPAKVVR 169
Cdd:cd03358    87 TIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 51-165 1.77e-11

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: 60.58  E-value: 1.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  51 LFGKVLSQNARFWTniEIHPGATIGRRLFIDHG----------AGIVIGET------------AEIGDDVTIFHGVTLGG 108
Cdd:TIGR03570  75 LVEKLKAKGYRFAT--LIHPSAIVSPSASIGEGtvimagavinPDVRIGDNviintgaivehdCVIGDFVHIAPGVTLSG 152

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1251371426 109 tgkdcgkrHPTVGDGALVSAGAKVLGPVEIGAGARIGAGAVVLKDVPPGATVVGIPA 165
Cdd:TIGR03570 153 --------GVVIGEGVFIGAGATIIQGVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 72-136 6.81e-10

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: 53.41  E-value: 6.81e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1251371426  72 ATIGRRLFIDHGAgiVIGETAEIGDDVTIFHGVTLGGTGKDCGKRHPTVGDGALVSAGAKVLGPV 136
Cdd:cd00208     1 VFIGEGVKIHPKA--VIRGPVVIGDNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGANAVIHGGV 63
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 65-168 1.70e-09

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: 53.23  E-value: 1.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  65 NIEIHPGATIGRRLFIDHGAGIVIGETAEIGDDVTIF---HGVTLGGTGKDCGKRHP--------------------TVG 121
Cdd:cd04647     1 NISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYdhnHDIDDPERPIEQGVTSApivigddvwiganvvilpgvTIG 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1251371426 122 DGALVSAGAkvlgpveigagarigagaVVLKDVPPGATVVGIPAKVV 168
Cdd:cd04647    81 DGAVVGAGS------------------VVTKDVPPNSIVAGNPAKVI 109
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 86-169 2.92e-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: 53.32  E-value: 2.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  86 IVIGETAEIGDDVTIFHGVTlggtgkdcgkrhptVGDGALVSAGAkvlgpveigagarigagaVVLKDVPPGATVVGIPA 165
Cdd:cd03349    74 VIIGNDVWIGHGATILPGVT--------------IGDGAVIAAGA------------------VVTKDVPPYAIVGGNPA 121


                  ....
gi 1251371426 166 KVVR 169
Cdd:cd03349   122 KVIR 125
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 51-164 2.10e-08

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: 52.10  E-value: 2.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  51 LFGKVLSQNARFwTNIeIHPGATIGRRLFIdhGAGIVIGETA------------------------EIGDDVTIFHGVTL 106
Cdd:cd03360    72 LAEKLLAAGYRF-ATL-IHPSAVVSPSAVI--GEGCVIMAGAvinpdarigdnviintgavighdcVIGDFVHIAPGVVL 147

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1251371426 107 GGtgkDCgkrhpTVGDGALVSAGAKVLGPVEIGAGARIGAGAVVLKDVPPGATVVGIP 164
Cdd:cd03360   148 SG---GV-----TIGEGAFIGAGATIIQGVTIGAGAIIGAGAVVTKDVPDGSVVVGNP 197
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 68-169 4.83e-07

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 47.71  E-value: 4.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  68 IHPGAT------IGRRLFIDHGA-------GIVIGE----------------TAEIGDDVTIFHGVTLGGtgkdCgkrhp 118
Cdd:COG0663    19 VAPTAVvigdvtIGEDVSVWPGAvlrgdvgPIRIGEgsniqdgvvlhvdpgyPLTIGDDVTIGHGAILHG----C----- 89

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1251371426 119 TVGDGALVSAGAKVLGPVEIGAGARIGAGAVVL--KDVPPGATVVGIPAKVVR 169
Cdd:COG0663    90 TIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTegKVVPPGSLVVGSPAKVVR 142
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 39-132 9.62e-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: 9.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  39 RVANFFYrhkmvlfgkvlsQNARFWTNIE----IHPGATIGRRLFIdhGAGIVIGETAEIGDDVTIFHGVTLggtGKDCg 114
Cdd:COG1044    84 KLLQLFY------------PPPAPAPGIHpsavIDPSAKIGEGVSI--GPFAVIGAGVVIGDGVVIGPGVVI---GDGV- 145

                          90
                  ....*....|....*...
gi 1251371426 115 krhpTVGDGALVSAGAKV 132
Cdd:COG1044   146 ----VIGDDCVLHPNVTI 159
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 69-168 1.88e-06

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: 46.26  E-value: 1.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  69 HPGATIGRRLFIDHGAGIVIGETAEIGDDVTIFHGVTlggtgkdcgkrhptVGDGALVSAGAkvlgpveigagarigaga 148
Cdd:cd03357   102 HPLDPEERNRGLEYAKPITIGDNVWIGGGVIILPGVT--------------IGDNSVIGAGS------------------ 149

                          90       100
                  ....*....|....*....|
gi 1251371426 149 VVLKDVPPGATVVGIPAKVV 168
Cdd:cd03357   150 VVTKDIPANVVAAGNPARVI 169
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 66-169 6.03e-06

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: 44.32  E-value: 6.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  66 IEIHPGATIGRR--LFIDHGAGIVIGetaeigDDVTIFHGVTLGGtgkdCgkrhpTVGDGALVSAGAKVLGPVEIGAGAR 143
Cdd:cd04645    39 IRIGERTNIQDGsvLHVDPGYPTIIG------DNVTVGHGAVLHG----C-----TIGDNCLIGMGAIILDGAVIGKGSI 103

                          90       100
                  ....*....|....*....|....*...
gi 1251371426 144 IGAGAVVL--KDVPPGATVVGIPAKVVR 169
Cdd:cd04645   104 VAAGSLVPpgKVIPPGSLVAGSPAKVVR 131
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 68-134 6.30e-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: 45.78  E-value: 6.30e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1251371426  68 IHPGATIGRRLFIdhGAGIVIGETAEIGDDVTIFHGVTLggtGKDCgkrhpTVGDGALVSAGAkVLG 134
Cdd:COG1044   123 IGAGVVIGDGVVI--GPGVVIGDGVVIGDDCVLHPNVTI---YERC-----VIGDRVIIHSGA-VIG 178
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 65-168 2.93e-05

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: 2.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  65 NIEIHPGATIGRRLFIDHGAGIVIGetaeigDDVTIFHGVTLggtgkdCGKRHP-------------TVGDGALVSAGAK 131
Cdd:cd05825     3 NLTIGDNSWIGEGVWIYNLAPVTIG------SDACISQGAYL------CTGSHDyrspafplitapiVIGDGAWVAAEAF 70

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1251371426 132 VLGPVEIGAGARIGAGAVVLKDVPPGATVVGIPAKVV 168
Cdd:cd05825    71 VGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 51-169 4.67e-05

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 42.68  E-value: 4.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  51 LFGKVlSQNARFWTNIEIHPGATI--GRRLFIDHGAGIVIGETAEIGDDVTIFHGVTLGGTGkdcgkrHP---------- 118
Cdd:PRK09527   54 MFATV-GENAWVEPPVYFSYGSNIhiGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTG------HPvhhelrknge 126

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1251371426 119 ------TVGDGALVSAGAKVLGPVEIGAGARIGAGAVVLKDVPPGATVVGIPAKVVR 169
Cdd:PRK09527  127 mysfpiTIGNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAGVPCRVIR 183
PRK10502 PRK10502
putative acyl transferase; Provisional
 83-169 7.15e-05

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 41.86  E-value: 7.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  83 GAGIVIGETAEIGDDVTIFHGVTlggtgkdcgkrhptVGDGALVSAGAkvlgpveigagarigagaVVLKDVPPGATVVG 162
Cdd:PRK10502  122 TAPIVIGEGCWLAADVFVAPGVT--------------IGSGAVVGARS------------------SVFKSLPANTICRG 169


                  ....*..
gi 1251371426 163 IPAKVVR 169
Cdd:PRK10502  170 NPAVPIR 176
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 72-132 2.49e-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: 40.47  E-value: 2.49e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1251371426  72 ATIGRRLFIdhGAGIVIGETAEIGDDVTIFHGVTLGgtgkdcgkRHPTVGDGALVSAGAKV 132
Cdd:cd03352     2 AKIGENVSI--GPNAVIGEGVVIGDGVVIGPGVVIG--------DGVVIGDDCVIHPNVTI 52
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 68-166 2.62e-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: 40.47  E-value: 2.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  68 IHPGATIGRRLFIDHGAGIviGETAEIGDDVTIFHGVTLGGtgkdcgkrHPTVGDGALVSAGAkvlgpveigagarigag 147
Cdd:cd03352   129 IAHNVRIGENCLIAAQVGI--AGSTTIGDNVIIGGQVGIAG--------HLTIGDGVVIGAGS----------------- 181

                          90
                  ....*....|....*....
gi 1251371426 148 aVVLKDVPPGATVVGIPAK 166
Cdd:cd03352   182 -GVTSIVPPGEYVSGTPAQ 199
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 92-169 3.53e-04

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 39.80  E-value: 3.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  92 AEIGDDVTIFHGVTLGGTGKdcgkRHP--TVGDGALVSAGAkvlgpveigagarigagaVVLKDVPPGATVVGIPAKVVR 169
Cdd:PRK10092  124 AELGKPVTIGNNVWIGGRAV----INPgvTIGDNVVVASGA------------------VVTKDVPDNVVVGGNPARIIK 181
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 46-133 8.36e-04

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: 36.84  E-value: 8.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  46 RHKMVLFGKVLSQNARFWTNIEIHPGATIGRRLFIDHGAGIVIGETAEIGDDVTIFHGVtlggtgkdcgkrhpTVGDGAL 125
Cdd:cd00208     5 EGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGANAVIHGGV--------------KIGDNAV 70


                  ....*...
gi 1251371426 126 VSAGAKVL 133
Cdd:cd00208    71 IGAGAVVT 78
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 53-110 2.95e-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: 37.39  E-value: 2.95e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1251371426  53 GKVLSQNARFWTNIEIHPGATIGRRLFIDHG----AGIVIGETAEIGDDVTIFHGVTLGGTG 110
Cdd:cd03352    13 NAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDcvihPNVTIYEGCIIGDRVIIHSGAVIGSDG 74
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 94-171 3.36e-03

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: 37.31  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  94 IGDDVTIFHGVTLGGtgkdcgkrHPTVGDGALVS------------AGAKVLGpveigagarigaGAVVLKDVPPGATVV 161
Cdd:COG1043   125 VGNNVILANNATLAG--------HVEVGDHAIIGglsavhqfvrigAHAMVGG------------GSGVVKDVPPYVLAA 184

                          90
                  ....*....|
gi 1251371426 162 GIPAKVVRLN 171
Cdd:COG1043   185 GNPARLRGLN 194
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 94-176 4.52e-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: 37.03  E-value: 4.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  94 IGDDVTIFHGVTLGGtgkdcgkrHPTVGDGALVSAGAKVLGPVEIGAGARIGAGAVVLKDVPPGATVVGIPAKVVRLNgr 173
Cdd:cd03351   123 IGNNVILANNATLAG--------HVEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARLRGLN-- 192


                  ...
gi 1251371426 174 TVG 176
Cdd:cd03351   193 LVG 195
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 81-169 6.81e-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: 35.62  E-value: 6.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  81 DHGAGIVIGETAEIGDDVTIfHGVTLGGtgkdcgkrHPTVGDGALVSAGAKVlgpveiGAGARIGAGAVVL--KDVPPGA 158
Cdd:cd04650    57 DHGYPTEIGDYVTIGHNAVV-HGAKVGN--------YVIVGMGAILLNGAKI------GDHVIIGAGAVVTpgKEIPDYS 121

                          90
                  ....*....|.
gi 1251371426 159 TVVGIPAKVVR 169
Cdd:cd04650   122 LVLGVPAKVVR 132
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 86-169 8.13e-03

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 36.01  E-value: 8.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1251371426  86 IVIGETAEIGDDVTIFHGVTlggtgkdcgkrhptVGDGALVSAGAkvlgpveigagarigagaVVLKDVPPGATVVGIPA 165
Cdd:PRK09677  131 VVIGQRVWIGENVTILPGVS--------------IGNGCIVGANS------------------VVTKSIPENTVIAGNPA 178


                  ....
gi 1251371426 166 KVVR 169
Cdd:PRK09677  179 KIIK 182
 
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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