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Conserved domains on  [gi|297170342|gb|ADI21377|]
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serine acetyltransferase [uncultured gamma proteobacterium HF0010_20H22]

Protein Classification

LbetaH domain-containing protein( domain architecture ID 372)

LbetaH (left-handed parallel beta-helix) domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LbetaH super family cl00160
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 5-254 2.22e-102

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.


The actual alignment was detected with superfamily member PRK11132:

Pssm-ID: 469633 [Multi-domain]  Cd Length: 273  Bit Score: 298.92  E-value: 2.22e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342   5 NDIWADILKESENKISLEPESQSLFQEKILSCNGLDDSLSGKLADDLSTKEYSSKILKGKFNEVFSKN-EFLEKAVIDLK 83
Cdd:PRK11132   7 EIVWNNIKAEARALADCEPMLASFYHATLLKHENLGSALSYMLANKLASPIMPAIAIREVVEEAYAADpEMIASAACDIQ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342  84 AVKERDPASSGFVFTLLFSKGFAALQAHRIANYFMKAKQEVFAYFVQSRSSAIYEVDIHPNAEIGHGVMLDHATGIVIGE 163
Cdd:PRK11132  87 AVRTRDPAVDKYSTPLLYLKGFHALQAYRIGHWLWNQGRRALAIYLQNQISVAFQVDIHPAAKIGRGIMLDHATGIVIGE 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 164 TSVIENDVSIFQGVTLGGTGKETGDRHPKVREGVLISSAAQILGNVEIGRGAKVAAGSVVLSDVEPNTTVAGVPAIVVGK 243
Cdd:PRK11132 167 TAVIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVGK 246

                        250
                 ....*....|.
gi 297170342 244 PSSEKPATDVD 254
Cdd:PRK11132 247 PESDKPSMDMD 257
 
Name Accession Description Interval E-value
cysE PRK11132
serine acetyltransferase; Provisional
 5-254 2.22e-102

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 298.92  E-value: 2.22e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342   5 NDIWADILKESENKISLEPESQSLFQEKILSCNGLDDSLSGKLADDLSTKEYSSKILKGKFNEVFSKN-EFLEKAVIDLK 83
Cdd:PRK11132   7 EIVWNNIKAEARALADCEPMLASFYHATLLKHENLGSALSYMLANKLASPIMPAIAIREVVEEAYAADpEMIASAACDIQ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342  84 AVKERDPASSGFVFTLLFSKGFAALQAHRIANYFMKAKQEVFAYFVQSRSSAIYEVDIHPNAEIGHGVMLDHATGIVIGE 163
Cdd:PRK11132  87 AVRTRDPAVDKYSTPLLYLKGFHALQAYRIGHWLWNQGRRALAIYLQNQISVAFQVDIHPAAKIGRGIMLDHATGIVIGE 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 164 TSVIENDVSIFQGVTLGGTGKETGDRHPKVREGVLISSAAQILGNVEIGRGAKVAAGSVVLSDVEPNTTVAGVPAIVVGK 243
Cdd:PRK11132 167 TAVIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVGK 246

                        250
                 ....*....|.
gi 297170342 244 PSSEKPATDVD 254
Cdd:PRK11132 247 PESDKPSMDMD 257
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 81-247 9.26e-86

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: 253.08  E-value: 9.26e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342  81 DLKAVKERDPASSGFVFTLLFSKGFAALQAHRIANYFMKAKQEVFAYFVQSRSSAIYEVDIHPNAEIGHGVMLDHATGIV 160
Cdd:COG1045    8 DIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHPGATIGRGFFIDHGTGVV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 161 IGETSVIENDVSIFQGVTLGGTGKETGDRHPKVREGVLISSAAQILGNVEIGRGAKVAAGSVVLSDVEPNTTVAGVPAIV 240
Cdd:COG1045   88 IGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARI 167


                 ....*..
gi 297170342 241 VGKPSSE 247
Cdd:COG1045  168 VKRKGSK 174
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 81-238 2.85e-77

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


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 231.03  E-value: 2.85e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342   81 DLKAVKERDPASSGFVFTLLFSKGFAALQAHRIANYFMKAKQEVFAYFVQSRSSAIYEVDIHPNAEIGHGVMLDHATGIV 160
Cdd:TIGR01172   4 DIRAVRERDPAARSYLEVLLYYPGFHALWAYRFAHFLWKRGFKFLARLLSNFIRVLTGVDIHPGARIGRGVFIDHGTGVV 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297170342  161 IGETSVIENDVSIFQGVTLGGTGKETGDRHPKVREGVLISSAAQILGNVEIGRGAKVAAGSVVLSDVEPNTTVAGVPA 238
Cdd:TIGR01172  84 IGETAVIGDDVTIYHGVTLGGTGKEKGKRHPTIGEGVMIGAGAKVLGNIEVGENAKIGANSVVLKDVPPGATVVGVPA 161
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 139-237 9.64e-48

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: 153.75  E-value: 9.64e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 139 VDIHPNAEIGHGVMLDHATGIVIGETSVIENDVSIFQGVTLGGTGKETGDRHPKVREGVLISSAAQILGNVEIGRGAKVA 218
Cdd:cd03354    3 IDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVKIG 82

                         90
                 ....*....|....*....
gi 297170342 219 AGSVVLSDVEPNTTVAGVP 237
Cdd:cd03354   83 ANAVVTKDVPANSTVVGVP 101
SATase_N pfam06426
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 7-109 8.69e-22

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: 86.75  E-value: 8.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342    7 IWADILKESENKISLEPESQSLFQEKILSCNGLDDSLSGKLADDLSTKEYSSKILKGKFNEVFSKN-EFLEKAVIDLKAV 85
Cdd:pfam06426   1 VWARLRAEAEEAAEREPLLASFLYATILSHDSLESALAFRLANKLANSTLPATLLRELFEDALEADpEIVEAARADLQAV 80

                          90       100
                  ....*....|....*....|....
gi 297170342   86 KERDPASSGFVFTLLFSKGFAALQ 109
Cdd:pfam06426  81 YERDPACDRYLTPLLYFKGFHALQ 104
SATase_N smart00971
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 7-110 3.83e-21

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: 85.28  E-value: 3.83e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342     7 IWADILKESENKISLEPESQSLFQEKILSCNGLDDSLSGKLADDLSTKEYSSKILKGKFNEVFSKN-EFLEKAVIDLKAV 85
Cdd:smart00971   1 VWQRIRAEAREAAEREPILASFLYATILNHDSLEAALAYRLANKLGNADMSADLLRELFEDAYAADpEIVEAAAADIQAV 80

                           90       100
                   ....*....|....*....|....*
gi 297170342    86 KERDPASSGFVFTLLFSKGFAALQA 110
Cdd:smart00971  81 YDRDPACDRYLTPLLYFKGFHALQA 105
 
Name Accession Description Interval E-value
cysE PRK11132
serine acetyltransferase; Provisional
 5-254 2.22e-102

serine acetyltransferase; Provisional


Pssm-ID: 182987 [Multi-domain]  Cd Length: 273  Bit Score: 298.92  E-value: 2.22e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342   5 NDIWADILKESENKISLEPESQSLFQEKILSCNGLDDSLSGKLADDLSTKEYSSKILKGKFNEVFSKN-EFLEKAVIDLK 83
Cdd:PRK11132   7 EIVWNNIKAEARALADCEPMLASFYHATLLKHENLGSALSYMLANKLASPIMPAIAIREVVEEAYAADpEMIASAACDIQ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342  84 AVKERDPASSGFVFTLLFSKGFAALQAHRIANYFMKAKQEVFAYFVQSRSSAIYEVDIHPNAEIGHGVMLDHATGIVIGE 163
Cdd:PRK11132  87 AVRTRDPAVDKYSTPLLYLKGFHALQAYRIGHWLWNQGRRALAIYLQNQISVAFQVDIHPAAKIGRGIMLDHATGIVIGE 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 164 TSVIENDVSIFQGVTLGGTGKETGDRHPKVREGVLISSAAQILGNVEIGRGAKVAAGSVVLSDVEPNTTVAGVPAIVVGK 243
Cdd:PRK11132 167 TAVIENDVSILQSVTLGGTGKTSGDRHPKIREGVMIGAGAKILGNIEVGRGAKIGAGSVVLQPVPPHTTAAGVPARIVGK 246

                        250
                 ....*....|.
gi 297170342 244 PSSEKPATDVD 254
Cdd:PRK11132 247 PESDKPSMDMD 257
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 81-247 9.26e-86

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: 253.08  E-value: 9.26e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342  81 DLKAVKERDPASSGFVFTLLFSKGFAALQAHRIANYFMKAKQEVFAYFVQSRSSAIYEVDIHPNAEIGHGVMLDHATGIV 160
Cdd:COG1045    8 DIQAVFERDPAARSLLEVLLCYPGFHALALHRLAHWLWKRGLPLLARLLSERARFLTGIDIHPGATIGRGFFIDHGTGVV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 161 IGETSVIENDVSIFQGVTLGGTGKETGDRHPKVREGVLISSAAQILGNVEIGRGAKVAAGSVVLSDVEPNTTVAGVPAIV 240
Cdd:COG1045   88 IGETAVIGDNVTIYQGVTLGGTGKEKGKRHPTIGDNVVIGAGAKILGPITIGDNAKIGANSVVLKDVPPGSTVVGVPARI 167


                 ....*..
gi 297170342 241 VGKPSSE 247
Cdd:COG1045  168 VKRKGSK 174
PLN02694 PLN02694
serine O-acetyltransferase
 7-256 8.59e-78

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 237.23  E-value: 8.59e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342   7 IWADILKESENKISLEPESQSLFQEKILSCNGLDDSLSGKLADDLSTKEYSSKILKGKFNEVFSKNEFLEKA-VIDLKAV 85
Cdd:PLN02694  28 LWTQIKAEARRDAESEPALASYLYSTILSHSSLERSLSFHLGNKLCSSTLLSTLLYDLFLNTFSSDPSLRAAtVADLRAA 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342  86 KERDPASSGFVFTLLFSKGFAALQAHRIANYFMKAKQEVFAYFVQSRSSAIYEVDIHPNAEIGHGVMLDHATGIVIGETS 165
Cdd:PLN02694 108 RVRDPACVSFSHCLLNYKGFLACQAHRVAHKLWTQSRRPLALALHSRISDVFAVDIHPAAKIGKGILFDHATGVVIGETA 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 166 VIENDVSIFQGVTLGGTGKETGDRHPKVREGVLISSAAQILGNVEIGRGAKVAAGSVVLSDVEPNTTVAGVPAIVVG--- 242
Cdd:PLN02694 188 VIGNNVSILHHVTLGGTGKACGDRHPKIGDGVLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARLVGgke 267

                        250
                 ....*....|....*.
gi 297170342 243 KPS--SEKPATDVDHT 256
Cdd:PLN02694 268 KPAkhEECPGESMDHT 283
cysE TIGR01172
serine O-acetyltransferase; Cysteine biosynthesis [Amino acid biosynthesis, Serine family]
 81-238 2.85e-77

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


Pssm-ID: 200082 [Multi-domain]  Cd Length: 162  Bit Score: 231.03  E-value: 2.85e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342   81 DLKAVKERDPASSGFVFTLLFSKGFAALQAHRIANYFMKAKQEVFAYFVQSRSSAIYEVDIHPNAEIGHGVMLDHATGIV 160
Cdd:TIGR01172   4 DIRAVRERDPAARSYLEVLLYYPGFHALWAYRFAHFLWKRGFKFLARLLSNFIRVLTGVDIHPGARIGRGVFIDHGTGVV 83

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297170342  161 IGETSVIENDVSIFQGVTLGGTGKETGDRHPKVREGVLISSAAQILGNVEIGRGAKVAAGSVVLSDVEPNTTVAGVPA 238
Cdd:TIGR01172  84 IGETAVIGDDVTIYHGVTLGGTGKEKGKRHPTIGEGVMIGAGAKVLGNIEVGENAKIGANSVVLKDVPPGATVVGVPA 161
PLN02357 PLN02357
serine acetyltransferase
 4-256 2.03e-76

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 235.93  E-value: 2.03e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342   4 VNDIWADILKESENKISLEPESQSLFQEKILSCNGLDDSLSGKLADDLSTKEYSSKILKGKFNEVFSKN-EFLEKAVIDL 82
Cdd:PLN02357  91 DDDVWLKIQEEAKSDVEQEPILSSYYYASILSHRSLESALANHLSVKLSNLNLPSNTLFDLFIGVLEESpEIIESVKQDL 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342  83 KAVKERDPASSGFVFTLLFSKGFAALQAHRIANYFMKAKQEVFAYFVQSRSSAIYEVDIHPNAEIGHGVMLDHATGIVIG 162
Cdd:PLN02357 171 RAVKERDPACISYVHCFLNFKGFLACQAHRIAHKLWTQGRKILALLIQNRVSEAFAVDIHPGAKIGQGILLDHATGVVIG 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 163 ETSVIENDVSIFQGVTLGGTGKETGDRHPKVREGVLISSAAQILGNVEIGRGAKVAAGSVVLSDVEPNTTVAGVPAIVVG 242
Cdd:PLN02357 251 ETAVVGNNVSILHNVTLGGTGKQSGDRHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLIG 330

                        250
                 ....*....|....*....
gi 297170342 243 KPSSEK-----PATDVDHT 256
Cdd:PLN02357 331 GKENPIkhdkiPSLTMDQT 349
PLN02739 PLN02739
serine acetyltransferase
 7-255 6.61e-69

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 216.44  E-value: 6.61e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342   7 IWADILKESENKISLEPESQSLFQEKILSCNGLDDSLSGKLADDLSTKEYSSKILKGKFNEVFSKNEFLEKAV-IDLKAV 85
Cdd:PLN02739  73 IWDSIREEAKLEAEEEPVLSSFLYASILSHDCLEQALSFVLANRLQNPTLLATQLMDIFCNVMVHDRGIQSSIrLDVQAF 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342  86 KERDPASSGFVFTLLFSKGFAALQAHRIANYFMKAKQEVFAYFVQSRSSAIYEVDIHPNAEIGHGVMLDHATGIVIGETS 165
Cdd:PLN02739 153 KDRDPACLSYSSAILHLKGYLALQAYRVAHKLWKQGRKLLALALQSRVSEVFGIDIHPAARIGKGILLDHGTGVVIGETA 232

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 166 VIENDVSIFQGVTLGGTGKETGDRHPKVREGVLISSAAQILGNVEIGRGAKVAAGSVVLSDVEPNTTVAGVPAIVVGKPS 245
Cdd:PLN02739 233 VIGDRVSILHGVTLGGTGKETGDRHPKIGDGALLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFVD 312

                        250
                 ....*....|
gi 297170342 246 SEKPATDVDH 255
Cdd:PLN02739 313 EQDPSLTMEY 322
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 139-237 9.64e-48

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: 153.75  E-value: 9.64e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 139 VDIHPNAEIGHGVMLDHATGIVIGETSVIENDVSIFQGVTLGGTGKETGDRHPKVREGVLISSAAQILGNVEIGRGAKVA 218
Cdd:cd03354    3 IDIHPGAKIGPGLFIDHGTGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVKIG 82

                         90
                 ....*....|....*....
gi 297170342 219 AGSVVLSDVEPNTTVAGVP 237
Cdd:cd03354   83 ANAVVTKDVPANSTVVGVP 101
SATase_N pfam06426
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 7-109 8.69e-22

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: 86.75  E-value: 8.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342    7 IWADILKESENKISLEPESQSLFQEKILSCNGLDDSLSGKLADDLSTKEYSSKILKGKFNEVFSKN-EFLEKAVIDLKAV 85
Cdd:pfam06426   1 VWARLRAEAEEAAEREPLLASFLYATILSHDSLESALAFRLANKLANSTLPATLLRELFEDALEADpEIVEAARADLQAV 80

                          90       100
                  ....*....|....*....|....
gi 297170342   86 KERDPASSGFVFTLLFSKGFAALQ 109
Cdd:pfam06426  81 YERDPACDRYLTPLLYFKGFHALQ 104
SATase_N smart00971
Serine acetyltransferase, N-terminal; The N-terminal domain of serine acetyltransferase has a ...
 7-110 3.83e-21

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: 85.28  E-value: 3.83e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342     7 IWADILKESENKISLEPESQSLFQEKILSCNGLDDSLSGKLADDLSTKEYSSKILKGKFNEVFSKN-EFLEKAVIDLKAV 85
Cdd:smart00971   1 VWQRIRAEAREAAEREPILASFLYATILNHDSLEAALAYRLANKLGNADMSADLLRELFEDAYAADpEIVEAAAADIQAV 80

                           90       100
                   ....*....|....*....|....*
gi 297170342    86 KERDPASSGFVFTLLFSKGFAALQA 110
Cdd:smart00971  81 YDRDPACDRYLTPLLYFKGFHALQA 105
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
136-249 8.70e-21

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 85.31  E-value: 8.70e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 136 IYEVDIHPNAEIGHGVMLDHATGIVIGetsvieNDVSIFQGVTLGGTGKETGD--------RHPKVREGVLISSAAQILG 207
Cdd:COG0110   25 GGNITIGDNVYIGPGVTIDDPGGITIG------DNVLIGPGVTILTGNHPIDDpatfplrtGPVTIGDDVWIGAGATILP 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 297170342 208 NVEIGRGAKVAAGSVVLSDVEPNTTVAGVPAIVVGKPSSEKP 249
Cdd:COG0110   99 GVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIRKRDEEER 140
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 139-242 2.22e-19

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: 81.01  E-value: 2.22e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 139 VDIHPNAEIGHGVMLDhaTGIVIGETSVIENDVSIFQGVTLggtgkeTGDRHP-------------KVREGVLISSAAQI 205
Cdd:cd03358   11 VFIENDVKIGDNVKIQ--SNVSIYEGVTIEDDVFIGPNVVF------TNDLYPrskiyrkwelkgtTVKRGASIGANATI 82

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 297170342 206 LGNVEIGRGAKVAAGSVVLSDVEPNTTVAGVPAIVVG 242
Cdd:cd03358   83 LPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARIIG 119
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 141-238 1.61e-18

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: 81.00  E-value: 1.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342  141 IHPNAEIGHGVMLDhaTGIVIGETSVIENDVSIFQGVTLGGtgketgdrHPKVREGVLISSAAQILGNVEIGRGAKVAAG 220
Cdd:TIGR03570 114 INPDVRIGDNVIIN--TGAIVEHDCVIGDFVHIAPGVTLSG--------GVVIGEGVFIGAGATIIQGVTIGAGAIVGAG 183

                          90
                  ....*....|....*...
gi 297170342  221 SVVLSDVEPNTTVAGVPA 238
Cdd:TIGR03570 184 AVVTKDIPDGGVVVGVPA 201
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 141-237 3.04e-17

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: 77.52  E-value: 3.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 141 IHPNAEIGHGVMLDhaTGIVIGETSVIENDVSIFQGVTLGGtgketgdrHPKVREGVLISSAAQILGNVEIGRGAKVAAG 220
Cdd:cd03360  111 INPDARIGDNVIIN--TGAVIGHDCVIGDFVHIAPGVVLSG--------GVTIGEGAFIGAGATIIQGVTIGAGAIIGAG 180

                         90
                 ....*....|....*..
gi 297170342 221 SVVLSDVEPNTTVAGVP 237
Cdd:cd03360  181 AVVTKDVPDGSVVVGNP 197
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 139-241 8.80e-17

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


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 73.64  E-value: 8.80e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 139 VDIHPNAEIGHGVMLDHATGIVIGETSVIENDVSIF---QGVTLGGTGKETGDRHPKVR--EGVLISSAAQILGNVEIGR 213
Cdd:cd04647    2 ISIGDNVYIGPGCVISAGGGITIGDNVLIGPNVTIYdhnHDIDDPERPIEQGVTSAPIVigDDVWIGANVVILPGVTIGD 81

                         90       100
                 ....*....|....*....|....*...
gi 297170342 214 GAKVAAGSVVLSDVEPNTTVAGVPAIVV 241
Cdd:cd04647   82 GAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 145-224 3.41e-15

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: 68.43  E-value: 3.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 145 AEIGHGVMLDHatGIVIGETSVIENDVSIFQGVTLGGTGKETGDRHPKVREGVLISSAAQILGNVEIGRGAKVAAGSVVL 224
Cdd:cd00208    1 VFIGEGVKIHP--KAVIRGPVVIGDNVNIGPGAVIGAATGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 139-241 2.33e-11

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: 59.16  E-value: 2.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 139 VDIHPNAEIGHGVMLDHATGIVIGetsvieNDVSIFQGVTL-GGTGKETGDRHPKVR------EGVLISSAAQILGNVEI 211
Cdd:cd05825    4 LTIGDNSWIGEGVWIYNLAPVTIG------SDACISQGAYLcTGSHDYRSPAFPLITapivigDGAWVAAEAFVGPGVTI 77

                         90       100       110
                 ....*....|....*....|....*....|
gi 297170342 212 GRGAKVAAGSVVLSDVEPNTTVAGVPAIVV 241
Cdd:cd05825   78 GEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 141-241 3.72e-10

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: 57.43  E-value: 3.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 141 IHPNAEIGHG-VMLDHAtGIVIGETSVIENDVSIFQG-----VTLGGTGKETGdrHP-KVREGVLISSAAQILGNVEIGR 213
Cdd:cd03357   65 IGDNFYANFNcTILDVA-PVTIGDNVLIGPNVQIYTAghpldPEERNRGLEYA--KPiTIGDNVWIGGGVIILPGVTIGD 141

                         90       100
                 ....*....|....*....|....*...
gi 297170342 214 GAKVAAGSVVLSDVEPNTTVAGVPAIVV 241
Cdd:cd03357  142 NSVIGAGSVVTKDIPANVVAAGNPARVI 169
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 128-243 6.95e-10

Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 56.27  E-value: 6.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 128 FVQSRSSAIYEVDIHPNAEIGHGVML--DHATgIVIGETS----------------VIENDVSIFQGVTL-GGTgketgd 188
Cdd:cd04645    7 FIAPNATVIGDVTLGEGSSVWFGAVLrgDVNP-IRIGERTniqdgsvlhvdpgyptIIGDNVTVGHGAVLhGCT------ 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 297170342 189 rhpkVREGVLISSAAQILGNVEIGRGAKVAAGSVVLSD--VEPNTTVAGVPAIVVGK 243
Cdd:cd04645   80 ----IGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGkvIPPGSLVAGSPAKVVRE 132
PRK10191 PRK10191
putative acyl transferase; Provisional
 133-240 3.47e-09

putative acyl transferase; Provisional


Pssm-ID: 182295 [Multi-domain]  Cd Length: 146  Bit Score: 54.13  E-value: 3.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 133 SSAIYEVDIHPNAEIGHGVMLDHATGIVIGETSVIENDVSIFQGVTLGGTGKETgDRHPKVREGVLISSAAQILGNVEIG 212
Cdd:PRK10191  36 TECFFGYEIQAAATIGRRFTIHHGYAVVINKNVVAGDDFTIRHGVTIGNRGADN-MACPHIGNGVELGANVIILGDITIG 114

                         90       100
                 ....*....|....*....|....*...
gi 297170342 213 RGAKVAAGSVVLSDVEPNTTVAGVPAIV 240
Cdd:PRK10191 115 NNVTVGAGSVVLDSVPDNALVVGEKARV 142
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 166-243 4.75e-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: 53.70  E-value: 4.75e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 297170342 166 VIENDVSIFQGVTlggtgketgdrhpkvregvlissaaqILGNVEIGRGAKVAAGSVVLSDVEPNTTVAGVPAIVVGK 243
Cdd:cd03349   75 IIGNDVWIGHGAT--------------------------ILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVIRY 126
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 139-239 7.76e-09

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: 54.34  E-value: 7.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 139 VDIHPNAEIGHGVMLDHATG--IVIGETSVIENDVSIFQGVTLG-------GTG----KETGDRhpkvregVLISSAAQI 205
Cdd:cd03352   93 VIIGDDVEIGANTTIDRGALgdTVIGDGTKIDNLVQIAHNVRIGencliaaQVGiagsTTIGDN-------VIIGGQVGI 165

                         90       100       110
                 ....*....|....*....|....*....|....
gi 297170342 206 LGNVEIGRGAKVAAGSVVLSDVEPNTTVAGVPAI 239
Cdd:cd03352  166 AGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQ 199
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 139-241 1.19e-08

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 53.11  E-value: 1.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 139 VDIHPNAEIGHGVML--DHATgIVIGETS----------------VIENDVSIFQGVTL-GGTgketgdrhpkVREGVLI 199
Cdd:COG0663   29 VTIGEDVSVWPGAVLrgDVGP-IRIGEGSniqdgvvlhvdpgyplTIGDDVTIGHGAILhGCT----------IGDNVLI 97

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 297170342 200 SSAAQILGNVEIGRGAKVAAGSVVL--SDVEPNTTVAGVPAIVV 241
Cdd:COG0663   98 GMGAIVLDGAVIGDGSIVGAGALVTegKVVPPGSLVVGSPAKVV 141
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 147-239 1.56e-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: 51.56  E-value: 1.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 147 IGHGVMLD------HatGIVIGETSVIendVSifqGVTLGGTGKeTGDRhpkvregVLISSAAQILGNVEIGRGAKVAAG 220
Cdd:COG1044  225 IGDGTKIDnlvqiaH--NVRIGEHTAI---AA---QVGIAGSTK-IGDN-------VVIGGQVGIAGHLTIGDGVIIGAQ 288

                         90
                 ....*....|....*....
gi 297170342 221 SVVLSDVEPNTTVAGVPAI 239
Cdd:COG1044  289 SGVTKSIPEGGVYSGSPAQ 307
PRK10502 PRK10502
putative acyl transferase; Provisional
 147-248 4.53e-07

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 48.79  E-value: 4.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 147 IGHGVMLDHATGIVIGETSVIEndvsifQGVTLGgtgkeTGDRHPK------------VREGVLISSAAQILGNVEIGRG 214
Cdd:PRK10502  80 IGDDVWLYNLGEITIGAHCVIS------QKSYLC-----TGSHDYSdphfdlntapivIGEGCWLAADVFVAPGVTIGSG 148

                         90       100       110
                 ....*....|....*....|....*....|....
gi 297170342 215 AKVAAGSVVLSDVEPNTTVAGVPAIVVgKPSSEK 248
Cdd:PRK10502 149 AVVGARSSVFKSLPANTICRGNPAVPI-RPRVET 181
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
141-242 8.79e-06

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 45.86  E-value: 8.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 141 IHPNAEIGHGVMLD-HATgiVIGETsVIENDVSIFQGVTLGGT-------GKET----GDRHpKVREGVLI--------- 199
Cdd:PRK05289  29 IGPNVVIGDGTVIGsHVV--IDGHT-TIGKNNRIFPFASIGEDpqdlkykGEPTrlviGDNN-TIREFVTInrgtvqggg 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 200 ----------------------------SSAAQILGNVE------------------IGRGAKVAAGSVVLSDVEPNTTV 233
Cdd:PRK05289 105 vtrigdnnllmayvhvahdcvvgnhvilANNATLAGHVEvgdyaiiggltavhqfvrIGAHAMVGGMSGVSQDVPPYVLA 184


                 ....*....
gi 297170342 234 AGVPAIVVG 242
Cdd:PRK05289 185 EGNPARLRG 193
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 144-243 1.02e-05

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 44.99  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 144 NAEIGHGVMLDHATGIVIGETSVIENDVSIFQGVTLGGTG-------KETGDRHP---KVREGVLISSAAQILGNVEIGR 213
Cdd:PRK09527  75 NIHIGRNFYANFNLTIVDDYTVTIGDNVLIAPNVTLSVTGhpvhhelRKNGEMYSfpiTIGNNVWIGSHVVINPGVTIGD 154

                         90       100       110
                 ....*....|....*....|....*....|
gi 297170342 214 GAKVAAGSVVLSDVEPNTTVAGVPAIVVGK 243
Cdd:PRK09527 155 NSVIGAGSVVTKDIPPNVVAAGVPCRVIRE 184
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 166-242 1.46e-05

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: 45.12  E-value: 1.46e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 297170342 166 VIENDVSIFQGVTLGGtgketgdrHPKVREGVLISSAAQILGNVEIGRGAKVAAGSVVLSDVEPNTTVAGVPAIVVG 242
Cdd:cd03351  122 VIGNNVILANNATLAG--------HVEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARLRG 190
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 133-242 2.13e-05

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: 44.62  E-value: 2.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 133 SSAIyevdIHPNAEIGHGVmldhatgiVIGETSVIENDVSI------------------------FQGVTLGG------- 181
Cdd:COG1043    6 PTAI----VDPGAKLGENV--------EIGPFCVIGPDVEIgdgtvigshvviegpttigknnriFPFASIGEepqdlky 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 182 TGKET----GDRHpKVREGVLI-------------------------------------SSAAQILGNVE---------- 210
Cdd:COG1043   74 KGEPTrleiGDNN-TIREFVTIhrgtvqgggvtrigddnllmayvhvahdcvvgnnvilANNATLAGHVEvgdhaiiggl 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 297170342 211 --------IGRGAKVAAGSVVLSDVEPNTTVAGVPAIVVG 242
Cdd:COG1043  153 savhqfvrIGAHAMVGGGSGVVKDVPPYVLAAGNPARLRG 192
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 147-239 2.72e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 44.74  E-value: 2.72e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 147 IGHGVMLDH----ATGIVIGETSVIENDVSIFQGVTLGgtgketgdrhpkvrEGVLISSAAQILGNVEIGRGAKVAAGSV 222
Cdd:PRK00892 228 IGEGVKIDNlvqiAHNVVIGRHTAIAAQVGIAGSTKIG--------------RYCMIGGQVGIAGHLEIGDGVTITAMSG 293

                         90
                 ....*....|....*...
gi 297170342 223 VLSDV-EPNTTVAGVPAI 239
Cdd:PRK00892 294 VTKSIpEPGEYSSGIPAQ 311
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 99-228 1.83e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 42.05  E-value: 1.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342  99 LLFSKGFAALQAHRIANYFMKAKQEVFA----YFVQSRSSAiYEVDIHPNAeighgvmldhatgiVIGETSVIENDVSIF 174
Cdd:PRK00892  58 VIVSPDDAEFVPAGNALLVVKNPYLAFArlaqLFDPPATPS-PAAGIHPSA--------------VIDPSAKIGEGVSIG 122

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 297170342 175 QGVTLGgTGKETGDrhpkvreGVLISSAAQILGNVEIGRGAKVAAGSVVLSDVE 228
Cdd:PRK00892 123 PNAVIG-AGVVIGD-------GVVIGAGAVIGDGVKIGADCRLHANVTIYHAVR 168
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 144-231 3.44e-04

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 40.48  E-value: 3.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 144 NAEIGHGVMLDHATgiVIGetsvienDVSIFQGVTLG-GT------GKEtgdRHP-KVREGVLISSAAQILGNVEIGRGA 215
Cdd:cd03353  102 KSTIGEGSKANHLS--YLG-------DAEIGEGVNIGaGTitcnydGVN---KHRtVIGDNVFIGSNSQLVAPVTIGDGA 169

                         90
                 ....*....|....*.
gi 297170342 216 KVAAGSVVLSDVEPNT 231
Cdd:cd03353  170 TIAAGSTITKDVPPGA 185
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
141-223 3.47e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 40.85  E-value: 3.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 141 IHPNAEIGHGVmldhatgiVIGETSVIENDVSIfqgvtlggtgketGDrhpkvreGVLISSAAQILGNVEIGRGAKVAAG 220
Cdd:PRK05289  11 VEPGAKIGENV--------EIGPFCVIGPNVVI-------------GD-------GTVIGSHVVIDGHTTIGKNNRIFPF 62


                 ...
gi 297170342 221 SVV 223
Cdd:PRK05289  63 ASI 65
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 187-243 3.58e-04

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 40.01  E-value: 3.58e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 297170342 187 GDRHPKVREGVLISSAAQILGNVEIGRGAKVAAGSVVLSDVEPnttvagvpaIVVGK 243
Cdd:COG0663    7 DGKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRGDVGP---------IRIGE 54
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 144-231 1.74e-03

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 39.36  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 144 NAEIGHGVMLDHATgiVIGETsVIENDVSIFQG-VTLGGTGKEtgdRHPKVRE-GVLISSAAQILGNVEIGRGAKVAAGS 221
Cdd:PRK14357 341 KSTIGENTKAQHLT--YLGDA-TVGKNVNIGAGtITCNYDGKK---KNPTFIEdGAFIGSNSSLVAPVRIGKGALIGAGS 414

                         90
                 ....*....|
gi 297170342 222 VVLSDVEPNT 231
Cdd:PRK14357 415 VITEDVPPYS 424
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 138-228 2.02e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 38.46  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 138 EVDIHPNAEIGHGVMLDHATGI----VIGETSVIENDVSIFQGVTLGG-------TGKET----GDRHpKVREGVLISSA 202
Cdd:PRK12461  17 GVEIGPFAVIGANVEIGDGTWIgphaVILGPTRIGKNNKIHQGAVVGDepqdftyKGEESrleiGDRN-VIREGVTIHRG 95

                         90       100
                 ....*....|....*....|....*.
gi 297170342 203 AQILGNVEIGRGAKVAAGSVVLSDVE 228
Cdd:PRK12461  96 TKGGGVTRIGNDNLLMAYSHVAHDCQ 121
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 128-260 3.85e-03

Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three distinct groups of carbonic anhydrases - alpha, beta and gamma - which show no significant sequence identity or structural similarity. Gamma CAs are homotrimeric enzymes, with each subunit containing a left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 37.22  E-value: 3.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 128 FVQSRSSAIYEVDIHPNAEIGHGVML--DHATGIVIGETSVIENDVSIFqgvTLGGTGKETGDRhpkvregVLISSAAQI 205
Cdd:cd00710   10 YVHPTAVVIGDVIIGDNVFVGPGASIraDEGTPIIIGANVNIQDGVVIH---ALEGYSVWIGKN-------VSIAHGAIV 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 297170342 206 LGNVEIGRGAKVAAGSVVLSDVEPNTTVAGVPAIVVG---KPSSEKPATDVDHTLEEA 260
Cdd:cd00710   80 HGPAYIGDNCFIGFRSVVFNAKVGDNCVIGHNAVVDGveiPPGRYVPAGAVITSQTQA 137
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 145-223 4.21e-03

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


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 36.59  E-value: 4.21e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 297170342 145 AEIGHGVMLDhaTGIVIGETSVIENDVSIFQGVTLGGTGKETGDRHPKVREGVLISSAAQILGNVEIGRGAKVAAGSVV 223
Cdd:cd03350   32 AYVDEGTMVD--SWATVGSCAQIGKNVHLSAGAVIGGVLEPLQATPVIIEDDVFIGANCEVVEGVIVGKGAVLAAGVVL 108
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 141-226 4.29e-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: 4.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 141 IHPNAEIGHGVmldhatgiVIGETSVIENDVSIFQGVTLGgtgketgdRHPKVREGVLISSAAQILGNVEIGRGAKVAAG 220
Cdd:cd03352    4 IGENVSIGPNA--------VIGEGVVIGDGVVIGPGVVIG--------DGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSG 67


                 ....*.
gi 297170342 221 SVVLSD 226
Cdd:cd03352   68 AVIGSD 73
PLN02296 PLN02296
carbonate dehydratase
 107-238 5.91e-03

carbonate dehydratase


Pssm-ID: 215167 [Multi-domain]  Cd Length: 269  Bit Score: 37.41  E-value: 5.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 297170342 107 ALQAHR-IANYFMKAKQEVFAYFVQSRSSAIYEVDIHPNAEIGHG-VMLDHATGIVIG-ETSVIENDVSIFQGVTLGGTG 183
Cdd:PLN02296  38 QLSRHRtLMNIFDKAPVVDKDAFVAPSASVIGDVQVGRGSSIWYGcVLRGDVNSISVGsGTNIQDNSLVHVAKTNLSGKV 117

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 297170342 184 KET--GDR----HPKVREG------VLISSAAQILGNVEIGRGAKVAAGSVVLsdvePNTTV------AGVPA 238
Cdd:PLN02296 118 LPTiiGDNvtigHSAVLHGctvedeAFVGMGATLLDGVVVEKHAMVAAGALVR----QNTRIpsgevwAGNPA 186
 
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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