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Conserved domains on  [gi|446488112|ref|WP_000565966|]
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MULTISPECIES: acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase [Enterobacteriaceae]

Protein Classification

acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase( domain architecture ID 11480535)

acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell

CATH:  1.20.1180.10|2.160.10.10
EC:  2.3.1.129
Gene Ontology:  GO:0009245|GO:0008780
SCOP:  4002830

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
4-262 4.65e-172

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


:

Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 474.97  E-value: 4.65e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112   4 KSAFVHPTAIVEEGASIGANAHIGPFCIVGPHVEIGEGTVLKSHVVVNGHTKIGRDNEIYQFASIGEVNQDLKYAGEPTR 83
Cdd:PRK05289   1 MMAKIHPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIGEDPQDLKYKGEPTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112  84 VEIGDRNRIRESVTIHRGTVQGGGLTKVGSDNLLMINAHIAHDCTVGNRCILANNATLAGHVSVDDFAIIGGMTAVHQFC 163
Cdd:PRK05289  81 LVIGDNNTIREFVTINRGTVQGGGVTRIGDNNLLMAYVHVAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLTAVHQFV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112 164 IIGAHVMVGGCSGVAQDVPPYVIAQGNHATPFGVNIEGLKRRGFSREAITAIRNAYKLIYRSGKTLDEVKPEIAELAETY 243
Cdd:PRK05289 161 RIGAHAMVGGMSGVSQDVPPYVLAEGNPARLRGLNLVGLKRRGFSREEIHALRRAYKLLYRSGLTLEEALEELAEEYPDS 240

                        250
                 ....*....|....*....
gi 446488112 244 PEVKAFTDFFARSTRGLIR 262
Cdd:PRK05289 241 PEVKEILDFIESSKRGIIR 259
 
Name Accession Description Interval E-value
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
4-262 4.65e-172

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 474.97  E-value: 4.65e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112   4 KSAFVHPTAIVEEGASIGANAHIGPFCIVGPHVEIGEGTVLKSHVVVNGHTKIGRDNEIYQFASIGEVNQDLKYAGEPTR 83
Cdd:PRK05289   1 MMAKIHPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIGEDPQDLKYKGEPTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112  84 VEIGDRNRIRESVTIHRGTVQGGGLTKVGSDNLLMINAHIAHDCTVGNRCILANNATLAGHVSVDDFAIIGGMTAVHQFC 163
Cdd:PRK05289  81 LVIGDNNTIREFVTINRGTVQGGGVTRIGDNNLLMAYVHVAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLTAVHQFV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112 164 IIGAHVMVGGCSGVAQDVPPYVIAQGNHATPFGVNIEGLKRRGFSREAITAIRNAYKLIYRSGKTLDEVKPEIAELAETY 243
Cdd:PRK05289 161 RIGAHAMVGGMSGVSQDVPPYVLAEGNPARLRGLNLVGLKRRGFSREEIHALRRAYKLLYRSGLTLEEALEELAEEYPDS 240

                        250
                 ....*....|....*....
gi 446488112 244 PEVKAFTDFFARSTRGLIR 262
Cdd:PRK05289 241 PEVKEILDFIESSKRGIIR 259
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 5-262 1.85e-168

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: 465.65  E-value: 1.85e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112   5 SAFVHPTAIVEEGASIGANAHIGPFCIVGPHVEIGEGTVLKSHVVVNGHTKIGRDNEIYQFASIGEVNQDLKYAGEPTRV 84
Cdd:COG1043    1 MAMIHPTAIVDPGAKLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASIGEEPQDLKYKGEPTRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112  85 EIGDRNRIRESVTIHRGTVQGGGLTKVGSDNLLMINAHIAHDCTVGNRCILANNATLAGHVSVDDFAIIGGMTAVHQFCI 164
Cdd:COG1043   81 EIGDNNTIREFVTIHRGTVQGGGVTRIGDDNLLMAYVHVAHDCVVGNNVILANNATLAGHVEVGDHAIIGGLSAVHQFVR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112 165 IGAHVMVGGCSGVAQDVPPYVIAQGNHATPFGVNIEGLKRRGFSREAITAIRNAYKLIYRSGKTLDEVKPEIAELAETYP 244
Cdd:COG1043  161 IGAHAMVGGGSGVVKDVPPYVLAAGNPARLRGLNLVGLKRRGFSREQIRALKRAYRLLYRSGLTLEEALEELEAELPDSP 240

                        250
                 ....*....|....*...
gi 446488112 245 EVKAFTDFFARSTRGLIR 262
Cdd:COG1043  241 EVRELLDFIRASKRGIIR 258
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 8-260 5.79e-161

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: 446.49  E-value: 5.79e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112   8 VHPTAIVEEGASIGANAHIGPFCIVGPHVEIGEGTVLKSHVVVNGHTKIGRDNEIYQFASIGEVNQDLKYAGEPTRVEIG 87
Cdd:cd03351    2 IHPTAIVDPGAKIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIGEAPQDLKYKGEPTRLEIG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112  88 DRNRIRESVTIHRGTVQGGGLTKVGSDNLLMINAHIAHDCTVGNRCILANNATLAGHVSVDDFAIIGGMTAVHQFCIIGA 167
Cdd:cd03351   82 DNNTIREFVTIHRGTAQGGGVTRIGNNNLLMAYVHVAHDCVIGNNVILANNATLAGHVEIGDYAIIGGLSAVHQFCRIGR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112 168 HVMVGGCSGVAQDVPPYVIAQGNHATPFGVNIEGLKRRGFSREAITAIRNAYKLIYRSGKTLDEVKPEIAELAETYPEVK 247
Cdd:cd03351  162 HAMVGGGSGVVQDVPPYVIAAGNRARLRGLNLVGLKRRGFSREEIRALKRAYRILYRSGLTLEEALEELEEEAPDSPEVE 241

                        250
                 ....*....|...
gi 446488112 248 AFTDFFARSTRGL 260
Cdd:cd03351  242 ELVDFIRSSKRGI 254
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 8-261 2.72e-143

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


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 401.64  E-value: 2.72e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112    8 VHPTAIVEEGASIGANAHIGPFCIVGPHVEIGEGTVLKSHVVVNGHTKIGRDNEIYQFASIGEVNQDLKYAGEPTRVEIG 87
Cdd:TIGR01852   1 IHPTAIIEPGAEIGENVEIGPFCIVGPGVKIGDGVELKSHVVILGHTTIGEGTRIFPGAVIGGVPQDLKYKGEKTRLIIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112   88 DRNRIRESVTIHRGTVQGGGLTKVGSDNLLMINAHIAHDCTVGNRCILANNATLAGHVSVDDFAIIGGMTAVHQFCIIGA 167
Cdd:TIGR01852  81 DNNTIREFVTINRGTASGGGVTRIGNNNLLMAYSHIAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLVAVHQFVRIGR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112  168 HVMVGGCSGVAQDVPPYVIAQGNHATPFGVNIEGLKRRGFSREAITAIRNAYKLIYRSGKTLDEVKPEIAELAETYPEVK 247
Cdd:TIGR01852 161 YAMIGGLSAVSKDVPPYCLAEGNRARLRGLNIVGLRRRGFSREEITAIKRAYRTLFRSGLPLREAAQQVAEEYEDNPEVK 240

                         250
                  ....*....|....
gi 446488112  248 AFTDFFARSTRGLI 261
Cdd:TIGR01852 241 EILDFIRESKRGIC 254
Acetyltransf_11 pfam13720
Udp N-acetylglucosamine O-acyltransferase; Domain 2; This is domain 2, or the C-terminal ...
 180-261 1.42e-38

Udp N-acetylglucosamine O-acyltransferase; Domain 2; This is domain 2, or the C-terminal domain, of Udp N-acetylglucosamine O-acyltransferase. This enzyme is a zinc-dependent enzyme that catalyzes the deacetylation of UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine to form UDP-3-O-(R-hydroxymyristoyl)glucosamine and acetate.


Pssm-ID: 463967 [Multi-domain]  Cd Length: 82  Bit Score: 129.50  E-value: 1.42e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112  180 DVPPYVIAQGNHATPFGVNIEGLKRRGFSREAITAIRNAYKLIYRSGKTLDEVKPEIAELAETYPEVKAFTDFFARSTRG 259
Cdd:pfam13720   1 DVPPYVLAAGNPARLRGLNLVGLRRRGFSSEEIRALKRAYRLLYRSGLTLEEALEELEEEVPDSPEVQEILDFIRSSKRG 80


                  ..
gi 446488112  260 LI 261
Cdd:pfam13720  81 II 82
 
Name Accession Description Interval E-value
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
4-262 4.65e-172

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 474.97  E-value: 4.65e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112   4 KSAFVHPTAIVEEGASIGANAHIGPFCIVGPHVEIGEGTVLKSHVVVNGHTKIGRDNEIYQFASIGEVNQDLKYAGEPTR 83
Cdd:PRK05289   1 MMAKIHPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIGEDPQDLKYKGEPTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112  84 VEIGDRNRIRESVTIHRGTVQGGGLTKVGSDNLLMINAHIAHDCTVGNRCILANNATLAGHVSVDDFAIIGGMTAVHQFC 163
Cdd:PRK05289  81 LVIGDNNTIREFVTINRGTVQGGGVTRIGDNNLLMAYVHVAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLTAVHQFV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112 164 IIGAHVMVGGCSGVAQDVPPYVIAQGNHATPFGVNIEGLKRRGFSREAITAIRNAYKLIYRSGKTLDEVKPEIAELAETY 243
Cdd:PRK05289 161 RIGAHAMVGGMSGVSQDVPPYVLAEGNPARLRGLNLVGLKRRGFSREEIHALRRAYKLLYRSGLTLEEALEELAEEYPDS 240

                        250
                 ....*....|....*....
gi 446488112 244 PEVKAFTDFFARSTRGLIR 262
Cdd:PRK05289 241 PEVKEILDFIESSKRGIIR 259
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 5-262 1.85e-168

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: 465.65  E-value: 1.85e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112   5 SAFVHPTAIVEEGASIGANAHIGPFCIVGPHVEIGEGTVLKSHVVVNGHTKIGRDNEIYQFASIGEVNQDLKYAGEPTRV 84
Cdd:COG1043    1 MAMIHPTAIVDPGAKLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASIGEEPQDLKYKGEPTRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112  85 EIGDRNRIRESVTIHRGTVQGGGLTKVGSDNLLMINAHIAHDCTVGNRCILANNATLAGHVSVDDFAIIGGMTAVHQFCI 164
Cdd:COG1043   81 EIGDNNTIREFVTIHRGTVQGGGVTRIGDDNLLMAYVHVAHDCVVGNNVILANNATLAGHVEVGDHAIIGGLSAVHQFVR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112 165 IGAHVMVGGCSGVAQDVPPYVIAQGNHATPFGVNIEGLKRRGFSREAITAIRNAYKLIYRSGKTLDEVKPEIAELAETYP 244
Cdd:COG1043  161 IGAHAMVGGGSGVVKDVPPYVLAAGNPARLRGLNLVGLKRRGFSREQIRALKRAYRLLYRSGLTLEEALEELEAELPDSP 240

                        250
                 ....*....|....*...
gi 446488112 245 EVKAFTDFFARSTRGLIR 262
Cdd:COG1043  241 EVRELLDFIRASKRGIIR 258
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 8-260 5.79e-161

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: 446.49  E-value: 5.79e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112   8 VHPTAIVEEGASIGANAHIGPFCIVGPHVEIGEGTVLKSHVVVNGHTKIGRDNEIYQFASIGEVNQDLKYAGEPTRVEIG 87
Cdd:cd03351    2 IHPTAIVDPGAKIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIGEAPQDLKYKGEPTRLEIG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112  88 DRNRIRESVTIHRGTVQGGGLTKVGSDNLLMINAHIAHDCTVGNRCILANNATLAGHVSVDDFAIIGGMTAVHQFCIIGA 167
Cdd:cd03351   82 DNNTIREFVTIHRGTAQGGGVTRIGNNNLLMAYVHVAHDCVIGNNVILANNATLAGHVEIGDYAIIGGLSAVHQFCRIGR 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112 168 HVMVGGCSGVAQDVPPYVIAQGNHATPFGVNIEGLKRRGFSREAITAIRNAYKLIYRSGKTLDEVKPEIAELAETYPEVK 247
Cdd:cd03351  162 HAMVGGGSGVVQDVPPYVIAAGNRARLRGLNLVGLKRRGFSREEIRALKRAYRILYRSGLTLEEALEELEEEAPDSPEVE 241

                        250
                 ....*....|...
gi 446488112 248 AFTDFFARSTRGL 260
Cdd:cd03351  242 ELVDFIRSSKRGI 254
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 8-261 2.72e-143

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


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 401.64  E-value: 2.72e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112    8 VHPTAIVEEGASIGANAHIGPFCIVGPHVEIGEGTVLKSHVVVNGHTKIGRDNEIYQFASIGEVNQDLKYAGEPTRVEIG 87
Cdd:TIGR01852   1 IHPTAIIEPGAEIGENVEIGPFCIVGPGVKIGDGVELKSHVVILGHTTIGEGTRIFPGAVIGGVPQDLKYKGEKTRLIIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112   88 DRNRIRESVTIHRGTVQGGGLTKVGSDNLLMINAHIAHDCTVGNRCILANNATLAGHVSVDDFAIIGGMTAVHQFCIIGA 167
Cdd:TIGR01852  81 DNNTIREFVTINRGTASGGGVTRIGNNNLLMAYSHIAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLVAVHQFVRIGR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112  168 HVMVGGCSGVAQDVPPYVIAQGNHATPFGVNIEGLKRRGFSREAITAIRNAYKLIYRSGKTLDEVKPEIAELAETYPEVK 247
Cdd:TIGR01852 161 YAMIGGLSAVSKDVPPYCLAEGNRARLRGLNIVGLRRRGFSREEITAIKRAYRTLFRSGLPLREAAQQVAEEYEDNPEVK 240

                         250
                  ....*....|....
gi 446488112  248 AFTDFFARSTRGLI 261
Cdd:TIGR01852 241 EILDFIRESKRGIC 254
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 8-262 1.97e-114

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 328.91  E-value: 1.97e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112   8 VHPTAIVEEGASIGANAHIGPFCIVGPHVEIGEGTVLKSHVVVNGHTKIGRDNEIYQFASIGEVNQDLKYAGEPTRVEIG 87
Cdd:PRK12461   2 IHPTAVIDPSAKLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGDEPQDFTYKGEESRLEIG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112  88 DRNRIRESVTIHRGTvQGGGLTKVGSDNLLMINAHIAHDCTVGNRCILANNATLAGHVSVDDFAIIGGMTAVHQFCIIGA 167
Cdd:PRK12461  82 DRNVIREGVTIHRGT-KGGGVTRIGNDNLLMAYSHVAHDCQIGNNVILVNGALLAGHVTVGDRAIISGNCLVHQFCRIGA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112 168 HVMVGGCSGVAQDVPPYVIAQGNHATPFGVNIEGLKRRGFSREAITAIRNAYKLIYRSGKTLDEVKPEIAELAETYPEVK 247
Cdd:PRK12461 161 LAMMAGGSRISKDVPPYCMMAGHPTNVHGLNAVGLRRRGFSSRAIRALKRAYKIIYRSGLSVQQAVAELELQQFESPEVE 240

                        250
                 ....*....|....*
gi 446488112 248 AFTDFFARSTRGLIR 262
Cdd:PRK12461 241 ELIDFIKASKRGIVR 255
Acetyltransf_11 pfam13720
Udp N-acetylglucosamine O-acyltransferase; Domain 2; This is domain 2, or the C-terminal ...
 180-261 1.42e-38

Udp N-acetylglucosamine O-acyltransferase; Domain 2; This is domain 2, or the C-terminal domain, of Udp N-acetylglucosamine O-acyltransferase. This enzyme is a zinc-dependent enzyme that catalyzes the deacetylation of UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine to form UDP-3-O-(R-hydroxymyristoyl)glucosamine and acetate.


Pssm-ID: 463967 [Multi-domain]  Cd Length: 82  Bit Score: 129.50  E-value: 1.42e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112  180 DVPPYVIAQGNHATPFGVNIEGLKRRGFSREAITAIRNAYKLIYRSGKTLDEVKPEIAELAETYPEVKAFTDFFARSTRG 259
Cdd:pfam13720   1 DVPPYVLAAGNPARLRGLNLVGLRRRGFSSEEIRALKRAYRLLYRSGLTLEEALEELEEEVPDSPEVQEILDFIRSSKRG 80


                  ..
gi 446488112  260 LI 261
Cdd:pfam13720  81 II 82
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 1-194 3.38e-37

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: 130.22  E-value: 3.38e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112   1 MIDKSAFVHPTAIVEEGASIGANAHIGPFCIVGPHVEIGEGTVLKSHVVVNGHTKIGRDNEIYQFASIGE-----VNQDL 75
Cdd:cd03352    3 KIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIGSdgfgfAPDGG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112  76 KYAGEPT--RVEIGDRNRIRESVTIHRGTVqggGLTKVGS----DNLLminaHIAHDCTVGNRCILANNATLAGHVSVDD 149
Cdd:cd03352   83 GWVKIPQlgGVIIGDDVEIGANTTIDRGAL---GDTVIGDgtkiDNLV----QIAHNVRIGENCLIAAQVGIAGSTTIGD 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446488112 150 FAIIGGMTAVHQFCIIGAHVMVGGCSGVAQDVPPYVIAQGNHATP 194
Cdd:cd03352  156 NVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQP 200
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 2-183 9.99e-33

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: 121.66  E-value: 9.99e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112   2 IDKSAFVHPTAIVEEGASIGANAHIGPFCIVGPHVEIGEGTVLKSHVVVNGHTKIGRDNEIYQFASIGevnQD-LKYAGE 80
Cdd:COG1044  111 IGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVIGDRVIIHSGAVIG---ADgFGFAPD 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112  81 PT----------RVEIGDRNRIRESVTIHRGTVqggGLTKVGS----DNLLminaHIAHDCTVGNRCILANNATLAGHVS 146
Cdd:COG1044  188 EDggwvkipqlgRVVIGDDVEIGANTTIDRGAL---GDTVIGDgtkiDNLV----QIAHNVRIGEHTAIAAQVGIAGSTK 260

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 446488112 147 VDDFAIIGGMTAVHQFCIIGAHVMVGGCSGVAQDVPP 183
Cdd:COG1044  261 IGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPE 297
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 2-183 9.95e-31

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 116.78  E-value: 9.95e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112   2 IDKSAFVHPTAIVEEGASIGANA------------HIGPFCIVGPHVEIGEGTVLKSHVVVNGHTKIGRDNEIYQFASIG 69
Cdd:PRK00892 103 IHPSAVIDPSAKIGEGVSIGPNAvigagvvigdgvVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVIG 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112  70 evnQD-LKYAGEPT---------RVEIGDRNRIRESVTIHRG----TVQGGGlTKVgsDNLLminaHIAHDCTVGNRCIL 135
Cdd:PRK00892 183 ---SDgFGFANDRGgwvkipqlgRVIIGDDVEIGANTTIDRGalddTVIGEG-VKI--DNLV----QIAHNVVIGRHTAI 252

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 446488112 136 ANNATLAGHVSVDDFAIIGGMTAVHQFCIIGAHVMVGGCSGVAQDVPP 183
Cdd:PRK00892 253 AAQVGIAGSTKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPE 300
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 7-190 1.24e-14

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 70.21  E-value: 1.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112   7 FVHPTAIVEEGASIGANAHIGPFCIVGPHVEIGEgtvlksHVVVNghtkigrdneiyqfasigevnqdlkyageptrvei 86
Cdd:cd03360   86 LIHPSAVVSPSAVIGEGCVIMAGAVINPDARIGD------NVIIN----------------------------------- 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112  87 gdrnriresvtihrgtvqgggltkvgsdnllmINAHIAHDCTVGNRCILANNATLAGHVSVDDFAIIGGMTAVHQFCIIG 166
Cdd:cd03360  125 --------------------------------TGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEGAFIGAGATIIQGVTIG 172

                        170       180
                 ....*....|....*....|....
gi 446488112 167 AHVMVGGCSGVAQDVPPYVIAQGN 190
Cdd:cd03360  173 AGAIIGAGAVVTKDVPDGSVVVGN 196
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 8-192 1.93e-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: 61.36  E-value: 1.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112    8 VHPTAIVEEGASIGANAHIGPFCIVGPHVEIGEgtvlksHVVVNGhtkigrdneiyqfasigevnqdlkyageptrveig 87
Cdd:TIGR03570  90 IHPSAIVSPSASIGEGTVIMAGAVINPDVRIGD------NVIINT----------------------------------- 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112   88 drnriresvtihrgtvqgggltkvgsdnllmiNAHIAHDCTVGNRCILANNATLAGHVSVDDFAIIGGMTAVHQFCIIGA 167
Cdd:TIGR03570 129 --------------------------------GAIVEHDCVIGDFVHIAPGVTLSGGVVIGEGVFIGAGATIIQGVTIGA 176

                         170       180
                  ....*....|....*....|....*
gi 446488112  168 HVMVGGCSGVAQDVPPYVIAQGNHA 192
Cdd:TIGR03570 177 GAIVGAGAVVTKDIPDGGVVVGVPA 201
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 2-192 4.46e-09

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 54.26  E-value: 4.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112   2 IDKSAFVHPTAIVeegasIGaNAHIGPFCIVGPhveigeGTVLKshvvvnghtkigrdneiyqfasiGEVNqdlkyagep 81
Cdd:COG0663   13 IHPSAFVAPTAVV-----IG-DVTIGEDVSVWP------GAVLR-----------------------GDVG--------- 48

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112  82 tRVEIGDRNRIRESVTIHrgtVQGGGLTKVGSDNLLMINAHIaHDCTVGNRCILANNATlaghvsVDDFAIIGgmtavhQ 161
Cdd:COG0663   49 -PIRIGEGSNIQDGVVLH---VDPGYPLTIGDDVTIGHGAIL-HGCTIGDNVLIGMGAI------VLDGAVIG------D 111

                        170       180       190
                 ....*....|....*....|....*....|.
gi 446488112 162 FCIIGAHVMVGGcsgvAQDVPPYVIAQGNHA 192
Cdd:COG0663  112 GSIVGAGALVTE----GKVVPPGSLVVGSPA 138
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
83-196 8.02e-09

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 52.95  E-value: 8.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112  83 RVEIGDRNRIRESVTIHRGTVqgggltKVGSDNLLMINAHI--AHDCTVGNRCILANNATL----------------AGH 144
Cdd:COG0110    8 GARIGDGVVIGPGVRIYGGNI------TIGDNVYIGPGVTIddPGGITIGDNVLIGPGVTIltgnhpiddpatfplrTGP 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446488112 145 VSVDDFAIIGGMTAVHQFCIIGAHVMVGGCSGVAQDVPPYVIAQGNHATPFG 196
Cdd:COG0110   82 VTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVIR 133
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 2-62 9.49e-07

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: 48.25  E-value: 9.49e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446488112   2 IDKSAFVHPTAIVEEG------ASIGANAHIGPFCI------VGPHVEIGEGTVLKSHVVVNGHTKIGRDNEI 62
Cdd:cd03360   87 IHPSAVVSPSAVIGEGcvimagAVINPDARIGDNVIintgavIGHDCVIGDFVHIAPGVVLSGGVTIGEGAFI 159
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 2-173 1.13e-06

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


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 47.36  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112   2 IDKSAFVHPTAIVeegasIGaNAHIGPFCIVGPHVEIgegtvlkshvvvnghtkigrdneiyqfasigevnqdlkyAGEP 81
Cdd:cd04745    3 VDPSSFVHPTAVL-----IG-DVIIGKNCYIGPHASL---------------------------------------RGDF 37

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112  82 TRVEIGDRNRIRESVTIHRGTvqgggltkvGSDNLLMINAHIAHD-----CTVGNRCILANNATLAGHVSVDDFAIIGGM 156
Cdd:cd04745   38 GRIVIRDGANVQDNCVIHGFP---------GQDTVLEENGHIGHGailhgCTIGRNALVGMNAVVMDGAVIGEESIVGAM 108

                        170
                 ....*....|....*..
gi 446488112 157 TAVHQFCIIGAHVMVGG 173
Cdd:cd04745  109 AFVKAGTVIPPRSLIAG 125
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 6-171 3.84e-06

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 47.06  E-value: 3.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112   6 AFVHPTAIVEEGASIGANAHIGPFCIVGPHVEIGEGTVLKSHVVVNGHTKIGRDNEIYQfasigevnqdlkyageptrve 85
Cdd:PRK00892 101 AGIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHA--------------------- 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112  86 igdrnriresvtihrgtvqgggltkvgsdnllmiNAHIAHDCtvgnrcilannatlaghvsvddfaiiggmtavhqfcII 165
Cdd:PRK00892 160 ----------------------------------NVTIYHAV------------------------------------RI 169


                 ....*.
gi 446488112 166 GAHVMV 171
Cdd:PRK00892 170 GNRVII 175
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 2-173 5.04e-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: 45.10  E-value: 5.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112   2 IDKSAFVHPTAIVeegasIGAnahigpfcivgphVEIGEGTVLKSHVVVNGhtkigrDNEiyqfasigevnqdlkyagep 81
Cdd:cd04645    2 IDPSAFIAPNATV-----IGD-------------VTLGEGSSVWFGAVLRG------DVN-------------------- 37

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112  82 tRVEIGDRNRIRESVTIHrgtVQGGGLTKVGSDNLLMINAHIaHDCTVGNRCILANNATLAGHVSVDDFAIIGGMTAVHQ 161
Cdd:cd04645   38 -PIRIGERTNIQDGSVLH---VDPGYPTIIGDNVTVGHGAVL-HGCTIGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPP 112

                        170
                 ....*....|..
gi 446488112 162 FCIIGAHVMVGG 173
Cdd:cd04645  113 GKVIPPGSLVAG 124
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 92-192 2.30e-05

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: 42.87  E-value: 2.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112  92 IRESVTIHRGTVQGGGlTKVGSDNLLMINAHIAHDCTVGNRCILANNATLA---------------GHVSVDDFAIIGGM 156
Cdd:cd03358    1 IGDNCIIGTNVFIEND-VKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTndlyprskiyrkwelKGTTVKRGASIGAN 79

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 446488112 157 TAVHQFCIIGAHVMVGGCSGVAQDVPPYVIAQGNHA 192
Cdd:cd03358   80 ATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPA 115
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 32-131 4.36e-05

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 44.05  E-value: 4.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112  32 VGPHVEIGEGTVLKSHVVVNGHTKIGRDNEIYQFASIgevnqdlkyagepTRVEIGDRNRIRESVtIHRGTVqgGGLTKV 111
Cdd:PRK14354 262 IDADVEIGSDTVIEPGVVIKGNTVIGEDCVIGPGSRI-------------VDSTIGDGVTITNSV-IEESKV--GDNVTV 325

                         90       100
                 ....*....|....*....|
gi 446488112 112 GSdnllmiNAHIAHDCTVGN 131
Cdd:PRK14354 326 GP------FAHLRPGSVIGE 339
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 8-113 4.58e-05

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: 42.37  E-value: 4.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112   8 VHPTAIVEEGASIGANAHIGPFCIVGPHVEIGEGTVLKSHVVVNGHTKIGRDNEIYQFASIGEVNQDLKYAgePTRVE-- 85
Cdd:cd03350    4 VPPGAIIRDGAFIGPGAVLMMPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVIGGVLEPLQAT--PVIIEdd 81

                         90       100       110
                 ....*....|....*....|....*....|
gi 446488112  86 --IGDRNRIRESVTIHRGTVQGGGLTKVGS 113
Cdd:cd03350   82 vfIGANCEVVEGVIVGKGAVLAAGVVLTQS 111
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 36-124 9.78e-05

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 39.92  E-value: 9.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112  36 VEIGEGTVLKSHVVVNGHTKIGRDNEIYQFASIGEVNQDLKYAGeptrVEIGDRNRIRESVTIHRGtvqggglTKVGSDN 115
Cdd:cd00208    1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGPNEKNP----TIIGDNVEIGANAVIHGG-------VKIGDNA 69


                 ....*....
gi 446488112 116 LLMINAHIA 124
Cdd:cd00208   70 VIGAGAVVT 78
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 2-143 1.40e-04

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


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 41.46  E-value: 1.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112   2 IDKSAFVHPTAIVEEGASIGANAHIGPF----CIVGPHVEIGEGTVLKSHVVVNGHtkigrdneiyqfasigevnqdlky 77
Cdd:cd00710    5 IDPSAYVHPTAVVIGDVIIGDNVFVGPGasirADEGTPIIIGANVNIQDGVVIHAL------------------------ 60

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446488112  78 agEPTRVEIGDRNRIRESVTIHrgtvqggGLTKVGSDNLLMINAhIAHDCTVGNRCILANNATLAG 143
Cdd:cd00710   61 --EGYSVWIGKNVSIAHGAIVH-------GPAYIGDNCFIGFRS-VVFNAKVGDNCVIGHNAVVDG 116
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 81-194 1.49e-04

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: 40.28  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112  81 PTRVEIGDRNRIRESVTIHrgtvqgggltkvgsdNLLMInaHIAHDCTVGNRCIL---------ANNATLAGHVSVDDFA 151
Cdd:cd05825    1 PWNLTIGDNSWIGEGVWIY---------------NLAPV--TIGSDACISQGAYLctgshdyrsPAFPLITAPIVIGDGA 63

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 446488112 152 IIGGMTAVHQFCIIGAHVMVGGCSGVAQDVPPYVIAQGNHATP 194
Cdd:cd05825   64 WVAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVP 106
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 2-69 3.31e-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: 38.38  E-value: 3.31e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446488112   2 IDKSAFVHPTAIVEEGASIGANAHIGPFCIVG--------PHVEIGEGTVLKSHVVVNGHTKIGRDNEIYQFASIG 69
Cdd:cd00208    3 IGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGaatgpnekNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 1-57 7.41e-04

Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix (LbH) domain: Proteins in this family show simlarity to glucose-1-phosphate adenylyltransferases in that they contain N-terminal catalytic domains that resemble a dinucleotide-binding Rossmann fold and C-terminal LbH fold domains. Members in this family are predicted to be glucose-1-phosphate thymidylyltransferases, which are involved in the dTDP-L-rhamnose biosynthetic pathway. Glucose-1-phosphate thymidylyltransferase catalyzes the synthesis of deoxy-thymidine di-phosphate (dTDP)-L-rhamnose, an important component of the cell wall of many microorganisms. The C-terminal LbH domain contains multiple turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 39.11  E-value: 7.41e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446488112   1 MIDKSAFVHPTAIVE------EGASIGANAHIGPFCIVGPHVEIGEGTVLKSHVVVNGhTKIG 57
Cdd:cd05636   19 WIGEGAIVRSGAYIEgpviigKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSIIMDG-TKVP 80
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
17-46 1.08e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.78  E-value: 1.08e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 446488112   17 GASIGANAHIGPFCIVGPHVEIGEGTVLKS 46
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 1-56 1.08e-03

Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix (LbH) domain: Proteins in this family show simlarity to glucose-1-phosphate adenylyltransferases in that they contain N-terminal catalytic domains that resemble a dinucleotide-binding Rossmann fold and C-terminal LbH fold domains. Members in this family are predicted to be glucose-1-phosphate thymidylyltransferases, which are involved in the dTDP-L-rhamnose biosynthetic pathway. Glucose-1-phosphate thymidylyltransferase catalyzes the synthesis of deoxy-thymidine di-phosphate (dTDP)-L-rhamnose, an important component of the cell wall of many microorganisms. The C-terminal LbH domain contains multiple turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 38.72  E-value: 1.08e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446488112   1 MIDKSAFVHPTAIVEEGASIGANAHIGPFCIVGPHVEIGEGTVLKSHVVVNGHTKI 56
Cdd:cd05636   13 TIKGPVWIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEV 68
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 32-206 1.56e-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: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112  32 VGPHVEIGEGTVLKSHVVVNGHTKIGRDNEIYQFASIGE---------VNQDLKYAGEPTRVEIGDRNRIRESVTIHRGT 102
Cdd:PRK14357 252 IHYDVEIGMDTIIYPMTFIEGKTRIGEDCEIGPMTRIVDceignnvkiIRSECEKSVIEDDVSVGPFSRLREGTVLKKSV 331

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112 103 VQGGGL----TKVG----SDNLLMI-NAHIAHDCTVGNRCILANNATLAGHVS-VDDFAIIGGMTAVHQFCIIGAHVMVG 172
Cdd:PRK14357 332 KIGNFVeikkSTIGentkAQHLTYLgDATVGKNVNIGAGTITCNYDGKKKNPTfIEDGAFIGSNSSLVAPVRIGKGALIG 411

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 446488112 173 GCSGVAQDVPPYVIAQGNHATpfgVNIEG--LKRRG 206
Cdd:PRK14357 412 AGSVITEDVPPYSLALGRARQ---IVKEGwvLKKRK 444
PLN02357 PLN02357
serine acetyltransferase
 89-196 1.71e-03

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 39.09  E-value: 1.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112  89 RNRIRES--VTIHRGTvqgggltKVGSDNLL--MINAHIAHDCTVGNRCILANNATLAG--------HVSVDDFAIIGGM 156
Cdd:PLN02357 218 QNRVSEAfaVDIHPGA-------KIGQGILLdhATGVVIGETAVVGNNVSILHNVTLGGtgkqsgdrHPKIGDGVLIGAG 290

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 446488112 157 TAVHQFCIIGAHVMVGGCSGVAQDVPPYVIAQGNHATPFG 196
Cdd:PLN02357 291 TCILGNITIGEGAKIGAGSVVLKDVPPRTTAVGNPARLIG 330
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 30-172 2.21e-03

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 38.17  E-value: 2.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112  30 CIVGPHVEIGEGTVLKSHVVVNGHTKIGRDNEIYQFASIgevnqdlkyagepTRVEIGDRNRIRESVTIHrgtvqggglt 109
Cdd:cd03353   10 TYIDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVI-------------KDSTIGDGVVIKASSVIE---------- 66

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446488112 110 kvgsdnllmiNAHIAHDCTVGNRCILANNATLAGHVSVDDF-----AIIGGMTAVHQF-----CIIGAHVMVG 172
Cdd:cd03353   67 ----------GAVIGNGATVGPFAHLRPGTVLGEGVHIGNFveikkSTIGEGSKANHLsylgdAEIGEGVNIG 129
LbH_M1P_guanylylT_C cd05824
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 13-54 2.56e-03

Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Mannose-1-phosphate guanylyltransferase is also known as GDP-mannose pyrophosphorylase. It catalyzes the synthesis of GDP-mannose from GTP and mannose-1-phosphate, and is involved in the maintenance of cell wall integrity and glycosylation. Similar to ADP-glucose pyrophosphorylase, it contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain, presumably with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100062 [Multi-domain]  Cd Length: 80  Bit Score: 35.98  E-value: 2.56e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 446488112  13 IVEEGASIGANAHIGPFCIVGPHVEIGEGTVLKSHVVVNGHT 54
Cdd:cd05824    1 LIDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNST 42
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 2-59 2.65e-03

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: 37.85  E-value: 2.65e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446488112   2 IDKSAFVHPTAIVEEGASIGANAHIGPFCIVGPHVEIGEGTVLKSHVVVNGHTKIGRD 59
Cdd:cd03360  117 IGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEGAFIGAGATIIQGVTIGAG 174
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 1-205 3.16e-03

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 38.42  E-value: 3.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112   1 MIDKSAFVHPTAIVEeGASIGANAHIGPFCIVGPHVEIGEGTVLKSHVvvngHTKIGRDNEiyqfasiGEVNQDLKYAGE 80
Cdd:PRK14358 307 VLHEGAVIKPHSVLE-GAEVGAGSDVGPFARLRPGTVLGEGVHIGNFV----ETKNARLDA-------GVKAGHLAYLGD 374

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112  81 ptrVEIGDRNRIresvtihrgtvqGGGLTKVGSDNLLminahiAHDCTVGNRCILANNATLAGHVSVDDFAIIGGMTAVH 160
Cdd:PRK14358 375 ---VTIGAETNV------------GAGTIVANFDGVN------KHQSKVGAGVFIGSNTTLIAPRVVGDAAFIAAGSAVH 433

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 446488112 161 qfciigahvmvggcsgvaQDVP--PYVIAQGNHAtpfgvNIEGLKRR 205
Cdd:PRK14358 434 ------------------DDVPegAMAVARGKQR-----NLEGWSRR 457
PRK10502 PRK10502
putative acyl transferase; Provisional
 81-194 5.45e-03

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 36.85  E-value: 5.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112  81 PTRVEIGDRNRIRESVTIhrgtvqgggltkvgsDNLLMInahiahdcTVGNRCILANNATLAG--H-VSVDDFAIIGGMT 157
Cdd:PRK10502  69 PWKLTIGDYAWIGDDVWL---------------YNLGEI--------TIGAHCVISQKSYLCTgsHdYSDPHFDLNTAPI 125

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 446488112 158 AVHQFC------------IIGAHVMVGGCSGVAQDVPPYVIAQGNHATP 194
Cdd:PRK10502 126 VIGEGCwlaadvfvapgvTIGSGAVVGARSSVFKSLPANTICRGNPAVP 174
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 1-66 5.72e-03

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: 37.01  E-value: 5.72e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446488112   1 MIDKSAFVHPTAIVEEGASIGANAHIGPFCIVGPHV-----EIGEGTVLKSHVVVNGHTkIGRDNEIYQFA 66
Cdd:cd03353   11 YIDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCvikdsTIGDGVVIKASSVIEGAV-IGNGATVGPFA 80
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
109-137 6.10e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.46  E-value: 6.10e-03
                          10        20
                  ....*....|....*....|....*....
gi 446488112  109 TKVGSDNLLMINAHIAHDCTVGNRCILAN 137
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
12-40 7.57e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.08  E-value: 7.57e-03
                          10        20
                  ....*....|....*....|....*....
gi 446488112   12 AIVEEGASIGANAHIGPFCIVGPHVEIGE 40
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 83-190 9.71e-03

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: 35.12  E-value: 9.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446488112  83 RVEIGDRNRIRESVTIhrgtvQGGGLTKVGSDNLLMINAHIA---HDCTVGNRCILANNatLAGHVSVDDFAIIGGMTAV 159
Cdd:cd04647    1 NISIGDNVYIGPGCVI-----SAGGGITIGDNVLIGPNVTIYdhnHDIDDPERPIEQGV--TSAPIVIGDDVWIGANVVI 73

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446488112 160 HQFCIIGAHVMVGGCSGVAQDVPPYVIAQGN 190
Cdd:cd04647   74 LPGVTIGDGAVVGAGSVVTKDVPPNSIVAGN 104
 
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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