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Conserved domains on  [gi|873900231|ref|WP_048606664|]
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MULTISPECIES: acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase [Vibrio]

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 8.78e-148

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


:

Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 413.34  E-value: 8.78e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231   4 ETAKIHPAAVIEGDVTIGANVTVGPFTYIAGNVTIGDDTEVMSHVVIKGHTTIGKENRIFPHAVIGEENQDKKYGGEETT 83
Cdd:PRK05289   1 MMAKIHPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIGEDPQDLKYKGEPTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  84 VVIGDRNVIREAVQIHRGTVQDKATTVIGDDNLLCVNAHVAHDVIVGNHTHIGNNAILGGHVTVGDYAGVMALSAIHPFC 163
Cdd:PRK05289  81 LVIGDNNTIREFVTINRGTVQGGGVTRIGDNNLLMAYVHVAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLTAVHQFV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231 164 SIGAYAYIGGCSAVVQDVLPYVLAQGNHAAPFGLNLVGLKRNGFEKPEIRALQKAYKELYRSGKTLEEAKAALVEMAKEF 243
Cdd:PRK05289 161 RIGAHAMVGGMSGVSQDVPPYVLAEGNPARLRGLNLVGLKRRGFSREEIHALRRAYKLLYRSGLTLEEALEELAEEYPDS 240

                        250
                 ....*....|....*....
gi 873900231 244 TSVAPMLEMLENSERGIIR 262
Cdd:PRK05289 241 PEVKEILDFIESSKRGIIR 259
 
Name Accession Description Interval E-value
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
4-262 8.78e-148

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 413.34  E-value: 8.78e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231   4 ETAKIHPAAVIEGDVTIGANVTVGPFTYIAGNVTIGDDTEVMSHVVIKGHTTIGKENRIFPHAVIGEENQDKKYGGEETT 83
Cdd:PRK05289   1 MMAKIHPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIGEDPQDLKYKGEPTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  84 VVIGDRNVIREAVQIHRGTVQDKATTVIGDDNLLCVNAHVAHDVIVGNHTHIGNNAILGGHVTVGDYAGVMALSAIHPFC 163
Cdd:PRK05289  81 LVIGDNNTIREFVTINRGTVQGGGVTRIGDNNLLMAYVHVAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLTAVHQFV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231 164 SIGAYAYIGGCSAVVQDVLPYVLAQGNHAAPFGLNLVGLKRNGFEKPEIRALQKAYKELYRSGKTLEEAKAALVEMAKEF 243
Cdd:PRK05289 161 RIGAHAMVGGMSGVSQDVPPYVLAEGNPARLRGLNLVGLKRRGFSREEIHALRRAYKLLYRSGLTLEEALEELAEEYPDS 240

                        250
                 ....*....|....*....
gi 873900231 244 TSVAPMLEMLENSERGIIR 262
Cdd:PRK05289 241 PEVKEILDFIESSKRGIIR 259
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 5-262 1.02e-144

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: 405.56  E-value: 1.02e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231   5 TAKIHPAAVIEGDVTIGANVTVGPFTYIAGNVTIGDDTEVMSHVVIKGHTTIGKENRIFPHAVIGEENQDKKYGGEETTV 84
Cdd:COG1043    1 MAMIHPTAIVDPGAKLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASIGEEPQDLKYKGEPTRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  85 VIGDRNVIREAVQIHRGTVQDKATTVIGDDNLLCVNAHVAHDVIVGNHTHIGNNAILGGHVTVGDYAGVMALSAIHPFCS 164
Cdd:COG1043   81 EIGDNNTIREFVTIHRGTVQGGGVTRIGDDNLLMAYVHVAHDCVVGNNVILANNATLAGHVEVGDHAIIGGLSAVHQFVR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231 165 IGAYAYIGGCSAVVQDVLPYVLAQGNHAAPFGLNLVGLKRNGFEKPEIRALQKAYKELYRSGKTLEEAKAALVEMAKEFT 244
Cdd:COG1043  161 IGAHAMVGGGSGVVKDVPPYVLAAGNPARLRGLNLVGLKRRGFSREQIRALKRAYRLLYRSGLTLEEALEELEAELPDSP 240

                        250
                 ....*....|....*...
gi 873900231 245 SVAPMLEMLENSERGIIR 262
Cdd:COG1043  241 EVRELLDFIRASKRGIIR 258
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 7-260 5.41e-138

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: 388.33  E-value: 5.41e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231   7 KIHPAAVIEGDVTIGANVTVGPFTYIAGNVTIGDDTEVMSHVVIKGHTTIGKENRIFPHAVIGEENQDKKYGGEETTVVI 86
Cdd:cd03351    1 MIHPTAIVDPGAKIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIGEAPQDLKYKGEPTRLEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  87 GDRNVIREAVQIHRGTVQDKATTVIGDDNLLCVNAHVAHDVIVGNHTHIGNNAILGGHVTVGDYAGVMALSAIHPFCSIG 166
Cdd:cd03351   81 GDNNTIREFVTIHRGTAQGGGVTRIGNNNLLMAYVHVAHDCVIGNNVILANNATLAGHVEIGDYAIIGGLSAVHQFCRIG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231 167 AYAYIGGCSAVVQDVLPYVLAQGNHAAPFGLNLVGLKRNGFEKPEIRALQKAYKELYRSGKTLEEAKAALVEMAKEFTSV 246
Cdd:cd03351  161 RHAMVGGGSGVVQDVPPYVIAAGNRARLRGLNLVGLKRRGFSREEIRALKRAYRILYRSGLTLEEALEELEEEAPDSPEV 240

                        250
                 ....*....|....
gi 873900231 247 APMLEMLENSERGI 260
Cdd:cd03351  241 EELVDFIRSSKRGI 254
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 8-261 2.99e-112

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: 323.06  E-value: 2.99e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231    8 IHPAAVIEGDVTIGANVTVGPFTYIAGNVTIGDDTEVMSHVVIKGHTTIGKENRIFPHAVIGEENQDKKYGGEETTVVIG 87
Cdd:TIGR01852   1 IHPTAIIEPGAEIGENVEIGPFCIVGPGVKIGDGVELKSHVVILGHTTIGEGTRIFPGAVIGGVPQDLKYKGEKTRLIIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231   88 DRNVIREAVQIHRGTVQDKATTVIGDDNLLCVNAHVAHDVIVGNHTHIGNNAILGGHVTVGDYAGVMALSAIHPFCSIGA 167
Cdd:TIGR01852  81 DNNTIREFVTINRGTASGGGVTRIGNNNLLMAYSHIAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLVAVHQFVRIGR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  168 YAYIGGCSAVVQDVLPYVLAQGNHAAPFGLNLVGLKRNGFEKPEIRALQKAYKELYRSGKTLEEAKAALVEMAKEFTSVA 247
Cdd:TIGR01852 161 YAMIGGLSAVSKDVPPYCLAEGNRARLRGLNIVGLRRRGFSREEITAIKRAYRTLFRSGLPLREAAQQVAEEYEDNPEVK 240

                         250
                  ....*....|....
gi 873900231  248 PMLEMLENSERGII 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 2.09e-35

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: 121.41  E-value: 2.09e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  180 DVLPYVLAQGNHAAPFGLNLVGLKRNGFEKPEIRALQKAYKELYRSGKTLEEAKAALVEMAKEFTSVAPMLEMLENSERG 259
Cdd:pfam13720   1 DVPPYVLAAGNPARLRGLNLVGLRRRGFSSEEIRALKRAYRLLYRSGLTLEEALEELEEEVPDSPEVQEILDFIRSSKRG 80


                  ..
gi 873900231  260 II 261
Cdd:pfam13720  81 II 82
 
Name Accession Description Interval E-value
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
4-262 8.78e-148

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 413.34  E-value: 8.78e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231   4 ETAKIHPAAVIEGDVTIGANVTVGPFTYIAGNVTIGDDTEVMSHVVIKGHTTIGKENRIFPHAVIGEENQDKKYGGEETT 83
Cdd:PRK05289   1 MMAKIHPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIGEDPQDLKYKGEPTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  84 VVIGDRNVIREAVQIHRGTVQDKATTVIGDDNLLCVNAHVAHDVIVGNHTHIGNNAILGGHVTVGDYAGVMALSAIHPFC 163
Cdd:PRK05289  81 LVIGDNNTIREFVTINRGTVQGGGVTRIGDNNLLMAYVHVAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLTAVHQFV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231 164 SIGAYAYIGGCSAVVQDVLPYVLAQGNHAAPFGLNLVGLKRNGFEKPEIRALQKAYKELYRSGKTLEEAKAALVEMAKEF 243
Cdd:PRK05289 161 RIGAHAMVGGMSGVSQDVPPYVLAEGNPARLRGLNLVGLKRRGFSREEIHALRRAYKLLYRSGLTLEEALEELAEEYPDS 240

                        250
                 ....*....|....*....
gi 873900231 244 TSVAPMLEMLENSERGIIR 262
Cdd:PRK05289 241 PEVKEILDFIESSKRGIIR 259
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 5-262 1.02e-144

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: 405.56  E-value: 1.02e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231   5 TAKIHPAAVIEGDVTIGANVTVGPFTYIAGNVTIGDDTEVMSHVVIKGHTTIGKENRIFPHAVIGEENQDKKYGGEETTV 84
Cdd:COG1043    1 MAMIHPTAIVDPGAKLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASIGEEPQDLKYKGEPTRL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  85 VIGDRNVIREAVQIHRGTVQDKATTVIGDDNLLCVNAHVAHDVIVGNHTHIGNNAILGGHVTVGDYAGVMALSAIHPFCS 164
Cdd:COG1043   81 EIGDNNTIREFVTIHRGTVQGGGVTRIGDDNLLMAYVHVAHDCVVGNNVILANNATLAGHVEVGDHAIIGGLSAVHQFVR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231 165 IGAYAYIGGCSAVVQDVLPYVLAQGNHAAPFGLNLVGLKRNGFEKPEIRALQKAYKELYRSGKTLEEAKAALVEMAKEFT 244
Cdd:COG1043  161 IGAHAMVGGGSGVVKDVPPYVLAAGNPARLRGLNLVGLKRRGFSREQIRALKRAYRLLYRSGLTLEEALEELEAELPDSP 240

                        250
                 ....*....|....*...
gi 873900231 245 SVAPMLEMLENSERGIIR 262
Cdd:COG1043  241 EVRELLDFIRASKRGIIR 258
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 7-260 5.41e-138

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: 388.33  E-value: 5.41e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231   7 KIHPAAVIEGDVTIGANVTVGPFTYIAGNVTIGDDTEVMSHVVIKGHTTIGKENRIFPHAVIGEENQDKKYGGEETTVVI 86
Cdd:cd03351    1 MIHPTAIVDPGAKIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIGEAPQDLKYKGEPTRLEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  87 GDRNVIREAVQIHRGTVQDKATTVIGDDNLLCVNAHVAHDVIVGNHTHIGNNAILGGHVTVGDYAGVMALSAIHPFCSIG 166
Cdd:cd03351   81 GDNNTIREFVTIHRGTAQGGGVTRIGNNNLLMAYVHVAHDCVIGNNVILANNATLAGHVEIGDYAIIGGLSAVHQFCRIG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231 167 AYAYIGGCSAVVQDVLPYVLAQGNHAAPFGLNLVGLKRNGFEKPEIRALQKAYKELYRSGKTLEEAKAALVEMAKEFTSV 246
Cdd:cd03351  161 RHAMVGGGSGVVQDVPPYVIAAGNRARLRGLNLVGLKRRGFSREEIRALKRAYRILYRSGLTLEEALEELEEEAPDSPEV 240

                        250
                 ....*....|....
gi 873900231 247 APMLEMLENSERGI 260
Cdd:cd03351  241 EELVDFIRSSKRGI 254
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 8-261 2.99e-112

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: 323.06  E-value: 2.99e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231    8 IHPAAVIEGDVTIGANVTVGPFTYIAGNVTIGDDTEVMSHVVIKGHTTIGKENRIFPHAVIGEENQDKKYGGEETTVVIG 87
Cdd:TIGR01852   1 IHPTAIIEPGAEIGENVEIGPFCIVGPGVKIGDGVELKSHVVILGHTTIGEGTRIFPGAVIGGVPQDLKYKGEKTRLIIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231   88 DRNVIREAVQIHRGTVQDKATTVIGDDNLLCVNAHVAHDVIVGNHTHIGNNAILGGHVTVGDYAGVMALSAIHPFCSIGA 167
Cdd:TIGR01852  81 DNNTIREFVTINRGTASGGGVTRIGNNNLLMAYSHIAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLVAVHQFVRIGR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  168 YAYIGGCSAVVQDVLPYVLAQGNHAAPFGLNLVGLKRNGFEKPEIRALQKAYKELYRSGKTLEEAKAALVEMAKEFTSVA 247
Cdd:TIGR01852 161 YAMIGGLSAVSKDVPPYCLAEGNRARLRGLNIVGLRRRGFSREEITAIKRAYRTLFRSGLPLREAAQQVAEEYEDNPEVK 240

                         250
                  ....*....|....
gi 873900231  248 PMLEMLENSERGII 261
Cdd:TIGR01852 241 EILDFIRESKRGIC 254
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 1-262 1.48e-103

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 301.17  E-value: 1.48e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231   1 MIHETAKIHPAAviegdvTIGANVTVGPFTYIAGNVTIGDDTEVMSHVVIKGHTTIGKENRIFPHAVIGEENQDKKYGGE 80
Cdd:PRK12461   1 MIHPTAVIDPSA------KLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGDEPQDFTYKGE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  81 ETTVVIGDRNVIREAVQIHRGTvQDKATTVIGDDNLLCVNAHVAHDVIVGNHTHIGNNAILGGHVTVGDYAGVMALSAIH 160
Cdd:PRK12461  75 ESRLEIGDRNVIREGVTIHRGT-KGGGVTRIGNDNLLMAYSHVAHDCQIGNNVILVNGALLAGHVTVGDRAIISGNCLVH 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231 161 PFCSIGAYAYIGGCSAVVQDVLPYVLAQGNHAAPFGLNLVGLKRNGFEKPEIRALQKAYKELYRSGKTLEEAKAALVEMA 240
Cdd:PRK12461 154 QFCRIGALAMMAGGSRISKDVPPYCMMAGHPTNVHGLNAVGLRRRGFSSRAIRALKRAYKIIYRSGLSVQQAVAELELQQ 233

                        250       260
                 ....*....|....*....|..
gi 873900231 241 KEFTSVAPMLEMLENSERGIIR 262
Cdd:PRK12461 234 FESPEVEELIDFIKASKRGIVR 255
Acetyltransf_11 pfam13720
Udp N-acetylglucosamine O-acyltransferase; Domain 2; This is domain 2, or the C-terminal ...
 180-261 2.09e-35

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: 121.41  E-value: 2.09e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  180 DVLPYVLAQGNHAAPFGLNLVGLKRNGFEKPEIRALQKAYKELYRSGKTLEEAKAALVEMAKEFTSVAPMLEMLENSERG 259
Cdd:pfam13720   1 DVPPYVLAAGNPARLRGLNLVGLRRRGFSSEEIRALKRAYRLLYRSGLTLEEALEELEEEVPDSPEVQEILDFIRSSKRG 80


                  ..
gi 873900231  260 II 261
Cdd:pfam13720  81 II 82
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 2-160 1.74e-31

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: 118.58  E-value: 1.74e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231   2 IHETAKIHPAAVIEGDVTIGANVTVGPFTYIAGNVTIGDDTEVMSHVVIKGHTTIGKENRIFPHAVIGEE------NQDK 75
Cdd:COG1044  111 IGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVIGDRVIIHSGAVIGADgfgfapDEDG 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  76 KY------GGeettVVIGDRnvireaVQI------HRGTVQDkatTVIGD----DNLLcvnaHVAHDVIVGNH------- 132
Cdd:COG1044  191 GWvkipqlGR----VVIGDD------VEIganttiDRGALGD---TVIGDgtkiDNLV----QIAHNVRIGEHtaiaaqv 253

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 873900231 133 -----THIGNNAILGG------HVTVGDYAGVMALSAIH 160
Cdd:COG1044  254 giagsTKIGDNVVIGGqvgiagHLTIGDGVIIGAQSGVT 292
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 1-194 2.64e-31

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: 114.81  E-value: 2.64e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231   1 MIHETAKIHPAAVIEGDVTIGANVTVGPFTYIAGNVTIGDDTEVMSHVVIKGHTTIGKENRIFPHAVIGEE-----NQDK 75
Cdd:cd03352    3 KIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIGSDgfgfaPDGG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  76 KY------GGeettVVIGDRNVIREAVQIHRGTVQDkatTVIGD----DNLLcvnaHVAHDVIVGNHTHIGNNAILGGHV 145
Cdd:cd03352   83 GWvkipqlGG----VIIGDDVEIGANTTIDRGALGD---TVIGDgtkiDNLV----QIAHNVRIGENCLIAAQVGIAGST 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 873900231 146 TVGDYAGVMALSAIHPFCSIGAYAYIGGCSAVVQDVLPYVLAQGNHAAP 194
Cdd:cd03352  152 TIGDNVIIGGQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQP 200
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 2-160 6.58e-27

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 106.38  E-value: 6.58e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231   2 IHETAK------IHPAAVIEGDVTIGANVTVGPFTYIAGNVTIGDDTEVMSHVVIKGHTTIGKENRIFPHAVIGEE---- 71
Cdd:PRK00892 109 IDPSAKigegvsIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVIGSDgfgf 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  72 -NQDKKY------GGeettVVIGDRNVIREAVQIHRGTVQDkatTVIGD----DNLLcvnaHVAHDVIVGNH-------- 132
Cdd:PRK00892 189 aNDRGGWvkipqlGR----VIIGDDVEIGANTTIDRGALDD---TVIGEgvkiDNLV----QIAHNVVIGRHtaiaaqvg 257

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 873900231 133 ----THIGNNAILGG------HVTVGDYAGVMALSAIH 160
Cdd:PRK00892 258 iagsTKIGRYCMIGGqvgiagHLEIGDGVTITAMSGVT 295
lipid_A_lpxD TIGR01853
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD; This model describes LpxD, an ...
 2-159 1.79e-22

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD; This model describes LpxD, 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. This protein represents the third step from UDP-N-acetyl-D-glucosamine. The group added at this step generally is 14:0(3-OH) (myristate) but may vary; in Aquifex it appears to be 16:0(3-OH) (palmitate). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 273834 [Multi-domain]  Cd Length: 324  Bit Score: 94.28  E-value: 1.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231    2 IHETAKIHPAAVIEGDVTIGANVTVG------------PFTYIAGNVTIGDDTEVMSHVVIKGHTTIGKENRIFPHAVIG 69
Cdd:TIGR01853  94 IHPTAVVDPSAKIGDGVTIGPNVVIGagveigenviigPGVVIGDDVVIGDGSRIHPNVVIYERVQLGKNVIIHSGAVIG 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231   70 EE-------NQDKKYGGEET-TVVIGDRNVIREAVQIHRGTVQDkatTVIGD----DNLLcvnaHVAHDVIVGNH----- 132
Cdd:TIGR01853 174 SDgfgyahtANGGHVKIPQIgRVIIEDDVEIGANTTIDRGAFDD---TIIGEgtkiDNLV----QIAHNCRIGENciiva 246

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 873900231  133 -------THIGNNAILGG------HVTVGDYAGVMALSAI 159
Cdd:TIGR01853 247 qvgiagsTKIGRNVIIGGqvgvagHLEIGDNVTIGAKSGV 286
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 83-190 4.46e-15

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


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 71.36  E-value: 4.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  83 TVVIGDRNVIREAVQIHRG-TVQdkATTVIGDDNLLCVNAHVAHDVIVGNHTHIGNNAILGGHVTVGDYAGVMALSAIHP 161
Cdd:cd03360   90 SAVVSPSAVIGEGCVIMAGaVIN--PDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEGAFIGAGATIIQ 167

                         90       100
                 ....*....|....*....|....*....
gi 873900231 162 FCSIGAYAYIGGCSAVVQDVLPYVLAQGN 190
Cdd:cd03360  168 GVTIGAGAIIGAGAVVTKDVPDGSVVVGN 196
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 83-192 9.24e-14

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: 67.90  E-value: 9.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231   83 TVVIGDRNVIREAVQIHRG-TVQdkATTVIGDDNLLCVNAHVAHDVIVGNHTHIGNNAILGGHVTVGDYAGVMALSAIHP 161
Cdd:TIGR03570  93 SAIVSPSASIGEGTVIMAGaVIN--PDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVIGEGVFIGAGATIIQ 170

                          90       100       110
                  ....*....|....*....|....*....|.
gi 873900231  162 FCSIGAYAYIGGCSAVVQDVLPYVLAQGNHA 192
Cdd:TIGR03570 171 GVTIGAGAIVGAGAVVTKDIPDGGVVVGVPA 201
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 2-161 3.98e-11

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 60.04  E-value: 3.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231   2 IHETAKIHPAAVIEGDVTIGANVTVGPFtyiagnvtigddtevmshVVIKghttigkenrifphavigeenqdkkygGEE 81
Cdd:COG0663   13 IHPSAFVAPTAVVIGDVTIGEDVSVWPG------------------AVLR---------------------------GDV 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  82 TTVVIGDRNVIREAVQIHrgtVQDKATTVIGDdnllcvNAHVAHDVI-----VGNHTHIGNNAILGGHVTVGDYAGVMAL 156
Cdd:COG0663   48 GPIRIGEGSNIQDGVVLH---VDPGYPLTIGD------DVTIGHGAIlhgctIGDNVLIGMGAIVLDGAVIGDGSIVGAG 118


                 ....*
gi 873900231 157 SAIHP 161
Cdd:COG0663  119 ALVTE 123
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 8-172 9.79e-10

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: 56.66  E-value: 9.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231   8 IHPAAV-IEGDVTIGANVTVGPFTYIAGNVTIGDDTEVMSHVVIKGhTTIGKENRIFPHAVIgeenqdkkyggeettvvi 86
Cdd:cd03353    5 IDPETTyIDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIKD-STIGDGVVIKASSVI------------------ 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  87 gdrnvirEAVQIHRGtvqdkatTVIGDdnllcvNAHVAHDVIVGNHTHIGN-----NAILG-----GHVT-VGDyagvma 155
Cdd:cd03353   66 -------EGAVIGNG-------ATVGP------FAHLRPGTVLGEGVHIGNfveikKSTIGegskaNHLSyLGD------ 119

                        170
                 ....*....|....*..
gi 873900231 156 lsaihpfCSIGAYAYIG 172
Cdd:cd03353  120 -------AEIGEGVNIG 129
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 20-192 2.73e-09

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: 53.66  E-value: 2.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  20 IGANVTVGPFTYIAGNVTIGDDTEVMSHVVIKGHTTIGKENRIFPHAVIgeenqdkkyggeettvvIGDRNVireavqih 99
Cdd:cd03358    1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVF-----------------TNDLYP-------- 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231 100 RGTVQDKattvigdDNLLcvnahvahDVIVGNHTHIGNNAILGGHVTvgdyagvmalsaihpfcsIGAYAYIGGCSAVVQ 179
Cdd:cd03358   56 RSKIYRK-------WELK--------GTTVKRGASIGANATILPGVT------------------IGEYALVGAGAVVTK 102

                        170
                 ....*....|...
gi 873900231 180 DVLPYVLAQGNHA 192
Cdd:cd03358  103 DVPPYALVVGNPA 115
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 2-159 4.96e-09

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 56.38  E-value: 4.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231   2 IHETAKIHPAAVIEGDV------TIGANVTVGPFTYIAgNVTIGDDTEVMSHVV----IKGHTTIGKENRIFPHAVIGEE 71
Cdd:PRK14354 262 IDADVEIGSDTVIEPGVvikgntVIGEDCVIGPGSRIV-DSTIGDGVTITNSVIeeskVGDNVTVGPFAHLRPGSVIGEE 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  72 nqdkkyggeettVVIGDrnvireAVQIHRGTVQDKAT----TVIGDdnllcvnAHVAHDVIVG-------------NHTH 134
Cdd:PRK14354 341 ------------VKIGN------FVEIKKSTIGEGTKvshlTYIGD-------AEVGENVNIGcgtitvnydgknkFKTI 395

                        170       180       190
                 ....*....|....*....|....*....|.
gi 873900231 135 IGNNAILGGH------VTVGDYAGVMALSAI 159
Cdd:PRK14354 396 IGDNAFIGCNsnlvapVTVGDNAYIAAGSTI 426
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 30-149 5.20e-09

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 55.99  E-value: 5.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  30 TYIAGNVTIGDDTEVMSHVVIKGHTTIGKENRIFPHAVIgeenqdkkyggeeTTVVIGDRNVIREAVqIHRGTVQDKATt 109
Cdd:PRK14354 260 TYIDADVEIGSDTVIEPGVVIKGNTVIGEDCVIGPGSRI-------------VDSTIGDGVTITNSV-IEESKVGDNVT- 324

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 873900231 110 vIGDdnllcvNAHVAHDVIVGNHTHIGN-----NAILG-----GHVT-VGD 149
Cdd:PRK14354 325 -VGP------FAHLRPGSVIGEEVKIGNfveikKSTIGegtkvSHLTyIGD 368
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 2-144 1.47e-08

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


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 52.41  E-value: 1.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231   2 IHETAKIHPAAVIEGDVTIGANVTVGPFTYIAGNV---TIGDDTEVMSHVVIkgHTTIGkenriFPhavigeenqdkkyg 78
Cdd:cd04645    2 IDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRGDVnpiRIGERTNIQDGSVL--HVDPG-----YP-------------- 60

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 873900231  79 geettVVIGDRNVIREAVQIHRGTVQDKAttVIGDdnllcvNAhvahdvIVGNHTHIGNNAILGGH 144
Cdd:cd04645   61 -----TIIGDNVTVGHGAVLHGCTIGDNC--LIGM------GA------IILDGAVIGKGSIVAAG 107
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
49-190 3.16e-08

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 51.41  E-value: 3.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  49 VIKGHTTIGKENRIFPHAVIGEENqdkkyggeettVVIGDRNVIREAVQIHrgtvqDKATTVIGDdnllcvNAHVAHDVI 128
Cdd:COG0110    4 LLLFGARIGDGVVIGPGVRIYGGN-----------ITIGDNVYIGPGVTID-----DPGGITIGD------NVLIGPGVT 61

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 873900231 129 VGNHTH----------------IGNNAILGGHVTVGDyaGVmalsaihpfcSIGAYAYIGGCSAVVQDVLPYVLAQGN 190
Cdd:COG0110   62 ILTGNHpiddpatfplrtgpvtIGDDVWIGAGATILP--GV----------TIGDGAVVGAGSVVTKDVPPYAIVAGN 127
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 30-150 4.15e-08

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 53.49  E-value: 4.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  30 TYIAGNVTIGDDTEVMSHVVIKGHTTIGKENRIFPHAVIgeenqdkkyggeeTTVVIGDRnvireaVQIHRgtvqdkatT 109
Cdd:COG1207  261 TYIDGDVEIGRDVVIDPNVILEGKTVIGEGVVIGPNCTL-------------KDSTIGDG------VVIKY--------S 313

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 873900231 110 VIgddnllcVNAHVAHDVIVGNHTHIGNNAILGGHVTVGDY 150
Cdd:COG1207  314 VI-------EDAVVGAGATVGPFARLRPGTVLGEGVKIGNF 347
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 1-70 8.60e-08

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: 50.66  E-value: 8.60e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 873900231   1 MIHETAKIHPAAVIEGDVTIGANVTVGPFTYIAGNVTIGDDTEVMSHVVIKgHTTIGKENRIfPH------AVIGE 70
Cdd:cd05636   19 WIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVK-NSIIMDGTKV-PHlnyvgdSVLGE 92
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 2-70 9.54e-08

UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.


Pssm-ID: 274908 [Multi-domain]  Cd Length: 393  Bit Score: 52.21  E-value: 9.54e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 873900231    2 IHETAKIHPAAVIEGDVTIGANVTVGPFTYIAGNVTIGDDTEVMSHVVIKGhTTIGKENRIfPH------AVIGE 70
Cdd:TIGR03992 251 IGEGAVIRSGTYIEGPVYIGKNCDIGPNAYIRPYTVIGNNVHIGNAVEIKN-SIIMEGTKI-PHlsyvgdSVIGE 323
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 8-187 2.02e-07

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 51.18  E-value: 2.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231   8 IHPAAV-IEGDVTIGANVTVGPFTYIAGNVTIGDDTEVMSHVVIKgHTTIGKENRI-FPH---AVIGEEnqdkkyggeet 82
Cdd:COG1207  256 IDPATTyIDGDVEIGRDVVIDPNVILEGKTVIGEGVVIGPNCTLK-DSTIGDGVVIkYSViedAVVGAG----------- 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  83 tVVIGDRNVIREAVQIHRGT-----VQDKATTV-----------IGDdnllcvnAHVAHDVIVG-------------NHT 133
Cdd:COG1207  324 -ATVGPFARLRPGTVLGEGVkignfVEVKNSTIgegskvnhlsyIGD-------AEIGEGVNIGagtitcnydgvnkHRT 395

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231 134 HIGNNAILGGH------VTVGDyagvmalsaihpfcsigaYAYIGGCSAVVQDVLPYVLA 187
Cdd:COG1207  396 VIGDGAFIGSNtnlvapVTIGD------------------GATIGAGSTITKDVPAGALA 437
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 2-143 2.42e-07

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: 49.16  E-value: 2.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231   2 IHETAKIHPAAVIEGDVTIGANVTVGPFTYIAGN----VTIGDDTEVMSHVVIkghttigkenrifpHAVigeenqdkky 77
Cdd:cd00710    5 IDPSAYVHPTAVVIGDVIIGDNVFVGPGASIRADegtpIIIGANVNIQDGVVI--------------HAL---------- 60

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 873900231  78 ggEETTVVIGDRNVIREAVQIHrGTVqdkattVIGDDNLLCVNAhVAHDVIVGNHTHIGNNAILGG 143
Cdd:cd00710   61 --EGYSVWIGKNVSIAHGAIVH-GPA------YIGDNCFIGFRS-VVFNAKVGDNCVIGHNAVVDG 116
LbH_unknown cd05635
Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group ...
 10-62 2.52e-07

Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group are uncharacterized bacterial proteins containing a LbH domain with 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: 100059 [Multi-domain]  Cd Length: 101  Bit Score: 47.66  E-value: 2.52e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 873900231  10 PAAVI---EGDVTIGANVTVGPFTYIAGNVTIGDDTEVMSHVVIKGHTTIGKENRI 62
Cdd:cd05635    1 PGAVLdaeDGPIYIGKDAVIEPFAVIEGPVYIGPGSRVKMGARIYGNTTIGPTCKI 56
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 8-69 3.79e-07

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: 49.41  E-value: 3.79e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 873900231    8 IHPAAVIEGDVTIGANVTVGPFTYIAGNVTIGDDTEVMSHVVIKGHTTIGKenrifpHAVIG 69
Cdd:TIGR03570 126 INTGAIVEHDCVIGDFVHIAPGVTLSGGVVIGEGVFIGAGATIIQGVTIGA------GAIVG 181
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 2-159 5.15e-07

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 49.93  E-value: 5.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231   2 IHETAKIHPAAVIE------GDVTIGANVTVGPFTYIAgNVTIGDDTEVMSHVV----IKGHTTIGKENRIFPHAVIGEE 71
Cdd:PRK14360 259 ISETVELGPDVIIEpqthlrGNTVIGSGCRIGPGSLIE-NSQIGENVTVLYSVVsdsqIGDGVKIGPYAHLRPEAQIGSN 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  72 NQ-------DKKYGGEETTV----VIGDrNVIREAVQIHRGTV------QDKATTVIGDdnllcvnahvahdvivgnHTH 134
Cdd:PRK14360 338 CRignfveiKKSQLGEGSKVnhlsYIGD-ATLGEQVNIGAGTItanydgVKKHRTVIGD------------------RSK 398

                        170       180
                 ....*....|....*....|....*
gi 873900231 135 IGNNAILGGHVTVGDYAGVMALSAI 159
Cdd:PRK14360 399 TGANSVLVAPITLGEDVTVAAGSTI 423
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 8-68 7.77e-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: 7.77e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 873900231   8 IHPAAVIEGDVTIGANVTVGPFTYIAGNVTIGDDTEVMSHVVIKGHTTIGKENRIFPHAVI 68
Cdd:cd03360  123 INTGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEGAFIGAGATIIQGVTIGAGAIIGAGAVV 183
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 2-69 9.53e-07

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 45.70  E-value: 9.53e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 873900231   2 IHETAKIHPAAVIEGDVTIGANVTVGPFTYIAGN--------VTIGDDTEVMSHVVIKGHTTIGKENRIFPHAVIG 69
Cdd:cd00208    3 IGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAAtgpneknpTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 2-68 1.88e-06

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: 47.09  E-value: 1.88e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 873900231   2 IHETAKIHPAAVIEGDVTIGANVTVGPFTYIAGNVTIGDDTEVMSHVVIKGHTTIGKENRIFPHAVI 68
Cdd:cd03360   99 IGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEGAFIGAGATI 165
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 2-178 4.56e-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: 45.44  E-value: 4.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231   2 IHETAKIHPAAVIEGDVTIGANVTVGPftyiagnvtigddtevmsHVVIKGHttigkenrifphavigeenqdkkyGGEe 81
Cdd:cd04745    3 VDPSSFVHPTAVLIGDVIIGKNCYIGP------------------HASLRGD------------------------FGR- 39

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  82 ttVVIGDRNVIREAVQIHRGtvqdkattvIGDDNLLCVNAHVAHDVIV-----GNHTHIGNNAILGGHVTVGDYAGVMAL 156
Cdd:cd04745   40 --IVIRDGANVQDNCVIHGF---------PGQDTVLEENGHIGHGAILhgctiGRNALVGMNAVVMDGAVIGEESIVGAM 108

                        170       180
                 ....*....|....*....|..
gi 873900231 157 SAIHPFCSIGAYAYIGGCSAVV 178
Cdd:cd04745  109 AFVKAGTVIPPRSLIAGSPAKV 130
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 8-183 1.35e-05

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


Pssm-ID: 100049 [Multi-domain]  Cd Length: 161  Bit Score: 44.13  E-value: 1.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231   8 IHPAAVIEGDVtigANVTVGPFTYIAGNVTI------GDDTEVMSHVVIKGHttigkenrifphavigeenqdkkyggee 81
Cdd:cd03359   30 IQSDVIIRGDL---ATVSIGRYCILSEGCVIrppfkkFSKGVAFFPLHIGDY---------------------------- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  82 ttVVIGDRNVIrEAVQIhrgtvqdkattvigddnllcvnahvahdvivGNHTHIGNNAILGGHVTVGDYAGVMALSAIHP 161
Cdd:cd03359   79 --VFIGENCVV-NAAQI-------------------------------GSYVHIGKNCVIGRRCIIKDCVKILDGTVVPP 124

                        170       180
                 ....*....|....*....|..
gi 873900231 162 FCSIGAYAYIGGCSAVVQDVLP 183
Cdd:cd03359  125 DTVIPPYSVVSGRPARFIGELP 146
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 2-70 5.70e-05

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 42.79  E-value: 5.70e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 873900231   2 IHETAKIHPAAVIEGdVTIGANVTVGPFTYIAGNVTIGDDTEVMSHVVIKGhTTIGKENRIfPH------AVIGE 70
Cdd:cd03353   53 IGDGVVIKASSVIEG-AVIGNGATVGPFAHLRPGTVLGEGVHIGNFVEIKK-STIGEGSKA-NHlsylgdAEIGE 124
PLN02694 PLN02694
serine O-acetyltransferase
 92-210 9.40e-05

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 43.09  E-value: 9.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  92 IREAVQIHRGTVQDKATTVIgddnllcvnahVAHDVIVGNHTHIGNNAILGG--------HVTVGDYAGVMALSAIHPFC 163
Cdd:PLN02694 163 IHPAAKIGKGILFDHATGVV-----------IGETAVIGNNVSILHHVTLGGtgkacgdrHPKIGDGVLIGAGATILGNV 231

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 873900231 164 SIGAYAYIGGCSAVVQDVLPYVLAQGNHAapfglNLVGlkrnGFEKP 210
Cdd:PLN02694 232 KIGEGAKIGAGSVVLIDVPPRTTAVGNPA-----RLVG----GKEKP 269
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 2-71 1.17e-04

Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 39.53  E-value: 1.17e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231   2 IHETAKIHPAaVIEGDVTIGANVTVGPfTYIAGNVTIGDDTEVmSHVVIKGHTTIGKENRIFPHAVIGEE 71
Cdd:cd03356    8 IGENAIIKNS-VIGDNVRIGDGVTITN-SILMDNVTIGANSVI-VDSIIGDNAVIGENVRVVNLCIIGDD 74
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 13-147 1.23e-04

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 42.71  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  13 VIEGDVTIGANVTVGpftyiAG----NVTIGDDTEVMSHVVIKGHT-----TIGKENRIFPHAVIGEENQ-------DKK 76
Cdd:PRK09451 279 IIEGNVTLGNRVKIG-----AGcvlkNCVIGDDCEISPYSVVEDANlgaacTIGPFARLRPGAELAEGAHvgnfvemKKA 353

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  77 YGGEETTV----VIGDRNvIREAVQIHRGTVQ------DKATTVIGDdnllcvnahvahDVIVGNHTH------IGNNAI 140
Cdd:PRK09451 354 RLGKGSKAghltYLGDAE-IGDNVNIGAGTITcnydgaNKFKTIIGD------------DVFVGSDTQlvapvtVGKGAT 420


                 ....*..
gi 873900231 141 LGGHVTV 147
Cdd:PRK09451 421 IGAGTTV 427
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 25-177 1.35e-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: 41.42  E-value: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  25 TVGPFTYIAGNVTIGDDTEVMSHVVIKGHTTIGKENRIFPHAVIgeenqdkkyggeETTVVIGDRNVIREAVQIhrgtvq 104
Cdd:cd05636    7 TVEEGVTIKGPVWIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYI------------RGYTVLGDGCVVGNSVEV------ 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231 105 dkATTVIGDdnllcvNAHVAH-----DVIVGNHTHIGNNAIL------GGHVTV------------------GDYAGVMA 155
Cdd:cd05636   69 --KNSIIMD------GTKVPHlnyvgDSVLGENVNLGAGTITanlrfdDKPVKVrlkgervdtgrrklgaiiGDGVKTGI 140

                        170       180
                 ....*....|....*....|..
gi 873900231 156 LSAIHPFCSIGAYAYIGGCSAV 177
Cdd:cd05636  141 NVSLNPGVKIGPGSWVYPGCVV 162
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 111-194 1.98e-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: 39.90  E-value: 1.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231 111 IGDD----NLLCVnaHVAHDVIVGNHTHI--GNN-------AILGGHVTVGDYAGVMALSAIHPFCSIGAYAYIGGCSAV 177
Cdd:cd05825   12 IGEGvwiyNLAPV--TIGSDACISQGAYLctGSHdyrspafPLITAPIVIGDGAWVAAEAFVGPGVTIGEGAVVGARSVV 89

                         90
                 ....*....|....*..
gi 873900231 178 VQDVLPYVLAQGNHAAP 194
Cdd:cd05825   90 VRDLPAWTVYAGNPAVP 106
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-209 2.14e-04

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 42.06  E-value: 2.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231   1 MIHETAKIHPAAV-IEGDVTIGANVTVGPFTYIAGNVTIGDDTEV--MSHVVikgHTTIGKENRIFPHAVIGEENQDKKY 77
Cdd:PRK14357 238 MENGVTILDPNTTyIHYDVEIGMDTIIYPMTFIEGKTRIGEDCEIgpMTRIV---DCEIGNNVKIIRSECEKSVIEDDVS 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  78 GG-----EETTVVigDRNV-IREAVQIHRGTV--QDKAT--TVIGDdnllcvnAHVAHDVIVG-------------NHTH 134
Cdd:PRK14357 315 VGpfsrlREGTVL--KKSVkIGNFVEIKKSTIgeNTKAQhlTYLGD-------ATVGKNVNIGagtitcnydgkkkNPTF 385

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 873900231 135 IGNNAILGGHVtvgdyagvmalSAIHPfCSIGAYAYIGGCSAVVQDVLPYVLAQGNHAAPFGLNLVgLKRNGFEK 209
Cdd:PRK14357 386 IEDGAFIGSNS-----------SLVAP-VRIGKGALIGAGSVITEDVPPYSLALGRARQIVKEGWV-LKKRKEEE 447
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 1-35 2.81e-04

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 40.95  E-value: 2.81e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 873900231   1 MIHETAKIHPAAVIEGDVTIGANVTVGPFTYIAGN 35
Cdd:PRK13627  12 VVHPTAFVHPSAVLIGDVIVGAGVYIGPLASLRGD 46
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 2-173 3.59e-04

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 41.46  E-value: 3.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231   2 IHETAKIHPAAVIEGDVTIGANVTVGPFTYIAgNVTIGDDTEVM-SHV---VIKGHTTIGKENRIFPHAVIGEENqdkKY 77
Cdd:PRK14352 274 IGRDVVIHPGTQLLGRTTIGEDAVVGPDTTLT-DVTVGEGASVVrTHGsesEIGAGATVGPFTYLRPGTVLGEEG---KL 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  78 GG--EETTVVIGDRNVIReavqiHRGTVQDkATtvIGDD-NLLCVNAHVAHD------VIVGNHTHIGNNAILGGHVTVG 148
Cdd:PRK14352 350 GAfvETKNATIGRGTKVP-----HLTYVGD-AD--IGEHsNIGASSVFVNYDgvnkhrTTIGSHVRTGSDTMFVAPVTVG 421

                        170       180
                 ....*....|....*....|....*
gi 873900231 149 DYAGVMALSAIHPFCSIGAYAYIGG 173
Cdd:PRK14352 422 DGAYTGAGTVIREDVPPGALAVSEG 446
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 17-189 3.64e-04

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 41.39  E-value: 3.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  17 DVTIGANVTVGPFTYIAGNVTIGDDTEV--MSHV---VIKGHTTIGKENRIFPHAVIGEEnqdkkyggeettVVIGdrN- 90
Cdd:PRK14353 268 DTVIGRDVVIEPNVVFGPGVTVASGAVIhaFSHLegaHVGEGAEVGPYARLRPGAELGEG------------AKVG--Nf 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  91 VIREAVQIHRGTvqdKAT--TVIGDdnllcvnAHvahdviVGNHTHIGNNAI------LGGHVT-VGDYAGVMALSAIHP 161
Cdd:PRK14353 334 VEVKNAKLGEGA---KVNhlTYIGD-------AT------IGAGANIGAGTItcnydgFNKHRTeIGAGAFIGSNSALVA 397

                        170       180
                 ....*....|....*....|....*...
gi 873900231 162 FCSIGAYAYIGGCSAVVQDVLPYVLAQG 189
Cdd:PRK14353 398 PVTIGDGAYIASGSVITEDVPDDALALG 425
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 102-189 4.17e-04

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 40.37  E-value: 4.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231 102 TVQDKATTVIGDDNLLCVNAHVAhdvIVGNHTH---------------IGNNAILGGHVTvgdyagvmalsaIHPFCSIG 166
Cdd:PRK09527  89 TIVDDYTVTIGDNVLIAPNVTLS---VTGHPVHhelrkngemysfpitIGNNVWIGSHVV------------INPGVTIG 153

                         90       100
                 ....*....|....*....|...
gi 873900231 167 AYAYIGGCSAVVQDVLPYVLAQG 189
Cdd:PRK09527 154 DNSVIGAGSVVTKDIPPNVVAAG 176
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
2-69 5.04e-04

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 39.47  E-value: 5.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231   2 IHETAKIHPAAVIE--GDVTIGANVTVGPFTYI----------------AGNVTIGDDTEVMSHVVIKGHTTIGKenrif 63
Cdd:COG0110   30 IGDNVYIGPGVTIDdpGGITIGDNVLIGPGVTIltgnhpiddpatfplrTGPVTIGDDVWIGAGATILPGVTIGD----- 104


                 ....*.
gi 873900231  64 pHAVIG 69
Cdd:COG0110  105 -GAVVG 109
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 8-68 5.29e-04

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: 38.58  E-value: 5.29e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 873900231   8 IHPAAVIEGDVTIGANVTVG--PFTYIAGNVTIGDDTEVMSHVVIKGHTTIGKENRIFPHAVI 68
Cdd:cd03354   25 IGETAVIGDNCTIYQGVTLGgkGKGGGKRHPTIGDNVVIGAGAKILGNITIGDNVKIGANAVV 87
PLN02739 PLN02739
serine acetyltransferase
 92-224 7.16e-04

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 40.40  E-value: 7.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  92 IREAVQIHRGTVQDKAT-TVIGDDNLLCVNAHVAHDVIVGN--------HTHIGNNAILGGHVTVgdyagvmaLSAIhpf 162
Cdd:PLN02739 208 IHPAARIGKGILLDHGTgVVIGETAVIGDRVSILHGVTLGGtgketgdrHPKIGDGALLGACVTI--------LGNI--- 276

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 873900231 163 cSIGAYAYIGGCSAVVQDVLPYVLAQGNHAapfglNLVGLKRNgfEKPEIRALQKAYKELYR 224
Cdd:PLN02739 277 -SIGAGAMVAAGSLVLKDVPSHSMVAGNPA-----KLIGFVDE--QDPSLTMEYDATREFFQ 330
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 14-173 8.57e-04

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 40.35  E-value: 8.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  14 IEGDVTIGANVTVGPF------TYIAGNVTIG-----DDTEVMSHVVIKGHTT-----------IGKENRIFPHAVIGEE 71
Cdd:PRK14358 267 IEDTVTLGRDVTIEPGvllrgqTRVADGVTIGaysvvTDSVLHEGAVIKPHSVlegaevgagsdVGPFARLRPGTVLGEG 346

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  72 NQDKKYggEETTVVIGDRNViREAVQIHRGTVQDKATTVIGDDNLLC----VNAHVAHdviVGNHTHIGNNAILGGHVTV 147
Cdd:PRK14358 347 VHIGNF--VETKNARLDAGV-KAGHLAYLGDVTIGAETNVGAGTIVAnfdgVNKHQSK---VGAGVFIGSNTTLIAPRVV 420

                        170       180
                 ....*....|....*....|....*.
gi 873900231 148 GDYAGVMALSAIHPFCSIGAYAYIGG 173
Cdd:PRK14358 421 GDAAFIAAGSAVHDDVPEGAMAVARG 446
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 20-178 1.27e-03

Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in iron acquisition. It binds iron when it is complexed with pyochelin. It adopts the left-handed parallel beta-helix (LbH) structure, and contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. Acyltransferase activity has not been observed in this group.


Pssm-ID: 100055 [Multi-domain]  Cd Length: 154  Bit Score: 38.32  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  20 IGANVTVGPFTYIAGNVTIGDDTEVMSHVVIKGhttigkenrifphavigeenqdkkyggEETTVVIGDRNVIREAVQIH 99
Cdd:cd04650    3 ISPKAYVHPTSYVIGDVVIGELTSVWHYAVIRG---------------------------DNDSIYIGKYSNVQENVSIH 55

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231 100 rgtvQDKATTV-IGDDNLLCVNAhVAHDVIVGNHTHIGNNAILGGHVTVGDYAGVMALSAIHPFCSIGAYAYIGGCSAVV 178
Cdd:cd04650   56 ----TDHGYPTeIGDYVTIGHNA-VVHGAKVGNYVIVGMGAILLNGAKIGDHVIIGAGAVVTPGKEIPDYSLVLGVPAKV 130
LbH_M1P_guanylylT_C cd05824
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 1-71 1.41e-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: 36.75  E-value: 1.41e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 873900231   1 MIHETAKIHPAAVIEGDVTIGANVTVGP-----FTYIAGNVTIGDDTEVMSHVViKGHTTIGKENRIFPHAVIGEE 71
Cdd:cd05824    1 LIDPSAKIGKTAKIGPNVVIGPNVTIGDgvrlqRCVILSNSTVRDHSWVKSSIV-GWNSTVGRWTRLENVTVLGDD 75
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 18-124 1.42e-03

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 36.46  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  18 VTIGANVTVGPFTYIAGNVTIGDDtevmshvvikghttigkeNRIFPHAVIGEENQDKKYGGeettVVIGDRNVIREAVQ 97
Cdd:cd00208    1 VFIGEGVKIHPKAVIRGPVVIGDN------------------VNIGPGAVIGAATGPNEKNP----TIIGDNVEIGANAV 58

                         90       100
                 ....*....|....*....|....*..
gi 873900231  98 IHRGtvqdkatTVIGDDNLLCVNAHVA 124
Cdd:cd00208   59 IHGG-------VKIGDNAVIGAGAVVT 78
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
17-44 1.58e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.01  E-value: 1.58e-03
                          10        20
                  ....*....|....*....|....*...
gi 873900231   17 DVTIGANVTVGPFTYIAGNVTIGDDTEV 44
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVII 28
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
109-137 2.86e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 34.62  E-value: 2.86e-03
                          10        20
                  ....*....|....*....|....*....
gi 873900231  109 TVIGDDNLLCVNAHVAHDVIVGNHTHIGN 137
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 13-69 3.03e-03

eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 35.63  E-value: 3.03e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 873900231  13 VIEGDVTIGANVTVGPfTYIAGNVTIGDDTEVmSHVVIKGHTTIGKENRIFPHAVIG 69
Cdd:cd05787   18 VIGRNCKIGKNVVIDN-SYIWDDVTIEDGCTI-HHSIVADGAVIGKGCTIPPGSLIS 72
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 30-150 3.90e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 38.19  E-value: 3.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  30 TYIAGNVTIGDDTEVMSHVVIKGHTTIGKENRIFPHAVIgeenqdkkyggeeTTVVIGDRnvireavqihrgtVQDKATT 109
Cdd:PRK14355 263 TYIDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVI-------------KGCRIGDD-------------VTVKAGS 316

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 873900231 110 VIGDdnllcvnAHVAHDVIVGNHTHIGNNAILGGHVTVGDY 150
Cdd:PRK14355 317 VLED-------SVVGDDVAIGPMAHLRPGTELSAHVKIGNF 350
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 7-216 4.91e-03

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


Pssm-ID: 100052 [Multi-domain]  Cd Length: 164  Bit Score: 36.92  E-value: 4.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231   7 KIHPAAVIEGDVTIGANVTVGPFTYIAGNVTIgddtevmshvvikghttigkenrifphavigeenqdkkyGGEETTVVI 86
Cdd:cd04646    1 KIAPGAVVCQESEIRGDVTIGPGTVVHPRATI---------------------------------------IAEAGPIII 41

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  87 GDRNVIREAVQIHRGTVQDKA---TTVIGDDNLLCVNAHVaHDVIVGNHTHIGNNAILGGHVTVGDYagvmalsaihpfC 163
Cdd:cd04646   42 GENNIIEEQVTIVNKKPKDPAepkPMIIGSNNVFEVGCKC-EALKIGNNNVFESKSFVGKNVIITDG------------C 108

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 873900231 164 SIGAyayigGCSAVVQDVLP-YVLAQGNHaapfglnlvGLKRNGFEKPEIRALQ 216
Cdd:cd04646  109 IIGA-----GCKLPSSEILPeNTVIYGAD---------CLRRTQTDRPKPQTLQ 148
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 121-172 7.66e-03

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: 36.92  E-value: 7.66e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 873900231 121 AHVAHDVIVGNHTHIGNNAILGGHVTVGDyaGVMalsaIHPFCSIGAYAYIG 172
Cdd:COG1044  103 AVIDPSAKIGEGVSIGPFAVIGAGVVIGD--GVV----IGPGVVIGDGVVIG 148
PLN02357 PLN02357
serine acetyltransferase
 124-205 8.16e-03

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 37.17  E-value: 8.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231 124 AHDVIVGNHTHIGNN------AILGG--------HVTVGDYAGVMALSAIHPFCSIGAYAYIGGCSAVVQDVLPYVLAQG 189
Cdd:PLN02357 244 ATGVVIGETAVVGNNvsilhnVTLGGtgkqsgdrHPKIGDGVLIGAGTCILGNITIGEGAKIGAGSVVLKDVPPRTTAVG 323

                         90
                 ....*....|....*.
gi 873900231 190 NHAapfglNLVGLKRN 205
Cdd:PLN02357 324 NPA-----RLIGGKEN 334
PRK10502 PRK10502
putative acyl transferase; Provisional
 86-194 9.01e-03

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 36.08  E-value: 9.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  86 IGDRNVIREAVQIH---RGTVQDKATtvIGDDnllcVNAHVAHDVIVGNHTHIGNNAIL--GGH-------------VTV 147
Cdd:PRK10502  54 IGKGVVIRPSVRITypwKLTIGDYAW--IGDD----VWLYNLGEITIGAHCVISQKSYLctGSHdysdphfdlntapIVI 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 873900231 148 GDYAGVMALSAIHPFCSIGAYAYIGGCSAVVQDVLPYVLAQGNHAAP 194
Cdd:PRK10502 128 GEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVP 174
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 17-190 9.61e-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: 9.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  17 DVTIGANVTVGPFTYIA--GNVTIGDDTEVMSHVVIKGHTtigkenrifphavigeenqdkkyggeettvvigdrnvire 94
Cdd:cd04647    1 NISIGDNVYIGPGCVISagGGITIGDNVLIGPNVTIYDHN---------------------------------------- 40

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 873900231  95 avqiHRgtvqdkattvIGDDNLLCVNAHVAHDVIVGNHTHIGNNAILGGHVTVGDYagvmalsaihpfCSIGAyayiggC 174
Cdd:cd04647   41 ----HD----------IDDPERPIEQGVTSAPIVIGDDVWIGANVVILPGVTIGDG------------AVVGA------G 88

                        170
                 ....*....|....*.
gi 873900231 175 SAVVQDVLPYVLAQGN 190
Cdd:cd04647   89 SVVTKDVPPNSIVAGN 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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