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Conserved domains on  [gi|446699695|ref|WP_000777041|]
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UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase [Helicobacter pylori]

Protein Classification

UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase( domain architecture ID 11493213)

UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase catalyzes the N-acylation of UDP-3-O-(hydroxytetradecanoyl)glucosamine using 3-hydroxytetradecanoyl-ACP as the acyl donor

CATH:  3.40.1390.10|2.160.10.10
Gene Ontology:  GO:0009245|GO:0103118
PubMed:  17360522|15500694|11747907
SCOP:  4004951|4002830

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
lipid_A_lpxD TIGR01853
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD; This model describes LpxD, an ...
 5-324 7.39e-161

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: 452.13  E-value: 7.39e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695    5 ELLNAYSIETEFSNDFEVHALAELNKATPNDISYIDQARYLKLLKDSKAGAVFIRKKESSkVPKRMQALVVDNPHLAFAK 84
Cdd:TIGR01853   1 ELAERLGAELKGNGDIVITGVAPLEKAKANHITFLANPKYLKHLKSSQAGAVIVSPDDQG-LPAKCAALVVKDPYLAFAK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695   85 ASHAFKIP------FFKNPESVNEPKHFERVTIMPNVVIGEGVEIGENSLIYPGVVIADGVKIGKNCILYPRVTLYQNTI 158
Cdd:TIGR01853  80 VAELFDPPpkreagIHPTAVVDPSAKIGDGVTIGPNVVIGAGVEIGENVIIGPGVVIGDDVVIGDGSRIHPNVVIYERVQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695  159 LEDNVTIHAGSVIGGDGFGYAHTALGEHVKIEHVGIVRIQKNVEIGANTAIDRAVFGETLIKEGVKIDNLVQIGHNCVLG 238
Cdd:TIGR01853 160 LGKNVIIHSGAVIGSDGFGYAHTANGGHVKIPQIGRVIIEDDVEIGANTTIDRGAFDDTIIGEGTKIDNLVQIAHNCRIG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695  239 EHSIVVSQVGLSGSTTTGRNVVFGGQVGIGGHLHVGEFTQIGGKSAVGKDLPPNTNFaGAIPAMEIHEWHHFLAHLRTNF 318
Cdd:TIGR01853 240 ENCIIVAQVGIAGSTKIGRNVIIGGQVGVAGHLEIGDNVTIGAKSGVTKSIPPPGVY-GGIPARPNKEWLRIAAKVKRLP 318


                  ....*.
gi 446699695  319 RKQQKT 324
Cdd:TIGR01853 319 ELRKRI 324
 
Name Accession Description Interval E-value
lipid_A_lpxD TIGR01853
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD; This model describes LpxD, an ...
 5-324 7.39e-161

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: 452.13  E-value: 7.39e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695    5 ELLNAYSIETEFSNDFEVHALAELNKATPNDISYIDQARYLKLLKDSKAGAVFIRKKESSkVPKRMQALVVDNPHLAFAK 84
Cdd:TIGR01853   1 ELAERLGAELKGNGDIVITGVAPLEKAKANHITFLANPKYLKHLKSSQAGAVIVSPDDQG-LPAKCAALVVKDPYLAFAK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695   85 ASHAFKIP------FFKNPESVNEPKHFERVTIMPNVVIGEGVEIGENSLIYPGVVIADGVKIGKNCILYPRVTLYQNTI 158
Cdd:TIGR01853  80 VAELFDPPpkreagIHPTAVVDPSAKIGDGVTIGPNVVIGAGVEIGENVIIGPGVVIGDDVVIGDGSRIHPNVVIYERVQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695  159 LEDNVTIHAGSVIGGDGFGYAHTALGEHVKIEHVGIVRIQKNVEIGANTAIDRAVFGETLIKEGVKIDNLVQIGHNCVLG 238
Cdd:TIGR01853 160 LGKNVIIHSGAVIGSDGFGYAHTANGGHVKIPQIGRVIIEDDVEIGANTTIDRGAFDDTIIGEGTKIDNLVQIAHNCRIG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695  239 EHSIVVSQVGLSGSTTTGRNVVFGGQVGIGGHLHVGEFTQIGGKSAVGKDLPPNTNFaGAIPAMEIHEWHHFLAHLRTNF 318
Cdd:TIGR01853 240 ENCIIVAQVGIAGSTKIGRNVIIGGQVGVAGHLEIGDNVTIGAKSGVTKSIPPPGVY-GGIPARPNKEWLRIAAKVKRLP 318


                  ....*.
gi 446699695  319 RKQQKT 324
Cdd:TIGR01853 319 ELRKRI 324
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 1-331 1.48e-150

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 426.86  E-value: 1.48e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695   1 MKLSELLNAYSIETEFSNDFEVHALAELNKATPNDISYIDQARYLKLLKDSKAGAVFIRKKESSKVPKRMQALVVDNPHL 80
Cdd:PRK00892   3 LTLAELAELLGAELVGDGDIEITGVASLEEAGPGQISFLANPKYRKQLATTKAGAVIVSPDDAEFVPAGNALLVVKNPYL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695  81 AFAKASHAFKIPFFKNPESVNEP--------KHFERVTIMPNVVIGEGVEIGENSLIYPGVVIADGVKIGKNCILYPRVT 152
Cdd:PRK00892  83 AFARLAQLFDPPATPSPAAGIHPsavidpsaKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 153 LYQNTILEDNVTIHAGSVIGGDGFGYAhTALGEHVKIEHVGIVRIQKNVEIGANTAIDRAVFGETLIKEGVKIDNLVQIG 232
Cdd:PRK00892 163 IYHAVRIGNRVIIHSGAVIGSDGFGFA-NDRGGWVKIPQLGRVIIGDDVEIGANTTIDRGALDDTVIGEGVKIDNLVQIA 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 233 HNCVLGEHSIVVSQVGLSGSTTTGRNVVFGGQVGIGGHLHVGEFTQIGGKSAVGKDLPPNTNFAGAIPAMEIHEWHHFLA 312
Cdd:PRK00892 242 HNVVIGRHTAIAAQVGIAGSTKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEPGEYSSGIPAQPNKEWLRTAA 321

                        330
                 ....*....|....*....
gi 446699695 313 HLRTNFRKQQKTSLLQKAK 331
Cdd:PRK00892 322 RLRRLDELRKRLKALEKKV 340
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 1-315 1.48e-139

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: 398.62  E-value: 1.48e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695   1 MKLSELLNAYSIETEFSNDFEVHALAELNKATPNDISYIDQARYLKLLKDSKAGAVFIRKKESSKVPKRmQALVVDNPHL 80
Cdd:COG1044    2 FTLAELAELLGGELVGDGDLEITGVAPLEEAGPGDLSFLANPKYAKQLATTKASAVIVPPDFAAALPGL-ALIVVDNPYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695  81 AFAKASHAFKiPFFKNPESVnEPKHF--------ERVTIMPNVVIGEGVEIGENSLIYPGVVIADGVKIGKNCILYPRVT 152
Cdd:COG1044   81 AFAKLLQLFY-PPPAPAPGI-HPSAVidpsakigEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 153 LYQNTILEDNVTIHAGSVIGGDGFGYAHTALGEHVKIEHVGIVRIQKNVEIGANTAIDRAVFGETLIKEGVKIDNLVQIG 232
Cdd:COG1044  159 IYERCVIGDRVIIHSGAVIGADGFGFAPDEDGGWVKIPQLGRVVIGDDVEIGANTTIDRGALGDTVIGDGTKIDNLVQIA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 233 HNCVLGEHSIVVSQVGLSGSTTTGRNVVFGGQVGIGGHLHVGEFTQIGGKSAVGKDLPPNTNFAGaIPAMEIHEWHHFLA 312
Cdd:COG1044  239 HNVRIGEHTAIAAQVGIAGSTKIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSG-SPAQPHREWLRNAA 317


                 ...
gi 446699695 313 HLR 315
Cdd:COG1044  318 ALR 320
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 107-308 1.21e-106

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: 310.11  E-value: 1.21e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 107 ERVTIMPNVVIGEGVEIGENSLIYPGVVIADGVKIGKNCILYPRVTLYQNTILEDNVTIHAGSVIGGDGFGYAHTAlGEH 186
Cdd:cd03352    6 ENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIGSDGFGFAPDG-GGW 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 187 VKIEHVGIVRIQKNVEIGANTAIDRAVFGETLIKEGVKIDNLVQIGHNCVLGEHSIVVSQVGLSGSTTTGRNVVFGGQVG 266
Cdd:cd03352   85 VKIPQLGGVIIGDDVEIGANTTIDRGALGDTVIGDGTKIDNLVQIAHNVRIGENCLIAAQVGIAGSTTIGDNVIIGGQVG 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446699695 267 IGGHLHVGEFTQIGGKSAVGKDLPPNTNFAGaIPAMEIHEWH 308
Cdd:cd03352  165 IAGHLTIGDGVVIGAGSGVTSIVPPGEYVSG-TPAQPHREWL 205
LpxD pfam04613
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase, LpxD; UDP-3-O-[3-hydroxymyristoyl] ...
 20-87 3.38e-21

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase, LpxD; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase (EC 2.3.1.-) catalyzes an early step in lipid A biosynthesis: UDP-3-O-(3-hydroxytetradecanoyl)glucosamine + (R)-3-hydroxytetradecanoyl- [acyl carrier protein] -> UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine + [acyl carrier protein]. Members of this family also contain a hexapeptide repeat (pfam00132). This family constitutes the non-repeating region of LPXD proteins.


Pssm-ID: 461366 [Multi-domain]  Cd Length: 69  Bit Score: 85.63  E-value: 3.38e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446699695   20 FEVHALAELNKATPNDISYIDQARYLKLLKDSKAGAVFIRKKESSKVPKRMQALVVDNPHLAFAKASH 87
Cdd:pfam04613   1 LEITGVAPLEEAGPGDLSFLANPKYAKYLATTKASAVIVPPDFAPQAPATATLLVVDNPYLAFAKLLQ 68
 
Name Accession Description Interval E-value
lipid_A_lpxD TIGR01853
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD; This model describes LpxD, an ...
 5-324 7.39e-161

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: 452.13  E-value: 7.39e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695    5 ELLNAYSIETEFSNDFEVHALAELNKATPNDISYIDQARYLKLLKDSKAGAVFIRKKESSkVPKRMQALVVDNPHLAFAK 84
Cdd:TIGR01853   1 ELAERLGAELKGNGDIVITGVAPLEKAKANHITFLANPKYLKHLKSSQAGAVIVSPDDQG-LPAKCAALVVKDPYLAFAK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695   85 ASHAFKIP------FFKNPESVNEPKHFERVTIMPNVVIGEGVEIGENSLIYPGVVIADGVKIGKNCILYPRVTLYQNTI 158
Cdd:TIGR01853  80 VAELFDPPpkreagIHPTAVVDPSAKIGDGVTIGPNVVIGAGVEIGENVIIGPGVVIGDDVVIGDGSRIHPNVVIYERVQ 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695  159 LEDNVTIHAGSVIGGDGFGYAHTALGEHVKIEHVGIVRIQKNVEIGANTAIDRAVFGETLIKEGVKIDNLVQIGHNCVLG 238
Cdd:TIGR01853 160 LGKNVIIHSGAVIGSDGFGYAHTANGGHVKIPQIGRVIIEDDVEIGANTTIDRGAFDDTIIGEGTKIDNLVQIAHNCRIG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695  239 EHSIVVSQVGLSGSTTTGRNVVFGGQVGIGGHLHVGEFTQIGGKSAVGKDLPPNTNFaGAIPAMEIHEWHHFLAHLRTNF 318
Cdd:TIGR01853 240 ENCIIVAQVGIAGSTKIGRNVIIGGQVGVAGHLEIGDNVTIGAKSGVTKSIPPPGVY-GGIPARPNKEWLRIAAKVKRLP 318


                  ....*.
gi 446699695  319 RKQQKT 324
Cdd:TIGR01853 319 ELRKRI 324
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 1-331 1.48e-150

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 426.86  E-value: 1.48e-150
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695   1 MKLSELLNAYSIETEFSNDFEVHALAELNKATPNDISYIDQARYLKLLKDSKAGAVFIRKKESSKVPKRMQALVVDNPHL 80
Cdd:PRK00892   3 LTLAELAELLGAELVGDGDIEITGVASLEEAGPGQISFLANPKYRKQLATTKAGAVIVSPDDAEFVPAGNALLVVKNPYL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695  81 AFAKASHAFKIPFFKNPESVNEP--------KHFERVTIMPNVVIGEGVEIGENSLIYPGVVIADGVKIGKNCILYPRVT 152
Cdd:PRK00892  83 AFARLAQLFDPPATPSPAAGIHPsavidpsaKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVT 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 153 LYQNTILEDNVTIHAGSVIGGDGFGYAhTALGEHVKIEHVGIVRIQKNVEIGANTAIDRAVFGETLIKEGVKIDNLVQIG 232
Cdd:PRK00892 163 IYHAVRIGNRVIIHSGAVIGSDGFGFA-NDRGGWVKIPQLGRVIIGDDVEIGANTTIDRGALDDTVIGEGVKIDNLVQIA 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 233 HNCVLGEHSIVVSQVGLSGSTTTGRNVVFGGQVGIGGHLHVGEFTQIGGKSAVGKDLPPNTNFAGAIPAMEIHEWHHFLA 312
Cdd:PRK00892 242 HNVVIGRHTAIAAQVGIAGSTKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEPGEYSSGIPAQPNKEWLRTAA 321

                        330
                 ....*....|....*....
gi 446699695 313 HLRTNFRKQQKTSLLQKAK 331
Cdd:PRK00892 322 RLRRLDELRKRLKALEKKV 340
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 1-315 1.48e-139

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: 398.62  E-value: 1.48e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695   1 MKLSELLNAYSIETEFSNDFEVHALAELNKATPNDISYIDQARYLKLLKDSKAGAVFIRKKESSKVPKRmQALVVDNPHL 80
Cdd:COG1044    2 FTLAELAELLGGELVGDGDLEITGVAPLEEAGPGDLSFLANPKYAKQLATTKASAVIVPPDFAAALPGL-ALIVVDNPYL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695  81 AFAKASHAFKiPFFKNPESVnEPKHF--------ERVTIMPNVVIGEGVEIGENSLIYPGVVIADGVKIGKNCILYPRVT 152
Cdd:COG1044   81 AFAKLLQLFY-PPPAPAPGI-HPSAVidpsakigEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 153 LYQNTILEDNVTIHAGSVIGGDGFGYAHTALGEHVKIEHVGIVRIQKNVEIGANTAIDRAVFGETLIKEGVKIDNLVQIG 232
Cdd:COG1044  159 IYERCVIGDRVIIHSGAVIGADGFGFAPDEDGGWVKIPQLGRVVIGDDVEIGANTTIDRGALGDTVIGDGTKIDNLVQIA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 233 HNCVLGEHSIVVSQVGLSGSTTTGRNVVFGGQVGIGGHLHVGEFTQIGGKSAVGKDLPPNTNFAGaIPAMEIHEWHHFLA 312
Cdd:COG1044  239 HNVRIGEHTAIAAQVGIAGSTKIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSG-SPAQPHREWLRNAA 317


                 ...
gi 446699695 313 HLR 315
Cdd:COG1044  318 ALR 320
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 107-308 1.21e-106

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: 310.11  E-value: 1.21e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 107 ERVTIMPNVVIGEGVEIGENSLIYPGVVIADGVKIGKNCILYPRVTLYQNTILEDNVTIHAGSVIGGDGFGYAHTAlGEH 186
Cdd:cd03352    6 ENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIGSDGFGFAPDG-GGW 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 187 VKIEHVGIVRIQKNVEIGANTAIDRAVFGETLIKEGVKIDNLVQIGHNCVLGEHSIVVSQVGLSGSTTTGRNVVFGGQVG 266
Cdd:cd03352   85 VKIPQLGGVIIGDDVEIGANTTIDRGALGDTVIGDGTKIDNLVQIAHNVRIGENCLIAAQVGIAGSTTIGDNVIIGGQVG 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446699695 267 IGGHLHVGEFTQIGGKSAVGKDLPPNTNFAGaIPAMEIHEWH 308
Cdd:cd03352  165 IAGHLTIGDGVVIGAGSGVTSIVPPGEYVSG-TPAQPHREWL 205
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 113-291 1.36e-25

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: 102.79  E-value: 1.36e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 113 PNVVIGEGVEIGensliyPGVVIADGVKIGKNCILYPRVTLYQNTILEDNVTIHAGSVIGGDG--FGYAhtalGEHVKie 190
Cdd:COG1043   12 PGAKLGENVEIG------PFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASIGEEPqdLKYK----GEPTR-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 191 hvgivriqknVEIGANtaidravfgeTLIKEGVKI---------------DNL----VQIGHNCVLGEHSIVVSQVGLSG 251
Cdd:COG1043   80 ----------LEIGDN----------NTIREFVTIhrgtvqgggvtrigdDNLlmayVHVAHDCVVGNNVILANNATLAG 139

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 446699695 252 STTTGRNVVFGGQVGIGGHLHVGEFTQIGGKSAVGKDLPP 291
Cdd:COG1043  140 HVEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDVPP 179
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 111-291 1.14e-24

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: 100.20  E-value: 1.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 111 IMPNVVIGEGVEIGensliyPGVVIADGVKIGKNCILYPRVTLYQNTILEDNVTIHAGSVIGGD--GFGYAhtalGEHVK 188
Cdd:cd03351    8 VDPGAKIGENVEIG------PFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIGEApqDLKYK----GEPTR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 189 iehvgivriqknVEIGANTaidravfgetLIKEGVKI---------------DNL----VQIGHNCVLGEHSIVVSQVGL 249
Cdd:cd03351   78 ------------LEIGDNN----------TIREFVTIhrgtaqgggvtrignNNLlmayVHVAHDCVIGNNVILANNATL 135

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446699695 250 SGSTTTGRNVVFGGQVGIGGHLHVGEFTQIGGKSAVGKDLPP 291
Cdd:cd03351  136 AGHVEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPP 177
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 111-291 6.81e-24

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: 98.49  E-value: 6.81e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695  111 IMPNVVIGEGVEIGENSLIYPGVVIADGVKIGKNCILYPRVTLYQNTILEDNVTIHAGSVIGGDGFGYAHTalGEhvkie 190
Cdd:TIGR01852   1 IHPTAIIEPGAEIGENVEIGPFCIVGPGVKIGDGVELKSHVVILGHTTIGEGTRIFPGAVIGGVPQDLKYK--GE----- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695  191 hvgivriQKNVEIGANTAIDRAVFGETLIKEGVKI-----DNL----VQIGHNCVLGEHSIVVSQVGLSGSTTTGRNVVF 261
Cdd:TIGR01852  74 -------KTRLIIGDNNTIREFVTINRGTASGGGVtrignNNLlmaySHIAHDCVVGNHVILANNATLAGHVEVGDYAII 146

                         170       180       190
                  ....*....|....*....|....*....|
gi 446699695  262 GGQVGIGGHLHVGEFTQIGGKSAVGKDLPP 291
Cdd:TIGR01852 147 GGLVAVHQFVRIGRYAMIGGLSAVSKDVPP 176
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
111-291 3.56e-23

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 96.32  E-value: 3.56e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 111 IMPNVVIGEGVEIGENSLIYPGVVIADGVKIGKNCILYPRVTLYQNTILEDNVTIHAGSVIGGD--GFGYAhtalGEHVK 188
Cdd:PRK05289   5 IHPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASIGEDpqDLKYK----GEPTR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 189 iehvgivriqknVEIGANtaidravfgeTLIKEGVKI---------------DNL----VQIGHNCVLGEHSIVVSQVGL 249
Cdd:PRK05289  81 ------------LVIGDN----------NTIREFVTInrgtvqgggvtrigdNNLlmayVHVAHDCVVGNHVILANNATL 138

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446699695 250 SGSTTTGRNVVFGGQVGIGGHLHVGEFTQIGGKSAVGKDLPP 291
Cdd:PRK05289 139 AGHVEVGDYAIIGGLTAVHQFVRIGAHAMVGGMSGVSQDVPP 180
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 111-291 3.68e-22

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 93.55  E-value: 3.68e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 111 IMPNVVIGEGVEIGENSLIYPGVVIADGVKIGKNCILYPRVTLYQNTILEDNVTIHAGSVIGGD--GFGYAhtalGEHVK 188
Cdd:PRK12461   2 IHPTAVIDPSAKLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGDEpqDFTYK----GEESR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 189 IEhvgivrIQKNVEIGANTAIDRAVFGETLIKEGVkiDNL----VQIGHNCVLGEHSIVVSQVGLSGSTTTGRNVVFGGQ 264
Cdd:PRK12461  78 LE------IGDRNVIREGVTIHRGTKGGGVTRIGN--DNLlmaySHVAHDCQIGNNVILVNGALLAGHVTVGDRAIISGN 149

                        170       180
                 ....*....|....*....|....*..
gi 446699695 265 VGIGGHLHVGEFTQIGGKSAVGKDLPP 291
Cdd:PRK12461 150 CLVHQFCRIGALAMMAGGSRISKDVPP 176
LpxD pfam04613
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase, LpxD; UDP-3-O-[3-hydroxymyristoyl] ...
 20-87 3.38e-21

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase, LpxD; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase (EC 2.3.1.-) catalyzes an early step in lipid A biosynthesis: UDP-3-O-(3-hydroxytetradecanoyl)glucosamine + (R)-3-hydroxytetradecanoyl- [acyl carrier protein] -> UDP-2,3-bis(3-hydroxytetradecanoyl)glucosamine + [acyl carrier protein]. Members of this family also contain a hexapeptide repeat (pfam00132). This family constitutes the non-repeating region of LPXD proteins.


Pssm-ID: 461366 [Multi-domain]  Cd Length: 69  Bit Score: 85.63  E-value: 3.38e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446699695   20 FEVHALAELNKATPNDISYIDQARYLKLLKDSKAGAVFIRKKESSKVPKRMQALVVDNPHLAFAKASH 87
Cdd:pfam04613   1 LEITGVAPLEEAGPGDLSFLANPKYAKYLATTKASAVIVPPDFAPQAPATATLLVVDNPYLAFAKLLQ 68
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 117-293 5.86e-13

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 69.39  E-value: 5.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 117 IGEGVEIGENSLIYPGVVIADGVKIGKNCILYPRVTLyQNTILEDNVTIHAGSVIGGDGFGyAHTALG--EHVKIEHVgi 194
Cdd:PRK14355 265 IDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVI-KGCRIGDDVTVKAGSVLEDSVVG-DDVAIGpmAHLRPGTE-- 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 195 vrIQKNVEIGANTAIDRAVFGetlikEGVKIDNLV-----QIGHNCVLGEHSIVVSQVGLSG-STTTGRNVVFGGQVGIG 268
Cdd:PRK14355 341 --LSAHVKIGNFVETKKIVMG-----EGSKASHLTylgdaTIGRNVNIGCGTITCNYDGVKKhRTVIEDDVFVGSDVQFV 413

                        170       180
                 ....*....|....*....|....*
gi 446699695 269 GHLHVGEFTQIGGKSAVGKDLPPNT 293
Cdd:PRK14355 414 APVTVGRNSLIAAGTTVTKDVPPDS 438
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 111-247 8.15e-13

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: 66.36  E-value: 8.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695  111 IMPNVVIGEGVEIGENSLIYPGVVIADGVKIGKNCILYPRVTLYQNTILEDNVTIHAGSVIGGDgfgyahtalgehvkie 190
Cdd:TIGR03570  90 IHPSAIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGG---------------- 153

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446699695  191 hvgiVRIQKNVEIGANTAIdravfgetlikegvkIDNlVQIGHNCVLGEHSIVVSQV 247
Cdd:TIGR03570 154 ----VVIGEGVFIGAGATI---------------IQG-VTIGAGAIVGAGAVVTKDI 190
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 108-207 3.28e-12

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: 64.36  E-value: 3.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 108 RVTIM-P-NVVIGEGVEIGENSLIYPGVVIADGVKIGKNCILYPRVTLyQNTILEDNVTIHAGSVI----GGDG--FG-Y 178
Cdd:cd03353    1 GVTLIdPeTTYIDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVI-KDSTIGDGVVIKASSVIegavIGNGatVGpF 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446699695 179 AH----TALGEHVkieHVG-IVRIqKNVEIGANT 207
Cdd:cd03353   80 AHlrpgTVLGEGV---HIGnFVEI-KKSTIGEGS 109
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 113-247 9.55e-12

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: 63.27  E-value: 9.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 113 PNVVIGEGVEIGENSLIYPGVVIADGVKIGKNCILYPRVTLYQNTILEDNVTIHAGSVIGGDgfgyahtalgehvkiehv 192
Cdd:cd03360   89 PSAVVSPSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGG------------------ 150

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446699695 193 giVRIQKNVEIGANTAIdravfgetlikegvkIDNlVQIGHNCVLGEHSIVVSQV 247
Cdd:cd03360  151 --VTIGEGAFIGAGATI---------------IQG-VTIGAGAIIGAGAVVTKDV 187
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
120-243 4.38e-11

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 59.88  E-value: 4.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 120 GVEIGENSLIYPGVVIADG-VKIGKNCILYPRVTLY--QNTILEDNVTIHAGSVIGGDGfgyaHTALGEHVKIEHVGIVR 196
Cdd:COG0110    8 GARIGDGVVIGPGVRIYGGnITIGDNVYIGPGVTIDdpGGITIGDNVLIGPGVTILTGN----HPIDDPATFPLRTGPVT 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446699695 197 IQKNVEIGANtaidravfgeTLIKEGVKidnlvqIGHNCVLGEHSIV 243
Cdd:COG0110   84 IGDDVWIGAG----------ATILPGVT------IGDGAVVGAGSVV 114
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 100-292 4.87e-11

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 63.31  E-value: 4.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 100 VNEpKHFER-VTIM-P-NVVIGEGVEIGENSLIYPGVVIADGVKIGKNCILYPRVTLyQNTILEDNVTIHAgSVIggdgf 176
Cdd:PRK14354 243 INE-KHMVNgVTIIdPeSTYIDADVEIGSDTVIEPGVVIKGNTVIGEDCVIGPGSRI-VDSTIGDGVTITN-SVI----- 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 177 gyAHTALGEHVKIEHVGIVR----IQKNVEIGANTAIDRAVFGetlikEGVKIDNL-----VQIGHNCVLGEHSIVVSQV 247
Cdd:PRK14354 315 --EESKVGDNVTVGPFAHLRpgsvIGEEVKIGNFVEIKKSTIG-----EGTKVSHLtyigdAEVGENVNIGCGTITVNYD 387

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446699695 248 GLSGSTTT-GRNVVFGGQVGIGGHLHVGEFTQIGGKSAVGKDLPPN 292
Cdd:PRK14354 388 GKNKFKTIiGDNAFIGCNSNLVAPVTVGDNAYIAAGSTITKDVPED 433
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 109-207 5.97e-10

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: 60.04  E-value: 5.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 109 VTIM-P-NVVIGEGVEIGENSLIYPGV------VIADGVKIGKNCILyprvtlyQNTILEDNVTIHA----GSVIGGD-- 174
Cdd:COG1207  253 VTIIdPaTTYIDGDVEIGRDVVIDPNVilegktVIGEGVVIGPNCTL-------KDSTIGDGVVIKYsvieDAVVGAGat 325

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446699695 175 -GfGYAH----TALGEHVKI-EHVGIvriqKNVEIGANT 207
Cdd:COG1207  326 vG-PFARlrpgTVLGEGVKIgNFVEV----KNSTIGEGS 359
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 109-171 4.68e-09

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: 55.57  E-value: 4.68e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446699695 109 VTIMPNVVIGEGVEIGENSLIYPGVVIADGVKIGKNCILYPRVTLYQNTILEDNVTIHAGSVI 171
Cdd:cd03360  103 CVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEGAFIGAGATI 165
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 109-171 2.19e-08

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: 51.73  E-value: 2.19e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446699695 109 VTIMPNVVIGEGVEIGENSLIYPGVVIADGVKIGKNCI----LYPRVT-----LYQNTILEDNVTIHAGSVI 171
Cdd:cd03358   11 VFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVftndLYPRSKiyrkwELKGTTVKRGASIGANATI 82
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 109-213 6.67e-08

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: 49.75  E-value: 6.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 109 VTIMPNVVIGEGVEIGEnsliYPGVVIADGVKIGKNCILYPRVTLYQNT--------ILEDNVTIHAGSVIGGDgfgyah 180
Cdd:cd03354    3 IDIHPGAKIGPGLFIDH----GTGIVIGETAVIGDNCTIYQGVTLGGKGkgggkrhpTIGDNVVIGAGAKILGN------ 72

                         90       100       110
                 ....*....|....*....|....*....|...
gi 446699695 181 talgehvkiehvgiVRIQKNVEIGANTAIDRAV 213
Cdd:cd03354   73 --------------ITIGDNVKIGANAVVTKDV 91
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 116-205 2.34e-07

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: 47.62  E-value: 2.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 116 VIGEGVEIGENSLIYPGVviadgvkIGKNCILYPRVTLyQNTILEDNVTIHAGSVIggdgfgyAHTALGEHVKIE----H 191
Cdd:cd03356    1 LIGESTVIGENAIIKNSV-------IGDNVRIGDGVTI-TNSILMDNVTIGANSVI-------VDSIIGDNAVIGenvrV 65

                         90
                 ....*....|....
gi 446699695 192 VGIVRIQKNVEIGA 205
Cdd:cd03356   66 VNLCIIGDDVVVED 79
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 107-172 2.71e-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: 47.63  E-value: 2.71e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446699695 107 ERVTIMPNVVIGEGVEIGENSLIYPGVVI--------ADGVKIGKNCILYPRVTLYQNTILEDNVTIHAGSVIG 172
Cdd:cd00208    5 EGVKIHPKAVIRGPVVIGDNVNIGPGAVIgaatgpneKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 108-167 5.77e-07

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: 46.47  E-value: 5.77e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446699695 108 RVTIMPNVVIGEGVEIgENSLIYPGVVIADGVKI-----GKNCILYPRVTLYQNTILEDNVTIHA 167
Cdd:cd03356   16 NSVIGDNVRIGDGVTI-TNSILMDNVTIGANSVIvdsiiGDNAVIGENVRVVNLCIIGDDVVVED 79
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 107-243 7.19e-07

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 48.48  E-value: 7.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 107 ERVTIMPN-VVIGEgVEIGENSLIYPGVVI-ADG--VKIGKncilyprvtlyqNTILEDNVTIHAGSviggdgfGYAhTA 182
Cdd:COG0663   15 PSAFVAPTaVVIGD-VTIGEDVSVWPGAVLrGDVgpIRIGE------------GSNIQDGVVLHVDP-------GYP-LT 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446699695 183 LGEHVKIEHVGIV---RIQKNVEIGANTAI-DRAVfgetlikegvkidnlvqIGHNCVLGEHSIV 243
Cdd:COG0663   74 IGDDVTIGHGAILhgcTIGDNVLIGMGAIVlDGAV-----------------IGDGSIVGAGALV 121
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 109-262 1.01e-06

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 50.15  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 109 VTIM-PNVV-IGEGVEIGENSLIYPGVVIADGVKIGKNCILYPrVTLYQNTILEDNVTIHAGSVIGGdgfgyahtalgeh 186
Cdd:PRK14357 242 VTILdPNTTyIHYDVEIGMDTIIYPMTFIEGKTRIGEDCEIGP-MTRIVDCEIGNNVKIIRSECEKS------------- 307

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446699695 187 vkiehvgivRIQKNVEIGANTAIDRAvfgeTLIKEGVKIDNLVQIgHNCVLGEHSiVVSQVGLSGSTTTGRNVVFG 262
Cdd:PRK14357 308 ---------VIEDDVSVGPFSRLREG----TVLKKSVKIGNFVEI-KKSTIGENT-KAQHLTYLGDATVGKNVNIG 368
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 107-172 1.37e-06

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: 46.30  E-value: 1.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 107 ERVTIMPNVVI--GEGVEIGENSLIYPGVVIADG-------------------VKIGKNCILYPRVtlyqnTILeDNVTI 165
Cdd:cd04647    6 DNVYIGPGCVIsaGGGITIGDNVLIGPNVTIYDHnhdiddperpieqgvtsapIVIGDDVWIGANV-----VIL-PGVTI 79


                 ....*..
gi 446699695 166 HAGSVIG 172
Cdd:cd04647   80 GDGAVVG 86
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 107-169 1.44e-06

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


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 47.41  E-value: 1.44e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446699695 107 ERVTIMPNVVIgEGVEIGENSLIYPGVVIADGVKIGKNCILYPRVTLYQNTILEDNvTIHAGS 169
Cdd:cd04645   65 DNVTVGHGAVL-HGCTIGDNCLIGMGAIILDGAVIGKGSIVAAGSLVPPGKVIPPG-SLVAGS 125
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 125-225 2.91e-06

Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Glucose-1-phosphate adenylyltransferase is also known as ADP-glucose synthase or ADP-glucose pyrophosphorylase. It catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for regulation of storage polysaccharide accumulation in plants and bacteria. The enzyme is a homotetramer, with each subunit containing an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain with at 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The LbH domain is involved in cooperative allosteric regulation and oligomerization.


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 45.15  E-value: 2.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 125 ENSLIYPGVVIADGvKIgKNCILYPRVTLYQNTILEDNVtIHAGSVIGgdgfgyahtalgEHVKIEHVGI---VRIQKNV 201
Cdd:cd04651   11 KNSLVSEGCIISGG-TV-ENSVLFRGVRVGSGSVVEDSV-IMPNVGIG------------RNAVIRRAIIdknVVIPDGV 75

                         90       100
                 ....*....|....*....|....*....
gi 446699695 202 EIGANTAIDRAVF-----GETLIKEGVKI 225
Cdd:cd04651   76 VIGGDPEEDRARFyvtedGIVVVGKGMVI 104
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 109-206 3.25e-06

Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440667 [Multi-domain]  Cd Length: 174  Bit Score: 46.62  E-value: 3.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 109 VTIMPNVVIGEGVEIGENSliypGVVIADGVKIGKNCILYPRVTL---YQNT-----ILEDNVTIHAGSVIGGDgfgyah 180
Cdd:COG1045   66 IDIHPGATIGRGFFIDHGT----GVVIGETAVIGDNVTIYQGVTLggtGKEKgkrhpTIGDNVVIGAGAKILGP------ 135

                         90       100
                 ....*....|....*....|....*.
gi 446699695 181 talgehvkiehvgiVRIQKNVEIGAN 206
Cdd:COG1045  136 --------------ITIGDNAKIGAN 147
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 114-203 3.40e-06

Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Glucose-1-phosphate adenylyltransferase is also known as ADP-glucose synthase or ADP-glucose pyrophosphorylase. It catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for regulation of storage polysaccharide accumulation in plants and bacteria. The enzyme is a homotetramer, with each subunit containing an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain with at 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The LbH domain is involved in cooperative allosteric regulation and oligomerization.


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 45.15  E-value: 3.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 114 NVVIGEGVEIGENSLIyPGVVIADGVKIGKNCILyprvtlyQNTILEDNVTIHAGSVIGGDGfgyAHTALGEHVKIEhvG 193
Cdd:cd04651   28 NSVLFRGVRVGSGSVV-EDSVIMPNVGIGRNAVI-------RRAIIDKNVVIPDGVVIGGDP---EEDRARFYVTED--G 94

                         90
                 ....*....|
gi 446699695 194 IVRIQKNVEI 203
Cdd:cd04651   95 IVVVGKGMVI 104
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 183-304 5.00e-06

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: 45.18  E-value: 5.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 183 LGEHVKI-EHVgivRIQKNVEIGANTAIDRAVFgetlIKEGVKIDNLVQIGHNCVLGE----HSIVVSQVGLSGsTTTGR 257
Cdd:cd03358    1 IGDNCIIgTNV---FIENDVKIGDNVKIQSNVS----IYEGVTIEDDVFIGPNVVFTNdlypRSKIYRKWELKG-TTVKR 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 446699695 258 NVVFGGQVGIGGHLHVGEFTQIGGKSAVGKDLPPNTNFAGaIPAMEI 304
Cdd:cd03358   73 GASIGANATILPGVTIGEYALVGAGAVVTKDVPPYALVVG-NPARII 118
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 195-304 7.82e-06

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: 44.37  E-value: 7.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 195 VRIQKNVEIGANTAIDRavfgetliKEGVKIDNLVQIGHNCVL--GEHSI-----VVSQVGLSGSTTTGRNVVFGGQVGI 267
Cdd:cd04647    2 ISIGDNVYIGPGCVISA--------GGGITIGDNVLIGPNVTIydHNHDIddperPIEQGVTSAPIVIGDDVWIGANVVI 73

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 446699695 268 GGHLHVGEFTQIGGKSAVGKDLPPNTNFAGaIPAMEI 304
Cdd:cd04647   74 LPGVTIGDGAVVGAGSVVTKDVPPNSIVAG-NPAKVI 109
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 109-146 9.67e-06

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: 45.56  E-value: 9.67e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 446699695  109 VTIMPNVVIGEGVEIGENSLIYPGVVIADGVKIGKNCI 146
Cdd:TIGR03570 142 VHIAPGVTLSGGVVIGEGVFIGAGATIIQGVTIGAGAI 179
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 111-243 9.83e-06

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


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 44.71  E-value: 9.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 111 IMPN-VVIGEgVEIGENSLIYPGVVI-ADG--VKIGKncilyprvtlyqNTILEDNVTIHAgsvigGDGFGyahTALGEH 186
Cdd:cd04645    8 IAPNaTVIGD-VTLGEGSSVWFGAVLrGDVnpIRIGE------------RTNIQDGSVLHV-----DPGYP---TIIGDN 66

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446699695 187 VKIEHVGIV---RIQKNVEIGANTAI-DRAVfgetlikegvkidnlvqIGHNCVLGEHSIV 243
Cdd:cd04645   67 VTVGHGAVLhgcTIGDNCLIGMGAIIlDGAV-----------------IGKGSIVAAGSLV 110
lacA PRK09527
galactoside O-acetyltransferase; Reviewed
 183-306 1.17e-05

galactoside O-acetyltransferase; Reviewed


Pssm-ID: 181930 [Multi-domain]  Cd Length: 203  Bit Score: 45.38  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 183 LGEHVKIEHVGIVRIQKNVEIGANTaidRAVFGETLIKE-GVKIDNLVQIGHNCVLG------EHSIVVSQVGLSGSTTT 255
Cdd:PRK09527  58 VGENAWVEPPVYFSYGSNIHIGRNF---YANFNLTIVDDyTVTIGDNVLIAPNVTLSvtghpvHHELRKNGEMYSFPITI 134

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446699695 256 GRNVVFGGQVGIGGHLHVGEFTQIGGKSAVGKDLPPNTNFAGaIPAMEIHE 306
Cdd:PRK09527 135 GNNVWIGSHVVINPGVTIGDNSVIGAGSVVTKDIPPNVVAAG-VPCRVIRE 184
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 107-207 1.25e-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: 45.10  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 107 ERVTIMPNVVIgEGVEIGENSLIYPGVVIaDGVKIGKNCILYPRVTLYQNTILEDNVtiHAG-------SVIggdgfgya 179
Cdd:cd03353   38 EDCVIGPNCVI-KDSTIGDGVVIKASSVI-EGAVIGNGATVGPFAHLRPGTVLGEGV--HIGnfveikkSTI-------- 105

                         90       100       110
                 ....*....|....*....|....*....|.
gi 446699695 180 htalGEHVKIEH---VGIVRIQKNVEIGANT 207
Cdd:cd03353  106 ----GEGSKANHlsyLGDAEIGEGVNIGAGT 132
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 115-189 1.78e-05

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 42.24  E-value: 1.78e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446699695 115 VVIGEGVEIGENSLIYPGVVIADGVKIGKNCIL--YPRVTLYQNTILEDNVTIHAGSVIGGdgfgyaHTALGEHVKI 189
Cdd:cd00208    1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIgaATGPNEKNPTIIGDNVEIGANAVIHG------GVKIGDNAVI 71
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 117-247 1.98e-05

WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of Xanthomonas campestris WcxM and proteins with similarity to the WcxM N-terminal domain. WcxM is thought to be bifunctional, catalyzing both the isomerization and transacetylation reactions of keto-hexoses. It contains an N-terminal LbH domain responsible for the transacetylation function and a C-terminal isomerase domain. The LbH domain contains imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), typical of enzymes with acyltransferase activity.


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 43.26  E-value: 1.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 117 IGEGVEIGENSLIYPGVVIADGVKIGKNCILYPRVTlyqntiLEDNVTIHAGSVIGGDGFGYAhtalGEHVKIEHVGIVr 196
Cdd:cd03358    1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVT------IEDDVFIGPNVVFTNDLYPRS----KIYRKWELKGTT- 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446699695 197 IQKNVEIGANTAIdraVFGetlikegvkidnlVQIGHNCVLGEHSIVVSQV 247
Cdd:cd03358   70 VKRGASIGANATI---LPG-------------VTIGEYALVGAGAVVTKDV 104
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 113-203 2.30e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 45.59  E-value: 2.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 113 PNVVIGEGVEIgENSliypgvVIADGVKIGKNCILYprvtlyqNTILEDNVTIHAGSVIGGDgfgYAHTALGEHVKIEhv 192
Cdd:PRK00844 336 PNVVVESGAEV-EDS------VLMDGVRIGRGAVVR-------RAILDKNVVVPPGATIGVD---LEEDRRRFTVSEG-- 396

                         90
                 ....*....|.
gi 446699695 193 GIVRIQKNVEI 203
Cdd:PRK00844 397 GIVVVPKGQRV 407
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 111-172 2.42e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 45.63  E-value: 2.42e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446699695 111 IMPNVVIGEGVEIgENSLIYPGVVIADGVKIG--KNCIlyprvtlyqnTILEDNVTIHAGSVIG 172
Cdd:PRK05293 328 IMPGAKIGENVVI-ERAIIGENAVIGDGVIIGggKEVI----------TVIGENEVIGVGTVIG 380
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 114-209 3.02e-05

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: 42.44  E-value: 3.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 114 NVVIGEGVEIGENSLIYPGvviaDGVKIGKNCILYPRVTLYQNtiledNVTIHAGSVIGGDGFGYAHTALGEHVKIehvG 193
Cdd:cd04647    1 NISIGDNVYIGPGCVISAG----GGITIGDNVLIGPNVTIYDH-----NHDIDDPERPIEQGVTSAPIVIGDDVWI---G 68

                         90
                 ....*....|....*..
gi 446699695 194 I-VRIQKNVEIGANTAI 209
Cdd:cd04647   69 AnVVILPGVTIGDGAVV 85
PLN02694 PLN02694
serine O-acetyltransferase
 182-297 3.97e-05

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 44.63  E-value: 3.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 182 ALGEHVKIEHVGIVRIQKNVEIGANTAIDRA---VFGETLIkegvkIDNLVQIGHNCVLGEhsivVSQVGLSGSTTTGRN 258
Cdd:PLN02694 148 ALALHSRISDVFAVDIHPAAKIGKGILFDHAtgvVIGETAV-----IGNNVSILHHVTLGG----TGKACGDRHPKIGDG 218

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446699695 259 VVFGGQVGIGGHLHVGEFTQIGGKSAVGKDLPPNTNFAG 297
Cdd:PLN02694 219 VLIGAGATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVG 257
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 107-173 4.02e-05

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 43.48  E-value: 4.02e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446699695 107 ERVTIMPNVVIgEGVEIGENSLIYPGVVIADGVKIGKNCILYPrvtlyqNTILEDNVTIHAGSVIGG 173
Cdd:COG0663   76 DDVTIGHGAIL-HGCTIGDNVLIGMGAIVLDGAVIGDGSIVGA------GALVTEGKVVPPGSLVVG 135
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 104-269 4.66e-05

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: 42.96  E-value: 4.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 104 KHFERVTIMPNVVIGEGVEIGENSLIYPGVVIADGVKIGKNCILYPRVTLYQNTILEDNVTIHAGSVIggdgfgyAHTAL 183
Cdd:cd05636    1 KDEIEGTVEEGVTIKGPVWIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEV-------KNSII 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 184 GEHVKIEH---VGIVRIQKNVEIGANTAIDRAVFGETLIKEGVKiDNLVQIGHN---CVLGEHsivvSQVGLSGSTTTGR 257
Cdd:cd05636   74 MDGTKVPHlnyVGDSVLGENVNLGAGTITANLRFDDKPVKVRLK-GERVDTGRRklgAIIGDG----VKTGINVSLNPGV 148

                        170
                 ....*....|..
gi 446699695 258 NVVFGGQVGIGG 269
Cdd:cd05636  149 KIGPGSWVYPGC 160
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
120-149 4.71e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 39.63  E-value: 4.71e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 446699695  120 GVEIGENSLIYPGVVIADGVKIGKNCILYP 149
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 115-290 4.85e-05

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 44.97  E-value: 4.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 115 VVIGEGVEIGENSLIYPGVV------IADGVKIGKncilYPRVTlyqNTILEDNVTIHAGSVIGGdgfgyAHTALGEHVK 188
Cdd:PRK14358 265 ILIEDTVTLGRDVTIEPGVLlrgqtrVADGVTIGA----YSVVT---DSVLHEGAVIKPHSVLEG-----AEVGAGSDVG 332

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 189 iehvGIVRIQKNVEIGANTAIDRavFGET---LIKEGVKIDNL-----VQIGHNCVLGEHSIVVSQVGLSG-STTTGRNV 259
Cdd:PRK14358 333 ----PFARLRPGTVLGEGVHIGN--FVETknaRLDAGVKAGHLaylgdVTIGAETNVGAGTIVANFDGVNKhQSKVGAGV 406

                        170       180       190
                 ....*....|....*....|....*....|.
gi 446699695 260 VFGGQVGIGGHLHVGEFTQIGGKSAVGKDLP 290
Cdd:PRK14358 407 FIGSNTTLIAPRVVGDAAFIAAGSAVHDDVP 437
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 116-173 5.79e-05

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: 41.02  E-value: 5.79e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446699695 116 VIGEGVEIGENSLIYpGVVIADGVKIGKNCILyprvtlyQNTILEDNVTIHAGSVIGG 173
Cdd:cd05787    1 VIGRGTSIGEGTTIK-NSVIGRNCKIGKNVVI-------DNSYIWDDVTIEDGCTIHH 50
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 200-297 7.25e-05

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


Pssm-ID: 100063 [Multi-domain]  Cd Length: 107  Bit Score: 41.44  E-value: 7.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 200 NVEIGANTAIDravfgetlikEGVKIDNL--VQIGHNCVL--------GEHSIVVSQVGL-SGSTTTGRNVVFGGQVGIG 268
Cdd:cd05825    3 NLTIGDNSWIG----------EGVWIYNLapVTIGSDACIsqgaylctGSHDYRSPAFPLiTAPIVIGDGAWVAAEAFVG 72

                         90       100
                 ....*....|....*....|....*....
gi 446699695 269 GHLHVGEFTQIGGKSAVGKDLPPNTNFAG 297
Cdd:cd05825   73 PGVTIGEGAVVGARSVVVRDLPAWTVYAG 101
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 195-298 7.61e-05

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: 41.27  E-value: 7.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 195 VRIQKNVEIGANTAIDRAVFgeTLIKEGVKIDNLVQIGHNCVLGehsiVVSQVGLSGSTTTGRNVVFGGQVGIGGHLHVG 274
Cdd:cd03354    3 IDIHPGAKIGPGLFIDHGTG--IVIGETAVIGDNCTIYQGVTLG----GKGKGGGKRHPTIGDNVVIGAGAKILGNITIG 76

                         90       100
                 ....*....|....*....|....
gi 446699695 275 EFTQIGGKSAVGKDLPPNTNFAGA 298
Cdd:cd03354   77 DNVKIGANAVVTKDVPANSTVVGV 100
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 108-171 1.20e-04

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: 40.95  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 108 RVTIMPNVVIGEGVEIGENSLIYPGVV---------------------IADGVKIGKNCILYPRVTLYQNTIlednvtIH 166
Cdd:cd03358   22 NVKIQSNVSIYEGVTIEDDVFIGPNVVftndlyprskiyrkwelkgttVKRGASIGANATILPGVTIGEYAL------VG 95


                 ....*
gi 446699695 167 AGSVI 171
Cdd:cd03358   96 AGAVV 100
PRK10502 PRK10502
putative acyl transferase; Provisional
 219-293 1.30e-04

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 42.24  E-value: 1.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 219 IKEGVKIDNL--VQIGHNCVL--------GEHSIVVSQVGL-SGSTTTGRNVVFGGQVGIGGHLHVGEFTQIGGKSAVGK 287
Cdd:PRK10502  80 IGDDVWLYNLgeITIGAHCVIsqksylctGSHDYSDPHFDLnTAPIVIGEGCWLAADVFVAPGVTIGSGAVVGARSSVFK 159


                 ....*.
gi 446699695 288 DLPPNT 293
Cdd:PRK10502 160 SLPANT 165
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
114-142 1.38e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 38.47  E-value: 1.38e-04
                          10        20
                  ....*....|....*....|....*....
gi 446699695  114 NVVIGEGVEIGENSLIYPGVVIADGVKIG 142
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIG 29
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 111-243 1.79e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 42.93  E-value: 1.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 111 IMPNVVIGEGVEIgENSLIYPGVVIADGVKigkNCILYPRVTLYQNTILEDNVtihagsviggdgfgyahtalgehvkie 190
Cdd:PRK05293 279 NLPPQYIAENAKV-KNSLVVEGCVVYGTVE---HSVLFQGVQVGEGSVVKDSV--------------------------- 327

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446699695 191 hvgivrIQKNVEIGANTAIDRAVFGE-TLIKEGVKI----DNLVQIGHNCVLGEHSIV 243
Cdd:PRK05293 328 ------IMPGAKIGENVVIERAIIGEnAVIGDGVIIgggkEVITVIGENEVIGVGTVI 379
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 104-173 1.90e-04

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: 41.43  E-value: 1.90e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446699695 104 KHFERVTIMPNVVIGEGVEIGENSLIYPG-----VVIADGVKIGKNCILYPRVTLYQNTILEDNVTIHAGSVIGG 173
Cdd:cd03359   62 KKFSKGVAFFPLHIGDYVFIGENCVVNAAqigsyVHIGKNCVIGRRCIIKDCVKILDGTVVPPDTVIPPYSVVSG 136
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 118-225 2.27e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 42.51  E-value: 2.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 118 GEGVEIGENSLIYPGVVIaDGVKIgKNCILYPRVTLYQNTILEDnvtihagSVIggdgFGYAHtaLGEHVKIEHVgIvrI 197
Cdd:PRK00844 307 GGRVGSAQDSLVSAGSII-SGATV-RNSVLSPNVVVESGAEVED-------SVL----MDGVR--IGRGAVVRRA-I--L 368

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446699695 198 QKNVEIGANTAI------DRAVF-----GETLIKEGVKI 225
Cdd:PRK00844 369 DKNVVVPPGATIgvdleeDRRRFtvsegGIVVVPKGQRV 407
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 115-243 3.69e-04

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


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 40.69  E-value: 3.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 115 VVIGEgVEIGENSLIYPGVVI----ADGVKIGKNCilyprvtlyqntILEDNVTIHA---GSVIGGDGFGYAHTAlgehv 187
Cdd:cd00710   16 VVIGD-VIIGDNVFVGPGASIradeGTPIIIGANV------------NIQDGVVIHAlegYSVWIGKNVSIAHGA----- 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446699695 188 kIEHvGIVRIQKNVEIGantaidravFGETLIKegvkidnlVQIGHNCVLGEHSIV 243
Cdd:cd00710   78 -IVH-GPAYIGDNCFIG---------FRSVVFN--------AKVGDNCVIGHNAVV 114
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 111-171 4.17e-04

Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Glucose-1-phosphate adenylyltransferase is also known as ADP-glucose synthase or ADP-glucose pyrophosphorylase. It catalyzes the first committed and rate-limiting step in starch biosynthesis in plants and glycogen biosynthesis in bacteria. It is the enzymatic site for regulation of storage polysaccharide accumulation in plants and bacteria. The enzyme is a homotetramer, with each subunit containing an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain with at 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The LbH domain is involved in cooperative allosteric regulation and oligomerization.


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 38.98  E-value: 4.17e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446699695 111 IMPNVVIGEGVEIgENSLIYPGVVIADGVKIGKNcilyPRVTLYQNTILEDNVT-IHAGSVI 171
Cdd:cd04651   48 IMPNVGIGRNAVI-RRAIIDKNVVIPDGVVIGGD----PEEDRARFYVTEDGIVvVGKGMVI 104
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 110-219 4.97e-04

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: 40.04  E-value: 4.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 110 TIMPNVVIGEGVEIGENSLI---YPGVVIADGVKIGKNCILYPRVTlyQNTILEDNVTIHAGSVIGGdgfgyahtalgeh 186
Cdd:cd04745   14 VLIGDVIIGKNCYIGPHASLrgdFGRIVIRDGANVQDNCVIHGFPG--QDTVLEENGHIGHGAILHG------------- 78

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446699695 187 vkiehvgiVRIQKNVEIGANTAI-DRAVFGETLI 219
Cdd:cd04745   79 --------CTIGRNALVGMNAVVmDGAVIGEESI 104
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 111-142 7.56e-04

Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 40.83  E-value: 7.56e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 446699695 111 IMPNVVIGEGVEIgENSLIYPGVVIADGVKIG 142
Cdd:COG0448  323 IMPGVVIGEGAVI-ENAIIDKNVVIPPGVVIG 353
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 116-172 1.05e-03

eIF-2B gamma subunit, C-terminal 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 gamma subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH domain with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 37.56  E-value: 1.05e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446699695 116 VIGEGVEIGE-----NSLIYPGVVIADGVKIgKNCILYPRVTLYQNTILEdNVTIHAGSVIG 172
Cdd:cd04652    1 LVGENTQVGEktsikRSVIGANCKIGKRVKI-TNCVIMDNVTIEDGCTLE-NCIIGNGAVIG 60
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 92-142 1.07e-03

Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of a large number of microbial enzymes that catalyze the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. Members of this class of enzymes include Enterococcus faecium streptogramin A acetyltransferase and Pseudomonas aeruginosa chloramphenicol acetyltransferase. They contain repeated copies of a six-residue hexapeptide repeat sequence motif (X-[STAV]-X-[LIV]-[GAED]-X) and adopt a left-handed parallel beta helix (LbH) structure. The active enzyme is a trimer with CoA and substrate binding sites at the interface of two separate LbH subunits. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients.


Pssm-ID: 100040 [Multi-domain]  Cd Length: 145  Bit Score: 38.68  E-value: 1.07e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446699695  92 PFFKNPESVNEPKHFERVTIMPNVVIGEGVEIGENSLIYPGVVIADGVKIG 142
Cdd:cd03349   51 PFYIFGGEWEDDAKFDDWPSKGDVIIGNDVWIGHGATILPGVTIGDGAVIA 101
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 99-161 1.13e-03

eIF-2B gamma subunit, C-terminal 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 gamma subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH domain with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 37.17  E-value: 1.13e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446699695  99 SVNEPKHFERVTIMPNVVIGEGVEIgENSLIYPGVVIADGVKIgKNCILYPRVTLYQNTILED 161
Cdd:cd04652    7 QVGEKTSIKRSVIGANCKIGKRVKI-TNCVIMDNVTIEDGCTL-ENCIIGNGAVIGEKCKLKD 67
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 123-229 1.67e-03

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: 38.73  E-value: 1.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 123 IGENSLIYPGVVI-AD--GVKIGKNCILYPrvtlyqntiledNVTIHAGSVIGGDGFGYAHTALGEHVKIEHVGIVR--- 196
Cdd:cd03359   24 LNGKTIIQSDVIIrGDlaTVSIGRYCILSE------------GCVIRPPFKKFSKGVAFFPLHIGDYVFIGENCVVNaaq 91

                         90       100       110
                 ....*....|....*....|....*....|....
gi 446699695 197 IQKNVEIGANTAIDRAVfgetLIKEGVKI-DNLV 229
Cdd:cd03359   92 IGSYVHIGKNCVIGRRC----IIKDCVKIlDGTV 121
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 118-307 1.90e-03

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 40.01  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 118 GEGVEIGENSLIYPGVVIADGVKIGKNCILyprvtlyQNTILEDNVTIHAGSVIGGDGFGYAHTalgehvkiehVG-IVR 196
Cdd:PRK09451 269 GRDVEIDTNVIIEGNVTLGNRVKIGAGCVL-------KNCVIGDDCEISPYSVVEDANLGAACT----------IGpFAR 331

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 197 IQKNVEIGANTAIDRAV-FGETLIKEGVKIDNL-----VQIGHNCVLGEHSIVVSQVGLSG-STTTGRNVVFGGQVGIGG 269
Cdd:PRK09451 332 LRPGAELAEGAHVGNFVeMKKARLGKGSKAGHLtylgdAEIGDNVNIGAGTITCNYDGANKfKTIIGDDVFVGSDTQLVA 411

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446699695 270 HLHVGEFTQIGGKSAVGKDLPPNTNFAGAIPAMEIHEW 307
Cdd:PRK09451 412 PVTVGKGATIGAGTTVTRDVAENELVISRVPQRHIQGW 449
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 117-291 2.44e-03

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 39.54  E-value: 2.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 117 IGEGVEIGENSLIYPGVVIADGVKIGKNCILYPRVTLYQNTILEDNVTIHA---GSVIGGDG----FGY--AHTALGEHV 187
Cdd:PRK14352 268 IDVDVTIGRDVVIHPGTQLLGRTTIGEDAVVGPDTTLTDVTVGEGASVVRThgsESEIGAGAtvgpFTYlrPGTVLGEEG 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 188 KIehvGIVRIQKNVEIGantaidravfgetlikEGVKIDNLVQIGhNCVLGEHS------IVVSQVGLSGSTTTgrnvvf 261
Cdd:PRK14352 348 KL---GAFVETKNATIG----------------RGTKVPHLTYVG-DADIGEHSnigassVFVNYDGVNKHRTT------ 401

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 446699695 262 ggqvgIGGHLHVGEFTQI------------GGKSAVGKDLPP 291
Cdd:PRK14352 402 -----IGSHVRTGSDTMFvapvtvgdgaytGAGTVIREDVPP 438
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 215-288 2.89e-03

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: 36.07  E-value: 2.89e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446699695 215 GETLIKEGVKIDNLVqIGHNCVLGEHSIVVSQVgLSGSTTTGRNVVFGGQVgIGGHLHVGEFTQIGGKSAVGKD 288
Cdd:cd03356    4 ESTVIGENAIIKNSV-IGDNVRIGDGVTITNSI-LMDNVTIGANSVIVDSI-IGDNAVIGENVRVVNLCIIGDD 74
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 109-142 3.22e-03

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


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 38.23  E-value: 3.22e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 446699695 109 VTIMP------NVVIGEGVEIGENSLIYPGVVIADGVKIG 142
Cdd:cd03360  139 VHIAPgvvlsgGVTIGEGAFIGAGATIIQGVTIGAGAIIG 178
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 119-170 3.74e-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: 37.69  E-value: 3.74e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446699695 119 EGVEIGENSLIYPGVVIADGVKIGKNCILYPRVTLYQNTILEDNVTIHAGSV 170
Cdd:cd04646   82 EALKIGNNNVFESKSFVGKNVIITDGCIIGAGCKLPSSEILPENTVIYGADC 133
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 114-174 4.81e-03

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 38.47  E-value: 4.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 114 NVVIGEGV-----------EIGENSLI--------YPGV-----VIADGVKIGKNCILYPRVTlyqntiLEDNVTIHAGS 169
Cdd:COG1207  352 NSTIGEGSkvnhlsyigdaEIGEGVNIgagtitcnYDGVnkhrtVIGDGAFIGSNTNLVAPVT------IGDGATIGAGS 425


                 ....*
gi 446699695 170 VIGGD 174
Cdd:COG1207  426 TITKD 430
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
107-131 5.57e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.85  E-value: 5.57e-03
                          10        20
                  ....*....|....*....|....*
gi 446699695  107 ERVTIMPNVVIGEGVEIGENSLIYP 131
Cdd:pfam00132   6 DNVLIGPNAVIGGGVIIGDNVIIGA 30
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 155-243 6.69e-03

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: 36.81  E-value: 6.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 155 QNTILEDNVTIHAGSVIGGDgfgYAHTALGEHVKIEHVGIVR----------------IQKNVEIGANTAIdravfgetl 218
Cdd:cd03359   20 QNIVLNGKTIIQSDVIIRGD---LATVSIGRYCILSEGCVIRppfkkfskgvaffplhIGDYVFIGENCVV--------- 87

                         90       100
                 ....*....|....*....|....*
gi 446699695 219 ikEGVKIDNLVQIGHNCVLGEHSIV 243
Cdd:cd03359   88 --NAAQIGSYVHIGKNCVIGRRCII 110
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 94-292 8.58e-03

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 37.60  E-value: 8.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695  94 FKNPESV--NEPKHFER-VTIMP------NVVIGEGVEIGENSLIypgvviaDGVKIGKNC-ILYPRVTlyqntiledNV 163
Cdd:PRK14360 251 FIDPASCtiSETVELGPdVIIEPqthlrgNTVIGSGCRIGPGSLI-------ENSQIGENVtVLYSVVS---------DS 314

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446699695 164 TIHAGSVIGgdgfGYAH---------------------TALGEHVKIEH---VGIVRIQKNVEIGANTAIdrAVFgetli 219
Cdd:PRK14360 315 QIGDGVKIG----PYAHlrpeaqigsncrignfveikkSQLGEGSKVNHlsyIGDATLGEQVNIGAGTIT--ANY----- 383

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446699695 220 kEGVKidnlvqiGHNCVLGEHSivvsqvglsgstTTGRNVVFGGQVGIGGHLhvgeftQIGGKSAVGKDLPPN 292
Cdd:PRK14360 384 -DGVK-------KHRTVIGDRS------------KTGANSVLVAPITLGEDV------TVAAGSTITKDVPDN 430
PRK09677 PRK09677
putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional
 115-147 9.63e-03

putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ; Provisional


Pssm-ID: 137467 [Multi-domain]  Cd Length: 192  Bit Score: 36.78  E-value: 9.63e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 446699695 115 VVIGEGVEIGENSLIYPGVVIADGVKIGKNCIL 147
Cdd:PRK09677 131 VVIGQRVWIGENVTILPGVSIGNGCIVGANSVV 163
 
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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