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Conserved domains on  [gi|119371983|sp|Q3AYS2|]
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RecName: Full=UDP-3-O-acylglucosamine N-acyltransferase

Protein Classification

UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase( domain architecture ID 11479317)

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:0103118|GO:0009245
PubMed:  17360522|15500694|11747907
SCOP:  4004951|4002830

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 24-347 4.07e-146

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


:

Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 416.08  E-value: 4.07e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983  24 ADPILAGAASLEQAKGDQLSFLEkGNALIAALTETGAGALLLPdqPDLIQCASErGIAFAVLANPRLAFAEALERLHPRL 103
Cdd:PRK00892  20 GDIEITGVASLEEAGPGQISFLA-NPKYRKQLATTKAGAVIVS--PDDAEFVPA-GNALLVVKNPYLAFARLAQLFDPPA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 104 RPLAE--IHPSAVVDERAVVGPGTFIAPRVCIGASSRIGANCIVHPGVVIYDDVEVGEGCELHANAVLHPGSRLGRGCVV 181
Cdd:PRK00892  96 TPSPAagIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVII 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 182 NSNAVIGSEGFGFVPTPRGWRKMPQTGQVVLEDGVEVGCGSTIDRPSVGETRIGAGSKIDNLVQIGHGVTTGRGCALASQ 261
Cdd:PRK00892 176 HSGAVIGSDGFGFANDRGGWVKIPQLGRVIIGDDVEIGANTTIDRGALDDTVIGEGVKIDNLVQIAHNVVIGRHTAIAAQ 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 262 VGIAGGAKLGHGVILAGQVGVANRAVVGDGAIASSKSGIHGEV-APGEVVSGYPAIPNRLWLRCSAAFSKLPEMAKTLRE 340
Cdd:PRK00892 256 VGIAGSTKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIpEPGEYSSGIPAQPNKEWLRTAARLRRLDELRKRLKA 335


                 ....*..
gi 119371983 341 LKRDISQ 347
Cdd:PRK00892 336 LEKKVEQ 342
 
Name Accession Description Interval E-value
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 24-347 4.07e-146

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 416.08  E-value: 4.07e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983  24 ADPILAGAASLEQAKGDQLSFLEkGNALIAALTETGAGALLLPdqPDLIQCASErGIAFAVLANPRLAFAEALERLHPRL 103
Cdd:PRK00892  20 GDIEITGVASLEEAGPGQISFLA-NPKYRKQLATTKAGAVIVS--PDDAEFVPA-GNALLVVKNPYLAFARLAQLFDPPA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 104 RPLAE--IHPSAVVDERAVVGPGTFIAPRVCIGASSRIGANCIVHPGVVIYDDVEVGEGCELHANAVLHPGSRLGRGCVV 181
Cdd:PRK00892  96 TPSPAagIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVII 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 182 NSNAVIGSEGFGFVPTPRGWRKMPQTGQVVLEDGVEVGCGSTIDRPSVGETRIGAGSKIDNLVQIGHGVTTGRGCALASQ 261
Cdd:PRK00892 176 HSGAVIGSDGFGFANDRGGWVKIPQLGRVIIGDDVEIGANTTIDRGALDDTVIGEGVKIDNLVQIAHNVVIGRHTAIAAQ 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 262 VGIAGGAKLGHGVILAGQVGVANRAVVGDGAIASSKSGIHGEV-APGEVVSGYPAIPNRLWLRCSAAFSKLPEMAKTLRE 340
Cdd:PRK00892 256 VGIAGSTKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIpEPGEYSSGIPAQPNKEWLRTAARLRRLDELRKRLKA 335


                 ....*..
gi 119371983 341 LKRDISQ 347
Cdd:PRK00892 336 LEKKVEQ 342
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 24-343 5.51e-144

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: 410.18  E-value: 5.51e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983  24 ADPILAGAASLEQAKGDQLSFLEkGNALIAALTETGAGALLLPdqPDLiqCASERGIAFAVLANPRLAFAEALERLHPRL 103
Cdd:COG1044   19 GDLEITGVAPLEEAGPGDLSFLA-NPKYAKQLATTKASAVIVP--PDF--AAALPGLALIVVDNPYLAFAKLLQLFYPPP 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 104 RPLAEIHPSAVVDERAVVGPGTFIAPRVCIGASSRIGANCIVHPGVVIYDDVEVGEGCELHANAVLHPGSRLGRGCVVNS 183
Cdd:COG1044   94 APAPGIHPSAVIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVIGDRVIIHS 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 184 NAVIGSEGFGFVPTPRG-WRKMPQTGQVVLEDGVEVGCGSTIDRPSVGETRIGAGSKIDNLVQIGHGVTTGRGCALASQV 262
Cdd:COG1044  174 GAVIGADGFGFAPDEDGgWVKIPQLGRVVIGDDVEIGANTTIDRGALGDTVIGDGTKIDNLVQIAHNVRIGEHTAIAAQV 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 263 GIAGGAKLGHGVILAGQVGVANRAVVGDGAIASSKSGIHGEVAPGEVVSGYPAIPNRLWLRCSAAFSKLPEMAKTLRELK 342
Cdd:COG1044  254 GIAGSTKIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSGSPAQPHREWLRNAAALRRLPELAKRLKELE 333


                 .
gi 119371983 343 R 343
Cdd:COG1044  334 K 334
lipid_A_lpxD TIGR01853
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD; This model describes LpxD, an ...
 21-338 2.87e-103

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: 306.52  E-value: 2.87e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983   21 QCGADPILAGAASLEQAKGDQLSFLEKGNALiAALTETGAGALLL-PDQPDLIQcaserGIAFAVLANPRLAFAEALERL 99
Cdd:TIGR01853  11 KGNGDIVITGVAPLEKAKANHITFLANPKYL-KHLKSSQAGAVIVsPDDQGLPA-----KCAALVVKDPYLAFAKVAELF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983  100 HPRLRPLAEIHPSAVVDERAVVGPGTFIAPRVCIGASSRIGANCIVHPGVVIYDDVEVGEGCELHANAVLHPGSRLGRGC 179
Cdd:TIGR01853  85 DPPPKREAGIHPTAVVDPSAKIGDGVTIGPNVVIGAGVEIGENVIIGPGVVIGDDVVIGDGSRIHPNVVIYERVQLGKNV 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983  180 VVNSNAVIGSEGFGFVPTPRG-WRKMPQTGQVVLEDGVEVGCGSTIDRPSVGETRIGAGSKIDNLVQIGHGVTTGRGCAL 258
Cdd:TIGR01853 165 IIHSGAVIGSDGFGYAHTANGgHVKIPQIGRVIIEDDVEIGANTTIDRGAFDDTIIGEGTKIDNLVQIAHNCRIGENCII 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983  259 ASQVGIAGGAKLGHGVILAGQVGVANRAVVGDGAIASSKSGIHGEVAPGEVVSGYPAIPNRLWLRCSAAFSKLPEMAKTL 338
Cdd:TIGR01853 245 VAQVGIAGSTKIGRNVIIGGQVGVAGHLEIGDNVTIGAKSGVTKSIPPPGVYGGIPARPNKEWLRIAAKVKRLPELRKRI 324
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 119-322 7.74e-95

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: 280.45  E-value: 7.74e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 119 AVVGPGTFIAPRVCIGASSRIGANCIVHPGVVIYDDVEVGEGCELHANAVLHPGSRLGRGCVVNSNAVIGSEGFGFVPTP 198
Cdd:cd03352    2 AKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIGSDGFGFAPDG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 199 RGWRKMPQTGQVVLEDGVEVGCGSTIDRPSVGETRIGAGSKIDNLVQIGHGVTTGRGCALASQVGIAGGAKLGHGVILAG 278
Cdd:cd03352   82 GGWVKIPQLGGVIIGDDVEIGANTTIDRGALGDTVIGDGTKIDNLVQIAHNVRIGENCLIAAQVGIAGSTTIGDNVIIGG 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 119371983 279 QVGVANRAVVGDGAIASSKSGIHGEVAPGEVVSGYPAIPNRLWL 322
Cdd:cd03352  162 QVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQPHREWL 205
LpxD pfam04613
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase, LpxD; UDP-3-O-[3-hydroxymyristoyl] ...
 26-98 2.07e-10

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: 55.97  E-value: 2.07e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119371983   26 PILAGAASLEQAKGDQLSFLEkGNALIAALTETGAGALLLPDQPDLIQCASERGIafaVLANPRLAFAEALER 98
Cdd:pfam04613   1 LEITGVAPLEEAGPGDLSFLA-NPKYAKYLATTKASAVIVPPDFAPQAPATATLL---VVDNPYLAFAKLLQL 69
 
Name Accession Description Interval E-value
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 24-347 4.07e-146

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 416.08  E-value: 4.07e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983  24 ADPILAGAASLEQAKGDQLSFLEkGNALIAALTETGAGALLLPdqPDLIQCASErGIAFAVLANPRLAFAEALERLHPRL 103
Cdd:PRK00892  20 GDIEITGVASLEEAGPGQISFLA-NPKYRKQLATTKAGAVIVS--PDDAEFVPA-GNALLVVKNPYLAFARLAQLFDPPA 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 104 RPLAE--IHPSAVVDERAVVGPGTFIAPRVCIGASSRIGANCIVHPGVVIYDDVEVGEGCELHANAVLHPGSRLGRGCVV 181
Cdd:PRK00892  96 TPSPAagIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVII 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 182 NSNAVIGSEGFGFVPTPRGWRKMPQTGQVVLEDGVEVGCGSTIDRPSVGETRIGAGSKIDNLVQIGHGVTTGRGCALASQ 261
Cdd:PRK00892 176 HSGAVIGSDGFGFANDRGGWVKIPQLGRVIIGDDVEIGANTTIDRGALDDTVIGEGVKIDNLVQIAHNVVIGRHTAIAAQ 255

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 262 VGIAGGAKLGHGVILAGQVGVANRAVVGDGAIASSKSGIHGEV-APGEVVSGYPAIPNRLWLRCSAAFSKLPEMAKTLRE 340
Cdd:PRK00892 256 VGIAGSTKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIpEPGEYSSGIPAQPNKEWLRTAARLRRLDELRKRLKA 335


                 ....*..
gi 119371983 341 LKRDISQ 347
Cdd:PRK00892 336 LEKKVEQ 342
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 24-343 5.51e-144

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: 410.18  E-value: 5.51e-144
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983  24 ADPILAGAASLEQAKGDQLSFLEkGNALIAALTETGAGALLLPdqPDLiqCASERGIAFAVLANPRLAFAEALERLHPRL 103
Cdd:COG1044   19 GDLEITGVAPLEEAGPGDLSFLA-NPKYAKQLATTKASAVIVP--PDF--AAALPGLALIVVDNPYLAFAKLLQLFYPPP 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 104 RPLAEIHPSAVVDERAVVGPGTFIAPRVCIGASSRIGANCIVHPGVVIYDDVEVGEGCELHANAVLHPGSRLGRGCVVNS 183
Cdd:COG1044   94 APAPGIHPSAVIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCVLHPNVTIYERCVIGDRVIIHS 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 184 NAVIGSEGFGFVPTPRG-WRKMPQTGQVVLEDGVEVGCGSTIDRPSVGETRIGAGSKIDNLVQIGHGVTTGRGCALASQV 262
Cdd:COG1044  174 GAVIGADGFGFAPDEDGgWVKIPQLGRVVIGDDVEIGANTTIDRGALGDTVIGDGTKIDNLVQIAHNVRIGEHTAIAAQV 253

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 263 GIAGGAKLGHGVILAGQVGVANRAVVGDGAIASSKSGIHGEVAPGEVVSGYPAIPNRLWLRCSAAFSKLPEMAKTLRELK 342
Cdd:COG1044  254 GIAGSTKIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSGSPAQPHREWLRNAAALRRLPELAKRLKELE 333


                 .
gi 119371983 343 R 343
Cdd:COG1044  334 K 334
lipid_A_lpxD TIGR01853
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD; This model describes LpxD, an ...
 21-338 2.87e-103

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: 306.52  E-value: 2.87e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983   21 QCGADPILAGAASLEQAKGDQLSFLEKGNALiAALTETGAGALLL-PDQPDLIQcaserGIAFAVLANPRLAFAEALERL 99
Cdd:TIGR01853  11 KGNGDIVITGVAPLEKAKANHITFLANPKYL-KHLKSSQAGAVIVsPDDQGLPA-----KCAALVVKDPYLAFAKVAELF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983  100 HPRLRPLAEIHPSAVVDERAVVGPGTFIAPRVCIGASSRIGANCIVHPGVVIYDDVEVGEGCELHANAVLHPGSRLGRGC 179
Cdd:TIGR01853  85 DPPPKREAGIHPTAVVDPSAKIGDGVTIGPNVVIGAGVEIGENVIIGPGVVIGDDVVIGDGSRIHPNVVIYERVQLGKNV 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983  180 VVNSNAVIGSEGFGFVPTPRG-WRKMPQTGQVVLEDGVEVGCGSTIDRPSVGETRIGAGSKIDNLVQIGHGVTTGRGCAL 258
Cdd:TIGR01853 165 IIHSGAVIGSDGFGYAHTANGgHVKIPQIGRVIIEDDVEIGANTTIDRGAFDDTIIGEGTKIDNLVQIAHNCRIGENCII 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983  259 ASQVGIAGGAKLGHGVILAGQVGVANRAVVGDGAIASSKSGIHGEVAPGEVVSGYPAIPNRLWLRCSAAFSKLPEMAKTL 338
Cdd:TIGR01853 245 VAQVGIAGSTKIGRNVIIGGQVGVAGHLEIGDNVTIGAKSGVTKSIPPPGVYGGIPARPNKEWLRIAAKVKRLPELRKRI 324
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 119-322 7.74e-95

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: 280.45  E-value: 7.74e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 119 AVVGPGTFIAPRVCIGASSRIGANCIVHPGVVIYDDVEVGEGCELHANAVLHPGSRLGRGCVVNSNAVIGSEGFGFVPTP 198
Cdd:cd03352    2 AKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVIGSDGFGFAPDG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 199 RGWRKMPQTGQVVLEDGVEVGCGSTIDRPSVGETRIGAGSKIDNLVQIGHGVTTGRGCALASQVGIAGGAKLGHGVILAG 278
Cdd:cd03352   82 GGWVKIPQLGGVIIGDDVEIGANTTIDRGALGDTVIGDGTKIDNLVQIAHNVRIGENCLIAAQVGIAGSTTIGDNVIIGG 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 119371983 279 QVGVANRAVVGDGAIASSKSGIHGEVAPGEVVSGYPAIPNRLWL 322
Cdd:cd03352  162 QVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQPHREWL 205
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 107-343 9.54e-27

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: 106.26  E-value: 9.54e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 107 AEIHPSAVVDERAvvgpgtfiaprvcigassRIGANCIVHPGVVIYDDVEVGEGCELHANAVLHPGSRLGRGCVVNSNAV 186
Cdd:COG1043    2 AMIHPTAIVDPGA------------------KLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFAS 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 187 IGSEgfgfvptprgwrkmPQ-------TGQVVLEDGVEVGCGSTIDRPSV---GETRIGAgskiDNL----VQIGHGVTT 252
Cdd:COG1043   64 IGEE--------------PQdlkykgePTRLEIGDNNTIREFVTIHRGTVqggGVTRIGD----DNLlmayVHVAHDCVV 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 253 GRGCALASQVGIAGGAKLGHGVILAGQVGVANRAVVGDGAIASSKSGIHGEVAPGEVVSGYPAIP---NRLWLRcSAAFS 329
Cdd:COG1043  126 GNNVILANNATLAGHVEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDVPPYVLAAGNPARLrglNLVGLK-RRGFS 204

                        250
                 ....*....|....
gi 119371983 330 KlpemaKTLRELKR 343
Cdd:COG1043  205 R-----EQIRALKR 213
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 109-343 2.13e-25

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: 102.51  E-value: 2.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 109 IHPSAVVDERAvvgpgtfiaprvcigassRIGANCIVHPGVVIYDDVEVGEGCELHANAVLHPGSRLGRGCVVNSNAVIG 188
Cdd:cd03351    2 IHPTAIVDPGA------------------KIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNNRIFPFASIG 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 189 SEgfgfvptprgwrkmPQ-------TGQVVLEDGVEVGCGSTIDRPSV---GETRIGAgskiDNL----VQIGHGVTTGR 254
Cdd:cd03351   64 EA--------------PQdlkykgePTRLEIGDNNTIREFVTIHRGTAqggGVTRIGN----NNLlmayVHVAHDCVIGN 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 255 GCALASQVGIAGGAKLGHGVILAGQVGVANRAVVGDGAIASSKSGIHGEVAPGEVVSGYPAIP---NRLWLRcSAAFSKl 331
Cdd:cd03351  126 NVILANNATLAGHVEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARLrglNLVGLK-RRGFSR- 203

                        250
                 ....*....|..
gi 119371983 332 pemaKTLRELKR 343
Cdd:cd03351  204 ----EEIRALKR 211
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
107-323 1.08e-22

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 95.55  E-value: 1.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 107 AEIHPSAVVDERAVvgpgtfiaprvcigassrIGANCIVHPGVVIYDDVEVGEGCELHANAVLHPGSRLGRGCVVNSNAV 186
Cdd:PRK05289   3 AKIHPTAIVEPGAK------------------IGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFAS 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 187 IGSE----GFGFVPTprgwrkmpqtgQVVLEDGVEVGCGSTIDRPSV---GETRIGAgskiDNL----VQIGHGVTTGRG 255
Cdd:PRK05289  65 IGEDpqdlKYKGEPT-----------RLVIGDNNTIREFVTINRGTVqggGVTRIGD----NNLlmayVHVAHDCVVGNH 129

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119371983 256 CALASQVGIAGGAKLGHGVILAGQVGVANRAVVGDGAIASSKSGIHGEVAPGEVVSGYPAIP---NRLWLR 323
Cdd:PRK05289 130 VILANNATLAGHVEVGDYAIIGGLTAVHQFVRIGAHAMVGGMSGVSQDVPPYVLAEGNPARLrglNLVGLK 200
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 127-317 2.87e-19

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 85.84  E-value: 2.87e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 127 IAPRVCIGASSRIGANCIVHPGVVIYDDVEVGEGCELHANAVLHPGSRLGRGCVVNSNAVIGSEgfgfvPTPRGWRKMPQ 206
Cdd:PRK12461   2 IHPTAVIDPSAKLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQGAVVGDE-----PQDFTYKGEES 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 207 tgQVVLEDGVEVGCGSTIDRPSVGE--TRIGAGSKIDNLVQIGHGVTTGRGCALASQVGIAGGAKLGHGVILAGQVGVAN 284
Cdd:PRK12461  77 --RLEIGDRNVIREGVTIHRGTKGGgvTRIGNDNLLMAYSHVAHDCQIGNNVILVNGALLAGHVTVGDRAIISGNCLVHQ 154

                        170       180       190
                 ....*....|....*....|....*....|...
gi 119371983 285 RAVVGDGAIASSKSGIHGEVAPGEVVSGYPAIP 317
Cdd:PRK12461 155 FCRIGALAMMAGGSRISKDVPPYCMMAGHPTNV 187
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 89-187 1.83e-18

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: 82.15  E-value: 1.83e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983  89 RLAFAEALERLHPRLRPLaeIHPSAVVDERAVVGPGTFIAPRVCIGASSRIGANCIVH------------------PGVV 150
Cdd:cd03360   69 RRKLAEKLLAAGYRFATL--IHPSAVVSPSAVIGEGCVIMAGAVINPDARIGDNVIINtgavighdcvigdfvhiaPGVV 146

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 119371983 151 IYDDVEVGEGCELHANAVLHPGSRLGRGCVVNSNAVI 187
Cdd:cd03360  147 LSGGVTIGEGAFIGAGATIIQGVTIGAGAIIGAGAVV 183
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 89-187 6.30e-17

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: 77.92  E-value: 6.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983   89 RLAFAEALERLHPRLRPLaeIHPSAVVDERAVVGPGTFIAPRVCIGASSRIGANCIVHPGVVIYDDVEVGEGCELHANAV 168
Cdd:TIGR03570  72 RRRLVEKLKAKGYRFATL--IHPSAIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVT 149

                          90
                  ....*....|....*....
gi 119371983  169 LHPGSRLGRGCVVNSNAVI 187
Cdd:TIGR03570 150 LSGGVVIGEGVFIGAGATI 168
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 109-301 1.21e-15

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: 75.37  E-value: 1.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983  109 IHPSAVVDERAVVGPGTfiaprvcigassRIGANCIVHPGVVIyddvevGEGCELHANAVLHPGSRLGRGCVVNSNAVIG 188
Cdd:TIGR01852   1 IHPTAIIEPGAEIGENV------------EIGPFCIVGPGVKI------GDGVELKSHVVILGHTTIGEGTRIFPGAVIG 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983  189 SEgfgfvptprgwrkmPQ----TGQvvlEDGVEVGCGSTIdRPSVgetRIGAGSKIdnlvqiGHGVTT-GRGCALASQVG 263
Cdd:TIGR01852  63 GV--------------PQdlkyKGE---KTRLIIGDNNTI-REFV---TINRGTAS------GGGVTRiGNNNLLMAYSH 115

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 119371983  264 IAGGAKLGHGVILAGQVGVANRAVVGDGAIASSKSGIH 301
Cdd:TIGR01852 116 IAHDCVVGNHVILANNATLAGHVEVGDYAIIGGLVAVH 153
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 125-238 7.13e-14

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


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 69.44  E-value: 7.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 125 TFIAPRVCIGASSRIGANCIVHPGVVIYDDVEVGEGCELHANAVLHPGSRLGRGCVVNSNAVIGsegfgfvptprgwrkm 204
Cdd:cd03360   85 TLIHPSAVVSPSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLS---------------- 148

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 119371983 205 pqtGQVVLEDGVEVGCGSTIdRP--SVGE-TRIGAGS 238
Cdd:cd03360  149 ---GGVTIGEGAFIGAGATI-IQgvTIGAgAIIGAGA 181
LpxD pfam04613
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase, LpxD; UDP-3-O-[3-hydroxymyristoyl] ...
 26-98 2.07e-10

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: 55.97  E-value: 2.07e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119371983   26 PILAGAASLEQAKGDQLSFLEkGNALIAALTETGAGALLLPDQPDLIQCASERGIafaVLANPRLAFAEALER 98
Cdd:pfam04613   1 LEITGVAPLEEAGPGDLSFLA-NPKYAKYLATTKASAVIVPPDFAPQAPATATLL---VVDNPYLAFAKLLQL 69
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 144-314 5.09e-10

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: 58.26  E-value: 5.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 144 IVHPGVVIYDDVEVGEGCELHANAVLHPGSRLGRGCVVNSNAVIGsegfgfvptprgwrkmpqtgqvvledgvevgcgst 223
Cdd:cd03360   86 LIHPSAVVSPSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIG----------------------------------- 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 224 idrpsvgetrigagskidnlvqigHGVTTGRGCALASQVGIAGGAKLGHGV------ILAGQVGVANRAVVGDGAIassk 297
Cdd:cd03360  131 ------------------------HDCVIGDFVHIAPGVVLSGGVTIGEGAfigagaTIIQGVTIGAGAIIGAGAV---- 182

                        170
                 ....*....|....*..
gi 119371983 298 sgIHGEVAPGEVVSGYP 314
Cdd:cd03360  183 --VTKDVPDGSVVVGNP 197
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 144-315 6.25e-10

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: 58.27  E-value: 6.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983  144 IVHPGVVIYDDVEVGEGCELHANAVLHPGSRLGRGCVVNSNAVIGsegfgfvptprgwrkmpqtgqvvledgvevgcgst 223
Cdd:TIGR03570  89 LIHPSAIVSPSASIGEGTVIMAGAVINPDVRIGDNVIINTGAIVE----------------------------------- 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983  224 idrpsvgetrigagskidnlvqigHGVTTGRGCALASQVGIAGGAKLGHGV------ILAGQVGVANRAVVGDGAIassk 297
Cdd:TIGR03570 134 ------------------------HDCVIGDFVHIAPGVTLSGGVVIGEGVfigagaTIIQGVTIGAGAIVGAGAV---- 185

                         170
                  ....*....|....*...
gi 119371983  298 sgIHGEVAPGEVVSGYPA 315
Cdd:TIGR03570 186 --VTKDIPDGGVVVGVPA 201
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 115-306 8.31e-10

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 57.43  E-value: 8.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 115 VDERAVVGPGTFIAPRVCIGASSRIGANCIVHPGVVIyDDVEVGEGCELHANAVLHpgsrlgrGCVVNSNAVIGsegfgf 194
Cdd:cd03353   12 IDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVI-KDSTIGDGVVIKASSVIE-------GAVIGNGATVG------ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 195 vptPRGwRKMPQTgqvVLEDGVEVGcgstiDRPSVGETRIGAGSKIDNLVQIGHgvttgrgcalaSQVGiaGGAKLGHGV 274
Cdd:cd03353   78 ---PFA-HLRPGT---VLGEGVHIG-----NFVEIKKSTIGEGSKANHLSYLGD-----------AEIG--EGVNIGAGT 132

                        170       180       190
                 ....*....|....*....|....*....|...
gi 119371983 275 ILAGQVGVA-NRAVVGDGAIASSKSGIhgeVAP 306
Cdd:cd03353  133 ITCNYDGVNkHRTVIGDNVFIGSNSQL---VAP 162
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 101-187 1.47e-09

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: 56.22  E-value: 1.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 101 PRLRPLAEIHPSAVVDERAVVGPGTFIAPRVC---------IGASSRIGANCIVH--PGVviydDVEVGEGCELHANAVL 169
Cdd:cd04745    1 PVVDPSSFVHPTAVLIGDVIIGKNCYIGPHASlrgdfgrivIRDGANVQDNCVIHgfPGQ----DTVLEENGHIGHGAIL 76

                         90
                 ....*....|....*...
gi 119371983 170 HpGSRLGRGCVVNSNAVI 187
Cdd:cd04745   77 H-GCTIGRNALVGMNAVV 93
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
107-187 1.72e-09

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 55.65  E-value: 1.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 107 AEIHPSAVV-DERAVVGPGTFIAPRVCIGASS--RIGANCIVHPGVVIYD----------------DVEVGEGCELHANA 167
Cdd:COG0110   15 VVIGPGVRIyGGNITIGDNVYIGPGVTIDDPGgiTIGDNVLIGPGVTILTgnhpiddpatfplrtgPVTIGDDVWIGAGA 94

                         90       100
                 ....*....|....*....|
gi 119371983 168 VLHPGSRLGRGCVVNSNAVI 187
Cdd:COG0110   95 TILPGVTIGDGAVVGAGSVV 114
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 113-188 1.81e-09

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 53.79  E-value: 1.81e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119371983 113 AVVDERAVVGPGTFIAPRVCIGASSRIGANCIVH--PGVVIYDDVEVGEGCELHANAVLHPGSRLGRGCVVNSNAVIG 188
Cdd:cd00208    1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGaaTGPNEKNPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 100-187 1.22e-08

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: 53.78  E-value: 1.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 100 HPRLRPLAEIHPSAVVDERAVVGPGTFIAPRVCI----GASSRIGANCIVHPGVVI----YDDVEVGEGCELHANAVLHP 171
Cdd:cd00710    2 EPVIDPSAYVHPTAVVIGDVIIGDNVFVGPGASIradeGTPIIIGANVNIQDGVVIhaleGYSVWIGKNVSIAHGAIVHG 81

                         90
                 ....*....|....*.
gi 119371983 172 GSRLGRGCVVNSNAVI 187
Cdd:cd00710   82 PAYIGDNCFIGFRSVV 97
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 114-188 2.49e-08

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: 50.65  E-value: 2.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 114 VVDERAVVGPGTFIAPRVcIGASSRIGANCIVHpGVVIYDDVEVGEGCELH-----ANAVLHPGSRLGRGCVVNSNAVIG 188
Cdd:cd05787    1 VIGRGTSIGEGTTIKNSV-IGRNCKIGKNVVID-NSYIWDDVTIEDGCTIHhsivaDGAVIGKGCTIPPGSLISFGVVIG 78
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 139-238 3.95e-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: 50.96  E-value: 3.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 139 IGANCIVHPGVVIYDDVEVGEGCELHANAVLHPGSRLGRGCVVNSNAVigsegFGFVPTPRG--WRKMPQTGqVVLEDGV 216
Cdd:cd03358    1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVV-----FTNDLYPRSkiYRKWELKG-TTVKRGA 74

                         90       100
                 ....*....|....*....|....
gi 119371983 217 EVGCGSTI-DRPSVGE-TRIGAGS 238
Cdd:cd03358   75 SIGANATIlPGVTIGEyALVGAGA 98
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 125-309 4.76e-08

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 54.45  E-value: 4.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 125 TFIAPR-VCIGASSRIGANCIVHPGVVIYDDVEVGEGCELHANAVLHpGSRLGRGCVVNSNAVIGSEgfgfvptprgwrk 203
Cdd:PRK14354 253 TIIDPEsTYIDADVEIGSDTVIEPGVVIKGNTVIGEDCVIGPGSRIV-DSTIGDGVTITNSVIEESK------------- 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 204 mpqtgqvvLEDGVEVGCGSTIdRPsvgETRIGAGSKIDNLVQIgHGVTTGRGcALASQVGIAGGAKLGHGV-ILAGQVGV 282
Cdd:PRK14354 319 --------VGDNVTVGPFAHL-RP---GSVIGEEVKIGNFVEI-KKSTIGEG-TKVSHLTYIGDAEVGENVnIGCGTITV 384

                        170       180       190
                 ....*....|....*....|....*....|...
gi 119371983 283 ------ANRAVVGDGAIASSKSGIhgeVAPGEV 309
Cdd:PRK14354 385 nydgknKFKTIIGDNAFIGCNSNL---VAPVTV 414
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 114-190 7.80e-08

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: 49.16  E-value: 7.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 114 VVDERAVVGPGTFIAPRVcigassrIGANCIVHPGV-----VIYDDVEVGEGCELHaNAVLHPGSRLGRGCVVNSNAVIG 188
Cdd:cd03356    1 LIGESTVIGENAIIKNSV-------IGDNVRIGDGVtitnsILMDNVTIGANSVIV-DSIIGDNAVIGENVRVVNLCIIG 72


                 ..
gi 119371983 189 SE 190
Cdd:cd03356   73 DD 74
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 100-187 1.41e-07

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 50.80  E-value: 1.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 100 HPRLRPLAEIHPSAVVDERAVVGPGTFIAP---------RVCIGASSRIGANCIVH--PG--VVIYDDVEVGEGCELHA- 165
Cdd:COG0663   10 TPQIHPSAFVAPTAVVIGDVTIGEDVSVWPgavlrgdvgPIRIGEGSNIQDGVVLHvdPGypLTIGDDVTIGHGAILHGc 89

                         90       100       110
                 ....*....|....*....|....*....|..
gi 119371983 166 ----------NAVLHPGSRLGRGCVVNSNAVI 187
Cdd:COG0663   90 tigdnvligmGAIVLDGAVIGDGSIVGAGALV 121
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
126-238 2.14e-07

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 49.48  E-value: 2.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 126 FIAPRVCIGASSRIGANCIVHPGvviydDVEVGEGCELHANAVLHP--GSRLGRGCVVNSNAVIGSEGFGFVPTPRGWRK 203
Cdd:COG0110    4 LLLFGARIGDGVVIGPGVRIYGG-----NITIGDNVYIGPGVTIDDpgGITIGDNVLIGPGVTILTGNHPIDDPATFPLR 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 119371983 204 mpqTGQVVLEDGVEVGCGSTIdRP--SVGE-TRIGAGS 238
Cdd:COG0110   79 ---TGPVTIGDDVWIGAGATI-LPgvTIGDgAVVGAGS 112
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
138-315 2.97e-07

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 49.10  E-value: 2.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 138 RIGANCIVHPGVVIYD-DVEVGEGCELHANAVLHP--GSRLGRGCVVNSNAVIGSEGFGFVPTPRGWRKmpqTGQVVLED 214
Cdd:COG0110   10 RIGDGVVIGPGVRIYGgNITIGDNVYIGPGVTIDDpgGITIGDNVLIGPGVTILTGNHPIDDPATFPLR---TGPVTIGD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 215 GVEVGCGSTIdrpsvgetrigagskidnlvqiGHGVTTGRGcalasqvgiaggaklghgvilagqvgvanrAVVGDGAIa 294
Cdd:COG0110   87 DVWIGAGATI----------------------LPGVTIGDG------------------------------AVVGAGSV- 113

                        170       180
                 ....*....|....*....|.
gi 119371983 295 ssksgIHGEVAPGEVVSGYPA 315
Cdd:COG0110  114 -----VTKDVPPYAIVAGNPA 129
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 105-240 7.13e-07

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: 48.35  E-value: 7.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 105 PLAEIHPSAVVDERAVVGPGTFIAPRVCIGASSRIGANCIVHPGVVIYDDVEVGEGCELhANAVLHPGSR---------- 174
Cdd:cd05636   10 EGVTIKGPVWIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEV-KNSIIMDGTKvphlnyvgds 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119371983 175 -------LGRGCVV------NSNAVIGSEGFGFVPtprGWRKMpqtgQVVLEDGVEVGCGSTIdrpSVGeTRIGAGSKI 240
Cdd:cd05636   89 vlgenvnLGAGTITanlrfdDKPVKVRLKGERVDT---GRRKL----GAIIGDGVKTGINVSL---NPG-VKIGPGSWV 156
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 115-255 7.99e-07

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 50.41  E-value: 7.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 115 VDERAVVGPGTFIAPRVCIGASSRIGANCIVHPGVVIyDDVEVGEGCELH----------ANAV------LHPGSRLGRG 178
Cdd:COG1207  263 IDGDVEIGRDVVIDPNVILEGKTVIGEGVVIGPNCTL-KDSTIGDGVVIKysviedavvgAGATvgpfarLRPGTVLGEG 341

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 179 CVV-N----SNAVIGsEGfgfvptprgwRKMPQ---TGQVVLEDGVEVGCGsTI----DrpsvGE----TRIGAGSKI-- 240
Cdd:COG1207  342 VKIgNfvevKNSTIG-EG----------SKVNHlsyIGDAEIGEGVNIGAG-TItcnyD----GVnkhrTVIGDGAFIgs 405

                        170
                 ....*....|....*....
gi 119371983 241 -DNL---VQIGHGVTTGRG 255
Cdd:COG1207  406 nTNLvapVTIGDGATIGAG 424
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 120-187 8.77e-07

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: 47.07  E-value: 8.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 120 VVGPGTFIAPRVCIGASS--RIGANCIVHPGVVIYD-------------------DVEVGEGCELHANAVLHPGSRLGRG 178
Cdd:cd04647    3 SIGDNVYIGPGCVISAGGgiTIGDNVLIGPNVTIYDhnhdiddperpieqgvtsaPIVIGDDVWIGANVVILPGVTIGDG 82


                 ....*....
gi 119371983 179 CVVNSNAVI 187
Cdd:cd04647   83 AVVGAGSVV 91
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 87-188 1.89e-06

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 49.36  E-value: 1.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983  87 NPRLAFAEALERLHPR------LRPLAEIHPSAV-VDERAVVGPGTFIAPRVCIGASSRIGANCIVHPGVVIyddvevgE 159
Cdd:PRK14355 230 NDRAQLAEAARVLRRRinrelmLAGVTLIDPETTyIDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVI-------K 302

                         90       100
                 ....*....|....*....|....*....
gi 119371983 160 GCELHANAVLHPGSRLgRGCVVNSNAVIG 188
Cdd:PRK14355 303 GCRIGDDVTVKAGSVL-EDSVVGDDVAIG 330
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 108-192 2.54e-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: 46.64  E-value: 2.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 108 EIHPSAVVDERAVV------GPGTFIAP---------RVCIGASSRIGANCIVHP----GVVIYDDVEVGEGCELHAnAV 168
Cdd:cd04645    1 EIDPSAFIAPNATVigdvtlGEGSSVWFgavlrgdvnPIRIGERTNIQDGSVLHVdpgyPTIIGDNVTVGHGAVLHG-CT 79

                         90       100
                 ....*....|....*....|....
gi 119371983 169 LHPGSRLGRGCVVNSNAVIGSEGF 192
Cdd:cd04645   80 IGDNCLIGMGAIILDGAVIGKGSI 103
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 95-199 3.16e-06

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 47.11  E-value: 3.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983  95 ALERLHPRLRPLAEIHPSAVVDERAVVGPGTFIAP---------RVCIGASSRIGANCIVH----PGVVIYDDVEVGEGC 161
Cdd:PRK13627   5 AFEGLIPVVHPTAFVHPSAVLIGDVIVGAGVYIGPlaslrgdygRLIVQAGANLQDGCIMHgycdTDTIVGENGHIGHGA 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 119371983 162 ELHAnAVLHPGSRLGRGCVVNSNAVIGSEGF---------GFVPTPR 199
Cdd:PRK13627  85 ILHG-CVIGRDALVGMNSVIMDGAVIGEESIvaamsfvkaGFQGEKR 130
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 103-273 7.97e-06

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: 45.87  E-value: 7.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 103 LRPLAEIHPSAVVDERAVVGPGTFIAPRVCIGASSRIGaNCIVHPGVVIYDDVeVGEGCELHANAVLHPGSRLGRGCVVN 182
Cdd:cd03353   12 IDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIK-DSTIGDGVVIKASS-VIEGAVIGNGATVGPFAHLRPGTVLG 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 183 SNAVIGSegfgFVptprgwrkmpQTGQVVLEDGVEVGCGSTIDRPSVGE-TRIGAGSKIDN-------LVQIGHGVTTGR 254
Cdd:cd03353   90 EGVHIGN----FV----------EIKKSTIGEGSKANHLSYLGDAEIGEgVNIGAGTITCNydgvnkhRTVIGDNVFIGS 155

                        170
                 ....*....|....*....
gi 119371983 255 GCALASQVGIAGGAKLGHG 273
Cdd:cd03353  156 NSQLVAPVTIGDGATIAAG 174
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 148-240 1.13e-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: 43.58  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 148 GVVIYDDVEVGEGCEL-HANA-VLHPGSRLGRGCVVNSNAVIGSEGFGfvptprgwrkmPQTGQVVLEDGVEVGCGSTId 225
Cdd:cd03354    2 GIDIHPGAKIGPGLFIdHGTGiVIGETAVIGDNCTIYQGVTLGGKGKG-----------GGKRHPTIGDNVVIGAGAKI- 69

                         90
                 ....*....|....*
gi 119371983 226 rpsVGETRIGAGSKI 240
Cdd:cd03354   70 ---LGNITIGDNVKI 81
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 90-283 1.17e-05

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 47.03  E-value: 1.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983  90 LAFAEALERLHPRLRPLAE---IHP--SAVVDERAVVGPGTFIAPRVCIGASSRIGA-----------NCIVHPGVVIY- 152
Cdd:PRK14356 236 LVRSEELLRARIVEKHLESgvlIHApeSVRIGPRATIEPGAEIYGPCEIYGASRIARgavihshcwlrDAVVSSGATIHs 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 153 ----DDVEVGEGCelhanaVLHPGSRLGRGCVVNSNAVIGSegfgFVptprgwrkmpQTGQVVLEDGVEVGCGSTIDRPS 228
Cdd:PRK14356 316 fshlEGAEVGDGC------SVGPYARLRPGAVLEEGARVGN----FV----------EMKKAVLGKGAKANHLTYLGDAE 375

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119371983 229 VG-ETRIGAGSKIDN-------LVQIGHGVTTGRGCALASQVGIAGGAKLGHGVIL-----AGQVGVA 283
Cdd:PRK14356 376 IGaGANIGAGTITCNydgvnkhRTVIGEGAFIGSNTALVAPVTIGDGALVGAGSVItkdvpDGSLAIA 443
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 109-189 1.26e-05

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: 45.01  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 109 IHPSAVVDERA------VVGPGTFIAPRVCIGASSR---IGANCIVHPGVVIYDDVEVGE----------------GCEL 163
Cdd:cd04646    2 IAPGAVVCQESeirgdvTIGPGTVVHPRATIIAEAGpiiIGENNIIEEQVTIVNKKPKDPaepkpmiigsnnvfevGCKC 81

                         90       100       110
                 ....*....|....*....|....*....|.
gi 119371983 164 HA-----NAVLHPGSRLGRGCVVNSNAVIGS 189
Cdd:cd04646   82 EAlkignNNVFESKSFVGKNVIITDGCIIGA 112
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 120-189 2.74e-05

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: 41.79  E-value: 2.74e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119371983 120 VVGPGTFIAPRVCIGASSrIGANCIVHPGV-----VIYDDVEVGEGCELhanavlhpgsrlgRGCVVNSNAVIGS 189
Cdd:cd04652    1 LVGENTQVGEKTSIKRSV-IGANCKIGKRVkitncVIMDNVTIEDGCTL-------------ENCIIGNGAVIGE 61
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 120-181 2.80e-05

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 43.86  E-value: 2.80e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119371983 120 VVGPGTFIAPRVCI-GAssRIGANCIVHPGVVIYDDVEVGEGCELHANAVLHPGSRLGRGCVV 181
Cdd:COG0663   73 TIGDDVTIGHGAILhGC--TIGDNVLIGMGAIVLDGAVIGDGSIVGAGALVTEGKVVPPGSLV 133
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 125-307 3.40e-05

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 45.36  E-value: 3.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 125 TFIAPRVCIGASSRIgANCIVHPGVVI-----YDDVEVGEGCELHANAVLHPGSRLGRGCVVNSnavigsegfgFVptpr 199
Cdd:PRK14358 289 TRVADGVTIGAYSVV-TDSVLHEGAVIkphsvLEGAEVGAGSDVGPFARLRPGTVLGEGVHIGN----------FV---- 353

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 200 gwrkmpQTGQVVLEDGVEVGCGSTIDRPSVG-ETRIGAGSKIDNLvqigHGVTTGRgcalasqvgiaggAKLGHGVILAG 278
Cdd:PRK14358 354 ------ETKNARLDAGVKAGHLAYLGDVTIGaETNVGAGTIVANF----DGVNKHQ-------------SKVGAGVFIGS 410

                        170       180
                 ....*....|....*....|....*....
gi 119371983 279 QVGVANRAVVGDGAIASSKSGIHGEVAPG 307
Cdd:PRK14358 411 NTTLIAPRVVGDAAFIAAGSAVHDDVPEG 439
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 108-187 5.85e-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: 41.66  E-value: 5.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 108 EIHPSAVVDERAVVGPGTFIAprvcIGASSRIGANCIVHPGVVI---YDDVE-----VGEGCELHANAVLHPGSRLGRGC 179
Cdd:cd03354    4 DIHPGAKIGPGLFIDHGTGIV----IGETAVIGDNCTIYQGVTLggkGKGGGkrhptIGDNVVIGAGAKILGNITIGDNV 79


                 ....*...
gi 119371983 180 VVNSNAVI 187
Cdd:cd03354   80 KIGANAVV 87
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 87-306 6.37e-05

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 44.37  E-value: 6.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983  87 NPRLAFAEALERLhpRLRPLAEIHPSAVvderAVVGPGTfiaprVCIGASSRIGANCIVHPGVVIYDDVEVGEGCElhan 166
Cdd:PRK14357 217 NTRIQLAWLEKQL--RMRILEELMENGV----TILDPNT-----TYIHYDVEIGMDTIIYPMTFIEGKTRIGEDCE---- 281

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 167 avLHPGSRLGRGCVVNSNAVIGSEGFGfvptprgwrkmpqtgqVVLEDGVEVGCGStidrpsvgetRIGAGSKIDNLVQI 246
Cdd:PRK14357 282 --IGPMTRIVDCEIGNNVKIIRSECEK----------------SVIEDDVSVGPFS----------RLREGTVLKKSVKI 333

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119371983 247 GHGVTTGR---GCALASQ-VGIAGGAKLGHGV-ILAGQV-----GV-ANRAVVGDGAIASSKSGIhgeVAP 306
Cdd:PRK14357 334 GNFVEIKKstiGENTKAQhLTYLGDATVGKNVnIGAGTItcnydGKkKNPTFIEDGAFIGSNSSL---VAP 401
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 87-255 8.34e-05

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 44.15  E-value: 8.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983  87 NPRLAFAEALERLHPRLRP--LAE----IHP-SAVVDERAVVGPGTFIAPRVCIGASSRIGANCIVHPGVVIyDDVEVGE 159
Cdd:PRK14360 224 NDRKQLAQCEEILQNRIKEkwMLAgvtfIDPaSCTISETVELGPDVIIEPQTHLRGNTVIGSGCRIGPGSLI-ENSQIGE 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 160 GCE-LHA---NAVLHPGSRLG-----RG-CVVNSNAVIGSegfgFVPTprgwrKMPQTGQ------------VVLEDGVE 217
Cdd:PRK14360 303 NVTvLYSvvsDSQIGDGVKIGpyahlRPeAQIGSNCRIGN----FVEI-----KKSQLGEgskvnhlsyigdATLGEQVN 373

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 119371983 218 VGCGsTI----DRPSVGETRIGAGSKID-NLV-----QIGHGVTTGRG 255
Cdd:PRK14360 374 IGAG-TItanyDGVKKHRTVIGDRSKTGaNSVlvapiTLGEDVTVAAG 420
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 155-247 1.14e-04

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 39.92  E-value: 1.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 155 VEVGEGCELHANAVLHPGSRLGRGCVVNSNAVIGSEGFGFVPTPrgwrkmpqtgqVVLEDGVEVGCGSTIdrpsVGETRI 234
Cdd:cd00208    1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGPNEKNP-----------TIIGDNVEIGANAVI----HGGVKI 65

                         90
                 ....*....|...
gi 119371983 235 GAGSKIDNLVQIG 247
Cdd:cd00208   66 GDNAVIGAGAVVT 78
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
136-165 1.17e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 38.86  E-value: 1.17e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 119371983  136 SSRIGANCIVHPGVVIYDDVEVGEGCELHA 165
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 134-315 1.94e-04

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 41.55  E-value: 1.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 134 GASSRIGANCIVHPGVVIYDDVEVGEGCELHANAVL----HPgSRLGRGCVVNSNAVI-GSEGFGfvptprgwrkmpqtg 208
Cdd:COG0663    8 GKTPQIHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLrgdvGP-IRIGEGSNIQDGVVLhVDPGYP--------------- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 209 qVVLEDGVEVGCGSTIdrpsvgetrigagskidnlvqigHGVTTGRGCaLasqVGIagGAklghgVILagqvgvaNRAVV 288
Cdd:COG0663   72 -LTIGDDVTIGHGAIL-----------------------HGCTIGDNV-L---IGM--GA-----IVL-------DGAVI 109

                        170       180
                 ....*....|....*....|....*....
gi 119371983 289 GDGAIASSKSGIHG--EVAPGEVVSGYPA 315
Cdd:COG0663  110 GDGSIVGAGALVTEgkVVPPGSLVVGSPA 138
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 121-187 2.36e-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: 40.18  E-value: 2.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 121 VGPGTFIAPRVCIGASSRIGANCIVHPGVVIYDDVEVG---------------------------EGCELHANAVLHPGS 173
Cdd:cd03358    7 IGTNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGpnvvftndlyprskiyrkwelkgttvkRGASIGANATILPGV 86

                         90
                 ....*....|....
gi 119371983 174 RLGRGCVVNSNAVI 187
Cdd:cd03358   87 TIGEYALVGAGAVV 100
LbH_FBP cd04650
Ferripyochelin Binding Protein (FBP): FBP is an outer membrane protein which plays a role in ...
 101-187 7.57e-04

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


Pssm-ID: 100055 [Multi-domain]  Cd Length: 154  Bit Score: 39.48  E-value: 7.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 101 PRLRPLAEIHPSAVVDERAVVGPGTFIAPRVCIGA---SSRIGANCIVHPGVVIYDD----VEVGEGCELHANAVLHpGS 173
Cdd:cd04650    1 PRISPKAYVHPTSYVIGDVVIGELTSVWHYAVIRGdndSIYIGKYSNVQENVSIHTDhgypTEIGDYVTIGHNAVVH-GA 79

                         90
                 ....*....|....
gi 119371983 174 RLGRGCVVNSNAVI 187
Cdd:cd04650   80 KVGNYVIVGMGAIL 93
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 109-240 1.06e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 40.59  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 109 IHPSAVVDERAVVGPGTFIAPRVCIGASSRIGA-----NCIVHPGVVIYDDV----EVGEGCELHANAVLHPGSRLGRGC 179
Cdd:PRK14354 262 IDADVEIGSDTVIEPGVVIKGNTVIGEDCVIGPgsrivDSTIGDGVTITNSVieesKVGDNVTVGPFAHLRPGSVIGEEV 341

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 180 -------VVNS---------------NAVIGSE---GFGFVPTPRGWRKMPQTgqvVLEDGVEVGCGSTIDRP-SVGE-T 232
Cdd:PRK14354 342 kignfveIKKStigegtkvshltyigDAEVGENvniGCGTITVNYDGKNKFKT---IIGDNAFIGCNSNLVAPvTVGDnA 418


                 ....*...
gi 119371983 233 RIGAGSKI 240
Cdd:PRK14354 419 YIAAGSTI 426
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 123-187 1.21e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 40.58  E-value: 1.21e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119371983 123 PGTFI--APRVCIGASSRIGANCIVHPGV----VIYDDVEVGEGCELHaNAVLHPGSRLGRGCVVNsNAVI 187
Cdd:PRK00844 300 PAKFVdgGGRVGSAQDSLVSAGSIISGATvrnsVLSPNVVVESGAEVE-DSVLMDGVRIGRGAVVR-RAIL 368
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 138-315 1.55e-03

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: 38.55  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 138 RIGANCIVHPGVVIYDDVEVGEGCELHANAVL----HPgSRLGRGCVVNSNAVI-GSEGFGfvptprgwrkmpqtgqVVL 212
Cdd:cd04645    1 EIDPSAFIAPNATVIGDVTLGEGSSVWFGAVLrgdvNP-IRIGERTNIQDGSVLhVDPGYP----------------TII 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 213 EDGVEVGCGSTIDrpsvgetrigaGSKIDNLVQIGHGVTtgrgcalasqvgIAGGAKLGHGVILAGQvgvanrAVVGDGA 292
Cdd:cd04645   64 GDNVTVGHGAVLH-----------GCTIGDNCLIGMGAI------------ILDGAVIGKGSIVAAG------SLVPPGK 114

                        170       180
                 ....*....|....*....|...
gi 119371983 293 iassksgihgEVAPGEVVSGYPA 315
Cdd:cd04645  115 ----------VIPPGSLVAGSPA 127
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 138-187 2.90e-03

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 38.26  E-value: 2.90e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119371983 138 RIGANCIVHPGVVIY------DDVEVGEGCELH------------ANAVLHPGSRLGRGCVVNSNAVI 187
Cdd:PRK10092  95 RIGDNCMLAPGVHIYtathplDPVARNSGAELGkpvtignnvwigGRAVINPGVTIGDNVVVASGAVV 162
PRK10502 PRK10502
putative acyl transferase; Provisional
 215-319 3.41e-03

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 38.01  E-value: 3.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 215 GVEVGCGSTIdRPSVGETR-----------IGAGSKIDNL--VQIGHGVTTGRGCALASqvG-----------IAGGAKL 270
Cdd:PRK10502  51 GAKIGKGVVI-RPSVRITYpwkltigdyawIGDDVWLYNLgeITIGAHCVISQKSYLCT--GshdysdphfdlNTAPIVI 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 119371983 271 GHGVILAGQVGVANRAVVGDGAIASSKSGIHGEVAPGEVVSGYPAIPNR 319
Cdd:PRK10502 128 GEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAVPIR 176
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 133-197 3.50e-03

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: 36.67  E-value: 3.50e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119371983 133 IGASSRIGANCIVHpGVVIYDDVEVGEGCELHaNAVLHPGSRLGRGCVVNSNAVIGSEGFGFVPT 197
Cdd:cd04651   31 LFRGVRVGSGSVVE-DSVIMPNVGIGRNAVIR-RAIIDKNVVIPDGVVIGGDPEEDRARFYVTED 93
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 69-306 4.24e-03

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 38.69  E-value: 4.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983  69 PDLIQCASERGIAFAVLANPR-----------LAFAEALerLHPRLRplaeihpsavvdERAVVGPGTFIAPR-VCIGAS 136
Cdd:PRK14353 203 TDIVAIARAEGLRVAVVEAPEdevrginsraeLAEAEAV--WQARRR------------RAAMLAGVTLIAPEtVFFSYD 268

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 137 SRIGANCIVHPGVVIYDDVEVGEGcelhanAVLHPGSRLgRGCVVNSNAVIGsegfgfvptPRGwRKMPQTgqvVLEDGV 216
Cdd:PRK14353 269 TVIGRDVVIEPNVVFGPGVTVASG------AVIHAFSHL-EGAHVGEGAEVG---------PYA-RLRPGA---ELGEGA 328

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 217 EVG--CgstidrpSVGETRIGAGSKIDNLVQIGHGVttgrgcalasqvgIAGGAKLGHGVILAGQVGVA-NRAVVGDGAI 293
Cdd:PRK14353 329 KVGnfV-------EVKNAKLGEGAKVNHLTYIGDAT-------------IGAGANIGAGTITCNYDGFNkHRTEIGAGAF 388

                        250
                 ....*....|...
gi 119371983 294 ASSKSGIhgeVAP 306
Cdd:PRK14353 389 IGSNSAL---VAP 398
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 234-317 4.72e-03

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: 36.43  E-value: 4.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 234 IGAGSKIDNL--VQIGHGVTTGRGCALASqvG-----------IAGGAKLGHGVILAGQVGVANRAVVGDGAIASSKSGI 300
Cdd:cd05825   12 IGEGVWIYNLapVTIGSDACISQGAYLCT--GshdyrspafplITAPIVIGDGAWVAAEAFVGPGVTIGEGAVVGARSVV 89

                         90
                 ....*....|....*..
gi 119371983 301 HGEVAPGEVVSGYPAIP 317
Cdd:cd05825   90 VRDLPAWTVYAGNPAVP 106
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 136-306 5.89e-03

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 38.17  E-value: 5.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 136 SSRIGANCIVHPGVVIYDDvevgegCELHANavlhpgSRLGRGCVVNS-----NAVIGSE--------------GFGFVP 196
Cdd:PRK14356 263 SVRIGPRATIEPGAEIYGP------CEIYGA------SRIARGAVIHShcwlrDAVVSSGatihsfshlegaevGDGCSV 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 197 TPRGwRKMPQTgqvVLEDGVEVGcgstiDRPSVGETRIGAGSKIDNLVQIGHgvttgrgcalaSQVGiaGGAKLGHGVIL 276
Cdd:PRK14356 331 GPYA-RLRPGA---VLEEGARVG-----NFVEMKKAVLGKGAKANHLTYLGD-----------AEIG--AGANIGAGTIT 388

                        170       180       190
                 ....*....|....*....|....*....|.
gi 119371983 277 AGQVGV-ANRAVVGDGAIASSKSGIhgeVAP 306
Cdd:PRK14356 389 CNYDGVnKHRTVIGEGAFIGSNTAL---VAP 416
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 118-317 7.12e-03

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


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 36.80  E-value: 7.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 118 RAVVGPGTFIAPRVCIGASSrigancIVHPGVVIYDDVEVGEGCELHANAVLHPGSRLGRGCVV-NSNAVIGSegfgfvp 196
Cdd:cd05636    5 EGTVEEGVTIKGPVWIGEGA------IVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVgNSVEVKNS------- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 197 tprgwrkmpqtgqvVLEDGVEVGCGSTIDRPSVGE-TRIGAGSKIDNL------VQI---GHGVTTGRgcalasqvgiag 266
Cdd:cd05636   72 --------------IIMDGTKVPHLNYVGDSVLGEnVNLGAGTITANLrfddkpVKVrlkGERVDTGR------------ 125

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119371983 267 gAKLGhgvilagqvgvanrAVVGDGAiassKSGIHGEVAPGEVVSGYPAIP 317
Cdd:cd05636  126 -RKLG--------------AIIGDGV----KTGINVSLNPGVKIGPGSWVY 157
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 139-340 8.19e-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: 36.42  E-value: 8.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 139 IGANCIVHPGVVIYDDVevgegcelhANAvlhpgsRLGRGCVVNSNAVIgsegfgfVPTPRGWRKMPQTGQVVLEDGVEV 218
Cdd:cd03359   24 LNGKTIIQSDVIIRGDL---------ATV------SIGRYCILSEGCVI-------RPPFKKFSKGVAFFPLHIGDYVFI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 219 GCGSTIDRPSVGetrigagskidNLVQIGHGVTTGRGCALASQVGIAGGAklghgVILAGQVgvanravvgdgaiassks 298
Cdd:cd03359   82 GENCVVNAAQIG-----------SYVHIGKNCVIGRRCIIKDCVKILDGT-----VVPPDTV------------------ 127

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 119371983 299 gihgeVAPGEVVSGYPAIPnrlwlrcsaaFSKLPEMAKTLRE 340
Cdd:cd03359  128 -----IPPYSVVSGRPARF----------IGELPECTQELME 154
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 138-186 8.51e-03

Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively at the C6 position of the nonreducing end glucosyl moiety. GAT specifically acetylates galactopyranosides. Furthermore, MAT shows higher affinity toward artificial substrates containing an alkyl or hydrophobic chain as well as a glucosyl unit. Active MAT and GAT are homotrimers, with each subunit consisting of an N-terminal alpha-helical region and a C-terminal left-handed parallel alpha-helix (LbH) subdomain with 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100047 [Multi-domain]  Cd Length: 169  Bit Score: 36.63  E-value: 8.51e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119371983 138 RIGANCIVHPGVVIY------------DDVE------VGEGCELHANAVLHPGSRLGRGCVVNSNAV 186
Cdd:cd03357   84 TIGDNVLIGPNVQIYtaghpldpeernRGLEyakpitIGDNVWIGGGVIILPGVTIGDNSVIGAGSV 150
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 101-188 8.60e-03

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 37.91  E-value: 8.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119371983 101 PRLRPLAEIHPSAVVDerAVVGPGTFIapRVC------IGASSRIGancivhPGVVIYDDVEVGEGC---ELHANAVLHP 171
Cdd:PLN02241 300 PRFLPPSKIEDCRITD--SIISHGCFL--RECkiehsvVGLRSRIG------EGVEIEDTVMMGADYyetEEEIASLLAE 369

                         90       100
                 ....*....|....*....|....*.
gi 119371983 172 G---------SRLgRGCVVNSNAVIG 188
Cdd:PLN02241 370 GkvpigigenTKI-RNAIIDKNARIG 394
 
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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