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Conserved domains on  [gi|502303567|ref|WP_012757318|]
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UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase [Rhizobium leguminosarum]

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
 12-344 5.86e-164

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


:

Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 461.53  E-value: 5.86e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567  12 GLKLAELAEFLGAELANSDhaDVVVRSVAPISRARAGDVCYILSRRNRDELATCEASAVICDKALADLVPPHIPVILSSN 91
Cdd:PRK00892   2 SLTLAELAELLGAELVGDG--DIEITGVASLEEAGPGQISFLANPKYRKQLATTKAGAVIVSPDDAEFVPAGNALLVVKN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567  92 PHAAFAMAGGLFYPAALRpvvfSGESEIAPSAVIDPSAKLEKGVIVEPMAVIGAHAEIGEGTRIGAQSIIGPNVKIGRDC 171
Cdd:PRK00892  80 PYLAFARLAQLFDPPATP----SPAAGIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADC 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 172 SIAAGASILCAL-LGNGVIIHNGARIGQDGFGYAPGPRGMIKIVQIGRVIIQDNVEIGANTSIDRGTMDDTVIGEGTKID 250
Cdd:PRK00892 156 RLHANVTIYHAVrIGNRVIIHSGAVIGSDGFGFANDRGGWVKIPQLGRVIIGDDVEIGANTTIDRGALDDTVIGEGVKID 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 251 NQVQIGHNVQIGRHCAIVAHVGIAGSAKIGNGVQIGGQVGIKGHVTIGDGVQIAAQSGIMTDLAAGGQY-GGTPGRPLND 329
Cdd:PRK00892 236 NLVQIAHNVVIGRHTAIAAQVGIAGSTKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEPGEYsSGIPAQPNKE 315

                        330
                 ....*....|....*
gi 502303567 330 YLRDVAQQMSRTKLR 344
Cdd:PRK00892 316 WLRTAARLRRLDELR 330
 
Name Accession Description Interval E-value
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 12-344 5.86e-164

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 461.53  E-value: 5.86e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567  12 GLKLAELAEFLGAELANSDhaDVVVRSVAPISRARAGDVCYILSRRNRDELATCEASAVICDKALADLVPPHIPVILSSN 91
Cdd:PRK00892   2 SLTLAELAELLGAELVGDG--DIEITGVASLEEAGPGQISFLANPKYRKQLATTKAGAVIVSPDDAEFVPAGNALLVVKN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567  92 PHAAFAMAGGLFYPAALRpvvfSGESEIAPSAVIDPSAKLEKGVIVEPMAVIGAHAEIGEGTRIGAQSIIGPNVKIGRDC 171
Cdd:PRK00892  80 PYLAFARLAQLFDPPATP----SPAAGIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADC 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 172 SIAAGASILCAL-LGNGVIIHNGARIGQDGFGYAPGPRGMIKIVQIGRVIIQDNVEIGANTSIDRGTMDDTVIGEGTKID 250
Cdd:PRK00892 156 RLHANVTIYHAVrIGNRVIIHSGAVIGSDGFGFANDRGGWVKIPQLGRVIIGDDVEIGANTTIDRGALDDTVIGEGVKID 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 251 NQVQIGHNVQIGRHCAIVAHVGIAGSAKIGNGVQIGGQVGIKGHVTIGDGVQIAAQSGIMTDLAAGGQY-GGTPGRPLND 329
Cdd:PRK00892 236 NLVQIAHNVVIGRHTAIAAQVGIAGSTKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEPGEYsSGIPAQPNKE 315

                        330
                 ....*....|....*
gi 502303567 330 YLRDVAQQMSRTKLR 344
Cdd:PRK00892 316 WLRTAARLRRLDELR 330
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 13-335 3.72e-157

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: 444.08  E-value: 3.72e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567  13 LKLAELAEFLGAELANsdHADVVVRSVAPISRARAGDVCYILSRRNRDELATCEASAVICDKALADLVPpHIPVILSSNP 92
Cdd:COG1044    2 FTLAELAELLGGELVG--DGDLEITGVAPLEEAGPGDLSFLANPKYAKQLATTKASAVIVPPDFAAALP-GLALIVVDNP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567  93 HAAFAMAGGLFYPAALRPvvfsgeSEIAPSAVIDPSAKLEKGVIVEPMAVIGAHAEIGEGTRIGAQSIIGPNVKIGRDCS 172
Cdd:COG1044   79 YLAFAKLLQLFYPPPAPA------PGIHPSAVIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 173 IAAGASIL-CALLGNGVIIHNGARIGQDGFGYAPGPRG-MIKIVQIGRVIIQDNVEIGANTSIDRGTMDDTVIGEGTKID 250
Cdd:COG1044  153 LHPNVTIYeRCVIGDRVIIHSGAVIGADGFGFAPDEDGgWVKIPQLGRVVIGDDVEIGANTTIDRGALGDTVIGDGTKID 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 251 NQVQIGHNVQIGRHCAIVAHVGIAGSAKIGNGVQIGGQVGIKGHVTIGDGVQIAAQSGIMTDLAAGGQYGGTPGRPLNDY 330
Cdd:COG1044  233 NLVQIAHNVRIGEHTAIAAQVGIAGSTKIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSGSPAQPHREW 312


                 ....*
gi 502303567 331 LRDVA 335
Cdd:COG1044  313 LRNAA 317
lipid_A_lpxD TIGR01853
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD; This model describes LpxD, an ...
 17-347 2.10e-131

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: 378.17  E-value: 2.10e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567   17 ELAEFLGAELanSDHADVVVRSVAPISRARAGDVCYILSRRNRDELATCEASAVICDKAlADLVPPHIPVILSSNPHAAF 96
Cdd:TIGR01853   1 ELAERLGAEL--KGNGDIVITGVAPLEKAKANHITFLANPKYLKHLKSSQAGAVIVSPD-DQGLPAKCAALVVKDPYLAF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567   97 AMAGGLFYPAALRpvvfsgESEIAPSAVIDPSAKLEKGVIVEPMAVIGAHAEIGEGTRIGAQSIIGPNVKIGRDCSIAAG 176
Cdd:TIGR01853  78 AKVAELFDPPPKR------EAGIHPTAVVDPSAKIGDGVTIGPNVVIGAGVEIGENVIIGPGVVIGDDVVIGDGSRIHPN 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567  177 ASILC-ALLGNGVIIHNGARIGQDGFGYAPGPRG-MIKIVQIGRVIIQDNVEIGANTSIDRGTMDDTVIGEGTKIDNQVQ 254
Cdd:TIGR01853 152 VVIYErVQLGKNVIIHSGAVIGSDGFGYAHTANGgHVKIPQIGRVIIEDDVEIGANTTIDRGAFDDTIIGEGTKIDNLVQ 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567  255 IGHNVQIGRHCAIVAHVGIAGSAKIGNGVQIGGQVGIKGHVTIGDGVQIAAQSGIMTDLAAGGQYGGTPGRPLNDYLRDV 334
Cdd:TIGR01853 232 IAHNCRIGENCIIVAQVGIAGSTKIGRNVIIGGQVGVAGHLEIGDNVTIGAKSGVTKSIPPPGVYGGIPARPNKEWLRIA 311

                         330
                  ....*....|...
gi 502303567  335 AQQMSRTKLRGTK 347
Cdd:TIGR01853 312 AKVKRLPELRKRI 324
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 128-331 4.80e-103

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: 301.63  E-value: 4.80e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 128 SAKLEKGVIVEPMAVIGAHAEIGEGTRIGAQSIIGPNVKIGRDCSIAAGASILC-ALLGNGVIIHNGARIGQDGFGYAPG 206
Cdd:cd03352    1 SAKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEgCIIGDRVIIHSGAVIGSDGFGFAPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 207 PRGMIKIVQIGRVIIQDNVEIGANTSIDRGTMDDTVIGEGTKIDNQVQIGHNVQIGRHCAIVAHVGIAGSAKIGNGVQIG 286
Cdd:cd03352   81 GGGWVKIPQLGGVIIGDDVEIGANTTIDRGALGDTVIGDGTKIDNLVQIAHNVRIGENCLIAAQVGIAGSTTIGDNVIIG 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 502303567 287 GQVGIKGHVTIGDGVQIAAQSGIMTDLAAGGQYGGTPGRPLNDYL 331
Cdd:cd03352  161 GQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQPHREWL 205
LpxD pfam04613
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase, LpxD; UDP-3-O-[3-hydroxymyristoyl] ...
 34-99 1.43e-16

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: 73.30  E-value: 1.43e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502303567   34 VVVRSVAPISRARAGDVCYILSRRNRDELATCEASAVICDKALADLVPPHIPVILSSNPHAAFAMA 99
Cdd:pfam04613   1 LEITGVAPLEEAGPGDLSFLANPKYAKYLATTKASAVIVPPDFAPQAPATATLLVVDNPYLAFAKL 66
 
Name Accession Description Interval E-value
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 12-344 5.86e-164

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 461.53  E-value: 5.86e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567  12 GLKLAELAEFLGAELANSDhaDVVVRSVAPISRARAGDVCYILSRRNRDELATCEASAVICDKALADLVPPHIPVILSSN 91
Cdd:PRK00892   2 SLTLAELAELLGAELVGDG--DIEITGVASLEEAGPGQISFLANPKYRKQLATTKAGAVIVSPDDAEFVPAGNALLVVKN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567  92 PHAAFAMAGGLFYPAALRpvvfSGESEIAPSAVIDPSAKLEKGVIVEPMAVIGAHAEIGEGTRIGAQSIIGPNVKIGRDC 171
Cdd:PRK00892  80 PYLAFARLAQLFDPPATP----SPAAGIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADC 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 172 SIAAGASILCAL-LGNGVIIHNGARIGQDGFGYAPGPRGMIKIVQIGRVIIQDNVEIGANTSIDRGTMDDTVIGEGTKID 250
Cdd:PRK00892 156 RLHANVTIYHAVrIGNRVIIHSGAVIGSDGFGFANDRGGWVKIPQLGRVIIGDDVEIGANTTIDRGALDDTVIGEGVKID 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 251 NQVQIGHNVQIGRHCAIVAHVGIAGSAKIGNGVQIGGQVGIKGHVTIGDGVQIAAQSGIMTDLAAGGQY-GGTPGRPLND 329
Cdd:PRK00892 236 NLVQIAHNVVIGRHTAIAAQVGIAGSTKIGRYCMIGGQVGIAGHLEIGDGVTITAMSGVTKSIPEPGEYsSGIPAQPNKE 315

                        330
                 ....*....|....*
gi 502303567 330 YLRDVAQQMSRTKLR 344
Cdd:PRK00892 316 WLRTAARLRRLDELR 330
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 13-335 3.72e-157

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: 444.08  E-value: 3.72e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567  13 LKLAELAEFLGAELANsdHADVVVRSVAPISRARAGDVCYILSRRNRDELATCEASAVICDKALADLVPpHIPVILSSNP 92
Cdd:COG1044    2 FTLAELAELLGGELVG--DGDLEITGVAPLEEAGPGDLSFLANPKYAKQLATTKASAVIVPPDFAAALP-GLALIVVDNP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567  93 HAAFAMAGGLFYPAALRPvvfsgeSEIAPSAVIDPSAKLEKGVIVEPMAVIGAHAEIGEGTRIGAQSIIGPNVKIGRDCS 172
Cdd:COG1044   79 YLAFAKLLQLFYPPPAPA------PGIHPSAVIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIGDDCV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 173 IAAGASIL-CALLGNGVIIHNGARIGQDGFGYAPGPRG-MIKIVQIGRVIIQDNVEIGANTSIDRGTMDDTVIGEGTKID 250
Cdd:COG1044  153 LHPNVTIYeRCVIGDRVIIHSGAVIGADGFGFAPDEDGgWVKIPQLGRVVIGDDVEIGANTTIDRGALGDTVIGDGTKID 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 251 NQVQIGHNVQIGRHCAIVAHVGIAGSAKIGNGVQIGGQVGIKGHVTIGDGVQIAAQSGIMTDLAAGGQYGGTPGRPLNDY 330
Cdd:COG1044  233 NLVQIAHNVRIGEHTAIAAQVGIAGSTKIGDNVVIGGQVGIAGHLTIGDGVIIGAQSGVTKSIPEGGVYSGSPAQPHREW 312


                 ....*
gi 502303567 331 LRDVA 335
Cdd:COG1044  313 LRNAA 317
lipid_A_lpxD TIGR01853
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase LpxD; This model describes LpxD, an ...
 17-347 2.10e-131

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: 378.17  E-value: 2.10e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567   17 ELAEFLGAELanSDHADVVVRSVAPISRARAGDVCYILSRRNRDELATCEASAVICDKAlADLVPPHIPVILSSNPHAAF 96
Cdd:TIGR01853   1 ELAERLGAEL--KGNGDIVITGVAPLEKAKANHITFLANPKYLKHLKSSQAGAVIVSPD-DQGLPAKCAALVVKDPYLAF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567   97 AMAGGLFYPAALRpvvfsgESEIAPSAVIDPSAKLEKGVIVEPMAVIGAHAEIGEGTRIGAQSIIGPNVKIGRDCSIAAG 176
Cdd:TIGR01853  78 AKVAELFDPPPKR------EAGIHPTAVVDPSAKIGDGVTIGPNVVIGAGVEIGENVIIGPGVVIGDDVVIGDGSRIHPN 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567  177 ASILC-ALLGNGVIIHNGARIGQDGFGYAPGPRG-MIKIVQIGRVIIQDNVEIGANTSIDRGTMDDTVIGEGTKIDNQVQ 254
Cdd:TIGR01853 152 VVIYErVQLGKNVIIHSGAVIGSDGFGYAHTANGgHVKIPQIGRVIIEDDVEIGANTTIDRGAFDDTIIGEGTKIDNLVQ 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567  255 IGHNVQIGRHCAIVAHVGIAGSAKIGNGVQIGGQVGIKGHVTIGDGVQIAAQSGIMTDLAAGGQYGGTPGRPLNDYLRDV 334
Cdd:TIGR01853 232 IAHNCRIGENCIIVAQVGIAGSTKIGRNVIIGGQVGVAGHLEIGDNVTIGAKSGVTKSIPPPGVYGGIPARPNKEWLRIA 311

                         330
                  ....*....|...
gi 502303567  335 AQQMSRTKLRGTK 347
Cdd:TIGR01853 312 AKVKRLPELRKRI 324
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 128-331 4.80e-103

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: 301.63  E-value: 4.80e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 128 SAKLEKGVIVEPMAVIGAHAEIGEGTRIGAQSIIGPNVKIGRDCSIAAGASILC-ALLGNGVIIHNGARIGQDGFGYAPG 206
Cdd:cd03352    1 SAKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEgCIIGDRVIIHSGAVIGSDGFGFAPD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 207 PRGMIKIVQIGRVIIQDNVEIGANTSIDRGTMDDTVIGEGTKIDNQVQIGHNVQIGRHCAIVAHVGIAGSAKIGNGVQIG 286
Cdd:cd03352   81 GGGWVKIPQLGGVIIGDDVEIGANTTIDRGALGDTVIGDGTKIDNLVQIAHNVRIGENCLIAAQVGIAGSTTIGDNVIIG 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 502303567 287 GQVGIKGHVTIGDGVQIAAQSGIMTDLAAGGQYGGTPGRPLNDYL 331
Cdd:cd03352  161 GQVGIAGHLTIGDGVVIGAGSGVTSIVPPGEYVSGTPAQPHREWL 205
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 116-326 5.45e-34

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: 125.90  E-value: 5.45e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 116 ESEIAPSAVIDPSAKLEKGVIVEPMAVIGAHAEIGEGTRIGAQSIIGPNVKIGRDCSIAAGASIlcallgngviihnGAr 195
Cdd:COG1043    1 MAMIHPTAIVDPGAKLGENVEIGPFCVIGPDVEIGDGTVIGSHVVIEGPTTIGKNNRIFPFASI-------------GE- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 196 IGQDgFGYAPGPrgmikivqiGRVIIQDNVEIGANTSIDRGTMDD---TVIGEGTKIDNQVQIGHNVQIGRHCAIVAHVG 272
Cdd:COG1043   67 EPQD-LKYKGEP---------TRLEIGDNNTIREFVTIHRGTVQGggvTRIGDDNLLMAYVHVAHDCVVGNNVILANNAT 136

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 502303567 273 IAGSAKIGNGVQIGGQVGIKGHVTIGDGVQIAAQSGIMTDLAAGGQYGGTPGRP 326
Cdd:COG1043  137 LAGHVEVGDHAIIGGLSAVHQFVRIGAHAMVGGGSGVVKDVPPYVLAAGNPARL 190
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 119-326 6.02e-34

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: 125.62  E-value: 6.02e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 119 IAPSAVIDPSAKLEKGVIVEPMAVIGAHAEIGEGTRIGAQSIIGPNVKIGRDCsiaagasilcallgngvIIHNGARIG- 197
Cdd:cd03351    2 IHPTAIVDPGAKIGENVEIGPFCVIGPNVEIGDGTVIGSHVVIDGPTTIGKNN-----------------RIFPFASIGe 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 198 --QDgFGYAPGPRgmikivqigRVIIQDNVEIGANTSIDRGTMDD---TVIGEGTKIDNQVQIGHNVQIGRHCAIVAHVG 272
Cdd:cd03351   65 apQD-LKYKGEPT---------RLEIGDNNTIREFVTIHRGTAQGggvTRIGNNNLLMAYVHVAHDCVIGNNVILANNAT 134

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 502303567 273 IAGSAKIGNGVQIGGQVGIKGHVTIGDGVQIAAQSGIMTDLAAGGQYGGTPGRP 326
Cdd:cd03351  135 LAGHVEIGDYAIIGGLSAVHQFCRIGRHAMVGGGSGVVQDVPPYVIAAGNRARL 188
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
117-326 2.60e-30

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 116.35  E-value: 2.60e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 117 SEIAPSAVIDPSAKLEKGVIVEPMAVIGAHAEIGEGTRIGAQSIIGPNVKIGRDCSIAAGASIlcallgngviihnGArI 196
Cdd:PRK05289   3 AKIHPTAIVEPGAKIGENVEIGPFCVIGPNVVIGDGTVIGSHVVIDGHTTIGKNNRIFPFASI-------------GE-D 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 197 GQDgFGYAPGPRgmikivqigRVIIQDNVEIGANTSIDRGTMDD---TVIGEGTKIDNQVQIGHNVQIGRHCAIVAHVGI 273
Cdd:PRK05289  69 PQD-LKYKGEPT---------RLVIGDNNTIREFVTINRGTVQGggvTRIGDNNLLMAYVHVAHDCVVGNHVILANNATL 138

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 502303567 274 AGSAKIGNGVQIGGQVGIKGHVTIGDGVQIAAQSGIMTDLAAGGQYGGTPGRP 326
Cdd:PRK05289 139 AGHVEVGDYAIIGGLTAVHQFVRIGAHAMVGGMSGVSQDVPPYVLAEGNPARL 191
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 119-313 4.17e-27

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 107.42  E-value: 4.17e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 119 IAPSAVIDPSAKLEKGVIVEPMAVIGAHAEIGEGTRIGAQSIIGPNVKIGRDCSiaagasilcallgngviIHNGARIGQ 198
Cdd:PRK12461   2 IHPTAVIDPSAKLGSGVEIGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNK-----------------IHQGAVVGD 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 199 D--GFGYAPGPrgmikivqiGRVIIQDNVEIGANTSIDRGTMDDTV--IGEGTKIDNQVQIGHNVQIGRHCAIVAHVGIA 274
Cdd:PRK12461  65 EpqDFTYKGEE---------SRLEIGDRNVIREGVTIHRGTKGGGVtrIGNDNLLMAYSHVAHDCQIGNNVILVNGALLA 135

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 502303567 275 GSAKIGNGVQIGGQVGIKGHVTIGDGVQIAAQSGIMTDL 313
Cdd:PRK12461 136 GHVTVGDRAIISGNCLVHQFCRIGALAMMAGGSRISKDV 174
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 119-326 3.20e-24

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


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 99.64  E-value: 3.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567  119 IAPSAVIDPSAKLEKGVIVEPMAVIGAHAEIGEGTRIGAQSIIGPNVKIGRDCSIAAGASILCAllgngviihngariGQ 198
Cdd:TIGR01852   1 IHPTAIIEPGAEIGENVEIGPFCIVGPGVKIGDGVELKSHVVILGHTTIGEGTRIFPGAVIGGV--------------PQ 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567  199 DgFGYAPGPrgmikivqiGRVIIQDNVEIGANTSIDRGTMDD---TVIGEGTKIDNQVQIGHNVQIGRHCAIVAHVGIAG 275
Cdd:TIGR01852  67 D-LKYKGEK---------TRLIIGDNNTIREFVTINRGTASGggvTRIGNNNLLMAYSHIAHDCVVGNHVILANNATLAG 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 502303567  276 SAKIGNGVQIGGQVGIKGHVTIGDGVQIAAQSGIMTDLAAGGQYGGTPGRP 326
Cdd:TIGR01852 137 HVEVGDYAIIGGLVAVHQFVRIGRYAMIGGLSAVSKDVPPYCLAEGNRARL 187
LpxD pfam04613
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase, LpxD; UDP-3-O-[3-hydroxymyristoyl] ...
 34-99 1.43e-16

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: 73.30  E-value: 1.43e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502303567   34 VVVRSVAPISRARAGDVCYILSRRNRDELATCEASAVICDKALADLVPPHIPVILSSNPHAAFAMA 99
Cdd:pfam04613   1 LEITGVAPLEEAGPGDLSFLANPKYAKYLATTKASAVIVPPDFAPQAPATATLLVVDNPYLAFAKL 66
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
211-327 1.45e-13

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 67.20  E-value: 1.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 211 IKIVQIGRVIIQDNVEIGANTSIDRGTM---DDTVIGEGTKIDNQ--VQIGHNVQIGRHCAIVAH----------VGIAG 275
Cdd:COG0110    1 MKLLLLFGARIGDGVVIGPGVRIYGGNItigDNVYIGPGVTIDDPggITIGDNVLIGPGVTILTGnhpiddpatfPLRTG 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 502303567 276 SAKIGNGVQIGGQVGIKGHVTIGDGVQIAAQSGIMTDLAAGGQYGGTPGRPL 327
Cdd:COG0110   81 PVTIGDDVWIGAGATILPGVTIGDGAVVGAGSVVTKDVPPYAIVAGNPARVI 132
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 218-323 3.43e-13

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: 67.51  E-value: 3.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 218 RVIIQDNVEIGANTSIDRgtmdDTVIGEGTKIDNQVQIGHNVQIGRHCAIVAHVGIAGSAKIGNGVQIGGQVGIKGHVTI 297
Cdd:cd03360   96 SAVIGEGCVIMAGAVINP----DARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVLSGGVTIGEGAFIGAGATIIQGVTI 171

                         90       100
                 ....*....|....*....|....*.
gi 502303567 298 GDGVQIAAQSGIMTDLAAGGQYGGTP 323
Cdd:cd03360  172 GAGAIIGAGAVVTKDVPDGSVVVGNP 197
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 218-323 1.85e-11

sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff.


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 62.51  E-value: 1.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567  218 RVIIQDNVEIGANTSIDRGTM--DDTVIGEGTKIDNQVQIGHNVQIGRHCAIVAHVGIAGSAKIGNGVQIGGQVGIKGHV 295
Cdd:TIGR03570  93 SAIVSPSASIGEGTVIMAGAVinPDVRIGDNVIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVIGEGVFIGAGATIIQGV 172

                          90       100
                  ....*....|....*....|....*...
gi 502303567  296 TIGDGVQIAAQSGIMTDLAAGGQYGGTP 323
Cdd:TIGR03570 173 TIGAGAIVGAGAVVTKDIPDGGVVVGVP 200
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 119-233 3.59e-11

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: 61.73  E-value: 3.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 119 IAPSAVIDPSAKLEKGVIVEPMAVIGAHAEIGEGTRIGAQSIIGPNVKIGRDCSIAAGASIlcallGNGVIIHNGARIGq 198
Cdd:cd03360   87 IHPSAVVSPSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIGHDCVIGDFVHIAPGVVL-----SGGVTIGEGAFIG- 160

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 502303567 199 dgfgyapgprgmikivqIGRVIIQdNVEIGANTSI 233
Cdd:cd03360  161 -----------------AGATIIQ-GVTIGAGAII 177
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 125-316 1.07e-10

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 62.35  E-value: 1.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 125 IDPSAKLEKGVIVEPMAVIGAHAEIGEGTRIGAQSIIgpnvkigRDCSIAAGASILCALLgNGVIIHNGARIGQdgfgYA 204
Cdd:COG1207  263 IDGDVEIGRDVVIDPNVILEGKTVIGEGVVIGPNCTL-------KDSTIGDGVVIKYSVI-EDAVVGAGATVGP----FA 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 205 ---PGprgmikivqigrviiqdnveigantsidrgtmddTVIGEGTKIDNQVQIgHNVQIGRHcAIVAHVGIAGSAKIGN 281
Cdd:COG1207  331 rlrPG----------------------------------TVLGEGVKIGNFVEV-KNSTIGEG-SKVNHLSYIGDAEIGE 374

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 282 GVQIG-GQV-----GIKGH-------------------VTIGDGVQIAAQSGIMTDLAAG 316
Cdd:COG1207  375 GVNIGaGTItcnydGVNKHrtvigdgafigsntnlvapVTIGDGATIGAGSTITKDVPAG 434
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 131-316 5.11e-10

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 60.62  E-value: 5.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 131 LEKGV-IVEPMAV-IGAHAEIGEGTRIGAQSIIGPNVKIGRDCSIAAGASILCALLGNGVIIHNGarigqdgfgyapgpr 208
Cdd:PRK14354 248 MVNGVtIIDPESTyIDADVEIGSDTVIEPGVVIKGNTVIGEDCVIGPGSRIVDSTIGDGVTITNS--------------- 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 209 gmikivQIGRVIIQDNVEIGANTSIDRGtmddTVIGEGTKIDNQVQIgHNVQIGRHcAIVAHVGIAGSAKIGNGVQIG-G 287
Cdd:PRK14354 313 ------VIEESKVGDNVTVGPFAHLRPG----SVIGEEVKIGNFVEI-KKSTIGEG-TKVSHLTYIGDAEVGENVNIGcG 380

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 502303567 288 QV-----GIKGH-------------------VTIGDGVQIAAQSGIMTDLAAG 316
Cdd:PRK14354 381 TItvnydGKNKFktiigdnafigcnsnlvapVTVGDNAYIAAGSTITKDVPED 433
PRK10502 PRK10502
putative acyl transferase; Provisional
 239-329 7.08e-10

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 57.65  E-value: 7.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 239 DDTVIGEGTKIDN--QVQIGHNVQI--------GRHCAIVAHVG-IAGSAKIGNGVQIGGQVGIKGHVTIGDGVQIAAQS 307
Cdd:PRK10502  76 DYAWIGDDVWLYNlgEITIGAHCVIsqksylctGSHDYSDPHFDlNTAPIVIGEGCWLAADVFVAPGVTIGSGAVVGARS 155

                         90       100
                 ....*....|....*....|..
gi 502303567 308 GIMTDLAAGGQYGGTPGRPLND 329
Cdd:PRK10502 156 SVFKSLPANTICRGNPAVPIRP 177
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 119-316 7.83e-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: 57.82  E-value: 7.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 119 IAPSAV-IDPSAKLEKGVIVEPMAVIGAHAEIGEGTRIGAQSIIgpnvkigRDCSIAAGASILCALLGNGVIIHNGARIG 197
Cdd:cd03353    5 IDPETTyIDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVI-------KDSTIGDGVVIKASSVIEGAVIGNGATVG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 198 QdgFGYapgprgmikivqigrviIQDNVEIGANTSIdrGT---MDDTVIGEGTKI-------DnqVQIGHNVQIGrhcai 267
Cdd:cd03353   78 P--FAH-----------------LRPGTVLGEGVHI--GNfveIKKSTIGEGSKAnhlsylgD--AEIGEGVNIG----- 129

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502303567 268 vahvgiAGS------------AKIGNGVQIGGQVGIKGHVTIGDGVQIAAQSGIMTDLAAG 316
Cdd:cd03353  130 ------AGTitcnydgvnkhrTVIGDNVFIGSNSQLVAPVTIGDGATIAAGSTITKDVPPG 184
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 221-323 8.94e-10

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: 55.14  E-value: 8.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 221 IQDNVEIGANTSIDRGTmdDTVIGEGTKIDNQVQIGHNVQIGRhcaiVAHVGIAGSAKIGNGVQIGGQVGIKGHVTIGDG 300
Cdd:cd03354    5 IHPGAKIGPGLFIDHGT--GIVIGETAVIGDNCTIYQGVTLGG----KGKGGGKRHPTIGDNVVIGAGAKILGNITIGDN 78

                         90       100
                 ....*....|....*....|...
gi 502303567 301 VQIAAQSGIMTDLAAGGQYGGTP 323
Cdd:cd03354   79 VKIGANAVVTKDVPANSTVVGVP 101
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 221-327 2.56e-09

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


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 54.43  E-value: 2.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 221 IQDNVEIGANTSIDRgtmdDTVIGEGTKIDNQVQIGHNVQIGRHCAIVAHVGIA---------------GSAKIGNGVQI 285
Cdd:cd03358    1 IGDNCIIGTNVFIEN----DVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFTndlyprskiyrkwelKGTTVKRGASI 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 502303567 286 GGQVGIKGHVTIGDGVQIAAQSGIMTDLAAGGQYGGTPGRPL 327
Cdd:cd03358   77 GANATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARII 118
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 224-327 4.28e-09

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: 53.61  E-value: 4.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 224 NVEIGANTSIDRGTmddtVIGEGTKIDnqvqIGHNVQIGRHCAIVAH-------------VGIAGSAKIGNGVQIGGQVG 290
Cdd:cd04647    1 NISIGDNVYIGPGC----VISAGGGIT----IGDNVLIGPNVTIYDHnhdiddperpieqGVTSAPIVIGDDVWIGANVV 72

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 502303567 291 IKGHVTIGDGVQIAAQSGIMTDLAAGGQYGGTPGRPL 327
Cdd:cd04647   73 ILPGVTIGDGAVVGAGSVVTKDVPPNSIVAGNPAKVI 109
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 119-233 7.44e-09

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: 54.81  E-value: 7.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567  119 IAPSAVIDPSAKLEKGVIVEPMAVIGAhaeigeGTRIGAQSIIGPNVKIGRDCSIAAGASILC-ALLGNGVIIHNGARIG 197
Cdd:TIGR03570  90 IHPSAIVSPSASIGEGTVIMAGAVINP------DVRIGDNVIINTGAIVEHDCVIGDFVHIAPgVTLSGGVVIGEGVFIG 163

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 502303567  198 qdgfgyapgprgmikivqIGRVIIQdNVEIGANTSI 233
Cdd:TIGR03570 164 ------------------AGATIIQ-GVTIGAGAIV 180
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 122-307 8.52e-09

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 56.47  E-value: 8.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 122 SAVIDPSAKLEKGVIVEPMAVIGAHAEIGEGTRIGAQSIIgPNVKIGRDCSIAagasilcallgNGVIIHngARIGqdgf 201
Cdd:PRK14360 256 SCTISETVELGPDVIIEPQTHLRGNTVIGSGCRIGPGSLI-ENSQIGENVTVL-----------YSVVSD--SQIG---- 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 202 gyapgprgmikivqigrviiqDNVEIGANTSIdRGtmdDTVIGEGTKIDNQVQIgHNVQIGRHCAiVAHVGIAGSAKIGN 281
Cdd:PRK14360 318 ---------------------DGVKIGPYAHL-RP---EAQIGSNCRIGNFVEI-KKSQLGEGSK-VNHLSYIGDATLGE 370

                        170       180       190
                 ....*....|....*....|....*....|...
gi 502303567 282 GVQIG-GQV-----GIKGHVT-IGDGVQIAAQS 307
Cdd:PRK14360 371 QVNIGaGTItanydGVKKHRTvIGDRSKTGANS 403
PLN02357 PLN02357
serine acetyltransferase
 225-325 5.31e-08

serine acetyltransferase


Pssm-ID: 215205 [Multi-domain]  Cd Length: 360  Bit Score: 54.12  E-value: 5.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 225 VEIGANTSIDRGTMDD----TVIGEGTKIDNQVQIGHNVQIG--------RHcaivahvgiagsAKIGNGVQIGGQVGIK 292
Cdd:PLN02357 227 VDIHPGAKIGQGILLDhatgVVIGETAVVGNNVSILHNVTLGgtgkqsgdRH------------PKIGDGVLIGAGTCIL 294

                         90       100       110
                 ....*....|....*....|....*....|...
gi 502303567 293 GHVTIGDGVQIAAQSGIMTDLAAGGQYGGTPGR 325
Cdd:PLN02357 295 GNITIGEGAKIGAGSVVLKDVPPRTTAVGNPAR 327
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 224-327 7.07e-08

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: 49.91  E-value: 7.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 224 NVEIGANTSIdrgtmddtviGEGTKIDNQ--VQIGHNVQIGRHCAI---------VAHVGIAGSAKIGNGVQIGGQVGIK 292
Cdd:cd05825    3 NLTIGDNSWI----------GEGVWIYNLapVTIGSDACISQGAYLctgshdyrsPAFPLITAPIVIGDGAWVAAEAFVG 72

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 502303567 293 GHVTIGDGVQIAAQSGIMTDLAAGGQYGGTPGRPL 327
Cdd:cd05825   73 PGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAVPV 107
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 131-307 1.12e-07

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 53.23  E-value: 1.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 131 LEKGV-IVEPMAV-IGAHAEIGEGTRIGAQSIIGPNVKIGRDCSIAAGASILCALLGNGVIIHNGarigqdgfgyapgpr 208
Cdd:PRK14357 238 MENGVtILDPNTTyIHYDVEIGMDTIIYPMTFIEGKTRIGEDCEIGPMTRIVDCEIGNNVKIIRS--------------- 302

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 209 gmikivQIGRVIIQDNVEIGANTSIDRGtmddTVIGEGTKIDNQVQIgHNVQIGRHCAiVAHVGIAGSAKIGNGVQIGGQ 288
Cdd:PRK14357 303 ------ECEKSVIEDDVSVGPFSRLREG----TVLKKSVKIGNFVEI-KKSTIGENTK-AQHLTYLGDATVGKNVNIGAG 370

                        170       180
                 ....*....|....*....|....*.
gi 502303567 289 V------GIKGHVT-IGDGVQIAAQS 307
Cdd:PRK14357 371 TitcnydGKKKNPTfIEDGAFIGSNS 396
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 117-256 1.16e-07

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 52.95  E-value: 1.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 117 SEIAPSAVIDPSAKLEKGVIVEPMAVIGaHAEigegtrigaQSIIGPNVKIGRdcsiaaGASIlcallgNGVIIHNGARI 196
Cdd:PRK05293 277 NPNLPPQYIAENAKVKNSLVVEGCVVYG-TVE---------HSVLFQGVQVGE------GSVV------KDSVIMPGAKI 334

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 197 GQDgfgyapgprgmikiVQIGRVIIQDNVEIGANTSIDRGTMDDTVIGEGTKIDNQVQIG 256
Cdd:PRK05293 335 GEN--------------VVIERAIIGENAVIGDGVIIGGGKEVITVIGENEVIGVGTVIG 380
PLN02694 PLN02694
serine O-acetyltransferase
 212-325 1.25e-07

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 52.34  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 212 KIVQIGRVIIQDNVEIGANTSIDRGTmdDTVIGEGTKIDNQVQIGHNVQIGrhcaivaHVGIAGS---AKIGNGVQIGGQ 288
Cdd:PLN02694 154 RISDVFAVDIHPAAKIGKGILFDHAT--GVVIGETAVIGNNVSILHHVTLG-------GTGKACGdrhPKIGDGVLIGAG 224

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 502303567 289 VGIKGHVTIGDGVQIAAQSGIMTDLAAGGQYGGTPGR 325
Cdd:PLN02694 225 ATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPAR 261
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 119-249 4.29e-07

Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; Tetrahydrodipicolinate N-succinyltransferase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 441774 [Multi-domain]  Cd Length: 268  Bit Score: 50.50  E-value: 4.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 119 IAPSAVIDPSAKLEKGVIVEPMAV-IGAHaeIGEGTRIGAQSIIGPNVKIGRDCSIAAGASILCALLGngviihngarig 197
Cdd:COG2171  100 IVPGARVRLGAYLAPGVVLMPSFVnIGAY--VDEGTMVDTWATVGSCAQIGKNVHLSGGAGIGGVLEP------------ 165

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 198 qdgfgyapgprgmikiVQIGRVIIQDNVEIGANTSIDRGTM--DDTVIGEG------TKI 249
Cdd:COG2171  166 ----------------LQAAPVIIEDNCFIGARSGVVEGVIvgEGAVLGAGvyltasTKI 209
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 116-249 4.38e-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: 49.12  E-value: 4.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 116 ESEIAPSAVIDPSAKLEKGVIVEPMAVIGAHAEIGEGTRIGAQ------SIIGPNVKIGRDCSIAA-------------- 175
Cdd:cd05636    5 EGTVEEGVTIKGPVWIGEGAIVRSGAYIEGPVIIGKGCEIGPNayirgyTVLGDGCVVGNSVEVKNsiimdgtkvphlny 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 176 -GASILCAL--LGNGVIIHN------GARIGQDGfgyapgprgmiKIVQIGR----VIIQDNVEIGANTSIDRGtmddTV 242
Cdd:cd05636   85 vGDSVLGENvnLGAGTITANlrfddkPVKVRLKG-----------ERVDTGRrklgAIIGDGVKTGINVSLNPG----VK 149


                 ....*..
gi 502303567 243 IGEGTKI 249
Cdd:cd05636  150 IGPGSWV 156
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 216-327 5.05e-07

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 48.87  E-value: 5.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 216 IGRVIIQDNVEIGANTSIdRGTMDDTVIGEGTKI-DN---------QVQIGHNVQIGrHCAIVaHvgiagSAKIGNGVQI 285
Cdd:COG0663   26 IGDVTIGEDVSVWPGAVL-RGDVGPIRIGEGSNIqDGvvlhvdpgyPLTIGDDVTIG-HGAIL-H-----GCTIGDNVLI 97

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 502303567 286 GGQVGIKGHVTIGDGVQIAAQSGIM--TDLAAGGQYGGTPGRPL 327
Cdd:COG0663   98 GMGAIVLDGAVIGDGSIVGAGALVTegKVVPPGSLVVGSPAKVV 141
PLN02739 PLN02739
serine acetyltransferase
 212-325 7.86e-07

serine acetyltransferase


Pssm-ID: 215394 [Multi-domain]  Cd Length: 355  Bit Score: 50.42  E-value: 7.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 212 KIVQIGRVIIQDNVEIGANTSIDRGTmdDTVIGEGTKIDNQVQIGHNVQIG--------RHcaivahvgiagsAKIGNGV 283
Cdd:PLN02739 199 RVSEVFGIDIHPAARIGKGILLDHGT--GVVIGETAVIGDRVSILHGVTLGgtgketgdRH------------PKIGDGA 264

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 502303567 284 QIGGQVGIKGHVTIGDGVQIAAQSGIMTDLAAGGQYGGTPGR 325
Cdd:PLN02739 265 LLGACVTILGNISIGAGAMVAAGSLVLKDVPSHSMVAGNPAK 306
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 160-249 8.23e-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: 8.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 160 IIGPNVKIGRDCSIAAGASILcalLGNGVIIHNGARIGQDGFGYAPGPRGMIKIVQIGRVIIQDNVEIGANTSIdrgtMD 239
Cdd:cd04647    3 SIGDNVYIGPGCVISAGGGIT---IGDNVLIGPNVTIYDHNHDIDDPERPIEQGVTSAPIVIGDDVWIGANVVI----LP 75

                         90
                 ....*....|
gi 502303567 240 DTVIGEGTKI 249
Cdd:cd04647   76 GVTIGDGAVV 85
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 149-249 8.29e-07

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


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 46.08  E-value: 8.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 149 IGEGTRIGAQSIIGPNVkIGRDCSIAAGASILCALLGNGVIIHNGARIGQDgfgyapgprgmikivqigrvIIQDNVEIG 228
Cdd:cd03356    2 IGESTVIGENAIIKNSV-IGDNVRIGDGVTITNSILMDNVTIGANSVIVDS--------------------IIGDNAVIG 60

                         90       100
                 ....*....|....*....|.
gi 502303567 229 ANTSIDrgtmDDTVIGEGTKI 249
Cdd:cd03356   61 ENVRVV----NLCIIGDDVVV 77
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 119-268 1.43e-06

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


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 46.99  E-value: 1.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 119 IAPSAVIDPSAKLEKGVIVEPMAVIGAHAEIGEGTRIGAQSIIGPNVKIGRDCSIAAGASIlcallgngviihngarigq 198
Cdd:cd03350    4 VPPGAIIRDGAFIGPGAVLMMPSYVNIGAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVI------------------- 64

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 199 dgfgyapgpRGMIKIVQIGRVIIQDNVEIGANtsidrgtmddTVIGEGTKIDNQVQIGHNVQIGRHCAIV 268
Cdd:cd03350   65 ---------GGVLEPLQATPVIIEDDVFIGAN----------CEVVEGVIVGKGAVLAAGVVLTQSTPIY 115
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 118-197 2.42e-06

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 46.94  E-value: 2.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 118 EIAPSAVIDPSA------KLEKGVIVEPMAVI---GAHAEIGEGTRIGAQSII----GPNVKIGRDCSIAAGAsIL--C- 181
Cdd:COG0663   12 QIHPSAFVAPTAvvigdvTIGEDVSVWPGAVLrgdVGPIRIGEGSNIQDGVVLhvdpGYPLTIGDDVTIGHGA-ILhgCt 90

                         90       100
                 ....*....|....*....|
gi 502303567 182 ----ALLGNGVIIHNGARIG 197
Cdd:COG0663   91 igdnVLIGMGAIVLDGAVIG 110
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 216-327 2.64e-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: 2.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 216 IGRVIIQDNVEIGANTSIdRGTMDDTVIGEGTKI-DN---------QVQIGHNVQIGrHCAIVaHvgiagSAKIGNGVQI 285
Cdd:cd04645   15 IGDVTLGEGSSVWFGAVL-RGDVNPIRIGERTNIqDGsvlhvdpgyPTIIGDNVTVG-HGAVL-H-----GCTIGDNCLI 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 502303567 286 GGQVGIKGHVTIGDGVQIAAQSGIM--TDLAAGGQYGGTPGRPL 327
Cdd:cd04645   87 GMGAIILDGAVIGKGSIVAAGSLVPpgKVIPPGSLVAGSPAKVV 130
LbH_MAT_GAT cd03357
Maltose O-acetyltransferase (MAT) and Galactoside O-acetyltransferase (GAT): MAT and GAT ...
 224-327 2.74e-06

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: 47.03  E-value: 2.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 224 NVEIGANTSIDRG-TMDDTvigegtkidNQVQIGHNVQIGRHCAIV------------AHVGIAGSAKIGNGVQIGGQVG 290
Cdd:cd03357   62 NIHIGDNFYANFNcTILDV---------APVTIGDNVLIGPNVQIYtaghpldpeernRGLEYAKPITIGDNVWIGGGVI 132

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 502303567 291 IKGHVTIGDGVQIAAQSGIMTDLAAGGQYGGTPGRPL 327
Cdd:cd03357  133 ILPGVTIGDNSVIGAGSVVTKDIPANVVAAGNPARVI 169
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 121-249 3.66e-06

2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 47.88  E-value: 3.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 121 PSAVIDPSAKLEKGVIVEPMAV-IGAHaeIGEGTRIGAQSIIGPNVKIGRDCSIAAGASIlcallgNGVIihngarigqd 199
Cdd:PRK11830 108 PGAVVRRGAYIAPNVVLMPSYVnIGAY--VDEGTMVDTWATVGSCAQIGKNVHLSGGVGI------GGVL---------- 169

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 502303567 200 gfgyAPgprgmikiVQIGRVIIQDNVEIGANTSIDRGTM--DDTVIGEGTKI 249
Cdd:PRK11830 170 ----EP--------LQANPVIIEDNCFIGARSEVVEGVIveEGSVLGMGVFL 209
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 242-307 4.56e-06

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: 44.16  E-value: 4.56e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502303567 242 VIGEGTKIDNQVQIGHNVQIGRHCAIVAHVGIAG--------SAKIGNGVQIGGQVGIKGHVTIGDGVQIAAQS 307
Cdd:cd00208    2 FIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAatgpneknPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGA 75
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 87-316 5.09e-06

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 48.20  E-value: 5.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567  87 ILSSNPHAAFAMAGGLFYPAALRPVVFSGESEIAPSAV-IDPSAKLEKGVIVEPMAVIGAHAEIGEGTRIGAQSIIgPNV 165
Cdd:PRK14355 226 IMGVNDRAQLAEAARVLRRRINRELMLAGVTLIDPETTyIDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVI-KGC 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 166 KIGRDCSIAAGASILCALLGNGVIIHNGARIgqdgfgyAPGprgmikivqigrVIIQDNVEIGANTSIDRgtmddTVIGE 245
Cdd:PRK14355 305 RIGDDVTVKAGSVLEDSVVGDDVAIGPMAHL-------RPG------------TELSAHVKIGNFVETKK-----IVMGE 360

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 246 GTKIDN-----QVQIGHNVQIGrhCAIVAhVGIAGSAK----IGNGVQIGGQVGIKGHVTIGDGVQIAAQSGIMTDLAAG 316
Cdd:PRK14355 361 GSKASHltylgDATIGRNVNIG--CGTIT-CNYDGVKKhrtvIEDDVFVGSDVQFVAPVTVGRNSLIAAGTTVTKDVPPD 437
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 117-180 6.42e-06

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: 43.78  E-value: 6.42e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502303567 117 SEIAPSAVIDPSAKLEKGVIVEPMAVIGA--------HAEIGEGTRIGAQSIIGPNVKIGRDCSIAAGASIL 180
Cdd:cd00208    7 VKIHPKAVIRGPVVIGDNVNIGPGAVIGAatgpneknPTIIGDNVEIGANAVIHGGVKIGDNAVIGAGAVVT 78
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 143-231 1.18e-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: 1.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 143 IGAHAEIGEGTRIGAQS--IIGPNVKIGRDCSIAAGASI---------LCALLGNGVIIHNGARIgqdgfgyapgprgmi 211
Cdd:cd03354    5 IHPGAKIGPGLFIDHGTgiVIGETAVIGDNCTIYQGVTLggkgkgggkRHPTIGDNVVIGAGAKI--------------- 69

                         90       100
                 ....*....|....*....|
gi 502303567 212 kivqIGRVIIQDNVEIGANT 231
Cdd:cd03354   70 ----LGNITIGDNVKIGANA 85
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 119-177 1.68e-05

sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff.


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 45.18  E-value: 1.68e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 502303567  119 IAPSAVIDPSAKLEKGVIVEPMAVIGAHAEIGEGTRIGAQSIIGPNVKIGRDCSIAAGA 177
Cdd:TIGR03570 126 INTGAIVEHDCVIGDFVHIAPGVTLSGGVVIGEGVFIGAGATIIQGVTIGAGAIVGAGA 184
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 214-347 1.75e-05

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: 44.28  E-value: 1.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 214 VQIGRVIIQDNVEIGANTSIdRGTMDDTVIGEGTKI-DNQVQIGHNvqiGRHCAI-----VAHVGIAGSAKIGNGVQIGG 287
Cdd:cd04745   14 VLIGDVIIGKNCYIGPHASL-RGDFGRIVIRDGANVqDNCVIHGFP---GQDTVLeenghIGHGAILHGCTIGRNALVGM 89

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502303567 288 QVGIKGHVTIGDGVQIAAQSGIM--TDLAAGGQYGGTPGRplndYLRDVAQQMSRTKLRGTK 347
Cdd:cd04745   90 NAVVMDGAVIGEESIVGAMAFVKagTVIPPRSLIAGSPAK----VIRELSDEEVAWKTRGTK 147
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 216-307 2.09e-05

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: 44.15  E-value: 2.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 216 IGRVIIQDNVEIGANTSIdRGTmddtvigEGTKIdnQVQIGHNVQIGrhcaIVAHvGIAGSA-KIGNGVQIGGQVGIKGH 294
Cdd:cd00710   18 IGDVIIGDNVFVGPGASI-RAD-------EGTPI--IIGANVNIQDG----VVIH-ALEGYSvWIGKNVSIAHGAIVHGP 82

                         90
                 ....*....|...
gi 502303567 295 VTIGDGVQIAAQS 307
Cdd:cd00710   83 AYIGDNCFIGFRS 95
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 220-305 2.99e-05

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: 41.84  E-value: 2.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 220 IIQDNVEIGANTSIDRGT-MDDTVIGEGTKIDNQVqIGHNVQIGRHCAIVAHVgiagsakIGNGVQIGGQVGIKGHVTIG 298
Cdd:cd03356    1 LIGESTVIGENAIIKNSViGDNVRIGDGVTITNSI-LMDNVTIGANSVIVDSI-------IGDNAVIGENVRVVNLCIIG 72


                 ....*..
gi 502303567 299 DGVQIAA 305
Cdd:cd03356   73 DDVVVED 79
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 142-263 3.58e-05

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


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 41.41  E-value: 3.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 142 VIGAHAEIGEGTRIgAQSIIGpnvkigRDCSIaagasilcallGNGVIIHNGarigqdgfgyapgprgmikivqigrvII 221
Cdd:cd05787    1 VIGRGTSIGEGTTI-KNSVIG------RNCKI-----------GKNVVIDNS--------------------------YI 36

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 502303567 222 QDNVEIGANTSIDRGTM-DDTVIGEGTKIDNQVQIGHNVQIGR 263
Cdd:cd05787   37 WDDVTIEDGCTIHHSIVaDGAVIGKGCTIPPGSLISFGVVIGD 79
LbH_THP_succinylT cd03350
2,3,4,5-tetrahydropyridine-2,6-dicarboxylate (THDP) N-succinyltransferase (also called THP ...
 220-305 5.50e-05

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


Pssm-ID: 100041 [Multi-domain]  Cd Length: 139  Bit Score: 42.75  E-value: 5.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 220 IIQDNVEIGANTSIDRGTMDD--TVIGEGTKIDNQVQIGHNVQIGRHCAIVAHVGIAG-----SAK---IGNGVQIGGQV 289
Cdd:cd03350    9 IIRDGAFIGPGAVLMMPSYVNigAYVDEGTMVDSWATVGSCAQIGKNVHLSAGAVIGGvleplQATpviIEDDVFIGANC 88

                         90
                 ....*....|....*.
gi 502303567 290 GIKGHVTIGDGVQIAA 305
Cdd:cd03350   89 EVVEGVIVGKGAVLAA 104
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 118-197 6.15e-05

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: 42.78  E-value: 6.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 118 EIAPSAVIDPSA------KLEKGVIVEPMAVI---GAHAEIGEGTRIGAQSII----GPNVKIGRDCSIAAGASILCALL 184
Cdd:cd04645    1 EIDPSAFIAPNAtvigdvTLGEGSSVWFGAVLrgdVNPIRIGERTNIQDGSVLhvdpGYPTIIGDNVTVGHGAVLHGCTI 80

                         90
                 ....*....|....*....
gi 502303567 185 GNGV------IIHNGARIG 197
Cdd:cd04645   81 GDNCligmgaIILDGAVIG 99
COG4801 COG4801
Predicted acyltransferase, contains DUF342 domain [General function prediction only];
224-303 7.52e-05

Predicted acyltransferase, contains DUF342 domain [General function prediction only];


Pssm-ID: 443829 [Multi-domain]  Cd Length: 283  Bit Score: 43.74  E-value: 7.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 224 NVEIGANTSIDRGTMDDTVI-GEGTKIDNQVQIGHNVQIGRHCAIVAHVGIAGSAKIGNGVQIGGQVGIKGHVTIGDGVQ 302
Cdd:COG4801   29 DVIVGGQSTIEYGVRGRNVIaGERVTFGGDIEAEGDCRLDMWCEVGGNVLVGEDAYLGERVHIGGKLVVSGDLDIGDDVD 108


                 .
gi 502303567 303 I 303
Cdd:COG4801  109 I 109
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 221-332 8.02e-05

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 44.35  E-value: 8.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 221 IQDNVEIGANTSIDRGTMDDTVIGEG-TKID-NQVQIGHNVQIGRHCAIVAHVGIAGSAKIGNGVQIGGQVGIKGhVTIG 298
Cdd:PRK14355 229 VNDRAQLAEAARVLRRRINRELMLAGvTLIDpETTYIDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVIKG-CRIG 307

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 502303567 299 DGVQIAA-----QSGIMTDLAAGGQYGGTPGRPLNDYLR 332
Cdd:PRK14355 308 DDVTVKAgsvleDSVVGDDVAIGPMAHLRPGTELSAHVK 346
PLN02694 PLN02694
serine O-acetyltransferase
 109-196 9.83e-05

serine O-acetyltransferase


Pssm-ID: 178297 [Multi-domain]  Cd Length: 294  Bit Score: 43.48  E-value: 9.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 109 RPVVFSGESEIAPSAVID--PSAKLEKG--------VIVEPMAVIG--------------------AHAEIGEGTRIGAQ 158
Cdd:PLN02694 145 RPLALALHSRISDVFAVDihPAAKIGKGilfdhatgVVIGETAVIGnnvsilhhvtlggtgkacgdRHPKIGDGVLIGAG 224

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 502303567 159 SIIGPNVKIGRDCSIAAGASILCALLGNGVIIHNGARI 196
Cdd:PLN02694 225 ATILGNVKIGEGAKIGAGSVVLIDVPPRTTAVGNPARL 262
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 149-247 1.10e-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: 41.33  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 149 IGEGTRIGAQSIIGPNVKIGRDCSIAAGASIlcallGNGVIIHNGARIG-QDGFGYAPGPRGMIK-IVQIGRVIIQDNVE 226
Cdd:cd03358    1 IGDNCIIGTNVFIENDVKIGDNVKIQSNVSI-----YEGVTIEDDVFIGpNVVFTNDLYPRSKIYrKWELKGTTVKRGAS 75

                         90       100
                 ....*....|....*....|.
gi 502303567 227 IGANTSIDRGtmddTVIGEGT 247
Cdd:cd03358   76 IGANATILPG----VTIGEYA 92
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
119-177 2.17e-04

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 41.01  E-value: 2.17e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502303567 119 IAPSAVIDPSAKL--EKGVIVEPMAVIGAHA----------------EIGEGTRIGAQSIIGPNVKIGRDCSIAAGA 177
Cdd:COG0110   36 IGPGVTIDDPGGItiGDNVLIGPGVTILTGNhpiddpatfplrtgpvTIGDDVWIGAGATILPGVTIGDGAVVGAGS 112
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
146-175 2.48e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 37.70  E-value: 2.48e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 502303567  146 HAEIGEGTRIGAQSIIGPNVKIGRDCSIAA 175
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 146-246 3.26e-04

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


Pssm-ID: 100040 [Multi-domain]  Cd Length: 145  Bit Score: 40.61  E-value: 3.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 146 HAEIGEGTRIG--AQSIIGPNVKIGRDCSIAAGASILCALlgngviIHNGARIGQDGFGYAPGPRGMIKI----VQIGRV 219
Cdd:cd03349    1 NISVGDYSYGSgpDCDVGGDKLSIGKFCSIAPGVKIGLGG------NHPTDWVSTYPFYIFGGEWEDDAKfddwPSKGDV 74

                         90       100
                 ....*....|....*....|....*...
gi 502303567 220 IIQDNVEIGANTSIDRGtmddtV-IGEG 246
Cdd:cd03349   75 IIGNDVWIGHGATILPG-----VtIGDG 97
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 87-316 3.34e-04

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 42.27  E-value: 3.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567  87 ILSSNPHAAFAMAGGLFYPAALRPVVFSGESEIAPSAV-IDPSAKLEKGVIVEPMAVIGAHAEIGEGTRIGAQSIIGPNV 165
Cdd:PRK14358 228 VLGANDRAGLAQLEATLRRRINEAHMKAGVTLQDPGTIlIEDTVTLGRDVTIEPGVLLRGQTRVADGVTIGAYSVVTDSV 307

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 166 kIGRDCSIAAGASILCALLGNGVIIHNGARIgqdgfgyAPGPRgMIKIVQIGRVIIQDNVEIGANTSIDR-GTMDDTVIG 244
Cdd:PRK14358 308 -LHEGAVIKPHSVLEGAEVGAGSDVGPFARL-------RPGTV-LGEGVHIGNFVETKNARLDAGVKAGHlAYLGDVTIG 378

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502303567 245 EGTKIDNQVQIGHNVQIGRHcaivahvgiagSAKIGNGVQIGGQVGIKGHVTIGDGVQIAAQSGIMTDLAAG 316
Cdd:PRK14358 379 AETNVGAGTIVANFDGVNKH-----------QSKVGAGVFIGSNTTLIAPRVVGDAAFIAAGSAVHDDVPEG 439
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 227-299 3.84e-04

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: 38.71  E-value: 3.84e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502303567 227 IGANTSIDRGTM-DDTVIGEGTKIDNQVQIGH-----NVQIGRHCaIVAHVGIAGSAKIGNGVQIGGQVGIKGHVTIGD 299
Cdd:cd05787    2 IGRGTSIGEGTTiKNSVIGRNCKIGKNVVIDNsyiwdDVTIEDGC-TIHHSIVADGAVIGKGCTIPPGSLISFGVVIGD 79
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 149-177 5.97e-04

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: 38.98  E-value: 5.97e-04
                         10        20
                 ....*....|....*....|....*....
gi 502303567 149 IGEGTRIGAQSIIGPNVKIGRDCSIAAGA 177
Cdd:cd04647   61 IGDDVWIGANVVILPGVTIGDGAVVGAGS 89
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
276-305 7.22e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 36.55  E-value: 7.22e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 502303567  276 SAKIGNGVQIGGQVGIKGHVTIGDGVQIAA 305
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
240-269 8.20e-04

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 36.16  E-value: 8.20e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 502303567  240 DTVIGEGTKIDNQVQIGHNVQIGRHCAIVA 269
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 178-326 9.17e-04

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


Pssm-ID: 100049 [Multi-domain]  Cd Length: 161  Bit Score: 39.51  E-value: 9.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 178 SILC----ALLGNGVIIHNGARIgqdgfgyapgpRGMIKIVQIGR-VIIQDNVEIGANTSIDRGTMDDTvigegtkidnQ 252
Cdd:cd03359   14 SVICgsqnIVLNGKTIIQSDVII-----------RGDLATVSIGRyCILSEGCVIRPPFKKFSKGVAFF----------P 72

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502303567 253 VQIGHNVQIGRHCAIVAhvgiagsAKIGNGVQIGGQVGIKGHVTIGDGVQIAAQSGIMTD--LAAGGQYGGTPGRP 326
Cdd:cd03359   73 LHIGDYVFIGENCVVNA-------AQIGSYVHIGKNCVIGRRCIIKDCVKILDGTVVPPDtvIPPYSVVSGRPARF 141
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 128-302 1.25e-03

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 40.48  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 128 SAKLEKGVIVEPMAVIGAHAEIGEGTRIGAQSIIGPNVKIgRDCSIAAGASI-------------LC-----ALLGNGVI 189
Cdd:PRK14356 263 SVRIGPRATIEPGAEIYGPCEIYGASRIARGAVIHSHCWL-RDAVVSSGATIhsfshlegaevgdGCsvgpyARLRPGAV 341

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 190 IHNGARIGQdgFGYAPGPRgMIKIVQIGRVIIQDNVEIGANTSIDRGTMDDTVIGEGTkidNQVQIGHNVQIGRHCAIVA 269
Cdd:PRK14356 342 LEEGARVGN--FVEMKKAV-LGKGAKANHLTYLGDAEIGAGANIGAGTITCNYDGVNK---HRTVIGEGAFIGSNTALVA 415

                        170       180       190
                 ....*....|....*....|....*....|...
gi 502303567 270 HVGIAGSAKIGNGVQIGGQVGiKGHVTIGDGVQ 302
Cdd:PRK14356 416 PVTIGDGALVGAGSVITKDVP-DGSLAIARGRQ 447
LbH_XAT cd03349
Xenobiotic acyltransferase (XAT): The XAT class of hexapeptide acyltransferases is composed of ...
 241-327 1.27e-03

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


Pssm-ID: 100040 [Multi-domain]  Cd Length: 145  Bit Score: 38.68  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 241 TVIGEGTKIDNQVQI--GHNVQIGRHCAIVAHVGI----------------------------------AGSAKIGNGVQ 284
Cdd:cd03349    2 ISVGDYSYGSGPDCDvgGDKLSIGKFCSIAPGVKIglggnhptdwvstypfyifggeweddakfddwpsKGDVIIGNDVW 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 502303567 285 IGGQVGIKGHVTIGDGVQIAAQSGIMTDLAAGGQYGGTPGRPL 327
Cdd:cd03349   82 IGHGATILPGVTIGDGAVIAAGAVVTKDVPPYAIVGGNPAKVI 124
PRK10092 PRK10092
maltose O-acetyltransferase; Provisional
 279-327 1.41e-03

maltose O-acetyltransferase; Provisional


Pssm-ID: 182235 [Multi-domain]  Cd Length: 183  Bit Score: 39.03  E-value: 1.41e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 502303567 279 IGNGVQIGGQVGIKGHVTIGDGVQIAAQSGIMTDLAAGGQYGGTPGRPL 327
Cdd:PRK10092 132 IGNNVWIGGRAVINPGVTIGDNVVVASGAVVTKDVPDNVVVGGNPARII 180
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 142-199 1.48e-03

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 40.06  E-value: 1.48e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 502303567 142 VIGAHAEIGEGTRIgAQSIIGPNVKIGRDCSIAagasilCALLGNGVIIHNGARIGQD 199
Cdd:COG0448  305 VLFRGVRVESGAVV-ENSVIMPGVVIGEGAVIE------NAIIDKNVVIPPGVVIGED 355
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 149-196 1.77e-03

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: 37.87  E-value: 1.77e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 502303567 149 IGEGTRIGAQSIIGPNVKIGRDCSIAAGASILCALLGNGVIIHNGARI 196
Cdd:cd03358   70 VKRGASIGANATILPGVTIGEYALVGAGAVVTKDVPPYALVVGNPARI 117
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 242-303 2.09e-03

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


Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 36.79  E-value: 2.09e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502303567 242 VIGEGTKIDNQVQIGHNVqIGRHCaivahvgiagsaKIGNGVQIGGQVgIKGHVTIGDGVQI 303
Cdd:cd04652    1 LVGENTQVGEKTSIKRSV-IGANC------------KIGKRVKITNCV-IMDNVTIEDGCTL 48
NRPS_term_dom TIGR02353
non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found ...
 152-264 2.15e-03

non-ribosomal peptide synthetase terminal domain of unknown function; This domain is found exclusively in non-ribosomal peptide synthetases and always as the final domain in the polypeptide. This domain is roughly 700 amino acids in size and is found in polypeptides roughly twice that size.


Pssm-ID: 274093 [Multi-domain]  Cd Length: 695  Bit Score: 40.12  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567  152 GTRIGAQSIIGPN-------VKIGRDCSIAAGASILCALLGNGVIihngarigqdgfgyapgprgmikivQIGRVIIQDN 224
Cdd:TIGR02353 112 GAKIGKGVDIGSLppvctdlLTIGAGTIVRKEVMLLGYRAERGRL-------------------------HTGPVTLGRD 166

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 502303567  225 VEIGANTSIDRgtmdDTVIGEGTKIDNQ--VQIGHNVQIGRH 264
Cdd:TIGR02353 167 AFIGTRSTLDI----DTSIGDGAQLGHGsaLQGGQSIPDGER 204
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 125-197 2.33e-03

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


Pssm-ID: 440667 [Multi-domain]  Cd Length: 174  Bit Score: 38.53  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 125 IDPSAKLEKGV-IVEPMA-VIGAHAEIGEGTRIGAQSIIG----------PnvKIGRDCSIAAGASIlcalLGNgVIIHN 192
Cdd:COG1045   68 IHPGATIGRGFfIDHGTGvVIGETAVIGDNVTIYQGVTLGgtgkekgkrhP--TIGDNVVIGAGAKI----LGP-ITIGD 140


                 ....*
gi 502303567 193 GARIG 197
Cdd:COG1045  141 NAKIG 145
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 172-262 2.63e-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: 37.06  E-value: 2.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 172 SIAAGASILCALLGNGVIIHNGarigqdgfgyapgprgmikivQIGRVIIQDNVEIGANTSIDRGT-MDDTVIGEGTK-- 248
Cdd:cd04651    3 YIGRRGEVKNSLVSEGCIISGG---------------------TVENSVLFRGVRVGSGSVVEDSViMPNVGIGRNAVir 61

                         90
                 ....*....|....*..
gi 502303567 249 ---IDNQVQIGHNVQIG 262
Cdd:cd04651   62 raiIDKNVVIPDGVVIG 78
PRK10502 PRK10502
putative acyl transferase; Provisional
 149-195 2.99e-03

putative acyl transferase; Provisional


Pssm-ID: 236703 [Multi-domain]  Cd Length: 182  Bit Score: 38.01  E-value: 2.99e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 502303567 149 IGEGTRIGAQSIIGPNVKIGRDCSIAAGASILCALLGNGVIIHNGAR 195
Cdd:PRK10502 127 IGEGCWLAADVFVAPGVTIGSGAVVGARSSVFKSLPANTICRGNPAV 173
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 116-220 3.23e-03

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


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 37.99  E-value: 3.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 116 ESEIAPSAVIDPSAKL------EKGVIVEPMAVIGA--------------------HA------EIGEGTRIGAQSIIGP 163
Cdd:cd00710    2 EPVIDPSAYVHPTAVVigdviiGDNVFVGPGASIRAdegtpiiiganvniqdgvviHAlegysvWIGKNVSIAHGAIVHG 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 502303567 164 NVKIGRDCSIAAGASILCALLGNGVIIHNGARIgqDGFGYAPGprgmiKIVQIGRVI 220
Cdd:cd00710   82 PAYIGDNCFIGFRSVVFNAKVGDNCVIGHNAVV--DGVEIPPG-----RYVPAGAVI 131
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 243-309 3.39e-03

2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 38.63  E-value: 3.39e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502303567 243 IGEGTKIDNQVQIGHNVQIGRHCaivahvgiagsaKIGNGVQIGG-----QvgiKGHVTIGDGVQIAAQSGI 309
Cdd:PRK11830 135 VDEGTMVDTWATVGSCAQIGKNV------------HLSGGVGIGGvleplQ---ANPVIIEDNCFIGARSEV 191
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 118-197 3.40e-03

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: 36.65  E-value: 3.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 118 EIAPSAVIDPSAKLEK--GVIVEPMAVIGAHAEIGEGTRIGAQSIIGPN--VKIGRDCSIAAGASIlcalLGNgVIIHNG 193
Cdd:cd03354    4 DIHPGAKIGPGLFIDHgtGIVIGETAVIGDNCTIYQGVTLGGKGKGGGKrhPTIGDNVVIGAGAKI----LGN-ITIGDN 78


                 ....
gi 502303567 194 ARIG 197
Cdd:cd03354   79 VKIG 82
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 147-237 3.76e-03

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 35.69  E-value: 3.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 147 AEIGEGTRIGAQSIIGPNVKIGRDCSIAAGASI---LCALLGNGVIIHNGARIGqdgfgyapgprgmikivqiGRVIIQD 223
Cdd:cd00208    1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIgaaTGPNEKNPTIIGDNVEIG-------------------ANAVIHG 61

                         90
                 ....*....|....
gi 502303567 224 NVEIGANTSIDRGT 237
Cdd:cd00208   62 GVKIGDNAVIGAGA 75
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 142-316 3.98e-03

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 38.85  E-value: 3.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 142 VIGAHAEIGEGTRIGAQSIIgPNVKIGRDCSIAAGASILCALLGNGVIIHNGARIgqdgfgyAPGprgmikivqigrvii 221
Cdd:PRK09451 279 IIEGNVTLGNRVKIGAGCVL-KNCVIGDDCEISPYSVVEDANLGAACTIGPFARL-------RPG--------------- 335

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 222 qdnVEIGANTSIdrGT---MDDTVIGEGTKIDN-----QVQIGHNVQIGrhcAIVAHVGIAGSAK----IGNGVQIGGQV 289
Cdd:PRK09451 336 ---AELAEGAHV--GNfveMKKARLGKGSKAGHltylgDAEIGDNVNIG---AGTITCNYDGANKfktiIGDDVFVGSDT 407

                        170       180
                 ....*....|....*....|....*..
gi 502303567 290 GIKGHVTIGDGVQIAAQSGIMTDLAAG 316
Cdd:PRK09451 408 QLVAPVTVGKGATIGAGTTVTRDVAEN 434
LbH_wcaF_like cd05825
wcaF-like: This group is composed of the protein product of the E. coli wcaF gene and similar ...
 140-195 4.65e-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: 4.65e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 502303567 140 MAVIGAHAEIGEGTRIGAQSIIGPNVKIGRDCSIAAGASILCALLGNGVIIHNGAR 195
Cdd:cd05825   50 FPLITAPIVIGDGAWVAAEAFVGPGVTIGEGAVVGARSVVVRDLPAWTVYAGNPAV 105
DapD COG2171
Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; ...
 243-309 5.87e-03

Tetrahydrodipicolinate N-succinyltransferase [Amino acid transport and metabolism]; Tetrahydrodipicolinate N-succinyltransferase is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 441774 [Multi-domain]  Cd Length: 268  Bit Score: 37.79  E-value: 5.87e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 243 IGEGTKIDNQVQIGHNVQIGRHCaivahvgiagsaKIGNGVQIGGqV---GIKGHVTIGDGVQIAAQSGI 309
Cdd:COG2171  129 VDEGTMVDTWATVGSCAQIGKNV------------HLSGGAGIGG-VlepLQAAPVIIEDNCFIGARSGV 185
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 242-304 6.35e-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: 6.35e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502303567 242 VIGEGTKIDNQVQIGHNVQIGRHCAIVAHVGIAGSAKIGNGVQIGGQVGIKgHVTIGDGVQIA 304
Cdd:cd05636   19 WIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVK-NSIIMDGTKVP 80
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 119-180 6.46e-03

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


Pssm-ID: 100049 [Multi-domain]  Cd Length: 161  Bit Score: 36.81  E-value: 6.46e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502303567 119 IAPSAVIDPSAKLEKGVIVEPMAVIGAHAEIGEGTRIGAQSI-----IGPNVKIGRDCSIAAGASIL 180
Cdd:cd03359   51 LSEGCVIRPPFKKFSKGVAFFPLHIGDYVFIGENCVVNAAQIgsyvhIGKNCVIGRRCIIKDCVKIL 117
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 149-196 7.69e-03

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


Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 34.86  E-value: 7.69e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 502303567 149 IGEGTRIGAQSIIGPNVkIGRDCSIAAGASILCALLGNGVIIHNGARI 196
Cdd:cd04652    2 VGENTQVGEKTSIKRSV-IGANCKIGKRVKITNCVIMDNVTIEDGCTL 48
dapD PRK11830
2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional
 135-168 8.45e-03

2,3,4,5-tetrahydropyridine-2,6-carboxylate N-succinyltransferase; Provisional


Pssm-ID: 236996 [Multi-domain]  Cd Length: 272  Bit Score: 37.48  E-value: 8.45e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 502303567 135 VIVEPMAVIGAHAEIGEGTRIGAQSIIGPNVKIG 168
Cdd:PRK11830 177 VIIEDNCFIGARSEVVEGVIVEEGSVLGMGVFLG 210
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 182-286 8.84e-03

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 34.92  E-value: 8.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303567 182 ALLGNGVIIHNGARIGqdgfgyapgprgmikivqiGRVIIQDNVEIGANTSIdrgtmddTVIGEGTKiDNQVQIGHNVQI 261
Cdd:cd00208    1 VFIGEGVKIHPKAVIR-------------------GPVVIGDNVNIGPGAVI-------GAATGPNE-KNPTIIGDNVEI 53

                         90       100
                 ....*....|....*....|....*
gi 502303567 262 GRHCAIVAHVGIAGSAKIGNGVQIG 286
Cdd:cd00208   54 GANAVIHGGVKIGDNAVIGAGAVVT 78
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 124-198 9.54e-03

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


Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 34.86  E-value: 9.54e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502303567 124 VIDPSAKLEKGVIVEpMAVIGAHAEIGEGTRIgAQSIIGPNVKIGRDCSIaagasilcallgNGVIIHNGARIGQ 198
Cdd:cd04652    1 LVGENTQVGEKTSIK-RSVIGANCKIGKRVKI-TNCVIMDNVTIEDGCTL------------ENCIIGNGAVIGE 61
 
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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