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Conserved domains on  [gi|2217346700|ref|XP_047305104|]
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translation initiation factor eIF2B subunit epsilon isoform X1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 43-257 1.23e-114

The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of epsilon subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


:

Pssm-ID: 133040 [Multi-domain]  Cd Length: 217  Bit Score: 338.04  E-value: 1.23e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700  43 LQAVLVADSFDRRFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLLKSKWCRPTS-LNVVR 121
Cdd:cd04197     1 LQAVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKSKWSKPKSsLMIVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700 122 IITSELYRSLGDVLRDVDAKALVRSDFLLVYGDVISNINITRALEEHRLRRKLEKNVsVMTMIFKESSPSHPTRCHEDNV 201
Cdd:cd04197    81 IIMSEDCRSLGDALRDLDAKGLIRGDFILVSGDVVSNIDLKEILEEHKERRKKDKNA-IMTMVLKEASPPHRTRRTGEEF 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217346700 202 VVAVDSTTNRVLHFQKTQGLRRFAF--PLSLFQGSSDGVEVRYDLLDCHISICSPQVA 257
Cdd:cd04197   160 VIAVDPKTSRLLHYEELPGSKYRSItdLPSELLGSNSEVEIRHDLLDCHIDICSPDVL 217
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 361-439 3.16e-33

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: 121.15  E-value: 3.16e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217346700 361 LLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQIHQSLLCDNAEVKERVTLKPRSVLTSQVVVGP 439
Cdd:cd05787     1 VIGRGTSIGEGTTIKNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIPPGSLISFGVVIGD 79
 
Name Accession Description Interval E-value
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 43-257 1.23e-114

The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of epsilon subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133040 [Multi-domain]  Cd Length: 217  Bit Score: 338.04  E-value: 1.23e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700  43 LQAVLVADSFDRRFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLLKSKWCRPTS-LNVVR 121
Cdd:cd04197     1 LQAVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKSKWSKPKSsLMIVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700 122 IITSELYRSLGDVLRDVDAKALVRSDFLLVYGDVISNINITRALEEHRLRRKLEKNVsVMTMIFKESSPSHPTRCHEDNV 201
Cdd:cd04197    81 IIMSEDCRSLGDALRDLDAKGLIRGDFILVSGDVVSNIDLKEILEEHKERRKKDKNA-IMTMVLKEASPPHRTRRTGEEF 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217346700 202 VVAVDSTTNRVLHFQKTQGLRRFAF--PLSLFQGSSDGVEVRYDLLDCHISICSPQVA 257
Cdd:cd04197   160 VIAVDPKTSRLLHYEELPGSKYRSItdLPSELLGSNSEVEIRHDLLDCHIDICSPDVL 217
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 361-439 3.16e-33

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: 121.15  E-value: 3.16e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217346700 361 LLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQIHQSLLCDNAEVKERVTLKPRSVLTSQVVVGP 439
Cdd:cd05787     1 VIGRGTSIGEGTTIKNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIPPGSLISFGVVIGD 79
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 345-408 6.85e-11

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: 63.50  E-value: 6.85e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217346700 345 GPEVSLGHGSILEENVLLGSGTVIGSNCfitnsVIGPGCHIGDNvvldqTYLWQGVRVAAGAQI 408
Cdd:COG1044   112 GEGVSIGPFAVIGAGVVIGDGVVIGPGV-----VIGDGVVIGDD-----CVLHPNVTIYERCVI 165
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 345-408 4.16e-10

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 61.31  E-value: 4.16e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217346700 345 GPEVSLGHGSILEENVLLGSGTVIGSNCFI-TNSVIGPGCHIGDNVVL-DQTYLWQGVRVAAGAQI 408
Cdd:PRK00892  116 GEGVSIGPNAVIGAGVVIGDGVVIGAGAVIgDGVKIGADCRLHANVTIyHAVRIGNRVIIHSGAVI 181
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
44-156 1.59e-09

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 58.33  E-value: 1.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700  44 QAVLVADSFDRRFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLLKSKWCrptslnvVRII 123
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALARPGPD-------VTFV 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2217346700 124 TSELYR---SLGDVLRdvdAKALVRSDFLLVYGDVI 156
Cdd:COG1213    74 YNPDYDetnNIYSLWL---AREALDEDFLLLNGDVV 106
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
365-391 1.11e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 41.94  E-value: 1.11e-05
                          10        20
                  ....*....|....*....|....*...
gi 2217346700 365 GTVIGSNCFI-TNSVIGPGCHIGDNVVL 391
Cdd:pfam00132   1 GTVIGDNVLIgPNAVIGGGVIIGDNVII 28
 
Name Accession Description Interval E-value
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 43-257 1.23e-114

The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of epsilon subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133040 [Multi-domain]  Cd Length: 217  Bit Score: 338.04  E-value: 1.23e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700  43 LQAVLVADSFDRRFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLLKSKWCRPTS-LNVVR 121
Cdd:cd04197     1 LQAVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKSKWSKPKSsLMIVI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700 122 IITSELYRSLGDVLRDVDAKALVRSDFLLVYGDVISNINITRALEEHRLRRKLEKNVsVMTMIFKESSPSHPTRCHEDNV 201
Cdd:cd04197    81 IIMSEDCRSLGDALRDLDAKGLIRGDFILVSGDVVSNIDLKEILEEHKERRKKDKNA-IMTMVLKEASPPHRTRRTGEEF 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217346700 202 VVAVDSTTNRVLHFQKTQGLRRFAF--PLSLFQGSSDGVEVRYDLLDCHISICSPQVA 257
Cdd:cd04197   160 VIAVDPKTSRLLHYEELPGSKYRSItdLPSELLGSNSEVEIRHDLLDCHIDICSPDVL 217
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 43-256 3.04e-81

The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; N-terminal domain of eEIF-2B epsilon and gamma, subunits of eukaryotic translation initiators, is a subfamily of glycosyltranferase 2 and is predicted to have glycosyltranferase activity. eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133001 [Multi-domain]  Cd Length: 216  Bit Score: 252.56  E-value: 3.04e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700  43 LQAVLVADSFDRRFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLLKSKWCRPTSLNVVRI 122
Cdd:cd02507     1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSKWSSLSSKMIVDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700 123 ITSELYRSLGDVLRDVDAKALVRSDFLLVYGDVISNINITRALEEhrlRRKLEKNvSVMTMIFKESSPSHPT---RCHED 199
Cdd:cd02507    81 ITSDLCESAGDALRLRDIRGLIRSDFLLLSCDLVSNIPLSELLEE---RRKKDKN-AIATLTVLLASPPVSTeqsKKTEE 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217346700 200 NVVVAVDSTTNR--VLHFQKTQGLRRFAFPLSLFQGSSDGVEVRYDLLDCHISICSPQV 256
Cdd:cd02507   157 EDVIAVDSKTQRllLLHYEEDLDEDLELIIRKSLLSKHPNVTIRTDLLDCHIYICSPDV 215
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 361-439 3.16e-33

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: 121.15  E-value: 3.16e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217346700 361 LLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQIHQSLLCDNAEVKERVTLKPRSVLTSQVVVGP 439
Cdd:cd05787     1 VIGRGTSIGEGTTIKNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIPPGSLISFGVVIGD 79
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 361-439 3.29e-28

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: 107.33  E-value: 3.29e-28
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217346700 361 LLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQIHQSLLCDNAEVKERVTLKPRSVLTSQVVVGP 439
Cdd:cd03356     1 LIGESTVIGENAIIKNSVIGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVNLCIIGDDVVVED 79
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 43-256 2.72e-21

The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 92.34  E-value: 2.72e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700  43 LQAVLVADSFDRRFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLLKSKWCRPTSLNVVRI 122
Cdd:cd04198     1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSFPLNLKQKLDEVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700 123 ITSELYRSLGDVLRDVDAKalVRSDFLLVYGDVISNINITRALEEHRlrrkleKNVSVMTMIFKESS------PSHPTRC 196
Cdd:cd04198    81 IVLDEDMGTADSLRHIRKK--IKKDFLVLSCDLITDLPLIELVDLHR------SHDASLTVLLYPPPvsseqkGGKGKSK 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700 197 HEDN-VVVAVDSTTNRVLH------FQKTQGLRR---FAFPlslfqgssdGVEVRYDLLDCHISICSPQV 256
Cdd:cd04198   153 KADErDVIGLDEKTQRLLFitseedLDEDLELRKsllKRHP---------RVTITTKLLDAHVYIFKRWV 213
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 55-216 4.39e-16

NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 77.24  E-value: 4.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700  55 RFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLLKSKWCRPTslnvVRIITSELYRSLGDV 134
Cdd:cd04181    11 RLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFGVN----IEYVVQEEPLGTAGA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700 135 LRDVdAKALVRSDFLLVYGDVISNINITRALEEHRLRRkleknvSVMTMIFKEssPSHPTRChednVVVAVDStTNRVLH 214
Cdd:cd04181    87 VRNA-EDFLGDDDFLVVNGDVLTDLDLSELLRFHREKG------ADATIAVKE--VEDPSRY----GVVELDD-DGRVTR 152


                  ..
gi 2217346700 215 FQ 216
Cdd:cd04181   153 FV 154
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 361-448 7.63e-12

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: 61.05  E-value: 7.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700 361 LLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQIHQSLLCDNAEVKERVTLKprsvltsQVVVGPN 440
Cdd:cd04652     1 LVGENTQVGEKTSIKRSVIGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLK-------DCLVGSG 73


                  ....*...
gi 2217346700 441 ITLPEGSV 448
Cdd:cd04652    74 YRVEAGTE 81
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 345-408 6.85e-11

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: 63.50  E-value: 6.85e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217346700 345 GPEVSLGHGSILEENVLLGSGTVIGSNCfitnsVIGPGCHIGDNvvldqTYLWQGVRVAAGAQI 408
Cdd:COG1044   112 GEGVSIGPFAVIGAGVVIGDGVVIGPGV-----VIGDGVVIGDD-----CVLHPNVTIYERCVI 165
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 345-408 4.16e-10

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 61.31  E-value: 4.16e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217346700 345 GPEVSLGHGSILEENVLLGSGTVIGSNCFI-TNSVIGPGCHIGDNVVL-DQTYLWQGVRVAAGAQI 408
Cdd:PRK00892  116 GEGVSIGPNAVIGAGVVIGDGVVIGAGAVIgDGVKIGADCRLHANVTIyHAVRIGNRVIIHSGAVI 181
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 345-408 7.73e-10

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: 58.57  E-value: 7.73e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217346700 345 GPEVSLGHGSILEENVLLGSGTVIGSNCFI-TNSVIGPGCHIGDNVVL-DQTYLWQGVRVAAGAQI 408
Cdd:cd03352     5 GENVSIGPNAVIGEGVVIGDGVVIGPGVVIgDGVVIGDDCVIHPNVTIyEGCIIGDRVIIHSGAVI 70
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 55-172 1.03e-09

NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133044 [Multi-domain]  Cd Length: 221  Bit Score: 58.74  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700  55 RFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLLKSKWcrptslnVVRIITSELYRSL--- 131
Cdd:cd06422    12 RMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGDSRF-------GLRITISDEPDELlet 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2217346700 132 -GDVLRdvdAKALVRSD-FLLVYGDVISNINITRALEEHRLRR 172
Cdd:cd06422    85 gGGIKK---ALPLLGDEpFLVVNGDILWDGDLAPLLLLHAWRM 124
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
44-156 1.59e-09

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 58.33  E-value: 1.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700  44 QAVLVADSFDRRFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLLKSKWCrptslnvVRII 123
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALARPGPD-------VTFV 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2217346700 124 TSELYR---SLGDVLRdvdAKALVRSDFLLVYGDVI 156
Cdd:COG1213    74 YNPDYDetnNIYSLWL---AREALDEDFLLLNGDVV 106
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 341-438 2.35e-09

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: 57.04  E-value: 2.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700 341 NIYRGPEVSLGHGSILEENVLLGSGTVIGSNCfitnsVIGPGCHIGDNVvldqtylwqgvrVAAGAQIHQSLLCDNAEVK 420
Cdd:cd03353     9 TTYIDGDVEIGVDVVIDPGVILEGKTVIGEDC-----VIGPNCVIKDST------------IGDGVVIKASSVIEGAVIG 71

                          90       100
                  ....*....|....*....|....
gi 2217346700 421 ERVT------LKPRSVLTSQVVVG 438
Cdd:cd03353    72 NGATvgpfahLRPGTVLGEGVHIG 95
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 345-404 5.41e-09

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: 53.01  E-value: 5.41e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217346700 345 GPEVSLGHGSILEENVLLGsGTVIGSNCFITNSVIGPGCHIGDNV-VLDQTYLWQGVRVAA 404
Cdd:cd03356    20 GDNVRIGDGVTITNSILMD-NVTIGANSVIVDSIIGDNAVIGENVrVVNLCIIGDDVVVED 79
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 341-408 8.13e-09

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: 57.73  E-value: 8.13e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217346700 341 NIYRGPEVSLGH------GSILEENVLLGSGTVIGSNCFITNSVIGPGCHIgDNVVLDqtylwqGVRVAAGAQI 408
Cdd:COG1207   260 TTYIDGDVEIGRdvvidpNVILEGKTVIGEGVVIGPNCTLKDSTIGDGVVI-KYSVIE------DAVVGAGATV 326
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 350-408 1.12e-08

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: 52.85  E-value: 1.12e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217346700 350 LGHGSILE----ENVLLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQI 408
Cdd:cd04651    15 VSEGCIISggtvENSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIIDKNVVIPDGVVI 77
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 45-168 1.47e-08

Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 55.32  E-value: 1.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700  45 AVLVADSFDRRFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLLKSKwcrptslnVVRIIT 124
Cdd:cd02523     1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYP--------NIKFVY 72

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2217346700 125 SELYRSLGDVLRDVDAKALVRSDFLLVYGDVISNINITRALEEH 168
Cdd:cd02523    73 NPDYAETNNIYSLYLARDFLDEDFLLLEGDVVFDPSILERLLSS 116
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 345-449 2.40e-08

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: 54.03  E-value: 2.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700 345 GPEVSLGHGSILEENVLLGSGTVIGSNCFI-TNSVIGPGCHIGDNVVLdqtylwqgvrvAAGAqihqsLLCDNAEVKERV 423
Cdd:cd03360    94 SPSAVIGEGCVIMAGAVINPDARIGDNVIInTGAVIGHDCVIGDFVHI-----------APGV-----VLSGGVTIGEGA 157

                          90       100
                  ....*....|....*....|....*.
gi 2217346700 424 TLKPRSVLTSQVVVGPNITLPEGSVI 449
Cdd:cd03360   158 FIGAGATIIQGVTIGAGAIIGAGAVV 183
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 340-391 3.88e-08

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: 53.57  E-value: 3.88e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217346700 340 HNIYRGPEVSLGHGSILEENVLLGSGTVIGSNCFI-TNSVIGPGCHIGDNVVL 391
Cdd:cd03352    12 PNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIhPNVTIYEGCIIGDRVII 64
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 355-438 4.68e-08

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: 53.57  E-value: 4.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700 355 ILEENVLLGSGTVIGSNCFI-TNSVIGPGCHIGDnvvldqtylwqGVRVAAGAQIHqsllcDNAEVKERVTLKPRSVLTS 433
Cdd:cd03352     3 KIGENVSIGPNAVIGEGVVIgDGVVIGPGVVIGD-----------GVVIGDDCVIH-----PNVTIYEGCIIGDRVIIHS 66


                  ....*
gi 2217346700 434 QVVVG 438
Cdd:cd03352    67 GAVIG 71
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 353-408 5.22e-08

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 55.08  E-value: 5.22e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217346700 353 GSILE---ENVLLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQI 408
Cdd:COG0448   294 GCIISgtvENSVLFRGVRVESGAVVENSVIMPGVVIGEGAVIENAIIDKNVVIPPGVVI 352
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 345-408 6.83e-08

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 54.37  E-value: 6.83e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217346700 345 GPEVSLGHGSILEENVLLGSGTVIGSNCFI-TNSVIGPGCHIGDNvvldqTYLWQGVRVAAGAQI 408
Cdd:PRK00892  110 DPSAKIGEGVSIGPNAVIGAGVVIGDGVVIgAGAVIGDGVKIGAD-----CRLHANVTIYHAVRI 169
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 343-450 6.94e-08

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 54.75  E-value: 6.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700 343 YRGPEVSLGHGSILEENVLLGSGTVIGSNCFITNSVIGPGCHIGDNVVldqtylwqgvrVAAGAQIHQSLLCDNAEVKER 422
Cdd:PRK14355  264 YIDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVIKGCRIGDDVT-----------VKAGSVLEDSVVGDDVAIGPM 332

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2217346700 423 VTLKPRSVLTSQVVVG-----PNITLPEGSVIS 450
Cdd:PRK14355  333 AHLRPGTELSAHVKIGnfvetKKIVMGEGSKAS 365
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 368-449 2.83e-07

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: 48.61  E-value: 2.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700 368 IGSNCFITNSVIGPGCHIGDNVVlDQTYLWQGVRVAAGAQIHQSLLCDNAEVKERVTLKprsvltsQVVVGPNITLPEGS 447
Cdd:cd04651     4 IGRRGEVKNSLVSEGCIISGGTV-ENSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIR-------RAIIDKNVVIPDGV 75


                  ..
gi 2217346700 448 VI 449
Cdd:cd04651    76 VI 77
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 342-446 3.79e-07

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


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 49.93  E-value: 3.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700 342 IYRGPEVSLGHGSILEENVLLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQIHQSllcDNAEVKE 421
Cdd:cd00710    65 VWIGKNVSIAHGAIVHGPAYIGDNCFIGFRSVVFNAKVGDNCVIGHNAVVDGVEIPPGRYVPAGAVITSQ---TQADALP 141

                          90       100
                  ....*....|....*....|....*
gi 2217346700 422 RVTLKPRsvLTSQVVVGPNITLPEG 446
Cdd:cd00710   142 DVTDSAR--EFNEKVITVNNELAEG 164
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 340-391 4.51e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 52.06  E-value: 4.51e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217346700 340 HNIYRGPEVSLGHGSILEENVLLGSGTVIGSNCFI-TNSVIGPGCHIGDNVVL 391
Cdd:PRK00892  123 PNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLhANVTIYHAVRIGNRVII 175
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
354-449 5.95e-07

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 48.71  E-value: 5.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700 354 SILEENVLLGSGTVIGSNCFI--TNSVIGPGCHIGDNVVLdqtYLWQGVRVAAGAQIHQ--SLLCDN---------AEVK 420
Cdd:COG0110     3 LLLLFGARIGDGVVIGPGVRIygGNITIGDNVYIGPGVTI---DDPGGITIGDNVLIGPgvTILTGNhpiddpatfPLRT 79

                          90       100
                  ....*....|....*....|....*....
gi 2217346700 421 ERVTLKPRSVLTSQVVVGPNITLPEGSVI 449
Cdd:COG0110    80 GPVTIGDDVWIGAGATILPGVTIGDGAVV 108
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 368-449 1.14e-06

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 50.64  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700 368 IGSNCFITNSVIGPGCHIGDNVvlDQTYLWQGVRVAAGAQIHQSLLCDNAEVKERVTLKprsvltsQVVVGPNITLPEGS 447
Cdd:PRK05293  285 IAENAKVKNSLVVEGCVVYGTV--EHSVLFQGVQVGEGSVVKDSVIMPGAKIGENVVIE-------RAIIGENAVIGDGV 355


                  ..
gi 2217346700 448 VI 449
Cdd:PRK05293  356 II 357
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 341-450 1.92e-06

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: 48.56  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700 341 NIYRGPEVSLGHGSILEENVLLGSGTVIGSNCFI-TNSVIG---------PGCH----------IGDNV----------- 389
Cdd:cd03352    31 GVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIhSGAVIGsdgfgfapdGGGWvkipqlggviIGDDVeiganttidrg 110

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217346700 390 VLDQTYLWQGVR------VAAGAQI--HqSLLCDNAEVKERVTLKPRSVLTSQVVVGPNITLPEGSVIS 450
Cdd:cd03352   111 ALGDTVIGDGTKidnlvqIAHNVRIgeN-CLIAAQVGIAGSTTIGDNVIIGGQVGIAGHLTIGDGVVIG 178
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 341-438 4.07e-06

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 49.44  E-value: 4.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700 341 NIYRGPEVSLGHGSILEENVLLGSGTVIGSNCFIT------NSVIGPGCHIGDNVVLDqtylwqgvrvaagaqihqsllc 414
Cdd:PRK14354  259 STYIDADVEIGSDTVIEPGVVIKGNTVIGEDCVIGpgsrivDSTIGDGVTITNSVIEE---------------------- 316

                          90       100       110
                  ....*....|....*....|....*....|
gi 2217346700 415 dnAEVKERVT------LKPRSVLTSQVVVG 438
Cdd:PRK14354  317 --SKVGDNVTvgpfahLRPGSVIGEEVKIG 344
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 344-419 5.53e-06

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: 46.43  E-value: 5.53e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217346700 344 RGPEVSLGHGSILEENVLLGSGTVIGSNCfitnsVIGPGCHIGDNVVLDqtylwQGVRVAAGAQIHQSLLCDNAEV 419
Cdd:cd05636    14 IKGPVWIGEGAIVRSGAYIEGPVIIGKGC-----EIGPNAYIRGYTVLG-----DGCVVGNSVEVKNSIIMDGTKV 79
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 55-172 8.41e-06

G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose.


Pssm-ID: 133032 [Multi-domain]  Cd Length: 236  Bit Score: 47.18  E-value: 8.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700  55 RFFPISKDQPRVLLPLANVALIDYTLEFLTATGVQETFVFCCWKAAQIKEHLLK-SKWcrptSLNVVRIITSELyRSLGD 133
Cdd:cd04189    13 RLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDgSRF----GVRITYILQEEP-LGLAH 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2217346700 134 -VLRdvdAKALV-RSDFLLVYGDVISNINITRALEEHRLRR 172
Cdd:cd04189    88 aVLA---ARDFLgDEPFVVYLGDNLIQEGISPLVRDFLEED 125
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 340-392 9.07e-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: 9.07e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217346700 340 HNIYRGPEVSLGHGSILEENVLLG--------SGTVIGSNCFI-TNSVIGPGCHIGDNVVLD 392
Cdd:cd00208    11 PKAVIRGPVVIGDNVNIGPGAVIGaatgpnekNPTIIGDNVEIgANAVIHGGVKIGDNAVIG 72
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
365-391 1.11e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 41.94  E-value: 1.11e-05
                          10        20
                  ....*....|....*....|....*...
gi 2217346700 365 GTVIGSNCFI-TNSVIGPGCHIGDNVVL 391
Cdd:pfam00132   1 GTVIGDNVLIgPNAVIGGGVIIGDNVII 28
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
338-406 1.67e-05

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 44.86  E-value: 1.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700 338 SRHNIYRGPEVSLGHGSIL----------EENVLLGSGTVIGSNCFI-TNSVIGPGCHIGDNVVldqtylwqgvrVAAGA 406
Cdd:COG0110    44 DPGGITIGDNVLIGPGVTIltgnhpiddpATFPLRTGPVTIGDDVWIgAGATILPGVTIGDGAV-----------VGAGS 112
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 345-408 2.25e-05

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


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 43.64  E-value: 2.25e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217346700 345 GPEVSLGHGSILEENVLLGSGTVIGSNCFIT-NSVIGPGCHIGDNVVL----------DQTYLWQGVRVAAGAQI 408
Cdd:cd03358     2 GDNCIIGTNVFIENDVKIGDNVKIQSNVSIYeGVTIEDDVFIGPNVVFtndlyprskiYRKWELKGTTVKRGASI 76
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 365-406 3.42e-05

Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 42.83  E-value: 3.42e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2217346700 365 GTVIGSNCFI-TNSVIGPGCHIGDNVVldqtylwqgvrVAAGA 406
Cdd:cd04647    58 PIVIGDDVWIgANVVILPGVTIGDGAV-----------VGAGS 89
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 359-449 8.04e-05

Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 42.06  E-value: 8.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700 359 NVLLGSGTVIGSNCFITNS---VIGPGCHIGDNVVLdqtylwqgvrVAAGAQIH-QSLLCDNAEVKERVTLKPRSVLTSQ 434
Cdd:cd04647     1 NISIGDNVYIGPGCVISAGggiTIGDNVLIGPNVTI----------YDHNHDIDdPERPIEQGVTSAPIVIGDDVWIGAN 70

                          90
                  ....*....|....*
gi 2217346700 435 VVVGPNITLPEGSVI 449
Cdd:cd04647    71 VVILPGVTIGDGAVV 85
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 345-391 8.57e-05

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: 44.24  E-value: 8.57e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2217346700 345 GPEVSLGHGSILEENVLLGSGTVIGSNCFIT-NSVIGPGCHIGDNVVL 391
Cdd:COG1043    17 GENVEIGPFCVIGPDVEIGDGTVIGSHVVIEgPTTIGKNNRIFPFASI 64
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 315-408 8.72e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 44.82  E-value: 8.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700 315 RRW----VYPLTPEANFTDSTTQSCtHSRHNIyrgpeVSLG---HGSILEENVLlGSGTVIGSNCFITNSVIGPGCHIGD 387
Cdd:PRK00844  287 REWpiytSSPNLPPAKFVDGGGRVG-SAQDSL-----VSAGsiiSGATVRNSVL-SPNVVVESGAEVEDSVLMDGVRIGR 359

                          90       100
                  ....*....|....*....|.
gi 2217346700 388 NVVLDQTYLWQGVRVAAGAQI 408
Cdd:PRK00844  360 GAVVRRAILDKNVVVPPGATI 380
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 358-424 1.08e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 44.82  E-value: 1.08e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217346700 358 ENVLLGSGTVIgSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQIHQSLLCDNAEVKERVT 424
Cdd:PRK00844  314 QDSLVSAGSII-SGATVRNSVLSPNVVVESGAEVEDSVLMDGVRIGRGAVVRRAILDKNVVVPPGAT 379
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 376-449 1.69e-04

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: 42.78  E-value: 1.69e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217346700 376 NSVIGPGCHIGDNVVLDqtylwQGVRVAAGAQIH-QSLLCDNAEVKERVTLKPRSVLTSQVVVGPNITLPEGSVI 449
Cdd:cd03352     1 SAKIGENVSIGPNAVIG-----EGVVIGDGVVIGpGVVIGDGVVIGDDCVIHPNVTIYEGCIIGDRVIIHSGAVI 70
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 348-449 2.35e-04

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: 42.47  E-value: 2.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700 348 VSLGHGS-ILEENVLLGSGTVIGSNCfitnsVIGPGCHIGDNVVldqtyLWQGVRVAagaqiHQSLLCDNaevkerVTLK 426
Cdd:cd03360    84 ATLIHPSaVVSPSAVIGEGCVIMAGA-----VINPDARIGDNVI-----INTGAVIG-----HDCVIGDF------VHIA 142

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2217346700 427 PRSVLTSQVVVG------------PNITLPEGSVI 449
Cdd:cd03360   143 PGVVLSGGVTIGegafigagatiiQGVTIGAGAII 177
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 347-449 2.65e-04

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: 41.63  E-value: 2.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700 347 EVSLGHGSILEENVLL----GSGTVIGSNCFITNSVIGPGCHIGDNVVldqtylwqgvrVAAGAQIhqsllCDNAEVKER 422
Cdd:cd04645    38 PIRIGERTNIQDGSVLhvdpGYPTIIGDNVTVGHGAVLHGCTIGDNCL-----------IGMGAII-----LDGAVIGKG 101

                          90       100
                  ....*....|....*....|....*..
gi 2217346700 423 VTLKPRSVLTsqvvvgPNITLPEGSVI 449
Cdd:cd04645   102 SIVAAGSLVP------PGKVIPPGSLV 122
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
345-391 3.04e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 42.78  E-value: 3.04e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2217346700 345 GPEVSLGHGSILEENVLLGSGTVIGSNCFIT-NSVIGPGCHIGDNVVL 391
Cdd:PRK05289   18 GENVEIGPFCVIGPNVVIGDGTVIGSHVVIDgHTTIGKNNRIFPFASI 65
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 345-391 3.81e-04

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: 42.42  E-value: 3.81e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2217346700 345 GPEVSLGHGSILEENVLLGSGTVIGSNCFIT-NSVIGPGCHIGDNVVL 391
Cdd:cd03351    15 GENVEIGPFCVIGPNVEIGDGTVIGSHVVIDgPTTIGKNNRIFPFASI 62
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 354-449 4.56e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 42.55  E-value: 4.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700 354 SILEENVLLGSGTVIgsncfiTNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGAQIhqsllcdnAEVKERVTlkprsvlts 433
Cdd:PRK05293  309 SVLFQGVQVGEGSVV------KDSVIMPGAKIGENVVIERAIIGENAVIGDGVII--------GGGKEVIT--------- 365

                          90
                  ....*....|....*.
gi 2217346700 434 qvVVGPNITLPEGSVI 449
Cdd:PRK05293  366 --VIGENEVIGVGTVI 379
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 345-390 6.03e-04

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 40.78  E-value: 6.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217346700 345 GPEVSLGHGSIL-----EENVLLGSG------TVIGSNCFIT-NSVIGPGCHIGDNVV 390
Cdd:COG0663    75 GDDVTIGHGAILhgctiGDNVLIGMGaivldgAVIGDGSIVGaGALVTEGKVVPPGSL 132
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 342-449 6.92e-04

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


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 40.26  E-value: 6.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700 342 IYRGPEVSLGHGSILEENVLLGSGTVIGSNCFITNSVIGPGCHI------GDNVvldqtyLWQGVRVAAGAQIhQSLLCD 415
Cdd:cd05636    36 VIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSIIMDGTKVphlnyvGDSV------LGENVNLGAGTIT-ANLRFD 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2217346700 416 NAEVKerVTLKPRSVLTSQ----------VVVGPNITLPEGSVI 449
Cdd:cd05636   109 DKPVK--VRLKGERVDTGRrklgaiigdgVKTGINVSLNPGVKI 150
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 378-449 7.73e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 41.66  E-value: 7.73e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217346700 378 VIGPGCHIGDNVVLD-QTYLWQGVRVAAGAQIH-QSLLCDNAEVKERVTLKPRSVLTSQVVVGPNITLPEGSVI 449
Cdd:PRK00892  108 VIDPSAKIGEGVSIGpNAVIGAGVVIGDGVVIGaGAVIGDGVKIGADCRLHANVTIYHAVRIGNRVIIHSGAVI 181
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 344-408 8.90e-04

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 41.94  E-value: 8.90e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217346700 344 RGpevSLGHGS--------ILEENVLLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDqtylwqGVRVAAGAQI 408
Cdd:PRK09451  263 RG---TLTHGRdveidtnvIIEGNVTLGNRVKIGAGCVLKNCVIGDDCEISPYSVVE------DANLGAACTI 326
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
353-386 2.22e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.78  E-value: 2.22e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2217346700 353 GSILEENVLLGSGTVIGSNCfitnsVIGPGCHIG 386
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGV-----IIGDNVIIG 29
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 343-391 5.11e-03

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: 38.95  E-value: 5.11e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217346700 343 YRGPEVSL--GHGSILEENVLLGSG-------TVIGSNCFI-TNSVIGPGCHIGDNVVL 391
Cdd:cd03351    71 YKGEPTRLeiGDNNTIREFVTIHRGtaqgggvTRIGNNNLLmAYVHVAHDCVIGNNVIL 129
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
343-391 6.51e-03

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 38.54  E-value: 6.51e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217346700 343 YRGPEVSL--GHGSILEENVLLGSGTV-------IGSNCFI-TNSVIGPGCHIGDNVVL 391
Cdd:PRK05289   74 YKGEPTRLviGDNNTIREFVTINRGTVqgggvtrIGDNNLLmAYVHVAHDCVVGNHVIL 132
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
353-410 7.05e-03

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 38.54  E-value: 7.05e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217346700 353 GSILEENVLLGSGTVIGSNCfitnsVIGPGCHIGDNVVLDqtylwQGVRVAAGAQIHQ 410
Cdd:PRK05289   14 GAKIGENVEIGPFCVIGPNV-----VIGDGTVIGSHVVID-----GHTTIGKNNRIFP 61
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 334-408 9.94e-03

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 38.37  E-value: 9.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217346700 334 SCTHSRhniyrgpEVSLGHGSILEENVLL------GSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTylwqgvrVAAGAQ 407
Cdd:PRK14360  256 SCTISE-------TVELGPDVIIEPQTHLrgntviGSGCRIGPGSLIENSQIGENVTVLYSVVSDSQ-------IGDGVK 321


                  .
gi 2217346700 408 I 408
Cdd:PRK14360  322 I 322
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 359-406 9.97e-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: 35.25  E-value: 9.97e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 2217346700 359 NVLLGSGTVIGSNCFITNSVIGPGCHIGDNVVLDQTYLWQGVRVAAGA 406
Cdd:cd04652    33 NCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLVGSGYRVEAGT 80
 
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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