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Conserved domains on  [gi|79328173|ref|NP_001031908|]
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transferases/nucleotidyltransferase [Arabidopsis thaliana]

Protein Classification

translation initiation factor eIF-2B subunit gamma( domain architecture ID 10135962)

translation initiation factor eIF-2B subunit gamma is an essential component of the the translation initiation factor 2B (eIF-2B), a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex

CATH:  2.160.10.10
Gene Ontology:  GO:0005851|GO:0003743|GO:0005085|GO:0032045
PubMed:  9438375|10521532|12691742|9445404|11747907|15500694|7893825
SCOP:  3000077

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-220 1.59e-71

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: 225.23  E-value: 1.59e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173   3 FQVVILAGGFSSYLVPLVAKeVPKALLPVANRPVLSYVLDLLESSNLKDLIVVVEGEDAALKVGGWISS--ACVDRLHVE 80
Cdd:cd04198   1 FQAVILAGGGGSRLYPLTDN-IPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSFplNLKQKLDEV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173  81 VAAVAENVGTAGALRAIAHHLTaKDILIVSGDIVSDIPPGAVAATHRRHDAAVTVMLCAQPVSGPSESGgsggKDKTKKP 160
Cdd:cd04198  80 TIVLDEDMGTADSLRHIRKKIK-KDFLVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVSSEQKGG----KGKSKKA 154

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173 161 ACDDIIGLDSLKQFLLYIAKGTEIKKDTRVKKSILCAAGKMEIRSDLMDSHIYAFKRAVL 220
Cdd:cd04198 155 DERDVIGLDEKTQRLLFITSEEDLDEDLELRKSLLKRHPRVTITTKLLDAHVYIFKRWVL 214
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 367-447 3.77e-36

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: 128.08  E-value: 3.77e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173 367 MLGEGSQVGDKCSVKRSVIGRHCRIGSNVKIVNSVVMDHATIGDGCSIQGSVICSNAQLQERVTLRDCQVEAGYVVCAGS 446
Cdd:cd04652   1 LVGENTQVGEKTSIKRSVIGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLVGSGYRVEAGT 80


                .
gi 79328173 447 E 447
Cdd:cd04652  81 E 81
 
Name Accession Description Interval E-value
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-220 1.59e-71

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: 225.23  E-value: 1.59e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173   3 FQVVILAGGFSSYLVPLVAKeVPKALLPVANRPVLSYVLDLLESSNLKDLIVVVEGEDAALKVGGWISS--ACVDRLHVE 80
Cdd:cd04198   1 FQAVILAGGGGSRLYPLTDN-IPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSFplNLKQKLDEV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173  81 VAAVAENVGTAGALRAIAHHLTaKDILIVSGDIVSDIPPGAVAATHRRHDAAVTVMLCAQPVSGPSESGgsggKDKTKKP 160
Cdd:cd04198  80 TIVLDEDMGTADSLRHIRKKIK-KDFLVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVSSEQKGG----KGKSKKA 154

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173 161 ACDDIIGLDSLKQFLLYIAKGTEIKKDTRVKKSILCAAGKMEIRSDLMDSHIYAFKRAVL 220
Cdd:cd04198 155 DERDVIGLDEKTQRLLFITSEEDLDEDLELRKSLLKRHPRVTITTKLLDAHVYIFKRWVL 214
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 367-447 3.77e-36

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: 128.08  E-value: 3.77e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173 367 MLGEGSQVGDKCSVKRSVIGRHCRIGSNVKIVNSVVMDHATIGDGCSIQGSVICSNAQLQERVTLRDCQVEAGYVVCAGS 446
Cdd:cd04652   1 LVGENTQVGEKTSIKRSVIGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLVGSGYRVEAGT 80


                .
gi 79328173 447 E 447
Cdd:cd04652  81 E 81
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 4-137 4.99e-25

NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 102.92  E-value: 4.99e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173   4 QVVILAGGFSSYLVPLVaKEVPKALLPVANRPVLSYVLDLLESSNLKDLIVVV--EGED--AALKVGgwissacvDRLHV 79
Cdd:COG1208   1 KAVILAGGLGTRLRPLT-DTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVgyLAEQieEYFGDG--------SRFGV 71

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173  80 EVAAVAENV--GTAGALRAIAHHLTAKDILIVSGDIVSDIPPGAVAATHRRHDAAVTVML 137
Cdd:COG1208  72 RITYVDEGEplGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALLAFHREKGADATLAL 131
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 349-419 2.32e-13

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: 70.82  E-value: 2.32e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79328173 349 IVHPSAELGSKTTVGPHCMLGEGSQVGDKCSVK-RSVIGRHCRIGSNVKIV-NSVVMDHATIGDGCSIQ-GSVI 419
Cdd:COG1044 104 VIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGpGVVIGDGVVIGDDCVLHpNVTIYERCVIGDRVIIHsGAVI 177
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 349-419 1.21e-11

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 65.55  E-value: 1.21e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79328173  349 IVHPSAELGSKTTVGPHCMLGEGSQVGDKCSV-------KRSVIGRHCRIGSNVKIVNSVVmdhatIGDGCSIQ-GSVI 419
Cdd:PRK00892 108 VIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIgagavigDGVKIGADCRLHANVTIYHAVR-----IGNRVIIHsGAVI 181
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 6-135 9.90e-09

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 55.72  E-value: 9.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173     6 VILAGGFSSYLVPLvAKEVPKALLPVANR-PVLSYVLDLLESSNLKDLIVVVEGEDAA-----LKVGGwissacvdRLHV 79
Cdd:pfam00483   3 IILAGGSGTRLWPL-TRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFmlnelLGDGS--------KFGV 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173    80 EVAAVAENV--GTAGALRAIAHHL--TAKDILIVSGDIVSDIPPGAVAATHRRHDAAVTV 135
Cdd:pfam00483  74 QITYALQPEgkGTAPAVALAADFLgdEKSDVLVLGGDHIYRMDLEQAVKFHIEKAADATV 133
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 340-446 1.15e-08

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: 1.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173   340 GYSFSahhNIVHPSAelgsktTVGPHCMLGEGSQVGDKCsvkrsVIGRHCRIGSNVkIVNS-VVMDH-ATIGDGCSIQ-G 416
Cdd:TIGR03570  83 GYRFA---TLIHPSA------IVSPSASIGEGTVIMAGA-----VINPDVRIGDNV-IINTgAIVEHdCVIGDFVHIApG 147

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 79328173   417 SVICSNAQLQERV------TLRD-CQVEAGYVVCAGS 446
Cdd:TIGR03570 148 VTLSGGVVIGEGVfigagaTIIQgVTIGAGAIVGAGA 184
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 78-431 2.47e-07

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 52.58  E-value: 2.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173   78 HVEVAAVAENV-------GTAGALRAIAHHLTAKDI---LIVSGDIVSDIPPGAVAATHRRHDAAVTVmlCAQPVsgpse 147
Cdd:PRK02862  81 FVEVLAAQQTPenpswfqGTADAVRKYLWHFQEWDVdeyLILSGDQLYRMDYRLFVQHHRETGADITL--AVLPV----- 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173  148 sggsggkdkTKKPACD-DIIGLDSLKQFLLYIAK--GTEIKkDTRVKKSILCAAGKMEIRSDLMDSH-IYAFKRAVLQEV 223
Cdd:PRK02862 154 ---------DEKDASGfGLMKTDDDGRITEFSEKpkGDELK-AMAVDTSRLGLSPEEAKGKPYLASMgIYVFSRDVLFDL 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173  224 LDQKPAFRSLKQDVLPYLVRT-QLRSDVFSDqsnveengngngknnmqnnevvlsqilsnasmpsfhqvYESGLGTrkth 302
Cdd:PRK02862 224 LNKNPEYTDFGKEIIPEAIRDyKVQSYLFDG--------------------------------------YWEDIGT---- 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173  303 kccvyiadeskyfvrlnsIQAFMDVNRDVIGESN-HLSGYSFSA----HHNIVHPSAELGSKTTvgpHCMLGEGSQVgDK 377
Cdd:PRK02862 262 ------------------IEAFYEANLALTQQPNpPFSFYDEKApiytRARYLPPSKLLDATIT---ESIIAEGCII-KN 319

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79328173  378 CSVKRSVIGRHCRIGSNVKIVNSVVM-------------------DHATIGDGCSIQGSVICSNAQLQERVTL 431
Cdd:PRK02862 320 CSIHHSVLGIRSRIESGCTIEDTLVMgadfyesseereelrkegkPPLGIGEGTTIKRAIIDKNARIGNNVRI 392
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
388-414 1.84e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.78  E-value: 1.84e-03
                          10        20
                  ....*....|....*....|....*...
gi 79328173   388 HCRIGSNVKI-VNSVVMDHATIGDGCSI 414
Cdd:pfam00132   1 GTVIGDNVLIgPNAVIGGGVIIGDNVII 28
 
Name Accession Description Interval E-value
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-220 1.59e-71

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: 225.23  E-value: 1.59e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173   3 FQVVILAGGFSSYLVPLVAKeVPKALLPVANRPVLSYVLDLLESSNLKDLIVVVEGEDAALKVGGWISS--ACVDRLHVE 80
Cdd:cd04198   1 FQAVILAGGGGSRLYPLTDN-IPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSFplNLKQKLDEV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173  81 VAAVAENVGTAGALRAIAHHLTaKDILIVSGDIVSDIPPGAVAATHRRHDAAVTVMLCAQPVSGPSESGgsggKDKTKKP 160
Cdd:cd04198  80 TIVLDEDMGTADSLRHIRKKIK-KDFLVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVSSEQKGG----KGKSKKA 154

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173 161 ACDDIIGLDSLKQFLLYIAKGTEIKKDTRVKKSILCAAGKMEIRSDLMDSHIYAFKRAVL 220
Cdd:cd04198 155 DERDVIGLDEKTQRLLFITSEEDLDEDLELRKSLLKRHPRVTITTKLLDAHVYIFKRWVL 214
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 3-220 1.58e-51

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: 173.21  E-value: 1.58e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173   3 FQVVILAGGFSSYLVPLvAKEVPKALLPVANRPVLSYVLDLLESSNLKDLIVVVEGEDAALKVGGWISSACVDR----LH 78
Cdd:cd02507   1 FQAVVLADGFGSRFLPL-TSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSKWSSLSskmiVD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173  79 VEVAAVAENVGTAGALRAIAHHLTaKDILIVSGDIVSDIPPGAVAAT----HRRHDAAVTVMLCAQPVsgpsesggsgGK 154
Cdd:cd02507  80 VITSDLCESAGDALRLRDIRGLIR-SDFLLLSCDLVSNIPLSELLEErrkkDKNAIATLTVLLASPPV----------ST 148

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79328173 155 DKTKKPACDDIIGLDSLKQFLLYIAKGTEIKKDTRV--KKSILCAAGKMEIRSDLMDSHIYAFKRAVL 220
Cdd:cd02507 149 EQSKKTEEEDVIAVDSKTQRLLLLHYEEDLDEDLELiiRKSLLSKHPNVTIRTDLLDCHIYICSPDVL 216
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 367-447 3.77e-36

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: 128.08  E-value: 3.77e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173 367 MLGEGSQVGDKCSVKRSVIGRHCRIGSNVKIVNSVVMDHATIGDGCSIQGSVICSNAQLQERVTLRDCQVEAGYVVCAGS 446
Cdd:cd04652   1 LVGENTQVGEKTSIKRSVIGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLVGSGYRVEAGT 80


                .
gi 79328173 447 E 447
Cdd:cd04652  81 E 81
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 4-137 4.99e-25

NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 102.92  E-value: 4.99e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173   4 QVVILAGGFSSYLVPLVaKEVPKALLPVANRPVLSYVLDLLESSNLKDLIVVV--EGED--AALKVGgwissacvDRLHV 79
Cdd:COG1208   1 KAVILAGGLGTRLRPLT-DTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVgyLAEQieEYFGDG--------SRFGV 71

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173  80 EVAAVAENV--GTAGALRAIAHHLTAKDILIVSGDIVSDIPPGAVAATHRRHDAAVTVML 137
Cdd:COG1208  72 RITYVDEGEplGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALLAFHREKGADATLAL 131
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 5-137 8.54e-23

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: 96.11  E-value: 8.54e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173   5 VVILAGGFSSYLVPLvAKEVPKALLPVANRPVLSYVLDLLESSNLKDLIVVVeGEDAAL---KVGGWissacvDRLHVEV 81
Cdd:cd04181   1 AVILAAGKGTRLRPL-TDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVV-GYLGEQieeYFGDG------SKFGVNI 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 79328173  82 AAVAENV--GTAGALRAIAHHLTAKDILIVSGDIVSDIPPGAVAATHRRHDAAVTVML 137
Cdd:cd04181  73 EYVVQEEplGTAGAVRNAEDFLGDDDFLVVNGDVLTDLDLSELLRFHREKGADATIAV 130
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 368-436 4.33e-22

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: 89.61  E-value: 4.33e-22
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79328173 368 LGEGSQVGDKCSVKRSVIGRHCRIGSNVKIVNSVVMDHATIGDGCSIQGSVICSNAQLQERVTLRDCQV 436
Cdd:cd03356   2 IGESTVIGENAIIKNSVIGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVNLCI 70
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 368-433 3.11e-20

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: 84.55  E-value: 3.11e-20
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79328173 368 LGEGSQVGDKCSVKRSVIGRHCRIGSNVKIVNSVVMDHATIGDGCSIQGSVICSNAQLQERVTLRD 433
Cdd:cd05787   2 IGRGTSIGEGTTIKNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIPP 67
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 5-243 1.35e-16

WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is involved in the biosynthesis, export or translocation of capsule. It is a subfamily of nucleotidyl transferases that transfer nucleotides onto phosphosugars.


Pssm-ID: 133065 [Multi-domain]  Cd Length: 223  Bit Score: 78.36  E-value: 1.35e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173   5 VVILAGGFSSYLVPLVaKEVPKALLPVANRPVLSYVLDLLESSNLKDLIVVVegedaalkvgGWISSACVDRLH------ 78
Cdd:cd06915   1 AVILAGGLGTRLRSVV-KDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSV----------GYLAEQIEEYFGdgyrgg 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173  79 VEVAAVAENV--GTAGALRAIAHHLTAKDILIVSGDIVSDIPPGAVAATHRRHDAAVTVMLcaqpvsgpsesggsggkdk 156
Cdd:cd06915  70 IRIYYVIEPEplGTGGAIKNALPKLPEDQFLVLNGDTYFDVDLLALLAALRASGADATMAL------------------- 130

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173 157 TKKPACDDiigldslkqfllyiaKGT-EIKKDTRVkksILCAAGKMEIRSDLMDSHIYAFKRAVLQEVLDQKPafrSLKQ 235
Cdd:cd06915 131 RRVPDASR---------------YGNvTVDGDGRV---IAFVEKGPGAAPGLINGGVYLLRKEILAEIPADAF---SLEA 189


                ....*...
gi 79328173 236 DVLPYLVR 243
Cdd:cd06915 190 DVLPALVK 197
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 349-419 2.32e-13

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: 70.82  E-value: 2.32e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79328173 349 IVHPSAELGSKTTVGPHCMLGEGSQVGDKCSVK-RSVIGRHCRIGSNVKIV-NSVVMDHATIGDGCSIQ-GSVI 419
Cdd:COG1044 104 VIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGpGVVIGDGVVIGDDCVLHpNVTIYERCVIGDRVIIHsGAVI 177
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-213 1.17e-12

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: 66.86  E-value: 1.17e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173   3 FQVVILAGGFSSYLVPLvAKEVPKALLPVANRPVLSYVLDLLESSNLKDLIVVVEGEDAALK--VGGWISSACVDRLHVE 80
Cdd:cd04197   1 LQAVVLADSFNRRFRPL-TKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKeyIEKSKWSKPKSSLMIV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173  81 VAAVAENVGTAG-ALRAI-AHHLTAKDILIVSGDIVSDIPPGAVAATHRRH-----DAAVTVML--CAQPVsgpsesggs 151
Cdd:cd04197  80 IIIMSEDCRSLGdALRDLdAKGLIRGDFILVSGDVVSNIDLKEILEEHKERrkkdkNAIMTMVLkeASPPH--------- 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79328173 152 ggkdKTKKPACDDIIGLDSLKQFLLYIAKGTEIKKDTRVK--KSILCAAGKMEIRSDLMDSHIY 213
Cdd:cd04197 151 ----RTRRTGEEFVIAVDPKTSRLLHYEELPGSKYRSITDlpSELLGSNSEVEIRHDLLDCHID 210
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 314-431 2.12e-12

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 68.18  E-value: 2.12e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173 314 YFVRLNSIQAFMDVNRDVIGESNHLSGYS-----FSAHHNivHPSAELGSKTTVGpHCMLGEGSQVGDKcsVKRSVIGRH 388
Cdd:COG0448 235 YWRDVGTIDSYYEANMDLLDPEPEFNLYDpewpiYTKQKD--LPPAKFVRGGKVK-NSLVSNGCIISGT--VENSVLFRG 309

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 79328173 389 CRIGSNVKIVNSVVMDHATIGDGCSIQGSVICSNAQLQERVTL 431
Cdd:COG0448 310 VRVESGAVVENSVIMPGVVIGEGAVIENAIIDKNVVIPPGVVI 352
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 7-137 2.54e-12

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: 66.06  E-value: 2.54e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173   7 ILAGGFSSYLVPLVAKeVPKALLPVANRPVLSYVLDLLESSNLKDLIVVVE--GE--DAALKVGGWIssacvDRLHV--E 80
Cdd:cd06422   4 ILAAGLGTRMRPLTDT-RPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHhlADqiEAHLGDSRFG-----LRITIsdE 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 79328173  81 VAAVAEnvgTAGALRAIAHHLTAKDILIVSGDIVSDIPPGAVAATHR-RHDAAVTVML 137
Cdd:cd06422  78 PDELLE---TGGGIKKALPLLGDEPFLVVNGDILWDGDLAPLLLLHAwRMDALLLLLP 132
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 349-419 1.21e-11

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 65.55  E-value: 1.21e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79328173  349 IVHPSAELGSKTTVGPHCMLGEGSQVGDKCSV-------KRSVIGRHCRIGSNVKIVNSVVmdhatIGDGCSIQ-GSVI 419
Cdd:PRK00892 108 VIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIgagavigDGVKIGADCRLHANVTIYHAVR-----IGNRVIIHsGAVI 181
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 367-432 5.13e-11

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: 59.40  E-value: 5.13e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79328173 367 MLGEGSQVgDKCSVKRSVIGRHCRIGSNVKIVNSVVMDHATIGDGCSIQGSVICSNAQLQERVTLR 432
Cdd:cd04651  14 LVSEGCII-SGGTVENSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIIDKNVVIPDGVVIG 78
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 353-419 2.21e-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: 60.11  E-value: 2.21e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173 353 SAELGSKTTVGPHCMLGEGSQVGDKCSVK-RSVIGRHCRIGSNVKI-VNSVVMDHATIGDGCSIQ-GSVI 419
Cdd:cd03352   1 SAKIGENVSIGPNAVIGEGVVIGDGVVIGpGVVIGDGVVIGDDCVIhPNVTIYEGCIIGDRVIIHsGAVI 70
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 349-419 3.90e-10

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: 60.03  E-value: 3.90e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79328173 349 IVHPSAELGSKTTVGPHCMLGEGsqVgdkcsvkrsVIGRHCRIGSNVkivnsVVMDHATIGDGCSI-QGSVI 419
Cdd:COG1043   9 IVDPGAKLGENVEIGPFCVIGPD--V---------EIGDGTVIGSHV-----VIEGPTTIGKNNRIfPFASI 64
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
4-135 1.44e-09

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 58.33  E-value: 1.44e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173   4 QVVILAGGFSSYLVPLvAKEVPKALLPVANRPVLSYVLDLLESSNLKDLIVVV-----EGEDAALKVGGwissaCVDRLH 78
Cdd:COG1213   1 KAVILAAGRGSRLGPL-TDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTgykaeLIEEALARPGP-----DVTFVY 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 79328173  79 VEVAAVAENVGTAgalrAIAHHLTAKDILIVSGDIVSDipPGAVAATHR-RHDAAVTV 135
Cdd:COG1213  75 NPDYDETNNIYSL----WLAREALDEDFLLLNGDVVFD--PAILKRLLAsDGDIVLLV 126
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 5-135 2.40e-09

NTP_trnasferase_like_2 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: 133048 [Multi-domain]  Cd Length: 220  Bit Score: 57.14  E-value: 2.40e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173   5 VVILAGGFSSYLVPLVaKEVPKALLPVANRPVLSYVLDLLESSNLKDLIVVVE--GE--DAALKVGgwissacvDRLHVE 80
Cdd:cd06426   1 VVIMAGGKGTRLRPLT-ENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNylAEmiEDYFGDG--------SKFGVN 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 79328173  81 VAAVAEN--VGTAGALRAIAHHLTAkDILIVSGDIVSDIPPGAVAATHRRHDAAVTV 135
Cdd:cd06426  72 ISYVREDkpLGTAGALSLLPEKPTD-PFLVMNGDILTNLNYEHLLDFHKENNADATV 127
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 321-433 4.90e-09

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 57.96  E-value: 4.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173  321 IQAFMDVNRDVIGESNHLSGYS-----FSahHNIVHPSAELGSKTTVgphcmlgEGSQVGDKC----SVKRSVIGRHCRI 391
Cdd:PRK05293 247 IESLWEANMELLRPENPLNLFDrnwriYS--VNPNLPPQYIAENAKV-------KNSLVVEGCvvygTVEHSVLFQGVQV 317

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 79328173  392 GSNVKIVNSVVMDHATIGDGCSIQGSVICSNAQLQERVTLRD 433
Cdd:PRK05293 318 GEGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVIIGG 359
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
349-419 6.97e-09

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 56.65  E-value: 6.97e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79328173  349 IVHPSAELGSKTTVGPHCMLGEgsQVgdkcsvkrsVIGRHCRIGSNVkivnsVVMDHATIGDGCSI-QGSVI 419
Cdd:PRK05289  10 IVEPGAKIGENVEIGPFCVIGP--NV---------VIGDGTVIGSHV-----VIDGHTTIGKNNRIfPFASI 65
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 6-135 9.90e-09

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 55.72  E-value: 9.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173     6 VILAGGFSSYLVPLvAKEVPKALLPVANR-PVLSYVLDLLESSNLKDLIVVVEGEDAA-----LKVGGwissacvdRLHV 79
Cdd:pfam00483   3 IILAGGSGTRLWPL-TRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFmlnelLGDGS--------KFGV 73

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173    80 EVAAVAENV--GTAGALRAIAHHL--TAKDILIVSGDIVSDIPPGAVAATHRRHDAAVTV 135
Cdd:pfam00483  74 QITYALQPEgkGTAPAVALAADFLgdEKSDVLVLGGDHIYRMDLEQAVKFHIEKAADATV 133
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 340-446 1.15e-08

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: 1.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173   340 GYSFSahhNIVHPSAelgsktTVGPHCMLGEGSQVGDKCsvkrsVIGRHCRIGSNVkIVNS-VVMDH-ATIGDGCSIQ-G 416
Cdd:TIGR03570  83 GYRFA---TLIHPSA------IVSPSASIGEGTVIMAGA-----VINPDVRIGDNV-IINTgAIVEHdCVIGDFVHIApG 147

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 79328173   417 SVICSNAQLQERV------TLRD-CQVEAGYVVCAGS 446
Cdd:TIGR03570 148 VTLSGGVVIGEGVfigagaTIIQgVTIGAGAIVGAGA 184
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 1-136 1.63e-08

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 56.57  E-value: 1.63e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173   1 MDFQVVILAGGF-----SSYlvplvakevPKALLPVANRPVLSYVLDLLESSNLKDLIVVV--EGEdaalKVggwisSAC 73
Cdd:COG1207   1 SPLAVVILAAGKgtrmkSKL---------PKVLHPLAGKPMLEHVLDAARALGPDRIVVVVghGAE----QV-----RAA 62

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79328173  74 VDRLHVEVAAVAENVGTAGALRAIAHHLTAKD--ILIVSGDIvsdipP-------GAVAATHRRHDAAVTVM 136
Cdd:COG1207  63 LADLDVEFVLQEEQLGTGHAVQQALPALPGDDgtVLVLYGDV-----PliraetlKALLAAHRAAGAAATVL 129
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 5-136 2.19e-08

N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain and a C-terminal Lefthanded-beta-Helix fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes, such as cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133047 [Multi-domain]  Cd Length: 233  Bit Score: 54.52  E-value: 2.19e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173   5 VVILAGGFSSYLVPLVAKeVPKALLPVANRPVLSYVLDLLESSNLKDLIVVV--EGEDAALKVGGWissacVDRLHVEVA 82
Cdd:cd06425   3 ALILVGGYGTRLRPLTLT-VPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVnyRPEDMVPFLKEY-----EKKLGIKIT 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79328173  83 AVAEN--VGTAGALRaiahhlTAKDILIVSG--------DIVSDIPPGAVAATHRRHDAAVTVM 136
Cdd:cd06425  77 FSIETepLGTAGPLA------LARDLLGDDDepffvlnsDVICDFPLAELLDFHKKHGAEGTIL 134
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 5-138 3.72e-08

N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively.


Pssm-ID: 133020 [Multi-domain]  Cd Length: 229  Bit Score: 54.06  E-value: 3.72e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173   5 VVILAGGF-----SSYlvplvakevPKALLPVANRPVLSYVLDLLESSNLKDLIVVV-EGEDAALKVggwissacVDRLH 78
Cdd:cd02540   1 AVILAAGKgtrmkSDL---------PKVLHPLAGKPMLEHVLDAARALGPDRIVVVVgHGAEQVKKA--------LANPN 63

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79328173  79 VEVAAVAENVGTAGALRAIAHHLT--AKDILIVSGDI----VSDIppGAVAATHRRHDAAVTVMLC 138
Cdd:cd02540  64 VEFVLQEEQLGTGHAVKQALPALKdfEGDVLVLYGDVplitPETL--QRLLEAHREAGADVTVLTA 127
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 349-419 5.68e-08

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: 53.59  E-value: 5.68e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79328173 349 IVHPSAELGSKTTVGPHCMLGEGsqvgdkcsvkrSVIGRHCRIGSNVkivnsVVMDHATIGDGCSI-QGSVI 419
Cdd:cd03351   7 IVDPGAKIGENVEIGPFCVIGPN-----------VEIGDGTVIGSHV-----VIDGPTTIGKNNRIfPFASI 62
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-133 6.46e-08

Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 52.50  E-value: 6.46e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173   1 MDFQVVILAGGFSSYLvplvakEVPKALLPVANRPVLSYVLDLLESSnLKDLIVVVEGEDAalkvggwissacVDRLHVE 80
Cdd:COG0746   3 MPITGVILAGGRSRRM------GQDKALLPLGGRPLLERVLERLRPQ-VDEVVIVANRPER------------YAALGVP 63

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173  81 VaaVAENVGTAGALRAIA---HHLTAKDILIVSGDIVsDIPPGAV----AATHRRHDAAV 133
Cdd:COG0746  64 V--VPDDPPGAGPLAGILaalEAAPAEWVLVLACDMP-FLPPDLVrrllEALEEGADAVV 120
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 348-442 6.65e-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: 52.49  E-value: 6.65e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173 348 NIVHPSAelgsktTVGPHCMLGEGSQVGdkcsvKRSVIGRHCRIGSNVkIVNS--VVMDHATIGDGCSI----------- 414
Cdd:cd03360  85 TLIHPSA------VVSPSAVIGEGCVIM-----AGAVINPDARIGDNV-IINTgaVIGHDCVIGDFVHIapgvvlsggvt 152

                        90       100       110
                ....*....|....*....|....*....|.
gi 79328173 415 --QGSVICSNAQLQERVTL-RDCQVEAGYVV 442
Cdd:cd03360 153 igEGAFIGAGATIIQGVTIgAGAIIGAGAVV 183
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 5-56 7.85e-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: 53.01  E-value: 7.85e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 79328173   5 VVILAGGFSSYLVPLvAKEVPKALLPVANRPVLSYVLDLLESSNLKDLIVVV 56
Cdd:cd02523   1 AIILAAGRGSRLRPL-TEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVT 51
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 78-431 2.47e-07

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 52.58  E-value: 2.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173   78 HVEVAAVAENV-------GTAGALRAIAHHLTAKDI---LIVSGDIVSDIPPGAVAATHRRHDAAVTVmlCAQPVsgpse 147
Cdd:PRK02862  81 FVEVLAAQQTPenpswfqGTADAVRKYLWHFQEWDVdeyLILSGDQLYRMDYRLFVQHHRETGADITL--AVLPV----- 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173  148 sggsggkdkTKKPACD-DIIGLDSLKQFLLYIAK--GTEIKkDTRVKKSILCAAGKMEIRSDLMDSH-IYAFKRAVLQEV 223
Cdd:PRK02862 154 ---------DEKDASGfGLMKTDDDGRITEFSEKpkGDELK-AMAVDTSRLGLSPEEAKGKPYLASMgIYVFSRDVLFDL 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173  224 LDQKPAFRSLKQDVLPYLVRT-QLRSDVFSDqsnveengngngknnmqnnevvlsqilsnasmpsfhqvYESGLGTrkth 302
Cdd:PRK02862 224 LNKNPEYTDFGKEIIPEAIRDyKVQSYLFDG--------------------------------------YWEDIGT---- 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173  303 kccvyiadeskyfvrlnsIQAFMDVNRDVIGESN-HLSGYSFSA----HHNIVHPSAELGSKTTvgpHCMLGEGSQVgDK 377
Cdd:PRK02862 262 ------------------IEAFYEANLALTQQPNpPFSFYDEKApiytRARYLPPSKLLDATIT---ESIIAEGCII-KN 319

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79328173  378 CSVKRSVIGRHCRIGSNVKIVNSVVM-------------------DHATIGDGCSIQGSVICSNAQLQERVTL 431
Cdd:PRK02862 320 CSIHHSVLGIRSRIESGCTIEDTLVMgadfyesseereelrkegkPPLGIGEGTTIKRAIIDKNARIGNNVRI 392
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 5-135 9.44e-07

MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 48.34  E-value: 9.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173     5 VVILAGGFSSYLvplvakEVPKALLPVANRPVLSYVLDLLESSNlKDLIVVVEGEDAAlkvggwissACVDRLHVEVAAV 84
Cdd:pfam12804   1 AVILAGGRSSRM------GGDKALLPLGGKPLLERVLERLRPAG-DEVVVVANDEEVL---------AALAGLGVPVVPD 64

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 79328173    85 A-ENVGTAGALR-AIAHHLTAKDILIVSGDIVsDIPPGAV---AATHRRHDAAVTV 135
Cdd:pfam12804  65 PdPGQGPLAGLLaALRAAPGADAVLVLACDMP-FLTPELLrrlLAAAEESGADIVV 119
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 349-430 9.70e-07

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 50.02  E-value: 9.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173  349 IVHPSAELGSKTTVGPHCMLGEGSQVGDKCSV-KRSVIGRHCRIGSNVKI-VNSVVMD------------HATIGDGCSI 414
Cdd:PRK12461   7 VIDPSAKLGSGVEIGPFAVIGANVEIGDGTWIgPHAVILGPTRIGKNNKIhQGAVVGDepqdftykgeesRLEIGDRNVI 86

                         90
                 ....*....|....*.
gi 79328173  415 QGSVICSNAQLQERVT 430
Cdd:PRK12461  87 REGVTIHRGTKGGGVT 102
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 365-416 1.05e-06

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


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 47.07  E-value: 1.05e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 79328173 365 HCMLGEGSQVGDKCSVKRSVIGRHCRIGSNVKIVNSVVMDHATIGDGCSIQG 416
Cdd:cd04651  28 NSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIIDKNVVIPDGVVIGG 79
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 6-56 1.08e-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: 49.49  E-value: 1.08e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 79328173   6 VILAGGFSSYLVPLvAKEVPKALLPVANRPVLSYVLDLLESSNLKDLIVVV 56
Cdd:cd04189   4 LILAGGKGTRLRPL-TYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVV 53
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
1-135 1.22e-06

CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 49.00  E-value: 1.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173   1 MDFQVVILAGGFSSYLvplvakEVPKALLPVANRPVLSYVLDLLESSNLKDLIVVVEGEDAALKvggwissACVDRLHVE 80
Cdd:COG2068   2 SKVAAIILAAGASSRM------GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVA-------AALAGLGVR 68

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79328173  81 VAAVAE-NVGTAGALRAIAHHL--TAKDILIVSGDIVsDIPPG---AVAATHRRHDAAVTV 135
Cdd:COG2068  69 VVVNPDwEEGMSSSLRAGLAALpaDADAVLVLLGDQP-LVTAEtlrRLLAAFRESPASIVA 128
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 350-430 1.62e-06

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 50.03  E-value: 1.62e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173 350 VHPSAELGSKTTVGPHCMLgEGsqvgdkcsvkRSVIGRHCRIGSNVKIVNSvvmdhaTIGDGCSIQGSVIcSNAQLQERV 429
Cdd:COG1207 263 IDGDVEIGRDVVIDPNVIL-EG----------KTVIGEGVVIGPNCTLKDS------TIGDGVVIKYSVI-EDAVVGAGA 324


                .
gi 79328173 430 T 430
Cdd:COG1207 325 T 325
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 349-429 1.75e-06

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 49.93  E-value: 1.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173  349 IVHPSAELGSKTTVGPHCMLG-----EGSQVGDKCSVKRSVIgRHCRIGSNVKI-VNSVVMDHATIGDGCSIQGSVICSN 422
Cdd:PRK14360 270 IIEPQTHLRGNTVIGSGCRIGpgsliENSQIGENVTVLYSVV-SDSQIGDGVKIgPYAHLRPEAQIGSNCRIGNFVEIKK 348


                 ....*..
gi 79328173  423 AQLQERV 429
Cdd:PRK14360 349 SQLGEGS 355
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 6-136 2.73e-06

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 49.48  E-value: 2.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173    6 VILAGGFSSYLvplvAKEVPKALLPVANRPVLSYVLDLLESSNLKDLIVVVeGEDAAlKVGgwissACVDRLHVEVAAV- 84
Cdd:PRK14353   9 IILAAGEGTRM----KSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVV-GPGAE-AVA-----AAAAKIAPDAEIFv 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 79328173   85 -AENVGTAGALRAIAHHLT--AKDILIVSGDiVSDIPPGAVAA--THRRHDAAVTVM 136
Cdd:PRK14353  78 qKERLGTAHAVLAAREALAggYGDVLVLYGD-TPLITAETLARlrERLADGADVVVL 133
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 5-139 2.88e-06

GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 47.55  E-value: 2.88e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173   5 VVILAGGFSSYLvplvakEVPKALLPVANRPVLSYVLDLLESSNLKDLIVVVEGEDAALKvgGWISSACVDRLHVEVAav 84
Cdd:cd04182   3 AIILAAGRSSRM------GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVR--AALAGLPVVVVINPDW-- 72

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173  85 AENVGT--AGALRAIAHHLTAkdILIVSGDIVsDIPPG---AVAATHRRHDAAVTVMLCA 139
Cdd:cd04182  73 EEGMSSslAAGLEALPADADA--VLILLADQP-LVTAEtlrALIDAFREDGAGIVAPVYQ 129
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 350-414 3.03e-06

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 49.36  E-value: 3.03e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79328173  350 VHPSAELGSKTTVGPHCMLGEGSQVGDKCSVKRSVIGRHCRIGSNVKIVNSVVMDHATIGDGCSI 414
Cdd:PRK14355 265 IDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVIKGCRIGDDVTVKAGSVLEDSVVGDDVAI 329
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 5-136 3.69e-06

G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; Alpha-D-Glucose-1-phosphate Cytidylyltransferase catalyzes the production of CDP-D-Glucose from alpha-D-Glucose-1-phosphate and MgCTP as substrate. CDP-D-Glucose is the precursor for synthesizing four of the five naturally occurring 3,6-dideoxy sugars-abequose (3,6-dideoxy-D-Xylo-hexose), ascarylose (3,6-dideoxy-L-arabino-hexose), paratose (3,6-dideoxy-D-ribohexose), and tyvelose (3,6-dideoxy-D-arabino-hexose. Deoxysugars are ubiquitous in nature where they function in a variety of biological processes, including cell adhesion, immune response, determination of ABO blood groups, fertilization, antibiotic function, and microbial pathogenicity.


Pssm-ID: 133015 [Multi-domain]  Cd Length: 253  Bit Score: 48.34  E-value: 3.69e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173   5 VVILAGGFSSYLvplvAKE---VPKALLPVANRPVLSYVLDLLESSNLKDLIVvvegedaALKVGGWI------------ 69
Cdd:cd02524   1 VVILAGGLGTRL----SEEtelKPKPMVEIGGRPILWHIMKIYSHYGHNDFIL-------CLGYKGHVikeyflnyflhn 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173  70 SSACVD------RLH--------VEVAAVAENVGTAGALRAIAHHL-TAKDILIVSGDIVSDIPPGAVAATHRRHDAAVT 134
Cdd:cd02524  70 SDVTIDlgtnriELHnsdiedwkVTLVDTGLNTMTGGRLKRVRRYLgDDETFMLTYGDGVSDVNINALIEFHRSHGKLAT 149


                ..
gi 79328173 135 VM 136
Cdd:cd02524 150 VT 151
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-135 3.69e-06

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 49.06  E-value: 3.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173    1 MDFQVVILAGG----FSSYLvplvakevPKALLPVANRPVLSYVLDLLESSNLKDLIVVV--EGEDAALKVGGwissacv 74
Cdd:PRK14354   1 MNRYAIILAAGkgtrMKSKL--------PKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVghGAEEVKEVLGD------- 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79328173   75 drlHVEVAAVAENVGTAGALRAIAHHLTAKD--ILIVSGD---IVSDIPPgAVAATHRRHDAAVTV 135
Cdd:PRK14354  66 ---RSEFALQEEQLGTGHAVMQAEEFLADKEgtTLVICGDtplITAETLK-NLIDFHEEHKAAATI 127
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
6-63 7.91e-06

dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 47.39  E-value: 7.91e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 79328173   6 VILAGGFSSYLVPLvAKEVPKALLPVANRPVLSYVLDLLESSNLKDLIVVVEGEDAAL 63
Cdd:COG1209   4 IILAGGSGTRLRPL-TLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQ 60
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 320-419 1.36e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 47.13  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173  320 SIQAFMDVNRDVIGESNHLSGYS-----FSAHHN-----IVHPSAELGSKTTvgphCMLGEGSQVgDKCSVKRSVIGRHC 389
Cdd:PRK00844 264 TIDAYYDAHMDLLSVHPVFNLYNrewpiYTSSPNlppakFVDGGGRVGSAQD----SLVSAGSII-SGATVRNSVLSPNV 338

                         90       100       110
                 ....*....|....*....|....*....|
gi 79328173  390 RIGSNVKIVNSVVMDHATIGDGCSIQGSVI 419
Cdd:PRK00844 339 VVESGAEVEDSVLMDGVRIGRGAVVRRAIL 368
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 349-439 1.48e-05

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


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 45.27  E-value: 1.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173 349 IVHPSAELGSKTTVGPHCMLGEGSQVGDKCSVKRSV-IGRHCRIGSNVKIVNSVVMDHA-----------TIGDGCSIQG 416
Cdd:cd05636  19 WIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTvLGDGCVVGNSVEVKNSIIMDGTkvphlnyvgdsVLGENVNLGA 98

                        90       100
                ....*....|....*....|....*.
gi 79328173 417 SVICSNAQLQE---RVTLRDCQVEAG 439
Cdd:cd05636  99 GTITANLRFDDkpvKVRLKGERVDTG 124
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 350-412 1.74e-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: 44.67  E-value: 1.74e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173 350 VHPSAELGSKTTVGPHC---------------MLGEGSQVGDKCsVKRSVIGRH-----------------CRIGSNVKI 397
Cdd:cd04745   9 VHPTAVLIGDVIIGKNCyigphaslrgdfgriVIRDGANVQDNC-VIHGFPGQDtvleenghighgailhgCTIGRNALV 87

                        90
                ....*....|....*.
gi 79328173 398 -VNSVVMDHATIGDGC 412
Cdd:cd04745  88 gMNAVVMDGAVIGEES 103
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 350-424 1.93e-05

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 45.10  E-value: 1.93e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79328173 350 VHPSAELGSKTTVGPHCMLgEGsqvgdkcsvkRSVIGRHCRIGSNVKIVNSVVMDHATIGDGCSIQGSVICSNAQ 424
Cdd:cd03353  12 IDGDVEIGVDVVIDPGVIL-EG----------KTVIGEDCVIGPNCVIKDSTIGDGVVIKASSVIEGAVIGNGAT 75
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 5-56 2.29e-05

CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 45.21  E-value: 2.29e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 79328173   5 VVILAGGFSSYLvplvAKEVPKALLPVANRPVLSYVLDLLESSNLKDLIVVV 56
Cdd:cd02516   3 AIILAAGSGSRM----GADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVV 50
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 3-136 2.31e-05

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 46.51  E-value: 2.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173    3 FQVVILAGGFSSYLvplvAKEVPKALLPVANRPVLSYVLDLLESSNLKDLIVVV----EGEDAALKVGGwissacvdrlh 78
Cdd:PRK14358   8 LDVVILAAGQGTRM----KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTghgaEQVEAALQGSG----------- 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79328173   79 VEVAAVAENVGTAGALRAIAHHLTAK--DILIVSGDIVSDIPPG--AVAATHRRHDAAVTVM 136
Cdd:PRK14358  73 VAFARQEQQLGTGDAFLSGASALTEGdaDILVLYGDTPLLRPDTlrALVADHRAQGSAMTIL 134
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
357-446 3.18e-05

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 43.71  E-value: 3.18e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173 357 GSKTTVGPHCMLGEGSQVGDKCSVKrsvIGRHCRIGSNVKIVNS-----------------VVMDHATIGDGCSI----- 414
Cdd:COG0110  25 GGNITIGDNVYIGPGVTIDDPGGIT---IGDNVLIGPGVTILTGnhpiddpatfplrtgpvTIGDDVWIGAGATIlpgvt 101

                        90       100       110
                ....*....|....*....|....*....|....
gi 79328173 415 --QGSVICSNAqlqerVTLRDcqVEAgYVVCAGS 446
Cdd:COG0110 102 igDGAVVGAGS-----VVTKD--VPP-YAIVAGN 127
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 6-56 5.76e-05

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440824  Cd Length: 224  Bit Score: 44.35  E-value: 5.76e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 79328173   6 VILAGGFSSYLvplvAKEVPKALLPVANRPVLSYVLDLLESSNLKDLIVVV 56
Cdd:COG1211   1 IIPAAGSGSRM----GAGIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVV 47
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 350-419 5.96e-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: 43.17  E-value: 5.96e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173 350 VHPSA------ELGSKTTVGPHCML---------GEGSQVGDKCSV-----KRSVIGRH-----------CRIGSNVKI- 397
Cdd:cd04645   8 IAPNAtvigdvTLGEGSSVWFGAVLrgdvnpiriGERTNIQDGSVLhvdpgYPTIIGDNvtvghgavlhgCTIGDNCLIg 87

                        90       100
                ....*....|....*....|...
gi 79328173 398 VNSVVMDHATIGDGCSIQ-GSVI 419
Cdd:cd04645  88 MGAIILDGAVIGKGSIVAaGSLV 110
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 350-419 1.01e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 44.44  E-value: 1.01e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173  350 VHPSAELGSKTTVGPHCMLgEGsqvgdkcsvkRSVIGRHCRIGSNVKIVNSvvmdhaTIGDGCSIQGSVI 419
Cdd:PRK14354 262 IDADVEIGSDTVIEPGVVI-KG----------NTVIGEDCVIGPGSRIVDS------TIGDGVTITNSVI 314
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 374-422 1.04e-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: 41.72  E-value: 1.04e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 79328173 374 VGDKCSVKRSV-IGRHCRIGSNVKIVNSV-VMDHATIGDGCSIQGSVICSN 422
Cdd:cd03358   1 IGDNCIIGTNVfIENDVKIGDNVKIQSNVsIYEGVTIEDDVFIGPNVVFTN 51
LbH_M1P_guanylylT_C cd05824
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 349-433 1.22e-04

Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) domain: Mannose-1-phosphate guanylyltransferase is also known as GDP-mannose pyrophosphorylase. It catalyzes the synthesis of GDP-mannose from GTP and mannose-1-phosphate, and is involved in the maintenance of cell wall integrity and glycosylation. Similar to ADP-glucose pyrophosphorylase, it contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain, presumably with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100062 [Multi-domain]  Cd Length: 80  Bit Score: 40.60  E-value: 1.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173 349 IVHPSAELGSKTTVGPHCMLGEGSQVGDKCSVKRSVIGRHCRIGSNVKIVNSVVMDHATIGDGCSIQGSVIcsnaqLQER 428
Cdd:cd05824   1 LIDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLENVTV-----LGDD 75


                ....*
gi 79328173 429 VTLRD 433
Cdd:cd05824  76 VTIKD 80
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 350-412 1.46e-04

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 42.32  E-value: 1.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173 350 VHPSA------ELGSKTTVGPHCML---------GEGSQVGDKCSV-----------KRSVIGRH-----CRIGSNVKI- 397
Cdd:COG0663  19 VAPTAvvigdvTIGEDVSVWPGAVLrgdvgpiriGEGSNIQDGVVLhvdpgypltigDDVTIGHGailhgCTIGDNVLIg 98

                        90
                ....*....|....*
gi 79328173 398 VNSVVMDHATIGDGC 412
Cdd:COG0663  99 MGAIVLDGAVIGDGS 113
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 374-426 2.62e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 43.34  E-value: 2.62e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 79328173  374 VGDKCSVKRSVIGRHCRIGSNVKIVNSVVMDHATIGD-GCSIQG--SVICSNAQLQ 426
Cdd:PRK02862 369 IGEGTTIKRAIIDKNARIGNNVRIVNKDNVEEADREDqGFYIRDgiVVVVKNAVIP 424
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 4-56 3.04e-04

Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose Pyrophosphorylase (UGPase) catalyzes a reversible production of UDP-Glucose and pyrophosphate (PPi) from glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids , glycoproteins , and proteoglycans. UGPase is found in both prokaryotes and eukaryotes, although prokaryotic and eukaryotic forms of UGPase catalyze the same reaction, they share low sequence similarity.


Pssm-ID: 133021 [Multi-domain]  Cd Length: 267  Bit Score: 42.52  E-value: 3.04e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 79328173   4 QVVILAGGFSSYLVPLvAKEVPKALLPVANRPVLSYVLDLLESSNLKDLIVVV 56
Cdd:cd02541   2 KAVIPAAGLGTRFLPA-TKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVT 53
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 353-442 4.47e-04

Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain hydroxyl group of L-serine to form O-acetylserine, as the first step of a two-step biosynthetic pathway in bacteria and plants leading to the formation of L-cysteine. This reaction represents a key metabolic point of regulation for the cysteine biosynthetic pathway due to its feedback inhibition by cysteine. The enzyme is a 175 kDa homohexamer, composed of a dimer of homotrimers. Each subunit contains an N-terminal alpha helical region and a C-terminal left-handed beta-helix (LbH) subdomain with 5 turns, each containing a hexapeptide repeat motif characteristic of the acyltransferase superfamily of enzymes. The trimer interface mainly involves the C-terminal LbH subdomain while the dimer (of trimers) interface is mediated by the N-terminal alpha helical subdomain.


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 39.35  E-value: 4.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173 353 SAELGSKTTVGPHCMLGEGSQVgdkcsvkrsVIGRHCRIGSNVKIVNSVVM---------DHATIGDGCsiqgsVICSNA 423
Cdd:cd03354   2 GIDIHPGAKIGPGLFIDHGTGI---------VIGETAVIGDNCTIYQGVTLggkgkgggkRHPTIGDNV-----VIGAGA 67

                        90       100
                ....*....|....*....|
gi 79328173 424 QLQERVTL-RDCQVEAGYVV 442
Cdd:cd03354  68 KILGNITIgDNVKIGANAVV 87
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
1-56 4.66e-04

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 41.66  E-value: 4.66e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 79328173    1 MDFQVVILAGGFSSYLvplvAKEVPKALLPVANRPVLSYVLDLLESSNLKDLIVVV 56
Cdd:PRK00155   2 MMVYAIIPAAGKGSRM----GADRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVV 53
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 349-414 5.09e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 42.13  E-value: 5.09e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 79328173  349 IVHPSAELGSKTTVGPHCMLGEGSQVGDkcsvkrsvigrhCRIGSNVKIVNSVVMDhATIGDGCSI 414
Cdd:PRK14354 273 VIEPGVVIKGNTVIGEDCVIGPGSRIVD------------STIGDGVTITNSVIEE-SKVGDNVTV 325
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 6-112 5.36e-04

MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 40.64  E-value: 5.36e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173   6 VILAGGFSS---YlvplvakevPKALLPVANRPVLSYVLDLLEssNLKDLIVVVEGEDAALKvggwissacvDRLHVEVA 82
Cdd:cd02503   4 VILAGGKSRrmgG---------DKALLELGGKPLLEHVLERLK--PLVDEVVISANRDQERY----------ALLGVPVI 62

                        90       100       110
                ....*....|....*....|....*....|.
gi 79328173  83 A-VAENVGTAGALRAIAHHLTAKDILIVSGD 112
Cdd:cd02503  63 PdEPPGKGPLAGILAALRAAPADWVLVLACD 93
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 6-63 5.55e-04

G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is the short 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 homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose. 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.


Pssm-ID: 133019 [Multi-domain]  Cd Length: 240  Bit Score: 41.41  E-value: 5.55e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 79328173   6 VILAGGFSSYLVPLvAKEVPKALLPVANRPVLSYVLDLLESSNLKDLIVVVEGEDAAL 63
Cdd:cd02538   4 IILAGGSGTRLYPL-TKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPL 60
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 376-419 5.92e-04

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 42.15  E-value: 5.92e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 79328173  376 DKCSVKRSVIGRHCRIgSNVKIVNSVVMDHATIGDGCSIQGSVI 419
Cdd:PLN02241 309 EDCRITDSIISHGCFL-RECKIEHSVVGLRSRIGEGVEIEDTVM 351
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 5-136 6.10e-04

N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose pyrophosphorylase; N-terminal domain of the M1P-guanylyltransferase A-isoform like proteins: The proteins of this family are likely to be a isoform of GDP-mannose pyrophosphorylase. Their sequences are highly conserved with mannose-1-phosphate guanyltransferase, but generally about 40-60 bases longer. GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes including cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133050 [Multi-domain]  Cd Length: 257  Bit Score: 41.47  E-value: 6.10e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173   5 VVILAGGFS--SYLVPLvAKEVPKALLPVANRPVLSYVLDLLES-SNLKDLIVVVEGEDAALKvgGWISSACVDrLHVEV 81
Cdd:cd06428   1 AVILVGGPQkgTRFRPL-SLDVPKPLFPVAGKPMIHHHIEACAKvPDLKEVLLIGFYPESVFS--DFISDAQQE-FNVPI 76

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173  82 AAVAE--NVGTAGALRAIAHHLTA---KDILIVSGDIVSDIPPGAVAATHRRHDAAVTVM 136
Cdd:cd06428  77 RYLQEykPLGTAGGLYHFRDQILAgnpSAFFVLNADVCCDFPLQELLEFHKKHGASGTIL 136
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 349-409 1.03e-03

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: 40.10  E-value: 1.03e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79328173 349 IVHPSAELGSKTTVGPHCMLGEGSQVGDkcsvkrSVIGRHCRIGSNVKIVNSVVMDHATIG 409
Cdd:cd03353  23 VIDPGVILEGKTVIGEDCVIGPNCVIKD------STIGDGVVIKASSVIEGAVIGNGATVG 77
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 379-442 1.28e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 40.98  E-value: 1.28e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79328173  379 SVKRSVIGRHCRIGSNVKIVNSVVMDHATIGDGCSIQGSVICsnaqlqervtlRDCQVEAGYVV 442
Cdd:PRK00725 340 VVRRSVLFSRVRVNSFSNVEDSVLLPDVNVGRSCRLRRCVID-----------RGCVIPEGMVI 392
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
388-414 1.84e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.78  E-value: 1.84e-03
                          10        20
                  ....*....|....*....|....*...
gi 79328173   388 HCRIGSNVKI-VNSVVMDHATIGDGCSI 414
Cdd:pfam00132   1 GTVIGDNVLIgPNAVIGGGVIIGDNVII 28
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 358-423 2.68e-03

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 39.84  E-value: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173  358 SKTTVGPHCMLGEgsqvgdkCSVKRSVIGRHCRIGSNVKIVNSVVM--DH-----------------ATIGDGCSIQGSV 418
Cdd:PLN02241 314 TDSIISHGCFLRE-------CKIEHSVVGLRSRIGEGVEIEDTVMMgaDYyeteeeiasllaegkvpIGIGENTKIRNAI 386


                 ....*
gi 79328173  419 ICSNA 423
Cdd:PLN02241 387 IDKNA 391
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 355-419 2.82e-03

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


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 37.44  E-value: 2.82e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173 355 ELGSKTTVGPHCML--------GEGSQVGDKCSV--------------------KRSVIGRHCRIGSNVkivnsVVMDHA 406
Cdd:cd04647   3 SIGDNVYIGPGCVIsagggitiGDNVLIGPNVTIydhnhdiddperpieqgvtsAPIVIGDDVWIGANV-----VILPGV 77

                        90
                ....*....|....
gi 79328173 407 TIGDGCSI-QGSVI 419
Cdd:cd04647  78 TIGDGAVVgAGSVV 91
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
2-142 3.15e-03

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 39.49  E-value: 3.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173    2 DFQVVILAGGFSSYLVPlVAKEVPKALLPVANRPVLSYVLDLLESSNLKDLIVVVegedaalkvggwissacvdrlHVEV 81
Cdd:PRK10122   3 NLKAVIPVAGLGMHMLP-ATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVT---------------------HASK 60

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79328173   82 AAVAENVGTAGALRAIAHHLTAKDILivsGDIVSDIPPGAVAATHRRHD--AAVTVMLCAQPV 142
Cdd:PRK10122  61 NAVENHFDTSYELESLLEQRVKRQLL---AEVQSICPPGVTIMNVRQGQplGLGHSILCARPA 120
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 1-60 3.73e-03

bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase protein; Provisional


Pssm-ID: 236492 [Multi-domain]  Cd Length: 378  Bit Score: 39.45  E-value: 3.73e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173    1 MDFQVVILAGGFSSYLvplvAKEVPKALLPVANRPVLSYVLDLLESSNLKDLIVVVEGED 60
Cdd:PRK09382   4 SDISLVIVAAGRSTRF----SAEVKKQWLRIGGKPLWLHVLENLSSAPAFKEIVVVIHPD 59
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 8-56 3.86e-03

GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 38.33  E-value: 3.86e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 79328173   8 LAGGFSSYLvplvaKEVPKALLPVANRPVLSYVLDLLESSNLKDLIVVV 56
Cdd:COG2266   1 MAGGKGTRL-----GGGEKPLLEICGKPMIDRVIDALEESCIDKIYVAV 44
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 375-445 3.86e-03

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


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 36.67  E-value: 3.86e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79328173 375 GDKCSVKRSVIGRHCRIgSNVKIVNSVVMDHATIGDGCSIQGSVICSNAQLQERVTLRDCQVEAGYVVCAG 445
Cdd:cd04651   5 GRRGEVKNSLVSEGCII-SGGTVENSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIIDKNVVIPDG 74
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 353-446 3.98e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 39.43  E-value: 3.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173  353 SAELGSKTTVGPH------CMLGEGSQVGDKCSVKRSVIGRH-----------CRIGSNVKI------VN--------SV 401
Cdd:PRK14354 316 ESKVGDNVTVGPFahlrpgSVIGEEVKIGNFVEIKKSTIGEGtkvshltyigdAEVGENVNIgcgtitVNydgknkfkTI 395

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 79328173  402 VMDHATIGdgcsiqgsvicSNAQLQERVTlrdcqVEAGYVVCAGS 446
Cdd:PRK14354 396 IGDNAFIG-----------CNSNLVAPVT-----VGDNAYIAAGS 424
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 355-420 4.94e-03

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 39.24  E-value: 4.94e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173 355 ELGSKTTVGPHCML---------------GEGSQVGDKCSVK-----R--SVIGRHCRIGSNVKIVNSVVMDH------- 405
Cdd:COG1207 286 VIGEGVVIGPNCTLkdstigdgvvikysvIEDAVVGAGATVGpfarlRpgTVLGEGVKIGNFVEVKNSTIGEGskvnhls 365

                        90       100
                ....*....|....*....|
gi 79328173 406 ----ATIGDGCSI-QGSVIC 420
Cdd:COG1207 366 yigdAEIGEGVNIgAGTITC 385
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 353-446 5.64e-03

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: 37.78  E-value: 5.64e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173 353 SAELGSKTTVGP------HCMLGEGSQVGDKCSVKRSVIGRH-----------CRIGSNVKI------VN-SVVMDHAT- 407
Cdd:cd03353  67 GAVIGNGATVGPfahlrpGTVLGEGVHIGNFVEIKKSTIGEGskanhlsylgdAEIGEGVNIgagtitCNyDGVNKHRTv 146

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 79328173 408 IGDGCSIqGsvicSNAQLQERVTlrdcqVEAGYVVCAGS 446
Cdd:cd03353 147 IGDNVFI-G----SNSQLVAPVT-----IGDGATIAAGS 175
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 348-434 6.28e-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: 37.19  E-value: 6.28e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79328173 348 NIVhpsaeLGSKTTVGPHCMLGegsqvGDKCSVKrsvIGRHCRIGSNVKIVNSVVM-------------DHATIGDGCSI 414
Cdd:cd03359  21 NIV-----LNGKTIIQSDVIIR-----GDLATVS---IGRYCILSEGCVIRPPFKKfskgvaffplhigDYVFIGENCVV 87

                        90       100
                ....*....|....*....|....*.
gi 79328173 415 Q----GS--VICSNAQLQERVTLRDC 434
Cdd:cd03359  88 NaaqiGSyvHIGKNCVIGRRCIIKDC 113
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 361-422 7.38e-03

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: 37.77  E-value: 7.38e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79328173 361 TVGPHCMLGegSQVGDKCSVKrsvIGRHCRIGSNVKIVnsvvmDHATIGDGCSIQG-SVICSN 422
Cdd:cd03352 134 RIGENCLIA--AQVGIAGSTT---IGDNVIIGGQVGIA-----GHLTIGDGVVIGAgSGVTSI 186
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 361-421 8.03e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 38.20  E-value: 8.03e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79328173  361 TVGPHCMLGegSQVGDKCSVKrsvIGRHCRIGSNVKIVNsvvmdHATIGDGCSI--QGSVICS 421
Cdd:PRK00892 245 VIGRHTAIA--AQVGIAGSTK---IGRYCMIGGQVGIAG-----HLEIGDGVTItaMSGVTKS 297
 
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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