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Conserved domains on  [gi|24653885|ref|NP_611046|]
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eukaryotic translation initiation factor 2B subunit gamma [Drosophila melanogaster]

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; ...
 4-215 6.89e-93

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: 279.93  E-value: 6.89e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885   4 FQAVVFAAGRGTRLPEVLGDAPKCLLPVGPYPLIWYPLNLLQQHNFTEVIVVVLEQEKLEIQSALENTPL--KLRLDYAT 81
Cdd:cd04198   1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSFPLnlKQKLDEVT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885  82 IPSDGDFGTADSLRYIYDKIKSDFLVVSCDLVSNVSLYPLINKFREHDAALAMLLFPSGFESDVVMPGPKSKHKPERDLI 161
Cdd:cd04198  81 IVLDEDMGTADSLRHIRKKIKKDFLVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVSSEQKGGKGKSKKADERDVI 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 24653885 162 GIHAATQRLAFVSAASDCEETLNIQRHLLKNRGRLDVYSRLVDAHVYVLKKWVI 215
Cdd:cd04198 161 GLDEKTQRLLFITSEEDLDEDLELRKSLLKRHPRVTITTKLLDAHVYIFKRWVL 214
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 357-437 2.43e-33

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: 120.38  E-value: 2.43e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885 357 IAADNAKLSEKTSLNFSVFGPNCIISPKNIVANSLIMSNAIVEEGCNIDNCIIGHRAQVKSGSVLKNCIIGPNYVVEEGT 436
Cdd:cd04652   1 LVGENTQVGEKTSIKRSVIGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLVGSGYRVEAGT 80


                .
gi 24653885 437 H 437
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; ...
 4-215 6.89e-93

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: 279.93  E-value: 6.89e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885   4 FQAVVFAAGRGTRLPEVLGDAPKCLLPVGPYPLIWYPLNLLQQHNFTEVIVVVLEQEKLEIQSALENTPL--KLRLDYAT 81
Cdd:cd04198   1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSFPLnlKQKLDEVT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885  82 IPSDGDFGTADSLRYIYDKIKSDFLVVSCDLVSNVSLYPLINKFREHDAALAMLLFPSGFESDVVMPGPKSKHKPERDLI 161
Cdd:cd04198  81 IVLDEDMGTADSLRHIRKKIKKDFLVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVSSEQKGGKGKSKKADERDVI 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 24653885 162 GIHAATQRLAFVSAASDCEETLNIQRHLLKNRGRLDVYSRLVDAHVYVLKKWVI 215
Cdd:cd04198 161 GLDEKTQRLLFITSEEDLDEDLELRKSLLKRHPRVTITTKLLDAHVYIFKRWVL 214
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 357-437 2.43e-33

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: 120.38  E-value: 2.43e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885 357 IAADNAKLSEKTSLNFSVFGPNCIISPKNIVANSLIMSNAIVEEGCNIDNCIIGHRAQVKSGSVLKNCIIGPNYVVEEGT 436
Cdd:cd04652   1 LVGENTQVGEKTSIKRSVIGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLVGSGYRVEAGT 80


                .
gi 24653885 437 H 437
Cdd:cd04652  81 E 81
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 5-239 5.56e-28

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: 111.01  E-value: 5.56e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885   5 QAVVFAAGRGTRLPEVLGDAPKCLLPVGPYPLIWYPLNLLQQHNFTEVIVVV--LEQeklEIQSALENT-PLKLRLDYat 81
Cdd:COG1208   1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVgyLAE---QIEEYFGDGsRFGVRITY-- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885  82 IPSDGDFGTADSLRYIYDKIKSD-FLVVSCDLVSNVSLYPLINKFREHDAALAMLLF----PSGFeSDVVMpgpkskhkp 156
Cdd:COG1208  76 VDEGEPLGTGGALKRALPLLGDEpFLVLNGDILTDLDLAALLAFHREKGADATLALVpvpdPSRY-GVVEL--------- 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885 157 erdligihaatqrlafvsaasdcEETLNIQRHLLKNRGrldVYSRLVDAHVYVLKKWVIDYLRRKENISTfkGEFLPHLI 236
Cdd:COG1208 146 -----------------------DGDGRVTRFVEKPEE---PPSNLINAGIYVLEPEIFDYIPEGEPFDL--EDLLPRLI 197


                ...
gi 24653885 237 KKQ 239
Cdd:COG1208 198 AEG 200
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 6-138 8.17e-13

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: 68.05  E-value: 8.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885     6 AVVFAAGRGTRL-PEVLGDAPKCLLPVGPYPLIWYPLNLLQQHNFTEVIVVVLEQEKLEIQSALENTP-LKLRLDYATIP 83
Cdd:pfam00483   2 AIILAGGSGTRLwPLTRTLAKPLVPVGGKYPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSkFGVQITYALQP 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 24653885    84 SDGdfGTADSLRYIYDKI---KSDFLVVSCDLVSNVSLYPLINKFREHDAALAMLLFP 138
Cdd:pfam00483  82 EGK--GTAPAVALAADFLgdeKSDVLVLGGDHIYRMDLEQAVKFHIEKAADATVTFGI 137
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 362-437 1.38e-10

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 62.79  E-value: 1.38e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24653885 362 AKLSEKTSLNFSVFGPNCIISpkNIVANSLIMSNAIVEEGCNIDNCIIGHRAQVKSGSVLKNCIIGPNYVVEEGTH 437
Cdd:COG0448 278 AKFVRGGKVKNSLVSNGCIIS--GTVENSVLFRGVRVESGAVVENSVIMPGVVIGEGAVIENAIIDKNVVIPPGVV 351
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 373-436 3.43e-07

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 52.14  E-value: 3.43e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24653885  373 SVFGPNCIISpKNIVANSLIMSNAIVEEGCNIDNCIIGHRAQVKSGSVLKNCIIGPNYVVEEGT 436
Cdd:PRK00844 316 SLVSAGSIIS-GATVRNSVLSPNVVVESGAEVEDSVLMDGVRIGRGAVVRRAILDKNVVVPPGA 378
glgD TIGR02092
glucose-1-phosphate adenylyltransferase, GlgD subunit; This family is GlgD, an apparent ...
 387-437 3.15e-05

glucose-1-phosphate adenylyltransferase, GlgD subunit; This family is GlgD, an apparent regulatory protein that appears in an alpha2/beta2 heterotetramer with GlgC (glucose-1-phosphate adenylyltransferase, TIGR02091) in a subset of bacteria that use GlgC for glycogen biosynthesis. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 273966 [Multi-domain]  Cd Length: 369  Bit Score: 45.84  E-value: 3.15e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 24653885   387 VANSLIMSNAIVEEgcNIDNCIIGHRAQVKSGSVLKNCIIGPNYVVEEGTH 437
Cdd:TIGR02092 287 VENSLVANGCIIEG--KVENSILSRGVHVGKDALIKNCIIMQRTVIGEGAH 335
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 1-86 3.19e-05

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 45.44  E-value: 3.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885    1 MTEFQAVVFAAGRGTRLPEVLGDAPKCLLPVGPYPLIWYPLNLLQQHNFTEVIVVVLEQEKLEIQSAL-ENTPLKLRLDY 79
Cdd:PRK15480   1 MKTRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLgDGSQWGLNLQY 80


                 ....*...
gi 24653885   80 ATIPS-DG 86
Cdd:PRK15480  81 KVQPSpDG 88
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 6-70 8.06e-05

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, the IspD protein of the deoxyxylulose pathway of IPP biosynthesis. In about twenty percent of bacterial genomes, this protein occurs as IspDF, a bifunctional fusion protein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 213532  Cd Length: 217  Bit Score: 43.82  E-value: 8.06e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24653885     6 AVVFAAGRGTRLPEvlgDAPKCLLPVGPYPLIWYPLNLLQQHN-FTEVIVVVLEQEKLEIQSALEN 70
Cdd:TIGR00453   2 AVIPAAGRGTRFGS---GVPKQYLELGGRPLLEHALDAFLAHPaIDEVVVVVSPDDTEFFQKYLVA 64
 
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; ...
 4-215 6.89e-93

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: 279.93  E-value: 6.89e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885   4 FQAVVFAAGRGTRLPEVLGDAPKCLLPVGPYPLIWYPLNLLQQHNFTEVIVVVLEQEKLEIQSALENTPL--KLRLDYAT 81
Cdd:cd04198   1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSFPLnlKQKLDEVT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885  82 IPSDGDFGTADSLRYIYDKIKSDFLVVSCDLVSNVSLYPLINKFREHDAALAMLLFPSGFESDVVMPGPKSKHKPERDLI 161
Cdd:cd04198  81 IVLDEDMGTADSLRHIRKKIKKDFLVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVSSEQKGGKGKSKKADERDVI 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 24653885 162 GIHAATQRLAFVSAASDCEETLNIQRHLLKNRGRLDVYSRLVDAHVYVLKKWVI 215
Cdd:cd04198 161 GLDEKTQRLLFITSEEDLDEDLELRKSLLKRHPRVTITTKLLDAHVYIFKRWVL 214
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 4-215 1.82e-62

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: 201.71  E-value: 1.82e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885   4 FQAVVFAAGRGTRLPEVLGDAPKCLLPVGPYPLIWYPLNLLQQHNFTEVIVVVLEQEKLEIQSALENTP----LKLRLDY 79
Cdd:cd02507   1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSKWsslsSKMIVDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885  80 ATIPSDGDFGTADSLRYIYDKIKSDFLVVSCDLVSNVSLYPLI----NKFREHDAALAMLLFPSGFESdvvmpgPKSKHK 155
Cdd:cd02507  81 ITSDLCESAGDALRLRDIRGLIRSDFLLLSCDLVSNIPLSELLeerrKKDKNAIATLTVLLASPPVST------EQSKKT 154

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24653885 156 PERDLIGIHAATQRLAFVSAASDCEETLN--IQRHLLKNRGRLDVYSRLVDAHVYVLKKWVI 215
Cdd:cd02507 155 EEEDVIAVDSKTQRLLLLHYEEDLDEDLEliIRKSLLSKHPNVTIRTDLLDCHIYICSPDVL 216
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 357-437 2.43e-33

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: 120.38  E-value: 2.43e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885 357 IAADNAKLSEKTSLNFSVFGPNCIISPKNIVANSLIMSNAIVEEGCNIDNCIIGHRAQVKSGSVLKNCIIGPNYVVEEGT 436
Cdd:cd04652   1 LVGENTQVGEKTSIKRSVIGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLVGSGYRVEAGT 80


                .
gi 24653885 437 H 437
Cdd:cd04652  81 E 81
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 5-239 5.56e-28

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: 111.01  E-value: 5.56e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885   5 QAVVFAAGRGTRLPEVLGDAPKCLLPVGPYPLIWYPLNLLQQHNFTEVIVVV--LEQeklEIQSALENT-PLKLRLDYat 81
Cdd:COG1208   1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVgyLAE---QIEEYFGDGsRFGVRITY-- 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885  82 IPSDGDFGTADSLRYIYDKIKSD-FLVVSCDLVSNVSLYPLINKFREHDAALAMLLF----PSGFeSDVVMpgpkskhkp 156
Cdd:COG1208  76 VDEGEPLGTGGALKRALPLLGDEpFLVLNGDILTDLDLAALLAFHREKGADATLALVpvpdPSRY-GVVEL--------- 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885 157 erdligihaatqrlafvsaasdcEETLNIQRHLLKNRGrldVYSRLVDAHVYVLKKWVIDYLRRKENISTfkGEFLPHLI 236
Cdd:COG1208 146 -----------------------DGDGRVTRFVEKPEE---PPSNLINAGIYVLEPEIFDYIPEGEPFDL--EDLLPRLI 197


                ...
gi 24653885 237 KKQ 239
Cdd:COG1208 198 AEG 200
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 6-138 5.10e-22

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: 93.80  E-value: 5.10e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885   6 AVVFAAGRGTRLPEVLGDAPKCLLPVGPYPLIWYPLNLLQQHNFTEVIVVVLEQEKLEIQSALENTPLKLRLDYATipSD 85
Cdd:cd04181   1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFGVNIEYVV--QE 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 24653885  86 GDFGTADSLRYIYDKIKSD-FLVVSCDLVSNVSLYPLINKFREHDAALAMLLFP 138
Cdd:cd04181  79 EPLGTAGAVRNAEDFLGDDdFLVVNGDVLTDLDLSELLRFHREKGADATIAVKE 132
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
5-113 9.67e-16

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 76.43  E-value: 9.67e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885   5 QAVVFAAGRGTRLPEVLGDAPKCLLPVGPYPLIWYPLNLLQQHNFTEVIVVVlEQEKLEIQSALENTPLKLRL----DYA 80
Cdd:COG1213   1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVT-GYKAELIEEALARPGPDVTFvynpDYD 79

                        90       100       110
                ....*....|....*....|....*....|...
gi 24653885  81 TipsdgdFGTADSLRYIYDKIKSDFLVVSCDLV 113
Cdd:COG1213  80 E------TNNIYSLWLAREALDEDFLLLNGDVV 106
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 6-147 1.40e-14

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: 72.65  E-value: 1.40e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885   6 AVVFAAGRGTRLPEVLGDAPKCLLPVGPYPLIWYPLNLLQQHNFTEVIVVV-LEQEKLEiqsALENTPLKLRL----DYA 80
Cdd:cd02523   1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTgYKKEQIE---ELLKKYPNIKFvynpDYA 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24653885  81 TipsdgdFGTADSLRYIYDKIKSDFLVVSCDLVSNVSlypLINKFREHDAALAMLLFPSGFESDVVM 147
Cdd:cd02523  78 E------TNNIYSLYLARDFLDEDFLLLEGDVVFDPS---ILERLLSSPADNAILVDKKTKEWEDEY 135
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 6-138 4.80e-14

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: 71.04  E-value: 4.80e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885   6 AVVFAAGRGTRLPEVLGDAPKCLLPVGPYPLIWYPLNLLQQHNFTEVIVVV---LEQekleIQSALENTPLKLRLDYAti 82
Cdd:cd06915   1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVgylAEQ----IEEYFGDGYRGGIRIYY-- 74

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 24653885  83 pSDGD--FGTADSLRYIYDKIKSD-FLVVSCDLVSNVSLYPLINKFREHDAALAMLLFP 138
Cdd:cd06915  75 -VIEPepLGTGGAIKNALPKLPEDqFLVLNGDTYFDVDLLALLAALRASGADATMALRR 132
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 4-206 8.08e-13

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: 67.25  E-value: 8.08e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885   4 FQAVVFAAGRGTRLPEVLGDAPKCLLPVGPYPLIWYPLNLLQQHNFTEVIVVVLEQEKlEIQSALENT----PLKLRLDY 79
Cdd:cd04197   1 LQAVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSD-QIKEYIEKSkwskPKSSLMIV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885  80 ATIPSDGDFGTADSLRYIYDK--IKSDFLVVSCDLVSNVSLYPLINKFREH-----DAALAMLLFPSGfesdvvmPGPKS 152
Cdd:cd04197  80 IIIMSEDCRSLGDALRDLDAKglIRGDFILVSGDVVSNIDLKEILEEHKERrkkdkNAIMTMVLKEAS-------PPHRT 152

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24653885 153 KHKPERDLIGIHAATQRLafvsaasdceetLNIQRH-LLKNRGRLDVYSRLVDAH 206
Cdd:cd04197 153 RRTGEEFVIAVDPKTSRL------------LHYEELpGSKYRSITDLPSELLGSN 195
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 6-138 8.17e-13

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: 68.05  E-value: 8.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885     6 AVVFAAGRGTRL-PEVLGDAPKCLLPVGPYPLIWYPLNLLQQHNFTEVIVVVLEQEKLEIQSALENTP-LKLRLDYATIP 83
Cdd:pfam00483   2 AIILAGGSGTRLwPLTRTLAKPLVPVGGKYPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSkFGVQITYALQP 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 24653885    84 SDGdfGTADSLRYIYDKI---KSDFLVVSCDLVSNVSLYPLINKFREHDAALAMLLFP 138
Cdd:pfam00483  82 EGK--GTAPAVALAADFLgdeKSDVLVLGGDHIYRMDLEQAVKFHIEKAADATVTFGI 137
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 360-434 3.24e-12

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: 61.87  E-value: 3.24e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24653885 360 DNAKLSEKTSLNFSVFGPNCIISPKNIVANSLIMSNAIVEEGCNIDNCIIGHRAQVKSGSVLKN-CIIGPNYVVEE 434
Cdd:cd03356   4 ESTVIGENAIIKNSVIGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVNlCIIGDDVVVED 79
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 6-136 1.29e-11

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: 64.13  E-value: 1.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885   6 AVVFAAGRGTRLPEVLGDAPKCLLPVGPYPLIWYPLNLLQQHNFTEVIVVVLEQeKLEIQSAL-ENTPLKLRLDYatIPS 84
Cdd:cd04189   3 GLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPT-GEEIKEALgDGSRFGVRITY--ILQ 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 24653885  85 DGDFGTADSLRYIYDKIK-SDFLVVSCDLVSNVSLYPLINKFREHDAALAMLL 136
Cdd:cd04189  80 EEPLGLAHAVLAARDFLGdEPFVVYLGDNLIQEGISPLVRDFLEEDADASILL 132
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 362-437 1.38e-10

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 62.79  E-value: 1.38e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24653885 362 AKLSEKTSLNFSVFGPNCIISpkNIVANSLIMSNAIVEEGCNIDNCIIGHRAQVKSGSVLKNCIIGPNYVVEEGTH 437
Cdd:COG0448 278 AKFVRGGKVKNSLVSNGCIIS--GTVENSVLFRGVRVESGAVVENSVIMPGVVIGEGAVIENAIIDKNVVIPPGVV 351
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 374-435 3.84e-10

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: 56.10  E-value: 3.84e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24653885 374 VFGPNCIISPKNIVANSLIMSNAIVEEGCNIDNCIIGHRAQVKSGSVLKNCIIGPNYVVEEG 435
Cdd:cd03356   1 LIGESTVIGENAIIKNSVIGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGEN 62
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 373-437 4.80e-10

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: 56.32  E-value: 4.80e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24653885 373 SVFGPNCIISPKNIVaNSLIMSNAIVEEGCNIDNCIIGHRAQVKSGSVLKNCIIGPNYVVEEGTH 437
Cdd:cd04651  13 SLVSEGCIISGGTVE-NSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIIDKNVVIPDGVV 76
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 6-134 1.07e-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: 58.29  E-value: 1.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885   6 AVVFAAGRGTRLPEVLGDAPKCLLPVGPYPLIWYPLNLLQQHNFTEVIVVV-------------LEQEKLEIQSALENTP 72
Cdd:cd06426   1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVnylaemiedyfgdGSKFGVNISYVREDKP 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24653885  73 LklrldyatipsdgdfGTADSLRYIYDKIKSDFLVVSCDLVSNVSLYPLINKFREHDAALAM 134
Cdd:cd06426  81 L---------------GTAGALSLLPEKPTDPFLVMNGDILTNLNYEHLLDFHKENNADATV 127
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 361-434 3.35e-09

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: 53.35  E-value: 3.35e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24653885 361 NAKLSEKTSLNFSVFGPNCIISPKNIVANSLIMSNAIVEEGCNIDNCIIGHRAQVKSGSVLKN-CIIGPNYVVEE 434
Cdd:cd05787   5 GTSIGEGTTIKNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIPPgSLISFGVVIGD 79
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 5-136 6.52e-09

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


Pssm-ID: 133044 [Multi-domain]  Cd Length: 221  Bit Score: 56.04  E-value: 6.52e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885   5 QAVVFAAGRGTRLPEVLGDAPKCLLPVGPYPLIWYPLNLLQQHNFTEVIVVV--LEqEKLE--IQSALENTPLKLRLDYA 80
Cdd:cd06422   1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNThhLA-DQIEahLGDSRFGLRITISDEPD 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24653885  81 TIpsdgdFGTADSLRYIYDKIKSD-FLVVSCDLVSNVSLYPLINKFREHDAALAMLL 136
Cdd:cd06422  80 EL-----LETGGGIKKALPLLGDEpFLVVNGDILWDGDLAPLLLLHAWRMDALLLLL 131
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 7-77 4.93e-08

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: 53.60  E-value: 4.93e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24653885   7 VVFAAGRGTRLPevlGDAPKCLLPVGPYPLIWYPLNLLQQH-NFTEVIVVVLEQEKLEIQSALENTPLKLRL 77
Cdd:COG1211   1 IIPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHpRIDEIVVVVPPDDIEYFEELLAKYGIDKPV 69
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 373-440 7.35e-08

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


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 50.15  E-value: 7.35e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24653885 373 SVFGPNCIISPKNIVANSLIMSNAIVEEGCNIDNCIIGhraqvksgsvlKNCIIGPNYVVEEGTHSQA 440
Cdd:cd04651  29 SVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIID-----------KNVVIPDGVVIGGDPEEDR 85
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 373-432 2.63e-07

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 52.38  E-value: 2.63e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885 373 SVFGPNCIISPKNIVANSLIMSNAIVEEGCNIDNCIIGhraqvksgsvlKNCIIGPNYVV 432
Cdd:COG0448 304 SVLFRGVRVESGAVVENSVIMPGVVIGEGAVIENAIID-----------KNVVIPPGVVI 352
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 6-141 2.86e-07

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: 51.36  E-value: 2.86e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885   6 AVVFAAGRGTRLpevLGDAPKCLLPVGPYPLIWYPLNLLQQHNFTEVIVVVLEQEKlEIQSALENTPLKlrldyaTIPSD 85
Cdd:cd02540   1 AVILAAGKGTRM---KSDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAE-QVKKALANPNVE------FVLQE 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24653885  86 GDFGTADSLRYIYDKIK---SDFLVVSCD--LVSNVSLYPLINKFREHDAALAMLLF----PSGF 141
Cdd:cd02540  71 EQLGTGHAVKQALPALKdfeGDVLVLYGDvpLITPETLQRLLEAHREAGADVTVLTAeledPTGY 135
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 373-436 3.43e-07

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 52.14  E-value: 3.43e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24653885  373 SVFGPNCIISpKNIVANSLIMSNAIVEEGCNIDNCIIGHRAQVKSGSVLKNCIIGPNYVVEEGT 436
Cdd:PRK00844 316 SLVSAGSIIS-GATVRNSVLSPNVVVESGAEVEDSVLMDGVRIGRGAVVRRAILDKNVVVPPGA 378
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 373-436 4.06e-07

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 51.79  E-value: 4.06e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24653885  373 SVFGPNCIISPKNIVANSLIMSNAIVEEGCNIDNCIIGHRAQVKSGSVL---KNCI--IGPNYVVEEGT 436
Cdd:PRK05293 309 SVLFQGVQVGEGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVIIgggKEVItvIGENEVIGVGT 377
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 6-141 5.21e-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: 49.12  E-value: 5.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885     6 AVVFAAGRGTRLpevlgDAPKCLLPVGPYPLIWYPLNLLQQHnfTEVIVVVLEQEklEIQSALENTPLKLRLDyatipSD 85
Cdd:pfam12804   1 AVILAGGRSSRM-----GGDKALLPLGGKPLLERVLERLRPA--GDEVVVVANDE--EVLAALAGLGVPVVPD-----PD 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885    86 GDFGTADSLRYIYDKIKSD--FLVVSCD--LVSNVSLYPLINKFREHDAALAMLLFPSGF 141
Cdd:pfam12804  67 PGQGPLAGLLAALRAAPGAdaVLVLACDmpFLTPELLRRLLAAAEESGADIVVPVYDGGR 126
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
1-133 1.41e-06

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 48.62  E-value: 1.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885   1 MTEFQAVVFAAGRGTRLpevlgDAPKCLLPVGPYPLIWYPLNLLQQHNFTEVIVVVLEQEKlEIQSALENTPLKLRL--D 78
Cdd:COG2068   1 MSKVAAIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAE-EVAAALAGLGVRVVVnpD 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24653885  79 YATipsdgdfGTADSLR----YIYDKIkSDFLVVSCD--LVSNVSLYPLINKFREHDAALA 133
Cdd:COG2068  75 WEE-------GMSSSLRaglaALPADA-DAVLVLLGDqpLVTAETLRRLLAAFRESPASIV 127
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 6-76 1.60e-06

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: 48.67  E-value: 1.60e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24653885   6 AVVFAAGRGTRLPevlGDAPKCLLPVGPYPLIWYPLNLLQQHN-FTEVIVVVLEQEKLEIQSALENTPLKLR 76
Cdd:cd02516   3 AIILAAGSGSRMG---ADIPKQFLELGGKPVLEHTLEAFLAHPaIDEIVVVVPPDDIDLAKELAKYGLSKVV 71
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 6-133 1.13e-05

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: 46.01  E-value: 1.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885   6 AVVFAAGRGTRLPEvlgdaPKCLLPVGPYPLIWYPLNLLQQHNFTEVIvVVLEQEKLEIQSALENTPLKLRldyatIPSD 85
Cdd:cd04182   3 AIILAAGRSSRMGG-----NKLLLPLDGKPLLRHALDAALAAGLSRVI-VVLGAEADAVRAALAGLPVVVV-----INPD 71

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 24653885  86 GDFGTADSLRYIYDKIKSD---FLVVSCD--LVSNVSLYPLINKFREHDAALA 133
Cdd:cd04182  72 WEEGMSSSLAAGLEALPADadaVLILLADqpLVTAETLRALIDAFREDGAGIV 124
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 377-437 1.52e-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: 45.49  E-value: 1.52e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24653885 377 PNCIISPKNIVANslimsNAIVEEGCNIDNCIIGHRAQVKSGSVLKNCIIG------------PNYVVEEGTH 437
Cdd:cd03353  26 PGVILEGKTVIGE-----DCVIGPNCVIKDSTIGDGVVIKASSVIEGAVIGngatvgpfahlrPGTVLGEGVH 93
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 10-163 1.62e-05

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: 45.26  E-value: 1.62e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885  10 AAGRGTRLpevlGDAPKCLLPVGPYPLIWYPLNLLQQHNFTEVIVVVleqekleiqSalENTP----LKLRLDYATIPSD 85
Cdd:COG2266   2 AGGKGTRL----GGGEKPLLEICGKPMIDRVIDALEESCIDKIYVAV---------S--PNTPktreYLKERGVEVIETP 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885  86 GDfGTADSLRYIYDKIKSDFLVVSCDLvsnvslyPLIN---------KFREHDA-ALAMLLFPSGFESDVVMPGPKSKHK 155
Cdd:COG2266  67 GE-GYVEDLNEALESISGPVLVVPADL-------PLLTpeiiddiidAYLESGKpSLTVVVPAALKRELGVSPDTTFEID 138


                ....*...
gi 24653885 156 PERDLIGI 163
Cdd:COG2266 139 GELVPTGI 146
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 6-94 2.09e-05

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: 45.64  E-value: 2.09e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885   6 AVVFAAGRGTRLPEVLGDAPKCLLPVGPYPLIWYPLNLLQQHNFTEVIVVVLEQEKLEIQSALEN-TPLKLRLDYATIPS 84
Cdd:cd02538   3 GIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDgSDLGIRITYAVQPK 82

                        90
                ....*....|
gi 24653885  85 DGdfGTADSL 94
Cdd:cd02538  83 PG--GLAQAF 90
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 364-444 2.28e-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: 2.28e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885 364 LSEKTSL-NFSVFGPNCIISPKNIVANSLIMSNAIVEEGCNIDNCIIGHRAQVKSGSVLK-NCIIGpNYV----VEEGTH 437
Cdd:cd03353  30 LEGKTVIgEDCVIGPNCVIKDSTIGDGVVIKASSVIEGAVIGNGATVGPFAHLRPGTVLGeGVHIG-NFVeikkSTIGEG 108


                ....*..
gi 24653885 438 SQAVHLS 444
Cdd:cd03353 109 SKANHLS 115
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 394-437 2.86e-05

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: 42.84  E-value: 2.86e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 24653885 394 SNAIVEEGC-----NIDNCIIGHRAQVKSGSVLKNCIIGPNYVVEEGTH 437
Cdd:cd04651  11 KNSLVSEGCiisggTVENSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAV 59
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 6-135 3.11e-05

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: 45.32  E-value: 3.11e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885   6 AVVFAAG--RGTRLPEVLGDAPKCLLPVGPYPLIWYPLNLLQQ-HNFTEVIVVVLEQE---KLEIQSALEntPLKLRLDY 79
Cdd:cd06428   1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKvPDLKEVLLIGFYPEsvfSDFISDAQQ--EFNVPIRY 78

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885  80 ATIPSdgDFGTADSLRYIYDKIK----SDFLVVSCDLVSNVSLYPLINKFREHDAALAML 135
Cdd:cd06428  79 LQEYK--PLGTAGGLYHFRDQILagnpSAFFVLNADVCCDFPLQELLEFHKKHGASGTIL 136
glgD TIGR02092
glucose-1-phosphate adenylyltransferase, GlgD subunit; This family is GlgD, an apparent ...
 387-437 3.15e-05

glucose-1-phosphate adenylyltransferase, GlgD subunit; This family is GlgD, an apparent regulatory protein that appears in an alpha2/beta2 heterotetramer with GlgC (glucose-1-phosphate adenylyltransferase, TIGR02091) in a subset of bacteria that use GlgC for glycogen biosynthesis. [Energy metabolism, Biosynthesis and degradation of polysaccharides]


Pssm-ID: 273966 [Multi-domain]  Cd Length: 369  Bit Score: 45.84  E-value: 3.15e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 24653885   387 VANSLIMSNAIVEEgcNIDNCIIGHRAQVKSGSVLKNCIIGPNYVVEEGTH 437
Cdd:TIGR02092 287 VENSLVANGCIIEG--KVENSILSRGVHVGKDALIKNCIIMQRTVIGEGAH 335
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 1-86 3.19e-05

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 45.44  E-value: 3.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885    1 MTEFQAVVFAAGRGTRLPEVLGDAPKCLLPVGPYPLIWYPLNLLQQHNFTEVIVVVLEQEKLEIQSAL-ENTPLKLRLDY 79
Cdd:PRK15480   1 MKTRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLgDGSQWGLNLQY 80


                 ....*...
gi 24653885   80 ATIPS-DG 86
Cdd:PRK15480  81 KVQPSpDG 88
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 342-441 3.44e-05

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: 45.78  E-value: 3.44e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885 342 ISPGAVVkstqtkeiiaADNAKLsektslnfsvfGPNCIISPknivaNSLIMSNAIVEEGCNID-NCIIGHRAQVksGsv 420
Cdd:COG1044  99 IHPSAVI----------DPSAKI-----------GEGVSIGP-----FAVIGAGVVIGDGVVIGpGVVIGDGVVI--G-- 148

                        90       100
                ....*....|....*....|....*....
gi 24653885 421 lKNCIIGPNYVVEEGT--------HSQAV 441
Cdd:COG1044 149 -DDCVLHPNVTIYERCvigdrviiHSGAV 176
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 6-54 4.17e-05

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: 44.87  E-value: 4.17e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 24653885   6 AVVFAAGRGTRLPEVLGDAPKCLLPVGPYPLIWYPLNLLQQHNFTEVIV 54
Cdd:cd02524   1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFIL 49
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
6-80 6.89e-05

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 44.70  E-value: 6.89e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24653885   6 AVVFAAGRGTRL-PEVLGdAPKCLLPVGPYPLIWYPLNLLQQHNFTEVIVVVLEQEKLEIQSALENTP-LKLRLDYA 80
Cdd:COG1209   3 GIILAGGSGTRLrPLTLT-VSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSqLGIKISYA 78
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 359-437 7.33e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 44.86  E-value: 7.33e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24653885  359 ADNAKLSEktslnfSVFGPNCIISPKniVANSLIMSNAIVEEGCNIDNCIIGHRAQVKSGSVLKNCIIGPNYVVEEGTH 437
Cdd:PRK05293 286 AENAKVKN------SLVVEGCVVYGT--VEHSVLFQGVQVGEGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVI 356
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 6-70 8.06e-05

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, the IspD protein of the deoxyxylulose pathway of IPP biosynthesis. In about twenty percent of bacterial genomes, this protein occurs as IspDF, a bifunctional fusion protein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 213532  Cd Length: 217  Bit Score: 43.82  E-value: 8.06e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24653885     6 AVVFAAGRGTRLPEvlgDAPKCLLPVGPYPLIWYPLNLLQQHN-FTEVIVVVLEQEKLEIQSALEN 70
Cdd:TIGR00453   2 AVIPAAGRGTRFGS---GVPKQYLELGGRPLLEHALDAFLAHPaIDEVVVVVSPDDTEFFQKYLVA 64
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 338-432 1.02e-04

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


Pssm-ID: 100049 [Multi-domain]  Cd Length: 161  Bit Score: 42.59  E-value: 1.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885 338 KHPLISPGAVVKSTQTKEiiaADNAKLSEKTSLNFSVFGPNCIISPKNIVANSLIMSNAIVEEGCNI-DNCIIghraqvk 416
Cdd:cd03359  47 RYCILSEGCVIRPPFKKF---SKGVAFFPLHIGDYVFIGENCVVNAAQIGSYVHIGKNCVIGRRCIIkDCVKI------- 116

                        90
                ....*....|....*.
gi 24653885 417 sgsvLKNCIIGPNYVV 432
Cdd:cd03359 117 ----LDGTVVPPDTVI 128
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 379-436 1.62e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 43.68  E-value: 1.62e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 24653885  379 CIISpKNIVANSLIMSNAIVEEGCNIDNCIIGHRAQVKSGSVLKNCIIGPNYVVEEGT 436
Cdd:PRK00725 334 CIIS-GAVVRRSVLFSRVRVNSFSNVEDSVLLPDVNVGRSCRLRRCVIDRGCVIPEGM 390
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
6-77 2.94e-04

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 42.04  E-value: 2.94e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24653885    6 AVVFAAGRGTRLPevlGDAPKCLLPVGPYPLIWYPLNLLQQHN-FTEVIVVVLEQEKLEIQSALENTPLKLRL 77
Cdd:PRK00155   6 AIIPAAGKGSRMG---ADRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAELLLAKDPKVTV 75
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 391-437 3.56e-04

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: 39.15  E-value: 3.56e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 24653885 391 LIMSNAIVEEGCNIDNCIIGHRAQVKSGSVLKNCIIGPNYVVEEGTH 437
Cdd:cd03356   1 LIGESTVIGENAIIKNSVIGDNVRIGDGVTITNSILMDNVTIGANSV 47
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 2-135 4.19e-04

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: 42.71  E-value: 4.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885   2 TEFQAVVFAAGRGTRLpevLGDAPKCLLPVGPYPLIWYPLNLLQQHNFTEVIVVV---LEQekleIQSALENTPLKL--- 75
Cdd:COG1207   1 SPLAVVILAAGKGTRM---KSKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVghgAEQ----VRAALADLDVEFvlq 73

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24653885  76 --RLdyatipsdgdfGTADSLRYIYDKIKSD---FLVVSCD--LVSNVSLYPLINKFREHDAALAML 135
Cdd:COG1207  74 eeQL-----------GTGHAVQQALPALPGDdgtVLVLYGDvpLIRAETLKALLAAHRAAGAAATVL 129
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 374-429 4.35e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 42.42  E-value: 4.35e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24653885  374 VFGPNCIISPK-NIVANSLIMSNAIVEEGCNIDNCIIGHRAQVKSGSVLKNCIIGPN 429
Cdd:PRK14355 270 VIGRDTTIYPGvCISGDTRIGEGCTIEQGVVIKGCRIGDDVTVKAGSVLEDSVVGDD 326
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 381-435 4.98e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 42.16  E-value: 4.98e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 24653885  381 ISPKNIVANSLIMSNAIVEEGC----NIDNCIIGHRAQVKSGSVLKNCIIGPNYVVEEG 435
Cdd:PRK05293 279 NLPPQYIAENAKVKNSLVVEGCvvygTVEHSVLFQGVQVGEGSVVKDSVIMPGAKIGEN 337
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 1-109 5.30e-04

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: 42.14  E-value: 5.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885    1 MTEFQAVVFAAGRGTRLPEvlgDAPKCLLPVGPYPLIWYPL-NLLQQHNFTEVIVVVLEQEKLEIQSALENtplklrLDY 79
Cdd:PRK09382   3 MSDISLVIVAAGRSTRFSA---EVKKQWLRIGGKPLWLHVLeNLSSAPAFKEIVVVIHPDDIAYMKKALPE------IKF 73

                         90       100       110
                 ....*....|....*....|....*....|
gi 24653885   80 ATIPSDGDFgTADSLRYIYDKIKSDFLVVS 109
Cdd:PRK09382  74 VTLVTGGAT-RQESVRNALEALDSEYVLIH 102
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 395-436 9.26e-04

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


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 39.70  E-value: 9.26e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 24653885 395 NAIVEeGCNI-DNCIIGHRAQVKSGSVL-KNCIIGPNYVVEEGT 436
Cdd:cd04645  72 GAVLH-GCTIgDNCLIGMGAIILDGAVIgKGSIVAAGSLVPPGK 114
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 7-139 1.06e-03

GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which 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.


Pssm-ID: 133026 [Multi-domain]  Cd Length: 231  Bit Score: 40.31  E-value: 1.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885   7 VVFAAGRGTRLPEVLGDAPKCLLPVGPYPLI-WYPLNLLQqhNFTEVIVVVLEQEKLEIQsALENTPLKLRLDYATIPSD 85
Cdd:cd04183   2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIeWVIESLAK--IFDSRFIFICRDEHNTKF-HLDESLKLLAPNATVVELD 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 24653885  86 GD-FGTADSLRYIYDKIKSD--FLVVSCDLVSNVSLYPLINKFREHDAALAMLLFPS 139
Cdd:cd04183  79 GEtLGAACTVLLAADLIDNDdpLLIFNCDQIVESDLLAFLAAFRERDLDGGVLTFFS 135
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 342-441 1.17e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 40.89  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885  342 ISPGAVVkstqtkeiiaADNAKLsektslnfsvfGPNCIISPknivaNSLIMSNAIVEEGCNID-NCIIGHRAQVksGSv 420
Cdd:PRK00892 103 IHPSAVI----------DPSAKI-----------GEGVSIGP-----NAVIGAGVVIGDGVVIGaGAVIGDGVKI--GA- 153

                         90       100
                 ....*....|....*....|....*....
gi 24653885  421 lkNCIIGPNYVVEEGT--------HSQAV 441
Cdd:PRK00892 154 --DCRLHANVTIYHAVrignrviiHSGAV 180
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-59 1.73e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 40.50  E-value: 1.73e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 24653885    1 MTEFQAVVFAAGRGTRLPEvlgDAPKCLLPVGPYPLIWYPLNLLQQHNFTEVIVVVLEQ 59
Cdd:PRK14355   1 MNNLAAIILAAGKGTRMKS---DLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQ 56
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 6-139 2.51e-03

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 40.09  E-value: 2.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885    6 AVVFAAGRGTRLPEvlgDAPKCLLPVGPYPLIWYPLNLLQQHnFTEVIVVVLEQEKLEIQSALENTPLKLRLdyatipSD 85
Cdd:PRK14356   8 ALILAAGKGTRMHS---DKPKVLQTLLGEPMLRFVYRALRPL-FGDNVWTVVGHRADMVRAAFPDEDARFVL------QE 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885   86 GDFGTADSLRYIYDKIKSD----FLVVSCD--LVSNVSLYPLINKFREHDAALAMLLFPS 139
Cdd:PRK14356  78 QQLGTGHALQCAWPSLTAAgldrVLVVNGDtpLVTTDTIDDFLKEAAGADLAFMTLTLPD 137
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 376-443 2.63e-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: 38.93  E-value: 2.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885 376 GPNCIISPKNIV-ANSLIMSNAIVEEGCNI-------------DNCIIGHRAQVKSGSVLKNCiiGPNYVVEEGTHSQAV 441
Cdd:cd03352  11 GPNAVIGEGVVIgDGVVIGPGVVIGDGVVIgddcvihpnvtiyEGCIIGDRVIIHSGAVIGSD--GFGFAPDGGGWVKIP 88


                ..
gi 24653885 442 HL 443
Cdd:cd03352  89 QL 90
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 376-435 3.58e-03

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: 38.12  E-value: 3.58e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24653885 376 GPNCIISPKNIVANSliMSNAIVEEGCNI-DNCI----------------IGHRAQVKSGSVLKNCIIGPNYVVEEG 435
Cdd:cd04745  22 GKNCYIGPHASLRGD--FGRIVIRDGANVqDNCVihgfpgqdtvleenghIGHGAILHGCTIGRNALVGMNAVVMDG 96
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 395-437 4.67e-03

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 37.70  E-value: 4.67e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 24653885 395 NAIVEeGCNI-DNCIIGHRAQVKSGSVL-KNCIIGPNYVVEEGTH 437
Cdd:COG0663  83 GAILH-GCTIgDNVLIGMGAIVLDGAVIgDGSIVGAGALVTEGKV 126
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 6-108 6.25e-03

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: 37.56  E-value: 6.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24653885   6 AVVFAAGRGTRLpevlgDAPKCLLPVGPYPLIWYPLNLLQQHNFTEVIVVVLEQEKLE-------------------IQS 66
Cdd:cd02503   3 GVILAGGKSRRM-----GGDKALLELGGKPLLEHVLERLKPLVDEVVISANRDQERYAllgvpvipdeppgkgplagILA 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 24653885  67 ALENTPLKLrldYATIPSDGDFGTADSLRYIYDKIKSDFLVV 108
Cdd:cd02503  78 ALRAAPADW---VLVLACDMPFLPPELLERLLAAAEEGADAV 116
 
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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