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Conserved domains on  [gi|119113879|ref|XP_314112|]
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AGAP005210-PA [Anopheles gambiae str. PEST]

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; ...
 6-217 1.50e-72

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: 227.54  E-value: 1.50e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879   6 FQAIVLAAGKGTRLPEILEGRPKCLLPIGPFPMIWYPLQLLQRHGFTEVIVVVQESEKSEIQQRLE--RLQLKLKLDYYS 83
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRsfPLNLKQKLDEVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879  84 IPTDSECGTADSLRLVSDKIKSDVVVLSCDSIIEINLYPLLSKFREKDASVQLLLLESGKDQDVVMPGPKSKYKAEKDII 163
Cdd:cd04198   81 IVLDEDMGTADSLRHIRKKIKKDFLVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVSSEQKGGKGKSKKADERDVI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119113879 164 GYDKATSRVLFMASASDFEETVKLSGHLLRENPDMIISSSMLDAHVYIMKKWVV 217
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 ...
 357-436 3.45e-29

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: 109.20  E-value: 3.45e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879 357 VGDMTTISEKTSLNQNVIANGCTVQPKTRINNSVLMDGVTVEETVVIDNCIVGEKAVIKSGSVLKNCIIGPHFVVAAGTK 436
Cdd:cd04652    2 VGENTQVGEKTSIKRSVIGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLVGSGYRVEAGTE 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; ...
 6-217 1.50e-72

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: 227.54  E-value: 1.50e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879   6 FQAIVLAAGKGTRLPEILEGRPKCLLPIGPFPMIWYPLQLLQRHGFTEVIVVVQESEKSEIQQRLE--RLQLKLKLDYYS 83
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRsfPLNLKQKLDEVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879  84 IPTDSECGTADSLRLVSDKIKSDVVVLSCDSIIEINLYPLLSKFREKDASVQLLLLESGKDQDVVMPGPKSKYKAEKDII 163
Cdd:cd04198   81 IVLDEDMGTADSLRHIRKKIKKDFLVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVSSEQKGGKGKSKKADERDVI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119113879 164 GYDKATSRVLFMASASDFEETVKLSGHLLRENPDMIISSSMLDAHVYIMKKWVV 217
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 ...
 357-436 3.45e-29

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: 109.20  E-value: 3.45e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879 357 VGDMTTISEKTSLNQNVIANGCTVQPKTRINNSVLMDGVTVEETVVIDNCIVGEKAVIKSGSVLKNCIIGPHFVVAAGTK 436
Cdd:cd04652    2 VGENTQVGEKTSIKRSVIGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLVGSGYRVEAGTE 81
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 7-138 1.65e-26

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: 106.78  E-value: 1.65e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879   7 QAIVLAAGKGTRLPEILEGRPKCLLPIGPFPMIWYPLQLLQRHGFTEVIVVVqeSEKSE-IQQRL-ERLQLKLKLDYysI 84
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINV--GYLAEqIEEYFgDGSRFGVRITY--V 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119113879  85 PTDSECGTADSLRLVSDKIKSD-VVVLSCDSIIEINLYPLLSKFREKDASVQLLL 138
Cdd:COG1208   77 DEGEPLGTGGALKRALPLLGDEpFLVLNGDILTDLDLAALLAFHREKGADATLAL 131
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 8-134 7.93e-18

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: 82.69  E-value: 7.93e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879    8 AIVLAAGKGTRLPEILEGRPKCLLPIG-PFPMIWYPLQLLQRHGFTEVIVVVQESEKSEIQQRLERL-QLKLKLDYysIP 85
Cdd:pfam00483   2 AIILAGGSGTRLWPLTRTLAKPLVPVGgKYPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGsKFGVQITY--AL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 119113879   86 TDSECGTADSLRLVSDKI---KSDVVVLSCDSIIEINLYPLLSKFREKDASV 134
Cdd:pfam00483  80 QPEGKGTAPAVALAADFLgdeKSDVLVLGGDHIYRMDLEQAVKFHIEKAADA 131
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
8-70 2.06e-08

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 54.75  E-value: 2.06e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119113879   8 AIVLAAGKGTRLPEileGRPKCLLPIGPFPMIWYPLQLLQRHG-FTEVIVVVQESEKSEIQQRL 70
Cdd:PRK00155   6 AIIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAELL 66
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 368-436 3.01e-08

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 55.26  E-value: 3.01e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119113879 368 SLNQNVIANGCTVQPKTRINNSVLMDGVTVEETVVIDNCIVGEKAVIKSGSVL---KNCI--IGPHFVVAAGTK 436
Cdd:PRK05293 305 TVEHSVLFQGVQVGEGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVIIgggKEVItvIGENEVIGVGTV 378
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 8-75 3.14e-08

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: 53.83  E-value: 3.14e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119113879    8 AIVLAAGKGTRLPeilEGRPKCLLPIGPFPMIWYPLQLLQRH-GFTEVIVVVQESEKSEIQQRLERLQL 75
Cdd:TIGR00453   2 AVIPAAGRGTRFG---SGVPKQYLELGGRPLLEHALDAFLAHpAIDEVVVVVSPDDTEFFQKYLVARAV 67
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 373-420 1.03e-07

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 53.54  E-value: 1.03e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 119113879 373 VIANGCTVQPKTRINNSVLMDGVTVEETVVIDNCIVGEKAVIKSGSVL 420
Cdd:COG0448  305 VLFRGVRVESGAVVENSVIMPGVVIGEGAVIENAIIDKNVVIPPGVVI 352
 
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; ...
 6-217 1.50e-72

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: 227.54  E-value: 1.50e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879   6 FQAIVLAAGKGTRLPEILEGRPKCLLPIGPFPMIWYPLQLLQRHGFTEVIVVVQESEKSEIQQRLE--RLQLKLKLDYYS 83
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRsfPLNLKQKLDEVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879  84 IPTDSECGTADSLRLVSDKIKSDVVVLSCDSIIEINLYPLLSKFREKDASVQLLLLESGKDQDVVMPGPKSKYKAEKDII 163
Cdd:cd04198   81 IVLDEDMGTADSLRHIRKKIKKDFLVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVSSEQKGGKGKSKKADERDVI 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 119113879 164 GYDKATSRVLFMASASDFEETVKLSGHLLRENPDMIISSSMLDAHVYIMKKWVV 217
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; ...
 6-217 8.33e-55

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: 181.68  E-value: 8.33e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879   6 FQAIVLAAGKGTRLPEILEGRPKCLLPIGPFPMIWYPLQLLQRHGFTEVIVVVQESEKSEIQQRLER----LQLKLKLDY 81
Cdd:cd02507    1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSkwssLSSKMIVDV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879  82 YSIPTDSECGTADSLRLVSDKIKSDVVVLSCDSIIEINLYPLLSKFREKDASVQLLLLESGKDQDVvmPGPKSKYKAEKD 161
Cdd:cd02507   81 ITSDLCESAGDALRLRDIRGLIRSDFLLLSCDLVSNIPLSELLEERRKKDKNAIATLTVLLASPPV--STEQSKKTEEED 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 119113879 162 IIGYDKATSRVLFMASASDFEE--TVKLSGHLLRENPDMIISSSMLDAHVYIMKKWVV 217
Cdd:cd02507  159 VIAVDSKTQRLLLLHYEEDLDEdlELIIRKSLLSKHPNVTIRTDLLDCHIYICSPDVL 216
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 357-436 3.45e-29

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: 109.20  E-value: 3.45e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879 357 VGDMTTISEKTSLNQNVIANGCTVQPKTRINNSVLMDGVTVEETVVIDNCIVGEKAVIKSGSVLKNCIIGPHFVVAAGTK 436
Cdd:cd04652    2 VGENTQVGEKTSIKRSVIGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLVGSGYRVEAGTE 81
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 7-138 1.65e-26

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: 106.78  E-value: 1.65e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879   7 QAIVLAAGKGTRLPEILEGRPKCLLPIGPFPMIWYPLQLLQRHGFTEVIVVVqeSEKSE-IQQRL-ERLQLKLKLDYysI 84
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINV--GYLAEqIEEYFgDGSRFGVRITY--V 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119113879  85 PTDSECGTADSLRLVSDKIKSD-VVVLSCDSIIEINLYPLLSKFREKDASVQLLL 138
Cdd:COG1208   77 DEGEPLGTGGALKRALPLLGDEpFLVLNGDILTDLDLAALLAFHREKGADATLAL 131
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 8-140 4.66e-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: 96.88  E-value: 4.66e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879   8 AIVLAAGKGTRLPEILEGRPKCLLPIGPFPMIWYPLQLLQRHGFTEVIVVVQEsEKSEIQQRL-ERLQLKLKLDYYSIPT 86
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGY-LGEQIEEYFgDGSKFGVNIEYVVQEE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119113879  87 DSecGTADSLRLVSDKIKSD-VVVLSCDSIIEINLYPLLSKFREKDASVQLLLLE 140
Cdd:cd04181   80 PL--GTAGAVRNAEDFLGDDdFLVVNGDVLTDLDLSELLRFHREKGADATIAVKE 132
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
7-113 3.29e-19

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 86.45  E-value: 3.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879   7 QAIVLAAGKGTRLPEILEGRPKCLLPIGPFPMIWYPLQLLQRHGFTEVIVVV-QESEKseIQQRLERLQLKLKL---DYY 82
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTgYKAEL--IEEALARPGPDVTFvynPDY 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 119113879  83 siptdSECGTADSLRLVSDKIKSDVVVLSCD 113
Cdd:COG1213   79 -----DETNNIYSLWLAREALDEDFLLLNGD 104
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 8-134 7.93e-18

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: 82.69  E-value: 7.93e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879    8 AIVLAAGKGTRLPEILEGRPKCLLPIG-PFPMIWYPLQLLQRHGFTEVIVVVQESEKSEIQQRLERL-QLKLKLDYysIP 85
Cdd:pfam00483   2 AIILAGGSGTRLWPLTRTLAKPLVPVGgKYPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGsKFGVQITY--AL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 119113879   86 TDSECGTADSLRLVSDKI---KSDVVVLSCDSIIEINLYPLLSKFREKDASV 134
Cdd:pfam00483  80 QPEGKGTAPAVALAADFLgdeKSDVLVLGGDHIYRMDLEQAVKFHIEKAADA 131
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 8-138 3.07e-17

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: 80.29  E-value: 3.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879   8 AIVLAAGKGTRLPEILEGRPKCLLPIGPFPMIWYPLQLLQRHGFTEVIVVVqeSEKSE-IQQRLERLQLKLKLDYYSIpT 86
Cdd:cd06915    1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSV--GYLAEqIEEYFGDGYRGGIRIYYVI-E 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119113879  87 DSECGTADSLRLVSDKIKSDVV-VLSCDSIIEINLYPLLSKFREKDASVQLLL 138
Cdd:cd06915   78 PEPLGTGGAIKNALPKLPEDQFlVLNGDTYFDVDLLALLAALRASGADATMAL 130
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 6-211 8.77e-17

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: 78.80  E-value: 8.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879   6 FQAIVLAAGKGTRLPEILEGRPKCLLPIGPFPMIWYPLQLLQRHGFTEVIVVVQeSEKSEIQQRLERLQ-LKLKLDYYSI 84
Cdd:cd04197    1 LQAVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCC-SHSDQIKEYIEKSKwSKPKSSLMIV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879  85 P--TDSECGTA-DSLRLVSDK--IKSDVVVLSCDSIIEINLYPLLSKFRE-----KDASVQLLLLESGkdqdvvmPGPKS 154
Cdd:cd04197   80 IiiMSEDCRSLgDALRDLDAKglIRGDFILVSGDVVSNIDLKEILEEHKErrkkdKNAIMTMVLKEAS-------PPHRT 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 119113879 155 KYKAEKDIIGYDKATSRVLFMAS--ASDFEETVKLSGHLLRENPDMIISSSMLDAHVYI 211
Cdd:cd04197  153 RRTGEEFVIAVDPKTSRLLHYEElpGSKYRSITDLPSELLGSNSEVEIRHDLLDCHIDI 211
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 8-117 2.07e-15

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: 75.35  E-value: 2.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879   8 AIVLAAGKGTRLPEILEGRPKCLLPIGPFPMIWYPLQLLQRHGFTEVIVVV-QESEKseIQQRLERLqlkLKLDYYSIPT 86
Cdd:cd02523    1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTgYKKEQ--IEELLKKY---PNIKFVYNPD 75

                         90       100       110
                 ....*....|....*....|....*....|.
gi 119113879  87 DSECGTADSLRLVSDKIKSDVVVLSCDSIIE 117
Cdd:cd02523   76 YAETNNIYSLYLARDFLDEDFLLLEGDVVFD 106
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 357-433 1.04e-14

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: 68.81  E-value: 1.04e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119113879 357 VGDMTTISEKTSLNQNVIANGCTVQPKTRINNSVLMDGVTVEETVVIDNCIVGEKAVIKSGSVLKN-CIIGPHFVVAA 433
Cdd:cd03356    2 IGESTVIGENAIIKNSVIGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVNlCIIGDDVVVED 79
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 8-140 1.20e-14

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: 72.99  E-value: 1.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879   8 AIVLAAGKGTRLPEILEGRPKCLLPIGPFPMIWYPLQLLQRHGFTEVIVVVQESeKSEIQQRL---ERLQLKLKLdyysI 84
Cdd:cd04189    3 GLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPT-GEEIKEALgdgSRFGVRITY----I 77

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 119113879  85 PTDSECGTADSLRLVSDKIKSD--VVVLScDSIIEINLYPLLSKFREKDASVQLLLLE 140
Cdd:cd04189   78 LQEEPLGLAHAVLAARDFLGDEpfVVYLG-DNLIQEGISPLVRDFLEEDADASILLAE 134
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
8-134 4.20e-12

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 66.65  E-value: 4.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879   8 AIVLAAGKGTRLPEILEGRPKCLLPIGPFPMIWYPLQLLQRHGFTEVIVVVQESEKSEIQQRLERL-QLKLKLDYysIPT 86
Cdd:COG1209    3 GIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGsQLGIKISY--AVQ 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 119113879  87 DSECGTADSLRLVSDKIKSD--VVVLScDSIIEIN-LYPLLSKF--REKDASV 134
Cdd:COG1209   81 PEPLGLAHAFIIAEDFIGGDpvALVLG-DNIFYGDgLSELLREAaaRESGATI 132
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 356-436 1.20e-11

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: 60.28  E-value: 1.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879 356 AVGDMTTISEKTSLNQNVIANGCTVQPKTRINNSVLMDGVTVEETVVIDNCIVGEKAVIKsgsvlKNCIIGPHFVVAAGT 435
Cdd:cd05787    1 VIGRGTSIGEGTTIKNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAVIG-----KGCTIPPGSLISFGV 75


                 .
gi 119113879 436 K 436
Cdd:cd05787   76 V 76
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 8-436 2.28e-11

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 65.10  E-value: 2.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879   8 AIVLAAGKGTRLPEILEGRPKCLLPIG------PFP---MIwyplqllqRHGFTEVIVVVQEseKSE-----IQQ----R 69
Cdd:COG0448    4 AIILAGGRGSRLGPLTKDRAKPAVPFGgkyriiDFPlsnCV--------NSGIRRVGVLTQY--KSHslndhIGSgkpwD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879  70 LERlqlklKLDYYSI--PTDSEC------GTAD----SLRLVsDKIKSD-VVVLSCDSIIEINLYPLLSKFREKDASVQL 136
Cdd:COG0448   74 LDR-----KRGGVFIlpPYQQREgedwyqGTADavyqNLDFI-ERSDPDyVLILSGDHIYKMDYRQMLDFHIESGADITV 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879 137 lllesgkdqdVVMPGPKSKYKAeKDIIGYDkATSRVLfmasasDFEETVKlsghllreNPDMIISSsMldaHVYIMKKwv 216
Cdd:COG0448  148 ----------ACIEVPREEASR-FGVMEVD-EDGRIT------EFEEKPK--------DPKSALAS-M---GIYVFNK-- 195

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879 217 veylavtellsavkgELLphiikKQLLQppavpendgasEYTAKPKVD---DIFQFAVytemdkkidkasvfnKEEKATS 293
Cdd:COG0448  196 ---------------DVL-----IELLE-----------EDAPNSSHDfgkDIIPRLL---------------DRGKVYA 229

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879 294 HPIRcyAYFADskafglrVNNVRSFLSCNLKIFEIFPALtgfterELVSQSSSIkstqITKcaVGDM--TTISEKTSLNQ 371
Cdd:COG0448  230 YEFD--GYWRD-------VGTIDSYYEANMDLLDPEPEF------NLYDPEWPI----YTK--QKDLppAKFVRGGKVKN 288

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119113879 372 NVIANGCTVqpKTRINNSVLMDGVTVEETVVIDNCIVGEKAVIKSGSVLKNCIIGPHFVVAAGTK 436
Cdd:COG0448  289 SLVSNGCII--SGTVENSVLFRGVRVESGAVVENSVIMPGVVIGEGAVIENAIIDKNVVIPPGVV 351
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 8-150 5.04e-11

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: 60.67  E-value: 5.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879    8 AIVLAAGKGTRLpeileGRPKCLLPIGPFPMIWYPLQLLQRHgFTEVIVVVQEsekSEIQQRLERLQLKLKLDyysipTD 87
Cdd:pfam12804   1 AVILAGGRSSRM-----GGDKALLPLGGKPLLERVLERLRPA-GDEVVVVAND---EEVLAALAGLGVPVVPD-----PD 66

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119113879   88 SECGTADSLR--LVSDKIKSDVVVLSCDSiieinlyPLLSKfrekdASVQLLLLESGKDQ-DVVMP 150
Cdd:pfam12804  67 PGQGPLAGLLaaLRAAPGADAVLVLACDM-------PFLTP-----ELLRRLLAAAEESGaDIVVP 120
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
8-113 8.02e-11

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 60.94  E-value: 8.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879   8 AIVLAAGKGTRLpeileGRPKCLLPIGPFPMIWYPLQLLQRHGFTEVIVVVQEsEKSEIQQRLERLQLKLkldyysIP-T 86
Cdd:COG2068    6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGA-DAEEVAAALAGLGVRV------VVnP 73

                         90       100       110
                 ....*....|....*....|....*....|
gi 119113879  87 DSECGTADSLRLVSDKIKSD---VVVLSCD 113
Cdd:COG2068   74 DWEEGMSSSLRAGLAALPADadaVLVLLGD 103
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 8-130 1.33e-10

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: 61.44  E-value: 1.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879   8 AIVLAAGKGTRLPEILEGRPKCLLPIGPFPMIWYPLQLLQRHGFTEVIVVVQESEKSEIQQRL-ERLQLKLKLDYysIPT 86
Cdd:cd02538    3 GIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLgDGSDLGIRITY--AVQ 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 119113879  87 DSECGTADSLRLVSDKIKSD-VVVLSCDSIIE-INLYPLLSKFREK 130
Cdd:cd02538   81 PKPGGLAQAFIIGEEFIGDDpVCLILGDNIFYgQGLSPILQRAAAQ 126
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 361-436 2.66e-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: 57.09  E-value: 2.66e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119113879 361 TTISEKTSLNQNVIANGCTVQPKTrINNSVLMDGVTVEETVVIDNCIVGEKAVIKSGSVLKNCIIGPHFVVAAGTK 436
Cdd:cd04651    2 PYIGRRGEVKNSLVSEGCIISGGT-VENSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIIDKNVVIPDGVV 76
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 8-200 3.50e-10

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: 59.11  E-value: 3.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879   8 AIVLAAGKGTRLpeileGRPKCLLPIGPFPMIWYPLQLLQRHGFTEVIVVVQEsEKSEIQQRLERLQLKLkldyySIPTD 87
Cdd:cd04182    3 AIILAAGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGA-EADAVRAALAGLPVVV-----VINPD 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879  88 SECGTADSLRLVSDKIKSD---VVVLSCDsiieinlYPLLSKfrekdASVQLLLlesgkdqdvvmpgpkSKYKAEKDIIg 164
Cdd:cd04182   72 WEEGMSSSLAAGLEALPADadaVLILLAD-------QPLVTA-----ETLRALI---------------DAFREDGAGI- 123

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 119113879 165 ydkATSR--------VLFmaSASDFEETVKLSG-----HLLRENPDMII 200
Cdd:cd04182  124 ---VAPVyqgrrghpVLF--PRSLFPELLALSGdkgarSLLRAHPDRVV 167
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 9-79 8.55e-10

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: 58.60  E-value: 8.55e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119113879   9 IVLAAGKGTRLPEileGRPKCLLPIGPFPMIWYPLQLLQRHG-FTEVIVVVQESEKSEIQQRLERLQLKLKL 79
Cdd:COG1211    1 IIPAAGSGSRMGA---GIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEELLAKYGIDKPV 69
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 8-132 1.77e-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: 57.52  E-value: 1.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879   8 AIVLAAGKGTRLPEILEGRPKCLLPIGPFPMIWYPLQLLQRHGFTEVIVVVqeSEKSEIqqrLER-----LQLKLKLDYy 82
Cdd:cd06426    1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISV--NYLAEM---IEDyfgdgSKFGVNISY- 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 119113879  83 sIPTDSECGTADSLRLVSDKIKSDVVVLSCDSIIEINLYPLLSKFREKDA 132
Cdd:cd06426   75 -VREDKPLGTAGALSLLPEKPTDPFLVMNGDILTNLNYEHLLDFHKENNA 123
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 373-434 1.05e-08

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


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 51.86  E-value: 1.05e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119113879 373 VIANGCTVQPKTRINNSVLMDGVTVEETVVIDNCIVGEKAVIKSGSVLKNCIIGPHFVVAAG 434
Cdd:cd03356    1 LIGESTVIGENAIIKNSVIGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGEN 62
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
8-70 2.06e-08

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 54.75  E-value: 2.06e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119113879   8 AIVLAAGKGTRLPEileGRPKCLLPIGPFPMIWYPLQLLQRHG-FTEVIVVVQESEKSEIQQRL 70
Cdd:PRK00155   6 AIIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAELL 66
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 8-78 2.23e-08

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: 54.45  E-value: 2.23e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119113879   8 AIVLAAGKGTRLPEileGRPKCLLPIGPFPMIWYPLQLLQRHG-FTEVIVVVQESEKSEIQQRLERLQLKLK 78
Cdd:cd02516    3 AIILAAGSGSRMGA---DIPKQFLELGGKPVLEHTLEAFLAHPaIDEIVVVVPPDDIDLAKELAKYGLSKVV 71
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 368-436 3.01e-08

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 55.26  E-value: 3.01e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119113879 368 SLNQNVIANGCTVQPKTRINNSVLMDGVTVEETVVIDNCIVGEKAVIKSGSVL---KNCI--IGPHFVVAAGTK 436
Cdd:PRK05293 305 TVEHSVLFQGVQVGEGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVIIgggKEVItvIGENEVIGVGTV 378
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 8-75 3.14e-08

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: 53.83  E-value: 3.14e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119113879    8 AIVLAAGKGTRLPeilEGRPKCLLPIGPFPMIWYPLQLLQRH-GFTEVIVVVQESEKSEIQQRLERLQL 75
Cdd:TIGR00453   2 AVIPAAGRGTRFG---SGVPKQYLELGGRPLLEHALDAFLAHpAIDEVVVVVSPDDTEFFQKYLVARAV 67
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 7-56 3.28e-08

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: 53.73  E-value: 3.28e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 119113879   7 QAIVLAAGKGTRLPEILEGRPKCLLPIGPFPMIWYPLQLLQRHGFTEVIV 56
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVV 50
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 373-422 4.85e-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: 50.92  E-value: 4.85e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 119113879 373 VIANGCTVQPKTRINNSVLMDGVTVEETVVIDNCIVGEKAVIKSGSVLKN 422
Cdd:cd04651   30 VLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIIDKNVVIPDGVVIGG 79
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 8-140 4.90e-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: 53.67  E-value: 4.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879   8 AIVLAAGKGTRlpeILEGRPKCLLPIGPFPMIWYPLQLLQRHGFTEVIVVVQEsEKSEIQQRLERLQLKLKLDyysiptD 87
Cdd:cd02540    1 AVILAAGKGTR---MKSDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGH-GAEQVKKALANPNVEFVLQ------E 70

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 119113879  88 SECGTADSLRLVSDKIK---SDVVVLSCDS-IIEIN-LYPLLSKFREKDASVQLLLLE 140
Cdd:cd02540   71 EQLGTGHAVKQALPALKdfeGDVLVLYGDVpLITPEtLQRLLEAHREAGADVTVLTAE 128
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 8-123 5.89e-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: 53.37  E-value: 5.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879   8 AIVLAAGKGTRLPEILEGRPKCLLPIGPFPMIWYPLQLLQRHGFTEVIVVV---QESEKSEIQQRLERLQLKLkldYYSI 84
Cdd:cd06425    3 ALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVnyrPEDMVPFLKEYEKKLGIKI---TFSI 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 119113879  85 PTDsECGTADSLRLVSDKIKSDV---VVLSCDSIIEinlYPL 123
Cdd:cd06425   80 ETE-PLGTAGPLALARDLLGDDDepfFVLNSDVICD---FPL 117
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 348-415 9.46e-08

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


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 49.16  E-value: 9.46e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119113879 348 KSTQITKCAVGDMTTISEKTSLNQNVIANGCTVQPKTRINNSVLMDGVTVEETV-VIDNCIVGEKAVIK 415
Cdd:cd03356   10 ENAIIKNSVIGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVrVVNLCIIGDDVVVE 78
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 373-420 1.03e-07

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 53.54  E-value: 1.03e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 119113879 373 VIANGCTVQPKTRINNSVLMDGVTVEETVVIDNCIVGEKAVIKSGSVL 420
Cdd:COG0448  305 VLFRGVRVESGAVVENSVIMPGVVIGEGAVIENAIIDKNVVIPPGVVI 352
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 9-110 1.32e-07

glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase homotetramer This model describes a tightly conserved but broadly distributed subfamily (here designated as short form) of known and putative bacterial glucose-1-phosphate thymidylyltransferases. It is well characterized in several species as the first of four enzymes involved in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 130274 [Multi-domain]  Cd Length: 286  Bit Score: 52.78  E-value: 1.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879    9 IVLAAGKGTRLPEILEGRPKCLLPIGPFPMIWYPLQLLQRHGFTEVIVVVQESEKSEIQQRL-ERLQLKLKLDYYSIPtd 87
Cdd:TIGR01207   3 IILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLgDGSQWGINLSYAVQP-- 80

                          90       100
                  ....*....|....*....|...
gi 119113879   88 SECGTADSLRLVSDKIKSDVVVL 110
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSAL 103
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 9-186 1.40e-07

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: 52.26  E-value: 1.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879   9 IVLAAGKGTRLPEILEGRPKCLLPIGPFPMIWYPLQLLQRHGFTEVIVVVQES--EKSEIQQRLerlqLKLKLDYYSIPT 86
Cdd:cd04183    2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFICRDEhnTKFHLDESL----KLLAPNATVVEL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879  87 DSEC-GTADSLRLVSDKIKSD--VVVLSCDSIIEINLYPLLSKFREKDASVQLLLLESgkdqdvvmPGPKSKY------- 156
Cdd:cd04183   78 DGETlGAACTVLLAADLIDNDdpLLIFNCDQIVESDLLAFLAAFRERDLDGGVLTFFS--------SHPRWSYvkldeng 149

                        170       180       190
                 ....*....|....*....|....*....|....
gi 119113879 157 ----KAEKDIIGyDKATSRVLFMASASDFEETVK 186
Cdd:cd04183  150 rvieTAEKEPIS-DLATAGLYYFKSGSLFVEAAK 182
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 8-56 3.34e-07

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: 51.42  E-value: 3.34e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 119113879   8 AIVLAAGKGTRLPEILEGRPKCLLPIGPFPMIWYPLQLLQRHGFTEVIV 56
Cdd:cd02524    1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFIL 49
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 361-436 3.50e-07

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: 50.50  E-value: 3.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879 361 TTISEKTslnqnVIANGCTVQPKTRINNSVLMDGVTVEETVVIDNCIVGEKAVI------KSGSVLK-NCIIGpHFV--- 430
Cdd:cd03353   28 VILEGKT-----VIGEDCVIGPNCVIKDSTIGDGVVIKASSVIEGAVIGNGATVgpfahlRPGTVLGeGVHIG-NFVeik 101


                 ....*....
gi 119113879 431 ---VAAGTK 436
Cdd:cd03353  102 kstIGEGSK 110
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 373-436 4.41e-07

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 51.75  E-value: 4.41e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119113879 373 VIANGCTVQpKTRINNSVLMDGVTVEETVVIDNCIVGEKAVIKSGSVLKNCIIGPHFVVAAGTK 436
Cdd:PRK00844 317 LVSAGSIIS-GATVRNSVLSPNVVVESGAEVEDSVLMDGVRIGRGAVVRRAILDKNVVVPPGAT 379
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 8-150 1.40e-06

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: 48.65  E-value: 1.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879   8 AIVLAAGKGTRLpeileGRPKCLLPIGPFPMIWYPLQLLQRHgFTEVIVVVQESEkseiqqRLERLQLKLKLDYYsiptd 87
Cdd:COG0746    7 GVILAGGRSRRM-----GQDKALLPLGGRPLLERVLERLRPQ-VDEVVIVANRPE------RYAALGVPVVPDDP----- 69

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119113879  88 SECGTADSLRLVSDKIKSD-VVVLSCDSiieinlyPLLSkfrekDASVQLLLLESGKDQDVVMP 150
Cdd:COG0746   70 PGAGPLAGILAALEAAPAEwVLVLACDM-------PFLP-----PDLVRRLLEALEEGADAVVP 121
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 8-434 1.86e-06

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 50.13  E-value: 1.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879   8 AIVLAAGKGTRLPEileGRPKCLLPIGPFPMIWYPLQLLQRHGFTEVIVVV-QESEKseIQQRL-ERLQLKLKLDyysip 85
Cdd:PRK14355   6 AIILAAGKGTRMKS---DLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVgHQAEK--VREHFaGDGDVSFALQ----- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879  86 tDSECGTADSLRLVSDKIK--SDVVVLSCDSIieinlyPLLSkfrekDASVQLLLLESGKDQDVV------MPGPkskYK 157
Cdd:PRK14355  76 -EEQLGTGHAVACAAPALDgfSGTVLILCGDV------PLLR-----AETLQGMLAAHRATGAAVtvltarLENP---FG 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879 158 AEKDIIGYDKATSRVLFMASASDFEETVklsghllREnpdmiisssmLDAHVYIMkkwvvEYLAVTELLSAVKgellphi 237
Cdd:PRK14355 141 YGRIVRDADGRVLRIVEEKDATPEERSI-------RE----------VNSGIYCV-----EAAFLFDAIGRLG------- 191

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879 238 ikkqllqppavpeNDGAS-EYTakpkVDDIFQFAVytemdkkidkasvfnkeekatSHPIRCYAYFADSKAfglrvnnvr 316
Cdd:PRK14355 192 -------------NDNAQgEYY----LTDIVAMAA---------------------AEGLRCLAFPVADPD--------- 224

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879 317 sflscnlkifEIFpaltGFTERELVSQSSSIKSTQITKCAVGDMTTI--SEKTSLNQNV-IANGCTVQPKTRIN-NSVLM 392
Cdd:PRK14355 225 ----------EIM----GVNDRAQLAEAARVLRRRINRELMLAGVTLidPETTYIDRGVvIGRDTTIYPGVCISgDTRIG 290

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 119113879 393 DGVTVEETVVIDNCIVGEKAVIKSGSVLKNCIIGPHfvVAAG 434
Cdd:PRK14355 291 EGCTIEQGVVIKGCRIGDDVTVKAGSVLEDSVVGDD--VAIG 330
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 7-86 1.94e-06

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 49.29  E-value: 1.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879   7 QAIVLAAGKGTRLPEILEGRPKCLLPIGPFPMIWYPLQLLQRHGFTEVIVVVQESEKSEIQQRL-ERLQLKLKLDYYSIP 85
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLgDGSQWGLNLQYKVQP 84


                 .
gi 119113879  86 T 86
Cdd:PRK15480  85 S 85
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 8-150 6.44e-06

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: 46.41  E-value: 6.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879   8 AIVLAAGKGTRLpeileGRPKCLLPIGPFPMIWYPLQLLQRHgFTEVIVVVQESekseiQQRLERLQLKLKLDyySIPtd 87
Cdd:cd02503    3 GVILAGGKSRRM-----GGDKALLELGGKPLLEHVLERLKPL-VDEVVISANRD-----QERYALLGVPVIPD--EPP-- 67

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879  88 sECG------TAdsLRlvsdKIKSD-VVVLSCDSiieinlyPLLSKfrekdASVQLLLLESGKDQDVVMP 150
Cdd:cd02503   68 -GKGplagilAA--LR----AAPADwVLVLACDM-------PFLPP-----ELLERLLAAAEEGADAVVP 118
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 373-436 6.47e-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: 48.10  E-value: 6.47e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119113879 373 VIANGCTVQPKTRINNSVLMDGVTVEETvVIDNCIVGEKAVI------KSGSVL-KNCIIGpHFV------VAAGTK 436
Cdd:COG1207  286 VIGEGVVIGPNCTLKDSTIGDGVVIKYS-VIEDAVVGAGATVgpfarlRPGTVLgEGVKIG-NFVevknstIGEGSK 360
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 363-440 6.73e-06

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 47.94  E-value: 6.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879 363 ISEKTSLNQNVIANGCTVQPKtrINNSVLMDGVTVEE-TVVID-----NCIVGEKAVIKSGSVLKNCIIGPHFVVAAGTK 436
Cdd:PRK05293 285 IAENAKVKNSLVVEGCVVYGT--VEHSVLFQGVQVGEgSVVKDsvimpGAKIGENVVIERAIIGENAVIGDGVIIGGGKE 362


                 ....
gi 119113879 437 KESV 440
Cdd:PRK05293 363 VITV 366
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 8-125 1.06e-05

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: 47.71  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879   8 AIVLAAGKGTRLpeiLEGRPKCLLPIGPFPMIWYPLQLLQRHGFTEVIVVV-QESEksEIQQRLERLQLK-------Lkl 79
Cdd:COG1207    5 VVILAAGKGTRM---KSKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVgHGAE--QVRAALADLDVEfvlqeeqL-- 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 119113879  80 dyysiptdsecGTADSLRLVSDKIKSD---VVVLSCDSiieinlyPLLS 125
Cdd:COG1207   78 -----------GTGHAVQQALPALPGDdgtVLVLYGDV-------PLIR 108
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 372-435 2.14e-05

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: 45.09  E-value: 2.14e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119113879 372 NVIANGCTVQPKTRI-NNSVLMDGVTVEETVVI-DNCIVGEKAVIKSGSVLK-NCIIGPHFVVAAGT 435
Cdd:cd03352    2 AKIGENVSIGPNAVIgEGVVIGDGVVIGPGVVIgDGVVIGDDCVIHPNVTIYeGCIIGDRVIIHSGA 68
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 8-134 6.98e-05

ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ADP-glucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase) catalyzes a very important step in the biosynthesis of alpha 1,4-glucans (glycogen or starch) in bacteria and plants: synthesis of the activated glucosyl donor, ADP-glucose, from glucose-1-phosphate and ATP. ADP-glucose pyrophosphorylase is a tetrameric allosterically regulated enzyme. While a homotetramer in bacteria, in plant chloroplasts and amyloplasts, it is a heterotetramer of two different, yet evolutionary related, subunits. There are a number of conserved regions in the sequence of bacterial and plant ADP-glucose pyrophosphorylase subunits. It is a subfamily of a very diverse glycosy transferase family 2.


Pssm-ID: 133002 [Multi-domain]  Cd Length: 200  Bit Score: 43.69  E-value: 6.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879   8 AIVLAAGKGTRLPEILEGRPKCLLPI-GPFPMIWYPLQLLQRHGFTEVIVVVQESEKSEIQ--QRLERLQLKLKLDYYSI 84
Cdd:cd02508    1 AIILAGGEGTRLSPLTKKRAKPAVPFgGRYRLIDFPLSNMVNSGIRNVGVLTQYKSRSLNDhlGSGKEWDLDRKNGGLFI 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119113879  85 -------PTDSECGTADSLRLVSDKI-KSD---VVVLSCDSIIEINLYPLLSKFREKDASV 134
Cdd:cd02508   81 lppqqrkGGDWYRGTADAIYQNLDYIeRSDpeyVLILSGDHIYNMDYREMLDFHIESGADI 141
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 361-421 7.34e-05

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


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 42.78  E-value: 7.34e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119113879 361 TTISEKTSLNQNVIANGCTVQPKTRI-NNSVLMDGVTVEetvviDNCIVGEKAVIKSGSVLK 421
Cdd:cd04645   61 TIIGDNVTVGHGAVLHGCTIGDNCLIgMGAIILDGAVIG-----KGSIVAAGSLVPPGKVIP 117
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 8-145 1.34e-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: 43.40  E-value: 1.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879   8 AIVLAAG--KGTRL-PEILEgRPKCLLPIGPFPMIWYPLQLL-QRHGFTEVIVV------VQESEKSEIQQRLeRLQLKL 77
Cdd:cd06428    1 AVILVGGpqKGTRFrPLSLD-VPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIgfypesVFSDFISDAQQEF-NVPIRY 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119113879  78 KLDYYSIptdsecGTADSLRLVSDKIK----SDVVVLSCDSIIEINLYPLLSKFREKDASVQLLLLESGKDQ 145
Cdd:cd06428   79 LQEYKPL------GTAGGLYHFRDQILagnpSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEASREQ 144
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 1-75 2.20e-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: 43.30  E-value: 2.20e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119113879   1 MGQLEFQAIVLAAGKGTRLPeilEGRPKCLLPIGPFPMIWYPLQLLQRHG-FTEVIVVVQESEKSEIQQRLERLQL 75
Cdd:PRK09382   1 TLMSDISLVIVAAGRSTRFS---AEVKKQWLRIGGKPLWLHVLENLSSAPaFKEIVVVIHPDDIAYMKKALPEIKF 73
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 8-58 2.31e-04

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 43.31  E-value: 2.31e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119113879   8 AIVLAAGKGTRLPEILegrPKCLLPIGPFPMIWYPLQLLQRHGFTEVIVVV 58
Cdd:PRK14353   8 AIILAAGEGTRMKSSL---PKVLHPVAGRPMLAHVLAAAASLGPSRVAVVV 55
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 361-422 3.25e-04

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 42.90  E-value: 3.25e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119113879 361 TTISEKTslnqnVIANGCTVQPKTRINNSVLMDGVTV-----EETVVIDNCIVGEKAVIKSGSVLKN 422
Cdd:PRK14354 278 VVIKGNT-----VIGEDCVIGPGSRIVDSTIGDGVTItnsviEESKVGDNVTVGPFAHLRPGSVIGE 339
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 361-435 3.28e-04

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 41.17  E-value: 3.28e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119113879 361 TTISEKTSLNQNVIANGCTVQPKTRI-NNSVLMDGVTVEetvviDNCIVGEKAVIKSGSVLknciigPHFVVAAGT 435
Cdd:COG0663   72 LTIGDDVTIGHGAILHGCTIGDNVLIgMGAIVLDGAVIG-----DGSIVGAGALVTEGKVV------PPGSLVVGS 136
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 358-436 3.63e-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: 40.86  E-value: 3.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879 358 GDMTTIsektslnqnVIANGCTVQpktriNNSVLM----------DGVTVEETVVI------DNCIVGEKAVIKSGSVL- 420
Cdd:cd04645   34 GDVNPI---------RIGERTNIQ-----DGSVLHvdpgyptiigDNVTVGHGAVLhgctigDNCLIGMGAIILDGAVIg 99

                         90
                 ....*....|....*.
gi 119113879 421 KNCIIGPHFVVAAGTK 436
Cdd:cd04645  100 KGSIVAAGSLVPPGKV 115
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 385-435 1.14e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 41.27  E-value: 1.14e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 119113879 385 RINNSVLMDGVTV--EETVVID-------------------NCIVGEKAVIKSGSVLKNCIIGPHFVVAAGT 435
Cdd:PRK14355 245 RINRELMLAGVTLidPETTYIDrgvvigrdttiypgvcisgDTRIGEGCTIEQGVVIKGCRIGDDVTVKAGS 316
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 385-431 1.66e-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: 40.78  E-value: 1.66e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119113879 385 RINNSVLMDGVT--------VEETV------VID-NCI------VGEKAVIKSGSVLKNCIIGPHFVV 431
Cdd:COG1207  243 RIAERLMRAGVTiidpattyIDGDVeigrdvVIDpNVIlegktvIGEGVVIGPNCTLKDSTIGDGVVI 310
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 355-420 1.66e-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: 39.70  E-value: 1.66e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119113879 355 CAVGDMTTISEktslnQNVIANGCTVQPKTRI-NNSVLMDGVTVEETVVI-DNCIVGEKAVIKSGSVL 420
Cdd:cd03352    8 VSIGPNAVIGE-----GVVIGDGVVIGPGVVIgDGVVIGDDCVIHPNVTIyEGCIIGDRVIIHSGAVI 70
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 373-435 1.79e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 40.59  E-value: 1.79e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119113879 373 VIANGCTVQpKTRINNSVLMDGVTVEETVVIDNCIVGEKAVIKSGSVLKNCIIGPHFVVAAGT 435
Cdd:PRK00725 329 LVSGGCIIS-GAVVRRSVLFSRVRVNSFSNVEDSVLLPDVNVGRSCRLRRCVIDRGCVIPEGM 390
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 358-420 1.85e-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: 38.89  E-value: 1.85e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119113879 358 GDMTTISEKTSLNQNVIANGCTVQPKTRIN-NSVLMDGVTVEEtvvidNCIVGEKAVIKSGSVL 420
Cdd:cd04745   59 GQDTVLEENGHIGHGAILHGCTIGRNALVGmNAVVMDGAVIGE-----ESIVGAMAFVKAGTVI 117
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 8-148 1.88e-03

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 40.48  E-value: 1.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879   8 AIVLAAGKGTRLPeilEGRPKCLLPIGPFPMIWYPLQLLqRHGFTEVIVVVQESEKSEIQQRLERLQLKLKLDyysiptD 87
Cdd:PRK14356   8 ALILAAGKGTRMH---SDKPKVLQTLLGEPMLRFVYRAL-RPLFGDNVWTVVGHRADMVRAAFPDEDARFVLQ------E 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119113879  88 SECGTADSLRLVSDKIKSD----VVVLSCDSiieinlyPLLSkfrekDASVQLLLLESgKDQDVV 148
Cdd:PRK14356  78 QQLGTGHALQCAWPSLTAAgldrVLVVNGDT-------PLVT-----TDTIDDFLKEA-AGADLA 129
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 340-427 2.05e-03

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: 36.79  E-value: 2.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879 340 LVSQSSSIKS-TQITKCAVGDMTTISEKTSLNQNVIANGCTVQPKTRINNSVLMDGVtveetvvidncIVGEKAVIKSGS 418
Cdd:cd05787    1 VIGRGTSIGEgTTIKNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGA-----------VIGKGCTIPPGS 69

                         90
                 ....*....|
gi 119113879 419 VLK-NCIIGP 427
Cdd:cd05787   70 LISfGVVIGD 79
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
 8-70 2.54e-03

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes which catalyze the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from cytidine triphosphate and 2-C-methyl-D-erythritol 4-phosphate (MEP).


Pssm-ID: 460075  Cd Length: 219  Bit Score: 39.36  E-value: 2.54e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119113879    8 AIVLAAGKGTRLPEileGRPKCLLPIGPFPMIWYPLQLLQRHGFTE-VIVVVQESEKSEIQQRL 70
Cdd:pfam01128   1 AVIPAAGSGKRMGA---GVPKQFLQLLGQPLLEHTVDAFLASPVVDrIVVAVSPDDTPEFRQLL 61
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 341-448 3.01e-03

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: 39.62  E-value: 3.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879 341 VSQSSSI-KSTQITK-CAVGDMTTISEKTSLNQNV-IANGCTVQPKTRI-NNSVLMDGVTVEEtvvidNCIVGEKAVIKS 416
Cdd:COG1044   99 IHPSAVIdPSAKIGEgVSIGPFAVIGAGVVIGDGVvIGPGVVIGDGVVIgDDCVLHPNVTIYE-----RCVIGDRVIIHS 173

                         90       100       110
                 ....*....|....*....|....*....|..
gi 119113879 417 GSVlknciIGphfvvaagtkkesvylsnADGF 448
Cdd:COG1044  174 GAV-----IG------------------ADGF 182
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 396-434 4.12e-03

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


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 37.95  E-value: 4.12e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 119113879 396 TVEETVVID-NCIVGEKAVIKSGSVLK-NCIIGPHFVVAAG 434
Cdd:cd05636    7 TVEEGVTIKgPVWIGEGAIVRSGAYIEgPVIIGKGCEIGPN 47
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-72 6.18e-03

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 38.82  E-value: 6.18e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119113879   5 EFQAIVLAAGKGTRLPEILegrPKCLLPIGPFPMIWYPLQllQRHGFTEVIVVVQESEKSEIQQRLER 72
Cdd:PRK14359   2 KLSIIILAAGKGTRMKSSL---PKVLHTICGKPMLFYILK--EAFAISDDVHVVLHHQKERIKEAVLE 64
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 363-435 8.82e-03

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


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 35.94  E-value: 8.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879 363 ISEKTSLNQNV-IANGCTVQPKTRI-NNSVLMDGVTVEETVVIDNC----------------------IVGEKAVIKSGS 418
Cdd:cd03358    1 IGDNCIIGTNVfIENDVKIGDNVKIqSNVSIYEGVTIEDDVFIGPNvvftndlyprskiyrkwelkgtTVKRGASIGANA 80

                         90
                 ....*....|....*...
gi 119113879 419 V-LKNCIIGPHFVVAAGT 435
Cdd:cd03358   81 TiLPGVTIGEYALVGAGA 98
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 350-435 9.34e-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: 37.40  E-value: 9.34e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119113879 350 TQITKCAVGDMTTISEKTSLNQNVIANGCTVQPKTRI-NNSVLMDGVTVEETVVIDNCIVGEKAVIKSGSVLKNCIIGPH 428
Cdd:cd03353   46 CVIKDSTIGDGVVIKASSVIEGAVIGNGATVGPFAHLrPGTVLGEGVHIGNFVEIKKSTIGEGSKANHLSYLGDAEIGEG 125


                 ....*..
gi 119113879 429 FVVAAGT 435
Cdd:cd03353  126 VNIGAGT 132
 
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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