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Conserved domains on  [gi|9966779|ref|NP_065098|]
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translation initiation factor eIF2B subunit gamma isoform 1 [Homo sapiens]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-212 2.56e-101

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: 301.11  E-value: 2.56e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779    3 FQAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTRDVQKALCAEFKM-----KMKPDIVC 77
Cdd:cd04198   1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSfplnlKQKLDEVT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779   78 IPDDADMGTADSLRYIYPKLKTDVLVLSCDLITDVALHEVVDLFRAYDASLAMLMRKGQDSIEPVPGqKGKKKAVEQRDF 157
Cdd:cd04198  81 IVLDEDMGTADSLRHIRKKIKKDFLVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVSSEQKGG-KGKSKKADERDV 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 9966779  158 IGVDSTGKRLLFMANEADLDEELVIKGSILQKHPRIRFHTGLVDAHLYCLKKYIV 212
Cdd:cd04198 160 IGLDEKTQRLLFITSEEDLDEDLELRKSLLKRHPRVTITTKLLDAHVYIFKRWVL 214
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 357-437 1.33e-36

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


:

Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 129.23  E-value: 1.33e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779  357 LIGPETQIGEKSSIKRSVIGSSCLIKDRVTITNCLLMNSVTVEEGSNIQGSVICNNAVIEKGADIKDCLIGSGQRIEAKA 436
Cdd:cd04652   1 LVGENTQVGEKTSIKRSVIGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLVGSGYRVEAGT 80


                .
gi 9966779  437 K 437
Cdd:cd04652  81 E 81
 
Name Accession Description Interval E-value
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-212 2.56e-101

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: 301.11  E-value: 2.56e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779    3 FQAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTRDVQKALCAEFKM-----KMKPDIVC 77
Cdd:cd04198   1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSfplnlKQKLDEVT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779   78 IPDDADMGTADSLRYIYPKLKTDVLVLSCDLITDVALHEVVDLFRAYDASLAMLMRKGQDSIEPVPGqKGKKKAVEQRDF 157
Cdd:cd04198  81 IVLDEDMGTADSLRHIRKKIKKDFLVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVSSEQKGG-KGKSKKADERDV 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 9966779  158 IGVDSTGKRLLFMANEADLDEELVIKGSILQKHPRIRFHTGLVDAHLYCLKKYIV 212
Cdd:cd04198 160 IGLDEKTQRLLFITSEEDLDEDLELRKSLLKRHPRVTITTKLLDAHVYIFKRWVL 214
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 357-437 1.33e-36

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


Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 129.23  E-value: 1.33e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779  357 LIGPETQIGEKSSIKRSVIGSSCLIKDRVTITNCLLMNSVTVEEGSNIQGSVICNNAVIEKGADIKDCLIGSGQRIEAKA 436
Cdd:cd04652   1 LVGENTQVGEKTSIKRSVIGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLVGSGYRVEAGT 80


                .
gi 9966779  437 K 437
Cdd:cd04652  81 E 81
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 4-137 4.14e-27

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: 108.70  E-value: 4.14e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779    4 QAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTT--RDVQKALCAEFKmKMKPDIVCIPDD 81
Cdd:COG1208   1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGylAEQIEEYFGDGS-RFGVRITYVDEG 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 9966779   82 ADMGTADSLRYIYPKLKTD-VLVLSCDLITDVALHEVVDLFRAYDASLAMLMRKGQD 137
Cdd:COG1208  80 EPLGTGGALKRALPLLGDEpFLVLNGDILTDLDLAALLAFHREKGADATLALVPVPD 136
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 5-126 1.79e-14

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: 72.67  E-value: 1.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779      5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNK-PLIWYPLNLLERVGFEEVIVVTTRdvQKALCAEFKM----KMKPDIVCIP 79
Cdd:pfam00483   2 AIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQ--EHRFMLNELLgdgsKFGVQITYAL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 9966779     80 DDADMGTADSLRYIYPKL---KTDVLVLSCDLITDVALHEVVDLFRAYDA 126
Cdd:pfam00483  80 QPEGKGTAPAVALAADFLgdeKSDVLVLGGDHIYRMDLEQAVKFHIEKAA 129
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 313-437 1.74e-08

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 56.03  E-value: 1.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779   313 VSTLGLYMEANRQvpkLLSalcpEEPPVHS---SAQIVSKhlvgvdSLIGPETQIGEKSSIKRSVIGSSCLIKDrvTITN 389
Cdd:PRK05293 244 VGTIESLWEANME---LLR----PENPLNLfdrNWRIYSV------NPNLPPQYIAENAKVKNSLVVEGCVVYG--TVEH 308

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 9966779   390 CLLMNSVTVEEGSNIQGSVICNNAVIEKGADIKDCLIGSGQRIEAKAK 437
Cdd:PRK05293 309 SVLFQGVQVGEGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVI 356
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-131 6.10e-07

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 51.40  E-value: 6.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779     5 AVVMAVGGGSRMTdltSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTRD---VQKALcaefkMKMKPDIVCIPDD 81
Cdd:PRK14353   8 AIILAAGEGTRMK---SSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGaeaVAAAA-----AKIAPDAEIFVQK 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 9966779    82 ADMGTADSLRYIYPKLKT---DVLVLSCD--LITDVALHEVVDLfRAYDASLAML 131
Cdd:PRK14353  80 ERLGTAHAVLAAREALAGgygDVLVLYGDtpLITAETLARLRER-LADGADVVVL 133
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 340-446 4.32e-05

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 43.86  E-value: 4.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779  340 VHSSAQIVSKHLVGVDSLIGP---------ETQIGEKSSIK-RSVI----GSSCLIKDRVTIT-NCLLmNSVTVEEGSNI 404
Cdd:COG0663  19 VAPTAVVIGDVTIGEDVSVWPgavlrgdvgPIRIGEGSNIQdGVVLhvdpGYPLTIGDDVTIGhGAIL-HGCTIGDNVLI 97

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 9966779  405 -QGSVICNNAVIEKGadikdCLIG------SGQRIEAkakrvNEVIVGN 446
Cdd:COG0663  98 gMGAIVLDGAVIGDG-----SIVGagalvtEGKVVPP-----GSLVVGS 136
 
Name Accession Description Interval E-value
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-212 2.56e-101

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: 301.11  E-value: 2.56e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779    3 FQAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTRDVQKALCAEFKM-----KMKPDIVC 77
Cdd:cd04198   1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSfplnlKQKLDEVT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779   78 IPDDADMGTADSLRYIYPKLKTDVLVLSCDLITDVALHEVVDLFRAYDASLAMLMRKGQDSIEPVPGqKGKKKAVEQRDF 157
Cdd:cd04198  81 IVLDEDMGTADSLRHIRKKIKKDFLVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVSSEQKGG-KGKSKKADERDV 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 9966779  158 IGVDSTGKRLLFMANEADLDEELVIKGSILQKHPRIRFHTGLVDAHLYCLKKYIV 212
Cdd:cd04198 160 IGLDEKTQRLLFITSEEDLDEDLELRKSLLKRHPRVTITTKLLDAHVYIFKRWVL 214
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 3-212 7.25e-73

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: 228.29  E-value: 7.25e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779    3 FQAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTRDVQKALCAEFKMK-------MKPDI 75
Cdd:cd02507   1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSKwsslsskMIVDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779   76 VCIPDDADMGTADSLRYIYPKLKTDVLVLSCDLITDVALHEVV----DLFRAYDASLAMLMRKGQDSIEPvpgqkgkKKA 151
Cdd:cd02507  81 ITSDLCESAGDALRLRDIRGLIRSDFLLLSCDLVSNIPLSELLeerrKKDKNAIATLTVLLASPPVSTEQ-------SKK 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9966779  152 VEQRDFIGVDSTGKRLLFMANEADLDE--ELVIKGSILQKHPRIRFHTGLVDAHLYCLKKYIV 212
Cdd:cd02507 154 TEEEDVIAVDSKTQRLLLLHYEEDLDEdlELIIRKSLLSKHPNVTIRTDLLDCHIYICSPDVL 216
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 357-437 1.33e-36

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


Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 129.23  E-value: 1.33e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779  357 LIGPETQIGEKSSIKRSVIGSSCLIKDRVTITNCLLMNSVTVEEGSNIQGSVICNNAVIEKGADIKDCLIGSGQRIEAKA 436
Cdd:cd04652   1 LVGENTQVGEKTSIKRSVIGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLVGSGYRVEAGT 80


                .
gi 9966779  437 K 437
Cdd:cd04652  81 E 81
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 4-137 4.14e-27

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: 108.70  E-value: 4.14e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779    4 QAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTT--RDVQKALCAEFKmKMKPDIVCIPDD 81
Cdd:COG1208   1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGylAEQIEEYFGDGS-RFGVRITYVDEG 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 9966779   82 ADMGTADSLRYIYPKLKTD-VLVLSCDLITDVALHEVVDLFRAYDASLAMLMRKGQD 137
Cdd:COG1208  80 EPLGTGGALKRALPLLGDEpFLVLNGDILTDLDLAALLAFHREKGADATLALVPVPD 136
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 5-235 8.28e-27

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: 107.28  E-value: 8.28e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779    5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTT---RDVQKALcaEFKMKMKPDIVCIPDD 81
Cdd:cd04181   1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGylgEQIEEYF--GDGSKFGVNIEYVVQE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779   82 ADMGTADSLRYIYPKLKTD-VLVLSCDLITDVALHEVVDLFRAYDASLAMLMRKGQDsiepvpgqkgkkkaveQRDFiGV 160
Cdd:cd04181  79 EPLGTAGAVRNAEDFLGDDdFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEVED----------------PSRY-GV 141

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9966779  161 dstgkrllfmaneADLDEELVIKGsILQKhPRIrFHTGLVDAHLYCLKKYIVDFLMENG-SITSIRSELIPYLVRK 235
Cdd:cd04181 142 -------------VELDDDGRVTR-FVEK-PTL-PESNLANAGIYIFEPEILDYIPEILpRGEDELTDAIPLLIEE 201
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 357-434 1.10e-26

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: 102.32  E-value: 1.10e-26
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9966779  357 LIGPETQIGEKSSIKRSVIGSSCLIKDRVTITNCLLMNSVTVEEGSNIQGSVICNNAVIEKGADIKD-CLIGSGQRIEA 434
Cdd:cd03356   1 LIGESTVIGENAIIKNSVIGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVNlCIIGDDVVVED 79
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 357-432 7.92e-17

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: 74.92  E-value: 7.92e-17
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 9966779  357 LIGPETQIGEKSSIKRSVIGSSCLIKDRVTITNCLLMNSVTVEEGSNIQGSVICNNAVIEKGADIKD-CLIGSGQRI 432
Cdd:cd05787   1 VIGRGTSIGEGTTIKNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIPPgSLISFGVVI 77
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
4-132 4.85e-16

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 77.20  E-value: 4.85e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779    4 QAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT--TRDVQKALCAEFKMKMKpdIVCIPDD 81
Cdd:COG1213   1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTgyKAELIEEALARPGPDVT--FVYNPDY 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 9966779   82 ADMGTADSLRYIYPKLKTDVLVLSCDLITDvalHEVVDLFRAYDASLAMLM 132
Cdd:COG1213  79 DETNNIYSLWLAREALDEDFLLLNGDVVFD---PAILKRLLASDGDIVLLV 126
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 5-126 5.08e-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: 74.19  E-value: 5.08e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779    5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT--TRDVQKALCAEFkmkMKPDIVCIPDDA 82
Cdd:cd02523   1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTgyKKEQIEELLKKY---PNIKFVYNPDYA 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 9966779   83 DMGTADSLRYIYPKLKTDVLVLSCDLITDVA-LHEVVDlFRAYDA 126
Cdd:cd02523  78 ETNNIYSLYLARDFLDEDFLLLEGDVVFDPSiLERLLS-SPADNA 121
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 5-134 1.09e-14

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: 72.93  E-value: 1.09e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779    5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTT--RDVQKALCAEFKmKMKPDIVCIPDDA 82
Cdd:cd06426   1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNylAEMIEDYFGDGS-KFGVNISYVREDK 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 9966779   83 DMGTADSLRYIYPKLKTDVLVLSCDLITDVALHEVVDLFRAYDASLAMLMRK 134
Cdd:cd06426  80 PLGTAGALSLLPEKPTDPFLVMNGDILTNLNYEHLLDFHKENNADATVCVRE 131
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 5-126 1.79e-14

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: 72.67  E-value: 1.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779      5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNK-PLIWYPLNLLERVGFEEVIVVTTRdvQKALCAEFKM----KMKPDIVCIP 79
Cdd:pfam00483   2 AIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQ--EHRFMLNELLgdgsKFGVQITYAL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 9966779     80 DDADMGTADSLRYIYPKL---KTDVLVLSCDLITDVALHEVVDLFRAYDA 126
Cdd:pfam00483  80 QPEGKGTAPAVALAADFLgdeKSDVLVLGGDHIYRMDLEQAVKFHIEKAA 129
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-205 7.59e-14

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: 70.33  E-value: 7.59e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779    3 FQAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTRDVQKAlcAEF-------KMKMKPDI 75
Cdd:cd04197   1 LQAVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQI--KEYiekskwsKPKSSLMI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779   76 V-CIPDDADMGTADSLRYIYPK--LKTDVLVLSCDLITDVALHEVVDLFRAY-----DASLAMLMRKGqdsIEPVPGQKG 147
Cdd:cd04197  79 ViIIMSEDCRSLGDALRDLDAKglIRGDFILVSGDVVSNIDLKEILEEHKERrkkdkNAIMTMVLKEA---SPPHRTRRT 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779  148 KKKAVeqrdfIGVDSTGKRLLFMANEADLDEE--LVIKGSILQKHPRIRFHTGLVDAHLY 205
Cdd:cd04197 156 GEEFV-----IAVDPKTSRLLHYEELPGSKYRsiTDLPSELLGSNSEVEIRHDLLDCHID 210
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 5-142 1.07e-13

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: 68.38  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779      5 AVVMAVGGGSRMTDltssiPKPLLPVGNKPLIWYPLNLLERVgFEEVIVVTTRDVQKALCAEFKMKMKPDivcipDDADM 84
Cdd:pfam12804   1 AVILAGGRSSRMGG-----DKALLPLGGKPLLERVLERLRPA-GDEVVVVANDEEVLAALAGLGVPVVPD-----PDPGQ 69

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9966779     85 GTADSLR--YIYPKLKTDVLVLSCD--LITDVALHEVVDLFRAYDASLAMLMRKGQDsIEPV 142
Cdd:pfam12804  70 GPLAGLLaaLRAAPGADAVLVLACDmpFLTPELLRRLLAAAEESGADIVVPVYDGGR-GHPL 130
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 5-137 1.47e-13

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: 69.50  E-value: 1.47e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779    5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIvvttrdvqkaLCAEFKMKM-----------KP 73
Cdd:cd06915   1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIV----------LSVGYLAEQieeyfgdgyrgGI 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 9966779   74 DIVCIPDDADMGTADSLRYIYPKLKTD-VLVLSCDLITDVALHEVVDLFRAYDASLAMLMRKGQD 137
Cdd:cd06915  71 RIYYVIEPEPLGTGGAIKNALPKLPEDqFLVLNGDTYFDVDLLALLAALRASGADATMALRRVPD 135
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 4-148 4.21e-12

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


Pssm-ID: 133044 [Multi-domain]  Cd Length: 221  Bit Score: 65.28  E-value: 4.21e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779    4 QAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTT--RD-VQKALCAEFKmkmKPDIVcIPD 80
Cdd:cd06422   1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHhlADqIEAHLGDSRF---GLRIT-ISD 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 9966779   81 DAD--MGTADSLRYIYPKLKTD-VLVLSCDLITDVALHEVVDLFRAYDASLAMLMRKgqdsiEPVPGQKGK 148
Cdd:cd06422  77 EPDelLETGGGIKKALPLLGDEpFLVVNGDILWDGDLAPLLLLHAWRMDALLLLLPL-----VRNPGHNGV 142
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 5-156 1.19e-11

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: 64.07  E-value: 1.19e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779    5 AVVMAVGGGSRMTdltSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTRD---VQKALCaefkmkmKPDIVCIPDD 81
Cdd:cd02540   1 AVILAAGKGTRMK---SDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGaeqVKKALA-------NPNVEFVLQE 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779   82 ADMGTADSLRYIYPKLKT---DVLVLSCD--LITDVALHEVVDLFRAYDASLAML-------------MRKGQDSIEpvp 143
Cdd:cd02540  71 EQLGTGHAVKQALPALKDfegDVLVLYGDvpLITPETLQRLLEAHREAGADVTVLtaeledptgygriIRDGNGKVL--- 147

                       170
                ....*....|...
gi 9966779  144 gqkgkkKAVEQRD 156
Cdd:cd02540 148 ------RIVEEKD 154
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 5-126 1.96e-11

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: 63.77  E-value: 1.96e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779    5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIV-VTTR-DVQKALCAEFKMKMKPDIVCIPDDA 82
Cdd:cd06425   3 ALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILaVNYRpEDMVPFLKEYEKKLGIKITFSIETE 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 9966779   83 DMGTADSLRYIYPKLKTDV---LVLSCDLITDVALHEVVDLFRAYDA 126
Cdd:cd06425  83 PLGTAGPLALARDLLGDDDepfFVLNSDVICDFPLAELLDFHKKHGA 129
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 5-128 3.48e-11

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


Pssm-ID: 133032 [Multi-domain]  Cd Length: 236  Bit Score: 62.97  E-value: 3.48e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779    5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVV---TTRDVQKALCAEFKMKMKpdIVCIPDD 81
Cdd:cd04189   3 GLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVvgpTGEEIKEALGDGSRFGVR--ITYILQE 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 9966779   82 ADMGTADSLRYIYPKLKTD--VLVLSCDLITDvALHEVVDLFRA--YDASL 128
Cdd:cd04189  81 EPLGLAHAVLAARDFLGDEpfVVYLGDNLIQE-GISPLVRDFLEedADASI 130
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
1-136 7.09e-11

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 61.33  E-value: 7.09e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779    1 MEFQAVVMAVGGGSRMtdltsSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT---TRDVQKALCAefkmkmkPDIVC 77
Cdd:COG2068   2 SKVAAIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLgadAEEVAAALAG-------LGVRV 69

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9966779   78 IP-DDADMGTADSLR----YIYPKLkTDVLVLSCD--LITDVALHEVVDLFRAYDASLAMLMRKGQ 136
Cdd:COG2068  70 VVnPDWEEGMSSSLRaglaALPADA-DAVLVLLGDqpLVTAETLRRLLAAFRESPASIVAPTYDGR 134
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
5-63 1.84e-10

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 61.64  E-value: 1.84e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9966779    5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTRD----VQKAL 63
Cdd:COG1209   3 GIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEdgpqFERLL 65
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 1-131 7.20e-10

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


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 60.81  E-value: 7.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779    1 MEFQAVVMAVGGGSRMTdltSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT--TRD-VQKALCAEfkmkmkpDIVC 77
Cdd:COG1207   1 SPLAVVILAAGKGTRMK---SKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVghGAEqVRAALADL-------DVEF 70

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 9966779   78 IPDDADMGTADSLRYIYPKLKTD---VLVLSCD--LITDVALHEVVDLFRAYDASLAML 131
Cdd:COG1207  71 VLQEEQLGTGHAVQQALPALPGDdgtVLVLYGDvpLIRAETLKALLAAHRAAGAAATVL 129
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 5-57 1.54e-09

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: 57.97  E-value: 1.54e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 9966779    5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTR 57
Cdd:cd02538   3 GIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTP 55
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 364-451 1.86e-09

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: 54.78  E-value: 1.86e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779  364 IGEKSSIKRSVIGSSCLIKDrVTITNCLLMNSVTVEEGSNIQGSVICNNAVIEKGADIKDCLIGSGQRIEAkakrvNEVI 443
Cdd:cd04651   4 IGRRGEVKNSLVSEGCIISG-GTVENSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIIDKNVVIPD-----GVVI 77


                ....*...
gi 9966779  444 VGNDQLME 451
Cdd:cd04651  78 GGDPEEDR 85
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 8-127 7.10e-09

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


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 55.28  E-value: 7.10e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779    8 MAVGGGSRMTDltssIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTRDVQKAlcAEFKMKMKPDIVCIPDDadmGTA 87
Cdd:COG2266   1 MAGGKGTRLGG----GEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSPNTPKT--REYLKERGVEVIETPGE---GYV 71

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 9966779   88 DSLRYIYPKLKTDVLVLSCDL--ITDVALHEVVDLFRAYDAS 127
Cdd:COG2266  72 EDLNEALESISGPVLVVPADLplLTPEIIDDIIDAYLESGKP 113
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 5-129 1.08e-08

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: 54.87  E-value: 1.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779    5 AVVMAVGGGSRMTDltssiPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT--TRDVQKALCAEFkmkmkPDIVCIPDDA 82
Cdd:cd04182   3 AIILAAGRSSRMGG-----NKLLLPLDGKPLLRHALDAALAAGLSRVIVVLgaEADAVRAALAGL-----PVVVVINPDW 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 9966779   83 DMGTADSLRYIYPKLKTD---VLVLSCD--LITDVALHEVVDLFRAYDASLA 129
Cdd:cd04182  73 EEGMSSSLAAGLEALPADadaVLILLADqpLVTAETLRALIDAFREDGAGIV 124
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 313-437 1.74e-08

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 56.03  E-value: 1.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779   313 VSTLGLYMEANRQvpkLLSalcpEEPPVHS---SAQIVSKhlvgvdSLIGPETQIGEKSSIKRSVIGSSCLIKDrvTITN 389
Cdd:PRK05293 244 VGTIESLWEANME---LLR----PENPLNLfdrNWRIYSV------NPNLPPQYIAENAKVKNSLVVEGCVVYG--TVEH 308

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 9966779   390 CLLMNSVTVEEGSNIQGSVICNNAVIEKGADIKDCLIGSGQRIEAKAK 437
Cdd:PRK05293 309 SVLFQGVQVGEGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVI 356
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 354-449 2.18e-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: 51.70  E-value: 2.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779  354 VDSLIGPETQIgEKSSIKRSVIGSSCLIKDRVTITNCLLMNSVTVEEGSNIQGSVICNNAVIEKGadikdCLIGSGQRIE 433
Cdd:cd04651  11 KNSLVSEGCII-SGGTVENSVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIIDKNVVIPDG-----VVIGGDPEED 84

                        90
                ....*....|....*....
gi 9966779  434 AKAKRVNE---VIVGNDQL 449
Cdd:cd04651  85 RARFYVTEdgiVVVGKGMV 103
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-144 4.50e-08

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


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 52.89  E-value: 4.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779    1 MEFQAVVMAVGGGSRM-TDltssipKPLLPVGNKPLIWYPLNLLERVgFEEVIVVTTRDVQKAlcaefkmkmKPDIVCIP 79
Cdd:COG0746   3 MPITGVILAGGRSRRMgQD------KALLPLGGRPLLERVLERLRPQ-VDEVVIVANRPERYA---------ALGVPVVP 66

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9966779   80 DD-ADMG------TAdsLRYIypklKTD-VLVLSCD--LITDvalhEVVD-LFRAYDASLAMLMRKGQDSIEPVPG 144
Cdd:COG0746  67 DDpPGAGplagilAA--LEAA----PAEwVLVLACDmpFLPP----DLVRrLLEALEEGADAVVPRSGGRLEPLFA 132
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 5-53 6.00e-08

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: 53.73  E-value: 6.00e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 9966779    5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIV 53
Cdd:cd02524   1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFIL 49
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 5-131 1.10e-07

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: 52.64  E-value: 1.10e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779    5 AVVMaVGG---GSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERV-GFEEVIVVT--TRDVQKALCAEFKMKMKPDIVCI 78
Cdd:cd06428   1 AVIL-VGGpqkGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVpDLKEVLLIGfyPESVFSDFISDAQQEFNVPIRYL 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 9966779   79 PDDADMGTADSLRY----IYPKLKTDVLVLSCDLITDVALHEVVDLFRAYDASLAML 131
Cdd:cd06428  80 QEYKPLGTAGGLYHfrdqILAGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTIL 136
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 5-79 1.12e-07

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: 52.14  E-value: 1.12e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9966779    5 AVVMAVGGGSRMTdltSSIPKPLLPVGNKPLIWYPLNLLERVG-FEEVIVVTTRDVQKALCAEFKMKMKPDIVCIP 79
Cdd:cd02516   3 AIILAAGSGSRMG---ADIPKQFLELGGKPVLEHTLEAFLAHPaIDEIVVVVPPDDIDLAKELAKYGLSKVVKIVE 75
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 340-446 1.91e-07

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: 50.49  E-value: 1.91e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779  340 VHSSAQIVSKHLVGVDSLIGP---------ETQIGEKSSIK-RSVI----GSSCLIKDRVTIT-NCLLmNSVTVEEGSNI 404
Cdd:cd04645   8 IAPNATVIGDVTLGEGSSVWFgavlrgdvnPIRIGERTNIQdGSVLhvdpGYPTIIGDNVTVGhGAVL-HGCTIGDNCLI 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 9966779  405 -QGSVICNNAVIEKGadikdCLIGSG------QRIEAkakrvNEVIVGN 446
Cdd:cd04645  87 gMGAIILDGAVIGKG-----SIVAAGslvppgKVIPP-----GSLVAGS 125
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 4-96 2.34e-07

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


Pssm-ID: 133021 [Multi-domain]  Cd Length: 267  Bit Score: 51.76  E-value: 2.34e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779    4 QAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTR---------DVQKALCAEFKMKMKPD 74
Cdd:cd02541   2 KAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRgkraiedhfDRSYELEETLEKKGKTD 81

                        90       100
                ....*....|....*....|....*.
gi 9966779   75 ----IVCIPDDADMgtadslRYIYPK 96
Cdd:cd02541  82 lleeVRIISDLANI------HYVRQK 101
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-131 6.10e-07

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 51.40  E-value: 6.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779     5 AVVMAVGGGSRMTdltSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTRD---VQKALcaefkMKMKPDIVCIPDD 81
Cdd:PRK14353   8 AIILAAGEGTRMK---SSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGaeaVAAAA-----AKIAPDAEIFVQK 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 9966779    82 ADMGTADSLRYIYPKLKT---DVLVLSCD--LITDVALHEVVDLfRAYDASLAML 131
Cdd:PRK14353  80 ERLGTAHAVLAAREALAGgygDVLVLYGDtpLITAETLARLRER-LADGADVVVL 133
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 4-56 9.50e-07

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 50.44  E-value: 9.50e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 9966779     4 QAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTT 56
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIIST 57
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 5-108 1.32e-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: 48.34  E-value: 1.32e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779    5 AVVMAVGGGSRMTDltssiPKPLLPVGNKPLIWYPLNLLERVgFEEVIVVTTRDVQKALcaefkmkmKPDIVCIPDDA-D 83
Cdd:cd02503   3 GVILAGGKSRRMGG-----DKALLELGGKPLLEHVLERLKPL-VDEVVISANRDQERYA--------LLGVPVIPDEPpG 68

                        90       100       110
                ....*....|....*....|....*....|..
gi 9966779   84 MG------TAdsLRYiypkLKTD-VLVLSCDL 108
Cdd:cd02503  69 KGplagilAA--LRA----APADwVLVLACDM 94
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 6-77 1.37e-06

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: 48.97  E-value: 1.37e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 9966779    6 VVMAVGGGSRMTdltSSIPKPLLPVGNKPLIWYPLNLLERVG-FEEVIVVTTRDVQ---KALCAEFKMKMKPDIVC 77
Cdd:COG1211   1 IIPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIeyfEELLAKYGIDKPVRVVA 73
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 6-156 6.72e-06

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 48.44  E-value: 6.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779     6 VVMAVGGGSRMTdltSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTRDVQKALCAefkmKMKPDIVCIPDDADMG 85
Cdd:PRK14358  11 VILAAGQGTRMK---SALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAA----LQGSGVAFARQEQQLG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779    86 TADSLRYIYPKLKT---DVLVLSCD--LITDVALHEVVDLFRAYDASLAMLMRKGQDSI---EPVPGQKGK-KKAVEQRD 156
Cdd:PRK14358  84 TGDAFLSGASALTEgdaDILVLYGDtpLLRPDTLRALVADHRAQGSAMTILTGELPDATgygRIVRGADGAvERIVEQKD 163
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 337-420 1.42e-05

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 47.06  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779   337 EPPVHSSAQIVSKHLVGVDSLIGPETQIGEKSSI-KRSVIGSSCLIKDRVTI-TNCLLMNSVTVEEGSNI-QGSVICNNA 413
Cdd:PRK00892 100 AAGIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIgDGVVIGAGAVIGDGVKIgADCRLHANVTIYHAVRIgNRVIIHSGA 179


                 ....*..
gi 9966779   414 VIekGAD 420
Cdd:PRK00892 180 VI--GSD 184
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
4-55 1.65e-05

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 46.44  E-value: 1.65e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 9966779     4 QAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT 55
Cdd:PRK13389  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVT 61
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 365-448 1.96e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 46.74  E-value: 1.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779   365 GEKSSIKRSVIGSSCLIkDRVTITNCLLMNSVTVEEGSNIQGSVICNNAVIEKGADI------KDCLIGSGQRI----EA 434
Cdd:PRK00844 308 GRVGSAQDSLVSAGSII-SGATVRNSVLSPNVVVESGAEVEDSVLMDGVRIGRGAVVrraildKNVVVPPGATIgvdlEE 386

                         90
                 ....*....|....*....
gi 9966779   435 KAKR--VNE---VIVGNDQ 448
Cdd:PRK00844 387 DRRRftVSEggiVVVPKGQ 405
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
5-68 2.85e-05

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 45.12  E-value: 2.85e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 9966779     5 AVVMAVGGGSRMTdltSSIPKPLLPVGNKPLIWYPLNLLERVG-FEEVIVVT----TRDVQKALCAEFK 68
Cdd:PRK00155   6 AIIPAAGKGSRMG---ADRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVppddRPDFAELLLAKDP 71
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 352-421 3.04e-05

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 44.72  E-value: 3.04e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779  352 VGVDSLIGPETQIGEKSsikrsVIGSSCLIKDRVTITNCllmnsvTVEEGSNIQGSVICNNAVIEKGADI 421
Cdd:cd03353  18 IGVDVVIDPGVILEGKT-----VIGEDCVIGPNCVIKDS------TIGDGVVIKASSVIEGAVIGNGATV 76
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 340-446 4.32e-05

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 43.86  E-value: 4.32e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779  340 VHSSAQIVSKHLVGVDSLIGP---------ETQIGEKSSIK-RSVI----GSSCLIKDRVTIT-NCLLmNSVTVEEGSNI 404
Cdd:COG0663  19 VAPTAVVIGDVTIGEDVSVWPgavlrgdvgPIRIGEGSNIQdGVVLhvdpGYPLTIGDDVTIGhGAIL-HGCTIGDNVLI 97

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 9966779  405 -QGSVICNNAVIEKGadikdCLIG------SGQRIEAkakrvNEVIVGN 446
Cdd:COG0663  98 gMGAIVLDGAVIGDG-----SIVGagalvtEGKVVPP-----GSLVVGS 136
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 352-415 7.14e-05

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 45.12  E-value: 7.14e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 9966779   352 VGVDSLIGPETQIGEKSsikrsVIGSSCLIKDRVTITNCLLMNSVTVEEGSNIQGSVICNNAVI 415
Cdd:PRK14355 271 IGRDTTIYPGVCISGDT-----RIGEGCTIEQGVVIKGCRIGDDVTVKAGSVLEDSVVGDDVAI 329
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 355-433 7.52e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 44.88  E-value: 7.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779   355 DSLIGpETQIGEKSSIKRSVIGSSCLIKDRVTITNCLLM-----------NSVTVEEGSNI---QGSVIcNNAVIEKGAD 420
Cdd:PRK02862 308 ESIIA-EGCIIKNCSIHHSVLGIRSRIESGCTIEDTLVMgadfyesseerEELRKEGKPPLgigEGTTI-KRAIIDKNAR 385

                         90
                 ....*....|....
gi 9966779   421 I-KDCLIGSGQRIE 433
Cdd:PRK02862 386 IgNNVRIVNKDNVE 399
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 313-421 8.05e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 44.82  E-value: 8.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779   313 VSTLGLYMEANRQvpkLLSALCP-----EEPPVHSS------AQIV---SKHLVGVDSLIGPETQIgEKSSIKRSVIGSS 378
Cdd:PRK00844 262 VGTIDAYYDAHMD---LLSVHPVfnlynREWPIYTSspnlppAKFVdggGRVGSAQDSLVSAGSII-SGATVRNSVLSPN 337

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 9966779   379 CLIKDRVTITNCLLMNSVTVEEGSNIQGSVICNNAVIEKGADI 421
Cdd:PRK00844 338 VVVESGAEVEDSVLMDGVRIGRGAVVRRAILDKNVVVPPGATI 380
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 355-422 1.15e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 44.09  E-value: 1.15e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9966779   355 DSLIGPETQIGEKSSIKRSVIGSSCLIKDRVTITNCLLMNSVTVEEGSNIQG-----SVICNNAVIEKGADIK 422
Cdd:PRK05293 308 HSVLFQGVQVGEGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVIIGGgkeviTVIGENEVIGVGTVIG 380
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 1-58 2.12e-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: 2.12e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 9966779     1 MEFQAVVMAVGGGSRmtdLTSSIPKPLLPVGNKPLIWYPL-NLLERVGFEEVIVVTTRD 58
Cdd:PRK09382   4 SDISLVIVAAGRSTR---FSAEVKKQWLRIGGKPLWLHVLeNLSSAPAFKEIVVVIHPD 59
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
3-55 2.77e-04

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 42.57  E-value: 2.77e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 9966779     3 FQAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT 55
Cdd:PRK10122   4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVT 56
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 373-432 4.40e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 42.52  E-value: 4.40e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779   373 SVIGSSCLIKDrVTITNCLLMNSVTVEEGSNIQGSVICNNAVIEKGADIKDCLIGSGQRI 432
Cdd:PRK00725 328 SLVSGGCIISG-AVVRRSVLFSRVRVNSFSNVEDSVLLPDVNVGRSCRLRRCVIDRGCVI 386
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 354-400 4.74e-04

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


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 38.76  E-value: 4.74e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 9966779  354 VDSLIGPETQIGEKSSIKRSVIGSSCLIKDRVTITN-CLLMNSVTVEE 400
Cdd:cd03356  32 TNSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVNlCIIGDDVVVED 79
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-131 8.73e-04

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 41.65  E-value: 8.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779     5 AVVMAVGGGSRMTdltSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTRDvQKALCAEFkmKMKPDIVCIPDDADM 84
Cdd:PRK14355   6 AIILAAGKGTRMK---SDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQ-AEKVREHF--AGDGDVSFALQEEQL 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 9966779    85 GTADSLRYIYPKLKT---DVLVLSCD--LITDVALHEVVDLFRAYDASLAML 131
Cdd:PRK14355  80 GTGHAVACAAPALDGfsgTVLILCGDvpLLRAETLQGMLAAHRATGAAVTVL 131
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-216 9.97e-04

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 41.25  E-value: 9.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779     5 AVVMAVGGGSRMtdlTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT---TRDVQKALCAEfkmkmkpDIVCIPDD 81
Cdd:PRK14356   8 ALILAAGKGTRM---HSDKPKVLQTLLGEPMLRFVYRALRPLFGDNVWTVVghrADMVRAAFPDE-------DARFVLQE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779    82 ADMGTADSLRYIYPKLK----TDVLVLSCD--LITDVALHEVVDlfRAYDASLAMLmrkgqdSIE-PVPGQKGKkkaveq 154
Cdd:PRK14356  78 QQLGTGHALQCAWPSLTaaglDRVLVVNGDtpLVTTDTIDDFLK--EAAGADLAFM------TLTlPDPGAYGR------ 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 9966779   155 rdfigVDSTGKRLLFMANEADLDEELvikgsilqKHPRirfhTGLVDAHLYCLKKYIVDFLM 216
Cdd:PRK14356 144 -----VVRRNGHVAAIVEAKDYDEAL--------HGPE----TGEVNAGIYYLRLDAVESLL 188
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 8-122 1.03e-03

GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133026 [Multi-domain]  Cd Length: 231  Bit Score: 40.70  E-value: 1.03e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779    8 MAvGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVttrdVQKALCAEFKMK-----MKPD--IVCIPD 80
Cdd:cd04183   5 MA-GLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFI----CRDEHNTKFHLDeslklLAPNatVVELDG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 9966779   81 DADmGTADSLRYIYPKLKTD--VLVLSCDLITDVALHEVVDLFR 122
Cdd:cd04183  80 ETL-GAACTVLLAADLIDNDdpLLIFNCDQIVESDLLAFLAAFR 122
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-110 1.40e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 40.97  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779     1 MEFQAVVMAVGGGSRMtdlTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT---TRDVQKALC--AEFKMKMKpdi 75
Cdd:PRK14354   1 MNRYAIILAAGKGTRM---KSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVghgAEEVKEVLGdrSEFALQEE--- 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 9966779    76 vcipddaDMGTADSLRYIYPKLKT---DVLVLSCD--LIT 110
Cdd:PRK14354  75 -------QLGTGHAVMQAEEFLADkegTTLVICGDtpLIT 107
LbH_Dynactin_6 cd04646
Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that ...
 345-452 1.47e-03

Dynactin 6 (or subunit p27): Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p27 is part of the pointed-end subcomplex in dynactin that also includes p25, p26, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain the imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100052 [Multi-domain]  Cd Length: 164  Bit Score: 39.23  E-value: 1.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779  345 QIVSKHLVGVDSLIGPETQIGEKSSIKRS----------VIGSSCLIKDRVTITNCLLMNSVTV-----------EEGSN 403
Cdd:cd04646   1 KIAPGAVVCQESEIRGDVTIGPGTVVHPRatiiaeagpiIIGENNIIEEQVTIVNKKPKDPAEPkpmiigsnnvfEVGCK 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 9966779  404 IQGSVICNNAVIEKGADI-KDCLIGSGQRIEAKAK-----RVNE--VIVGNDQLMEI 452
Cdd:cd04646  81 CEALKIGNNNVFESKSFVgKNVIITDGCIIGAGCKlpsseILPEntVIYGADCLRRT 137
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 5-69 1.61e-03

Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) 3-deoxy-manno-octulosonate cytidylyltransferase,, EC:2.7.7.38 catalysing the reaction:- CTP + 3-deoxy-D-manno-octulosonate <=> diphosphate + CMP-3-deoxy-D-manno-octulosonate, 2) acylneuraminate cytidylyltransferase EC:2.7.7.43,, catalysing the reaction:- CTP + N-acylneuraminate <=> diphosphate + CMP-N-acylneuraminate. NeuAc cytydilyltransferase of Mannheimia haemolytica has been characterized describing kinetics and regulation by substrate charge, energetic charge and amino-sugar demand.


Pssm-ID: 396773  Cd Length: 217  Bit Score: 39.63  E-value: 1.61e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779      5 AVVMAVGGGSRMTDltssipKPLLPVGNKPLIWYPL-NLLERVGFEEVIVVT----TRDVQKALCAEFKM 69
Cdd:pfam02348   2 AIIPARLGSKRLPG------KNLLDLGGKPLIHHVLeAALKSGAFEKVIVATdseeIADVAKEFGAGVVM 65
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
5-57 3.08e-03

UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 39.25  E-value: 3.08e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 9966779    5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNllERV--GFEEVIVVTTR 57
Cdd:COG1210   6 AVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVE--EAVaaGIEEIIFVTGR 58
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-218 3.27e-03

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 39.59  E-value: 3.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779     1 MEFQAVVMAVGGGSRMTdltSSIPKPLLPVGNKPLIWYPLNLLERVGfEEVIVVTTRD---VQKALCAEFkmkmkPDIVC 77
Cdd:PRK14359   1 MKLSIIILAAGKGTRMK---SSLPKVLHTICGKPMLFYILKEAFAIS-DDVHVVLHHQkerIKEAVLEYF-----PGVIF 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779    78 IPDDADM--GTADSLRYIYPKLKtDVLVLSCD--LITDVALHEVVDLfrayDASLAMLMRKGQDsiepvPGQKGK----- 148
Cdd:PRK14359  72 HTQDLENypGTGGALMGIEPKHE-RVLILNGDmpLVEKDELEKLLEN----DADIVMSVFHLAD-----PKGYGRvvien 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 9966779   149 ---KKAVEQRDfigvdstgkrllfmANEadldEELVIKgsilqkhprirfhtgLVDAHLYCLKKyivDFLMEN 218
Cdd:PRK14359 142 gqvKKIVEQKD--------------ANE----EELKIK---------------SVNAGVYLFDR---KLLEEY 178
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 352-432 6.73e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 38.66  E-value: 6.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 9966779   352 VGVDSLIGPETQIGEKSSIK-RSVIGSSCLIKDRVTITNCllmnsvTVEEGSNIQGSVIcNNAVIEKGADI-------KD 423
Cdd:PRK14354 262 IDADVEIGSDTVIEPGVVIKgNTVIGEDCVIGPGSRIVDS------TIGDGVTITNSVI-EESKVGDNVTVgpfahlrPG 334


                 ....*....
gi 9966779   424 CLIGSGQRI 432
Cdd:PRK14354 335 SVIGEEVKI 343
 
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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