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Conserved domains on  [gi|45447090|ref|NP_995319|]
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mannose-1-phosphate guanyltransferase alpha [Homo sapiens]

Protein Classification

mannose-1-phosphate guanylyltransferase( domain architecture ID 10157668)

mannose-1-phosphate guanylyltransferase catalyzes the formation of GDP-D-mannose from GTP and alpha-D-mannose-1-phosphate; similar to Homo sapiens mannose-1-phosphate guanyltransferase alpha

EC:  2.7.7.13
Gene Ontology:  GO:0016740|GO:0009058

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 4-261 1.86e-172

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: 482.52  E-value: 1.86e-172
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   4 AVILIGGPQKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVPGMQEILLIGFYqPDEPLTQFLEAAQQEFNLPVRYL 83
Cdd:cd06428   1 AVILVGGPQKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVPDLKEVLLIGFY-PESVFSDFISDAQQEFNVPIRYL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  84 QEFAPLGTGGGLYHFRDQILAGSPEAFFVLNADVCSDFPLSAMLEAHRRQRHPFLLLGTTANRTQSLNYGCIVENPQTHE 163
Cdd:cd06428  80 QEYKPLGTAGGLYHFRDQILAGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEASREQASNYGCIVEDPSTGE 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 164 VLHYVEKPSTFISDIINCGIYLFSPEALKPLRDVFQRNQQDGQLEDSPGLWPGAGTIRLEQDVFSALAGQGQIYVHLTDG 243
Cdd:cd06428 160 VLHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNREGRAEVIRLEQDVLTPLAGSGKLYVYKTDD 239

                       250
                ....*....|....*...
gi 45447090 244 IWSQIKSAGSALYASRLY 261
Cdd:cd06428 240 FWSQIKTAGSAIYANRLY 257
LbetaH super family cl00160
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 289-355 6.76e-23

Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.


The actual alignment was detected with superfamily member cd05824:

Pssm-ID: 469633 [Multi-domain]  Cd Length: 80  Bit Score: 91.83  E-value: 6.76e-23
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45447090 289 IHPTAKVAPSAVLGPNVSIGKGVTVGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVGRWARVEG 355
Cdd:cd05824   2 IDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLEN 68
 
Name Accession Description Interval E-value
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 4-261 1.86e-172

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: 482.52  E-value: 1.86e-172
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   4 AVILIGGPQKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVPGMQEILLIGFYqPDEPLTQFLEAAQQEFNLPVRYL 83
Cdd:cd06428   1 AVILVGGPQKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVPDLKEVLLIGFY-PESVFSDFISDAQQEFNVPIRYL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  84 QEFAPLGTGGGLYHFRDQILAGSPEAFFVLNADVCSDFPLSAMLEAHRRQRHPFLLLGTTANRTQSLNYGCIVENPQTHE 163
Cdd:cd06428  80 QEYKPLGTAGGLYHFRDQILAGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEASREQASNYGCIVEDPSTGE 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 164 VLHYVEKPSTFISDIINCGIYLFSPEALKPLRDVFQRNQQDGQLEDSPGLWPGAGTIRLEQDVFSALAGQGQIYVHLTDG 243
Cdd:cd06428 160 VLHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNREGRAEVIRLEQDVLTPLAGSGKLYVYKTDD 239

                       250
                ....*....|....*...
gi 45447090 244 IWSQIKSAGSALYASRLY 261
Cdd:cd06428 240 FWSQIKTAGSAIYANRLY 257
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 3-264 1.96e-47

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: 162.24  E-value: 1.96e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   3 KAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIGFYQPDEpLTQFLeAAQQEFNLPVRY 82
Cdd:COG1208   1 KAVILAGG--LGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAA-GITEIVINVGYLAEQ-IEEYF-GDGSRFGVRITY 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  83 LQEFAPLGTGGGLYHFRDQIlagSPEAFFVLNADVCSDFPLSAMLEAHRRQRHPFLLLgTTANRTQSlNYGCIVENPQtH 162
Cdd:COG1208  76 VDEGEPLGTGGALKRALPLL---GDEPFLVLNGDILTDLDLAALLAFHREKGADATLA-LVPVPDPS-RYGVVELDGD-G 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 163 EVLHYVEKPSTFISDIINCGIYLFSPEALKplrdvfqrnqqdgqledspgLWPGAGTIRLEqDVFSALAGQGQIYVHLTD 242
Cdd:COG1208 150 RVTRFVEKPEEPPSNLINAGIYVLEPEIFD--------------------YIPEGEPFDLE-DLLPRLIAEGRVYGYVHD 208

                       250       260
                ....*....|....*....|..
gi 45447090 243 GIWSQIKSAGSALYASRLYLSR 264
Cdd:COG1208 209 GYWLDIGTPEDLLEANALLLSG 230
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 2-348 1.25e-33

UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.


Pssm-ID: 274908 [Multi-domain]  Cd Length: 393  Bit Score: 129.64  E-value: 1.25e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090     2 LKAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIGFYQPDEpLTQFLEaAQQEFNLPVR 81
Cdd:TIGR03992   1 MKAVILAAG--KGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDA-GIDDFVFVVGYGKEK-VREYFG-DGSRGGVPIE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090    82 YLQEFAPLGTGGGLYHFRDQIlagsPEAFFVLNADVCSDFP-LSAMLEAHRrqrhPFLLLGTTANRTQslnYGCI-VENp 159
Cdd:TIGR03992  76 YVVQEEQLGTADALGSAKEYV----DDEFLVLNGDVLLDSDlLERLIRAEA----PAIAVVEVDDPSD---YGVVeTDG- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   160 qtHEVLHYVEKPSTFISDIINCGIYLFSPEALKPLRDVfqrnqqdgqlEDSPglwpgagtiRLE---QDVFSALAGQGQI 236
Cdd:TIGR03992 144 --GRVTGIVEKPENPPSNLINAGIYLFSPEIFELLEKT----------KLSP---------RGEyelTDALQLLIDEGKV 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   237 YVHLTDGIWSQIKSAGSALYASRLYLSRYQdthPERLAKHTPG-----------------GPWIRGNVYIHPTAKVAPSA 299
Cdd:TIGR03992 203 KAVELDGFWLDVGRPWDLLDANEALLDNLE---PRIEGTVEENvtikgpvvigegavirsGTYIEGPVYIGKNCDIGPNA 279

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 45447090   300 VLGPNVSIGKGVTVGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVG 348
Cdd:TIGR03992 280 YIRPYTVIGNNVHIGNAVEIKNSIIMEGTKIPHLSYVGDSVIGENCNFG 328
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 3-191 3.17e-30

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: 116.97  E-value: 3.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090     3 KAVILIGGpqKGTRFRPLSFEVPKPLFPVAG-VPMIQHHIEACAQVpGMQEILLIgFYQPDEPLTQFLEAAQQEFNLPVR 81
Cdd:pfam00483   1 KAIILAGG--SGTRLWPLTRTLAKPLVPVGGkYPLIDYPLSRLANA-GIREIIVI-LTQEHRFMLNELLGDGSKFGVQIT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090    82 YLQEFAPLGTGGGLYHFRDQILAGSPEaFFVLNADVCSDFPLSAMLEAHR-RQRHPFLLLGTTANRTQSlNYGCIVENPQ 160
Cdd:pfam00483  77 YALQPEGKGTAPAVALAADFLGDEKSD-VLVLGGDHIYRMDLEQAVKFHIeKAADATVTFGIVPVEPPT-GYGVVEFDDN 154

                         170       180       190
                  ....*....|....*....|....*....|..
gi 45447090   161 ThEVLHYVEKPSTF-ISDIINCGIYLFSPEAL 191
Cdd:pfam00483 155 G-RVIRFVEKPKLPkASNYASMGIYIFNSGVL 185
LbH_M1P_guanylylT_C cd05824
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 289-355 6.76e-23

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


Pssm-ID: 100062 [Multi-domain]  Cd Length: 80  Bit Score: 91.83  E-value: 6.76e-23
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45447090 289 IHPTAKVAPSAVLGPNVSIGKGVTVGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVGRWARVEG 355
Cdd:cd05824   2 IDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLEN 68
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 2-353 1.60e-11

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 65.77  E-value: 1.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090    2 LKAVILIGGpqKGTRFRPlsfEVPKPLFPVAGVPMIQHHIEAcAQVPGMQEILLIGFYQPDEpltqfLEAAQQEFNlpVR 81
Cdd:PRK14358   8 LDVVILAAG--QGTRMKS---ALPKVLHPVAGRPMVAWAVKA-ARDLGARKIVVVTGHGAEQ-----VEAALQGSG--VA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   82 YLQEFAPLGTGgglyhfrDQILAGSpEAFFVLNADVC---SDFP------LSAMLEAHRRQRHPFLLLgtTANRTQSLNY 152
Cdd:PRK14358  75 FARQEQQLGTG-------DAFLSGA-SALTEGDADILvlyGDTPllrpdtLRALVADHRAQGSAMTIL--TGELPDATGY 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  153 GCIVENPQTHEVLHYVEKPSTFISDII---NCGIYLFSPEALKPLRDVFQRNQQ-DGQLEDSPGLWPGAG----TIRLE- 223
Cdd:PRK14358 145 GRIVRGADGAVERIVEQKDATDAEKAIgefNSGVYVFDARAPELARRIGNDNKAgEYYLTDLLGLYRAGGaqvrAFKLSd 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  224 -QDVFSA--LAGQGQIYVHLTDGIWSQIKSAGSALyasrlylsryQDthperlakhtPGGPWIRGNVYIHPTAKVAPSAV 300
Cdd:PRK14358 225 pDEVLGAndRAGLAQLEATLRRRINEAHMKAGVTL----------QD----------PGTILIEDTVTLGRDVTIEPGVL 284

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 45447090  301 LGPNVSIGKGVTVGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVGRWARV 353
Cdd:PRK14358 285 LRGQTRVADGVTIGAYSVVTDSVLHEGAVIKPHSVLEGAEVGAGSDVGPFARL 337
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 230-353 5.40e-11

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 63.50  E-value: 5.40e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 230 LAGQGQIYVHltdGIwSQIKSAGS---ALYASRLYLSRYQDTH------PERLAKHTPGGPWIR-GNVY----------- 288
Cdd:COG1044  15 LVGDGDLEIT---GV-APLEEAGPgdlSFLANPKYAKQLATTKasavivPPDFAAALPGLALIVvDNPYlafakllqlfy 90

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45447090 289 --------IHPTAKVAPSAVLGPNVSIGKGVTVGEGVRLRESIVLHGatlqehtcvlHSIVGWGSTVGR----WARV 353
Cdd:COG1044  91 pppapapgIHPSAVIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGP----------GVVIGDGVVIGDdcvlHPNV 157
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 289-353 1.16e-09

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 59.38  E-value: 1.16e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45447090  289 IHPTAKVAPSAVLGPNVSIGKGVTVGEGVRLRESIVLHGatlqehtcvlHSIVGWGSTVGR----WARV 353
Cdd:PRK00892 103 IHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGA----------GAVIGDGVKIGAdcrlHANV 161
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
286-315 3.95e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 34.62  E-value: 3.95e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 45447090   286 NVYIHPTAKVAPSAVLGPNVSIGKGVTVGE 315
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 4-261 1.86e-172

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: 482.52  E-value: 1.86e-172
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   4 AVILIGGPQKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVPGMQEILLIGFYqPDEPLTQFLEAAQQEFNLPVRYL 83
Cdd:cd06428   1 AVILVGGPQKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVPDLKEVLLIGFY-PESVFSDFISDAQQEFNVPIRYL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  84 QEFAPLGTGGGLYHFRDQILAGSPEAFFVLNADVCSDFPLSAMLEAHRRQRHPFLLLGTTANRTQSLNYGCIVENPQTHE 163
Cdd:cd06428  80 QEYKPLGTAGGLYHFRDQILAGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEASREQASNYGCIVEDPSTGE 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 164 VLHYVEKPSTFISDIINCGIYLFSPEALKPLRDVFQRNQQDGQLEDSPGLWPGAGTIRLEQDVFSALAGQGQIYVHLTDG 243
Cdd:cd06428 160 VLHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNREGRAEVIRLEQDVLTPLAGSGKLYVYKTDD 239

                       250
                ....*....|....*...
gi 45447090 244 IWSQIKSAGSALYASRLY 261
Cdd:cd06428 240 FWSQIKTAGSAIYANRLY 257
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 4-248 4.65e-56

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: 183.94  E-value: 4.65e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   4 AVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIGFYQPDEPLTQFLEAAQqeFNLPVRYL 83
Cdd:cd04181   1 AVILAAG--KGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARA-GIDEIILVVGYLGEQIEEYFGDGSK--FGVNIEYV 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  84 QEFAPLGTGGGLYHFRDQIlagSPEAFFVLNADVCSDFPLSAMLEAHRRQRHPFLLLGTTANRTQSlnYGCIVENPQtHE 163
Cdd:cd04181  76 VQEEPLGTAGAVRNAEDFL---GDDDFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEVEDPSR--YGVVELDDD-GR 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 164 VLHYVEKPSTFISDIINCGIYLFSPEALKPLRDVFQRNqqdgqlEDspglwpgagtirLEQDVFSALAGQGQIYVHLTDG 243
Cdd:cd04181 150 VTRFVEKPTLPESNLANAGIYIFEPEILDYIPEILPRG------ED------------ELTDAIPLLIEEGKVYGYPVDG 211


                ....*
gi 45447090 244 IWSQI 248
Cdd:cd04181 212 YWLDI 216
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 2-262 1.04e-54

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: 181.25  E-value: 1.04e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   2 LKAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIGFYQPDEpLTQFLEAAQQEFNLPVR 81
Cdd:cd06425   1 MKALILVGG--YGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKA-GVKEIILAVNYRPED-MVPFLKEYEKKLGIKIT 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  82 YLQEFAPLGTGGGLYHFRDqILAGSPEAFFVLNADVCSDFPLSAMLEAHRRQRHPFLLLGTTAnrTQSLNYGCIVENPQT 161
Cdd:cd06425  77 FSIETEPLGTAGPLALARD-LLGDDDEPFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKV--EDPSKYGVVVHDENT 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 162 HEVLHYVEKPSTFISDIINCGIYLFSPEALK--PLRDVfqrnqqdgqledspglwpgagtiRLEQDVFSALAGQGQIYVH 239
Cdd:cd06425 154 GRIERFVEKPKVFVGNKINAGIYILNPSVLDriPLRPT-----------------------SIEKEIFPKMASEGQLYAY 210

                       250       260
                ....*....|....*....|...
gi 45447090 240 LTDGIWSQIKSAGSALYASRLYL 262
Cdd:cd06425 211 ELPGFWMDIGQPKDFLKGMSLYL 233
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 3-264 1.96e-47

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: 162.24  E-value: 1.96e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   3 KAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIGFYQPDEpLTQFLeAAQQEFNLPVRY 82
Cdd:COG1208   1 KAVILAGG--LGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAA-GITEIVINVGYLAEQ-IEEYF-GDGSRFGVRITY 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  83 LQEFAPLGTGGGLYHFRDQIlagSPEAFFVLNADVCSDFPLSAMLEAHRRQRHPFLLLgTTANRTQSlNYGCIVENPQtH 162
Cdd:COG1208  76 VDEGEPLGTGGALKRALPLL---GDEPFLVLNGDILTDLDLAALLAFHREKGADATLA-LVPVPDPS-RYGVVELDGD-G 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 163 EVLHYVEKPSTFISDIINCGIYLFSPEALKplrdvfqrnqqdgqledspgLWPGAGTIRLEqDVFSALAGQGQIYVHLTD 242
Cdd:COG1208 150 RVTRFVEKPEEPPSNLINAGIYVLEPEIFD--------------------YIPEGEPFDLE-DLLPRLIAEGRVYGYVHD 208

                       250       260
                ....*....|....*....|..
gi 45447090 243 GIWSQIKSAGSALYASRLYLSR 264
Cdd:COG1208 209 GYWLDIGTPEDLLEANALLLSG 230
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 2-348 1.25e-33

UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.


Pssm-ID: 274908 [Multi-domain]  Cd Length: 393  Bit Score: 129.64  E-value: 1.25e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090     2 LKAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIGFYQPDEpLTQFLEaAQQEFNLPVR 81
Cdd:TIGR03992   1 MKAVILAAG--KGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDA-GIDDFVFVVGYGKEK-VREYFG-DGSRGGVPIE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090    82 YLQEFAPLGTGGGLYHFRDQIlagsPEAFFVLNADVCSDFP-LSAMLEAHRrqrhPFLLLGTTANRTQslnYGCI-VENp 159
Cdd:TIGR03992  76 YVVQEEQLGTADALGSAKEYV----DDEFLVLNGDVLLDSDlLERLIRAEA----PAIAVVEVDDPSD---YGVVeTDG- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   160 qtHEVLHYVEKPSTFISDIINCGIYLFSPEALKPLRDVfqrnqqdgqlEDSPglwpgagtiRLE---QDVFSALAGQGQI 236
Cdd:TIGR03992 144 --GRVTGIVEKPENPPSNLINAGIYLFSPEIFELLEKT----------KLSP---------RGEyelTDALQLLIDEGKV 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   237 YVHLTDGIWSQIKSAGSALYASRLYLSRYQdthPERLAKHTPG-----------------GPWIRGNVYIHPTAKVAPSA 299
Cdd:TIGR03992 203 KAVELDGFWLDVGRPWDLLDANEALLDNLE---PRIEGTVEENvtikgpvvigegavirsGTYIEGPVYIGKNCDIGPNA 279

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 45447090   300 VLGPNVSIGKGVTVGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVG 348
Cdd:TIGR03992 280 YIRPYTVIGNNVHIGNAVEIKNSIIMEGTKIPHLSYVGDSVIGENCNFG 328
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 3-191 3.17e-30

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: 116.97  E-value: 3.17e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090     3 KAVILIGGpqKGTRFRPLSFEVPKPLFPVAG-VPMIQHHIEACAQVpGMQEILLIgFYQPDEPLTQFLEAAQQEFNLPVR 81
Cdd:pfam00483   1 KAIILAGG--SGTRLWPLTRTLAKPLVPVGGkYPLIDYPLSRLANA-GIREIIVI-LTQEHRFMLNELLGDGSKFGVQIT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090    82 YLQEFAPLGTGGGLYHFRDQILAGSPEaFFVLNADVCSDFPLSAMLEAHR-RQRHPFLLLGTTANRTQSlNYGCIVENPQ 160
Cdd:pfam00483  77 YALQPEGKGTAPAVALAADFLGDEKSD-VLVLGGDHIYRMDLEQAVKFHIeKAADATVTFGIVPVEPPT-GYGVVEFDDN 154

                         170       180       190
                  ....*....|....*....|....*....|..
gi 45447090   161 ThEVLHYVEKPSTF-ISDIINCGIYLFSPEAL 191
Cdd:pfam00483 155 G-RVIRFVEKPKLPkASNYASMGIYIFNSGVL 185
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 4-243 2.37e-27

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: 108.41  E-value: 2.37e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   4 AVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQvPGMQEILL-IGFyqpdepLTQFLEAAQQE---FNLP 79
Cdd:cd06915   1 AVILAGG--LGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLAR-QGISRIVLsVGY------LAEQIEEYFGDgyrGGIR 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  80 VRYLQEFAPLGTGGGLYHFRDQILAgspEAFFVLNADVCSDFPLSAMLEAHRRQRHPFLLLGtTANRTQSlNYGCIVENp 159
Cdd:cd06915  72 IYYVIEPEPLGTGGAIKNALPKLPE---DQFLVLNGDTYFDVDLLALLAALRASGADATMAL-RRVPDAS-RYGNVTVD- 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 160 QTHEVLHYVEKPSTFISDIINCGIYLFSPEALK--PLRDVFqrnqqdgqledspglwpgagtirLEQDVFSALAGQGQIY 237
Cdd:cd06915 146 GDGRVIAFVEKGPGAAPGLINGGVYLLRKEILAeiPADAFS-----------------------LEADVLPALVKRGRLY 202


                ....*.
gi 45447090 238 VHLTDG 243
Cdd:cd06915 203 GFEVDG 208
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 3-245 1.85e-25

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: 103.03  E-value: 1.85e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   3 KAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIGFYQPDEpLTQFLEAaqQEFNLPVRY 82
Cdd:cd06422   1 KAMILAAG--LGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAA-GIRRIVVNTHHLADQ-IEAHLGD--SRFGLRITI 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  83 LQE-FAPLGTGGGLYHFRDqiLAGSpEAFFVLNADVCSDFPLSAMLEAHRRQRHPFLLLGTTANRTQSLNYGCIVENPQT 161
Cdd:cd06422  75 SDEpDELLETGGGIKKALP--LLGD-EPFLVVNGDILWDGDLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFSLDADG 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 162 HevLHYveKPSTFISDIINCGIYLFSPEALKplrdvfqrnqqdgqledspGLWPGAGTIRleqDVFSALAGQGQIYVHLT 241
Cdd:cd06422 152 R--LRR--GGGGAVAPFTFTGIQILSPELFA-------------------GIPPGKFSLN---PLWDRAIAAGRLFGLVY 205


                ....
gi 45447090 242 DGIW 245
Cdd:cd06422 206 DGLW 209
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 4-192 1.73e-23

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: 97.58  E-value: 1.73e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   4 AVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIGFYQPDEPLTQFLEAaqQEFNLPVRYL 83
Cdd:cd06426   1 VVIMAGG--KGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQ-GFRNFYISVNYLAEMIEDYFGDG--SKFGVNISYV 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  84 QEFAPLGTGGGLYHFRDQIlagsPEAFFVLNADVCSDFPLSAMLEAHRRQRHpfllLGTTANRTQSLN--YGCIVENpqT 161
Cdd:cd06426  76 REDKPLGTAGALSLLPEKP----TDPFLVMNGDILTNLNYEHLLDFHKENNA----DATVCVREYEVQvpYGVVETE--G 145

                       170       180       190
                ....*....|....*....|....*....|.
gi 45447090 162 HEVLHYVEKPStfISDIINCGIYLFSPEALK 192
Cdd:cd06426 146 GRITSIEEKPT--HSFLVNAGIYVLEPEVLD 174
LbH_M1P_guanylylT_C cd05824
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 289-355 6.76e-23

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


Pssm-ID: 100062 [Multi-domain]  Cd Length: 80  Bit Score: 91.83  E-value: 6.76e-23
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45447090 289 IHPTAKVAPSAVLGPNVSIGKGVTVGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVGRWARVEG 355
Cdd:cd05824   2 IDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLEN 68
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 3-360 2.64e-22

glucose-1-phosphate thymidylylransferase, long form; The family of known and putative glucose-1-phosphate thymidyltransferase (also called dTDP-glucose synthase) shows a deep split into a short form (see TIGR01207) and a long form described by this model. The homotetrameric short form is found in numerous bacterial species that incorporate dTDP-L-rhamnose, which it helps synthesize, into the cell wall. It is subject to feedback inhibition. This form, in contrast, 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. Alternate name: dTDP-D-glucose synthase


Pssm-ID: 273500 [Multi-domain]  Cd Length: 353  Bit Score: 97.09  E-value: 2.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090     3 KAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEI-LLIGFYQPDEplTQFLEAAQQEFNLPVR 81
Cdd:TIGR01208   1 KALILAAG--KGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEA-GITDIgIVVGPVTGEE--IKEIVGEGERFGAKIT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090    82 YLQEFAPLGTGGGLYHFRDQIlagSPEAFFVLNADVCSDFPLSAMLEaHRRQRHP--FLLLGTTANRTQslnYGCIVENP 159
Cdd:TIGR01208  76 YIVQGEPLGLAHAVYTARDFL---GDDDFVVYLGDNLIQDGISRFVK-SFEEKDYdaLILLTKVRDPTA---FGVAVLED 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   160 QtHEVLHYVEKPSTFISDIINCGIYLFSPEALKPLRDvfqrnqqdgqLEDSpglWPGAGTIrleQDVFSALAGQGQ-IYV 238
Cdd:TIGR01208 149 G-KRILKLVEKPKEPPSNLAVVGLYMFRPLIFEAIKN----------IKPS---WRGELEI---TDAIQWLIEKGYkVGG 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   239 HLTDGIWSQIKSAGSALYASRLYLSRYqdthpERLAKHTPGGPWIRGNVYIHPTAKVAPSAVLGP----------NVSIG 308
Cdd:TIGR01208 212 SKVTGWWKDTGKPEDLLDANRLILDEV-----EREVQGVDDESKIRGRVVVGEGAKIVNSVIRGPavigedciieNSYIG 286

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 45447090   309 KGVTVGEGVRLRESIVLHGATLQEhtcvlHSIVGWG-----STVGRWARVEGTPSDP 360
Cdd:TIGR01208 287 PYTSIGEGVVIRDAEVEHSIVLDE-----SVIEGVQarivdSVIGKKVRIKGNRRRP 338
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 3-264 9.01e-22

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: 93.40  E-value: 9.01e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   3 KAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIGFYQPDEpltqfLEAAQQE---FNLP 79
Cdd:cd04189   2 KGLILAGG--KGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREA-GIEDIGIVVGPTGEE-----IKEALGDgsrFGVR 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  80 VRYLQEFAPLGTGGGLYHFRDQiLAGSPeaFFVLNADVCSDFPLSAMLEAHRRQRH-PFLLLGTTANRTQslnYGCIVen 158
Cdd:cd04189  74 ITYILQEEPLGLAHAVLAARDF-LGDEP--FVVYLGDNLIQEGISPLVRDFLEEDAdASILLAEVEDPRR---FGVAV-- 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 159 PQTHEVLHYVEKPSTFISDIINCGIYLFSPEALKPLRDvfqrnqqdgqLEDSpglWPGagtiRLE-QDVFSALAGQG-QI 236
Cdd:cd04189 146 VDDGRIVRLVEKPKEPPSNLALVGVYAFTPAIFDAISR----------LKPS---WRG----ELEiTDAIQWLIDRGrRV 208

                       250       260
                ....*....|....*....|....*...
gi 45447090 237 YVHLTDGIWSQIKSAGSALYASRLYLSR 264
Cdd:cd04189 209 GYSIVTGWWKDTGTPEDLLEANRLLLDK 236
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 2-352 2.28e-19

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: 89.70  E-value: 2.28e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   2 LKAVILIGGpqKGTRFRplSfEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIGFYQPDEpltqfLEAAQQEFNlpVR 81
Cdd:COG1207   3 LAVVILAAG--KGTRMK--S-KLPKVLHPLAGKPMLEHVLDAARAL-GPDRIVVVVGHGAEQ-----VRAALADLD--VE 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  82 Y-LQEfAPLGTG-------GGLYHFRDQILagspeaffVLNADVcsdfPL------SAMLEAHRRQRHPFLLLgtTANRT 147
Cdd:COG1207  70 FvLQE-EQLGTGhavqqalPALPGDDGTVL--------VLYGDV----PLiraetlKALLAAHRAAGAAATVL--TAELD 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 148 QSLNYGCIVENpQTHEVLHYVE-KpstfisD-------I--INCGIYLFSPEALkplrdvfqrnqqdgqledspglwpga 217
Cdd:COG1207 135 DPTGYGRIVRD-EDGRVLRIVEeK------DateeqraIreINTGIYAFDAAAL-------------------------- 181

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 218 gtirleqdvFSALAG------QGQIYvhLTDgIWSQIKSAGSALYA-------------SRLYLSRYQDTHPERLAKHtp 278
Cdd:COG1207 182 ---------REALPKlsndnaQGEYY--LTD-VIAIARADGLKVAAvqpedpwevlgvnDRVQLAEAERILQRRIAER-- 247

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 279 ggpWIRG--------NVYIHPTAKVAPSAVLGPNV------SIGKGVTVGEGVRLRESIVLHGATLQeHTCVLHSIVGWG 344
Cdd:COG1207 248 ---LMRAgvtiidpaTTYIDGDVEIGRDVVIDPNVilegktVIGEGVVIGPNCTLKDSTIGDGVVIK-YSVIEDAVVGAG 323


                ....*...
gi 45447090 345 STVGRWAR 352
Cdd:COG1207 324 ATVGPFAR 331
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
3-243 7.67e-17

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 79.13  E-value: 7.67e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   3 KAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIGFYQPDEpltqfLEAAQQEFNLPVRY 82
Cdd:COG1213   1 KAVILAAG--RGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAA-GIKDIVVVTGYKAEL-----IEEALARPGPDVTF 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  83 LQ--EFAPLGTGGGLYHFRDQIlagsPEAFFVLNAD-VCSDFPLSAMLEAhrrqRHPFLLLGTTANRTQSlnygcivenp 159
Cdd:COG1213  73 VYnpDYDETNNIYSLWLAREAL----DEDFLLLNGDvVFDPAILKRLLAS----DGDIVLLVDRKWEKPL---------- 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 160 qtHEVLHYVEKPSTFISDI--------INC---GIYLFSPEALKPLRDVFQRNQQDGQLEDSpglwpgagtirLEqDVFS 228
Cdd:COG1213 135 --DEEVKVRVDEDGRIVEIgkklppeeADGeyiGIFKFSAEGAAALREALEALIDEGGPNLY-----------YE-DALQ 200

                       250
                ....*....|....*.
gi 45447090 229 ALAGQG-QIYVHLTDG 243
Cdd:COG1213 201 ELIDEGgPVKAVDIGG 216
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 2-191 6.99e-16

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: 76.14  E-value: 6.99e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   2 LKAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLigFYQPDEplTQFLEAAQQEFNLPVR 81
Cdd:cd02507   1 FQAVVLADG--FGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKA-GVEEVFV--VCCEHS--QAIIEHLLKSKWSSLS 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  82 YLQEF--------APLGTGGGLYHFRDQIlagsPEAFFVLNADVCSDFPLSAMLEAhRRQRHP------FLLLGTTANRT 147
Cdd:cd02507  74 SKMIVdvitsdlcESAGDALRLRDIRGLI----RSDFLLLSCDLVSNIPLSELLEE-RRKKDKnaiatlTVLLASPPVST 148

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45447090 148 QSL----NYGCIVENPQTHE--VLHY---VEKPSTFI---------------SDIINCGIYLFSPEAL 191
Cdd:cd02507 149 EQSkkteEEDVIAVDSKTQRllLLHYeedLDEDLELIirksllskhpnvtirTDLLDCHIYICSPDVL 216
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 4-194 6.86e-15

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: 73.70  E-value: 6.86e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   4 AVILIGGpqKGTRFRplsFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIGFYQPDEpltqfLEAAQQEFNLPVrYL 83
Cdd:cd02540   1 AVILAAG--KGTRMK---SDLPKVLHPLAGKPMLEHVLDAARAL-GPDRIVVVVGHGAEQ-----VKKALANPNVEF-VL 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  84 QEfAPLGTGGGLYHFRDQiLAGSPEAFFVLNADVcsdfPL------SAMLEAHRRQRHPFLLLgtTANRTQSLNYGCIVE 157
Cdd:cd02540  69 QE-EQLGTGHAVKQALPA-LKDFEGDVLVLYGDV----PLitpetlQRLLEAHREAGADVTVL--TAELEDPTGYGRIIR 140

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 45447090 158 NpQTHEVLHYVE----KPSTFISDIINCGIYLFSPEALKPL 194
Cdd:cd02540 141 D-GNGKVLRIVEekdaTEEEKAIREVNAGIYAFDAEFLFEA 180
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 4-248 1.37e-14

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


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 72.65  E-value: 1.37e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   4 AVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIGFYQPDepltQFLEAAQQEFNLPVRYL 83
Cdd:cd02523   1 AIILAAG--RGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEA-GIDDIVIVTGYKKE----QIEELLKKYPNIKFVYN 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  84 QEFAPLGTGGGLYHFRDQIlagsPEAFFVLNADVCSDfplSAMLEAHRRQRHPFLLLGTTANRTQSLNYGCIVENPQthe 163
Cdd:cd02523  74 PDYAETNNIYSLYLARDFL----DEDFLLLEGDVVFD---PSILERLLSSPADNAILVDKKTKEWEDEYVKDLDDAG--- 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 164 VLHYVEKPSTFISDI--INCGIYLFSPEALKPLRDVFQRNQQDGQLEDSpglWPgagtirleqDVFSALAGQGQIYVH-L 240
Cdd:cd02523 144 VLLGIISKAKNLEEIqgEYVGISKFSPEDADRLAEALEELIEAGRVNLY---YE---------DALQRLISEEGVKVKdI 211


                ....*...
gi 45447090 241 TDGIWSQI 248
Cdd:cd02523 212 SDGFWYEI 219
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 2-132 7.99e-14

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: 70.00  E-value: 7.99e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   2 LKAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIgfyqPDEPLTQFLEAAQQEF--NLP 79
Cdd:cd04198   1 FQAVILAGG--GGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKA-GFEDVIVV----VPEEEQAEISTYLRSFplNLK 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 45447090  80 VRYLQEFAPL----GTGGGLYHFRDQIlagsPEAFFVLNADVCSDFPLSAMLEAHRR 132
Cdd:cd04198  74 QKLDEVTIVLdedmGTADSLRHIRKKI----KKDFLVLSCDLITDLPLIELVDLHRS 126
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
3-207 5.33e-13

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 68.96  E-value: 5.33e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   3 KAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIgfyqpdepLT-QFLEAAQQ------E 75
Cdd:COG1209   2 KGIILAGG--SGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLA-GIREILII--------STpEDGPQFERllgdgsQ 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  76 FNLPVRY-LQEfAPLGTGgglyhfrdqilagspEAF-----FVLNADVC---SD--F---PLSAMLEAHRRQRHpflllG 141
Cdd:COG1209  71 LGIKISYaVQP-EPLGLA---------------HAFiiaedFIGGDPVAlvlGDniFygdGLSELLREAAARES-----G 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 142 TTAnrtqslnYGCIVENPQ---------THEVLHYVEKPSTFISDIINCGIYLFSP------EALKP-------LRDVFQ 199
Cdd:COG1209 130 ATI-------FGYKVEDPErygvvefdeDGRVVSLEEKPKEPKSNLAVTGLYFYDNdvveiaKNLKPsargeleITDANQ 202


                ....*...
gi 45447090 200 RNQQDGQL 207
Cdd:COG1209 203 AYLERGKL 210
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 2-353 1.60e-11

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 65.77  E-value: 1.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090    2 LKAVILIGGpqKGTRFRPlsfEVPKPLFPVAGVPMIQHHIEAcAQVPGMQEILLIGFYQPDEpltqfLEAAQQEFNlpVR 81
Cdd:PRK14358   8 LDVVILAAG--QGTRMKS---ALPKVLHPVAGRPMVAWAVKA-ARDLGARKIVVVTGHGAEQ-----VEAALQGSG--VA 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   82 YLQEFAPLGTGgglyhfrDQILAGSpEAFFVLNADVC---SDFP------LSAMLEAHRRQRHPFLLLgtTANRTQSLNY 152
Cdd:PRK14358  75 FARQEQQLGTG-------DAFLSGA-SALTEGDADILvlyGDTPllrpdtLRALVADHRAQGSAMTIL--TGELPDATGY 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  153 GCIVENPQTHEVLHYVEKPSTFISDII---NCGIYLFSPEALKPLRDVFQRNQQ-DGQLEDSPGLWPGAG----TIRLE- 223
Cdd:PRK14358 145 GRIVRGADGAVERIVEQKDATDAEKAIgefNSGVYVFDARAPELARRIGNDNKAgEYYLTDLLGLYRAGGaqvrAFKLSd 224

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  224 -QDVFSA--LAGQGQIYVHLTDGIWSQIKSAGSALyasrlylsryQDthperlakhtPGGPWIRGNVYIHPTAKVAPSAV 300
Cdd:PRK14358 225 pDEVLGAndRAGLAQLEATLRRRINEAHMKAGVTL----------QD----------PGTILIEDTVTLGRDVTIEPGVL 284

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 45447090  301 LGPNVSIGKGVTVGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVGRWARV 353
Cdd:PRK14358 285 LRGQTRVADGVTIGAYSVVTDSVLHEGAVIKPHSVLEGAEVGAGSDVGPFARL 337
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 2-348 2.37e-11

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 65.15  E-value: 2.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090    2 LKAVILIGGpqKGTRFRPlsfEVPKPLFPVAGVPMIQHHIEAcAQVPGMQEILLIGFYQPDEPLTQFLEAAQQEFNlpvr 81
Cdd:PRK14355   4 LAAIILAAG--KGTRMKS---DLVKVMHPLAGRPMVSWPVAA-AREAGAGRIVLVVGHQAEKVREHFAGDGDVSFA---- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   82 yLQEfAPLGTGGGLYHFRDQiLAGSPEAFFVLnadvCSDFP------LSAMLEAHRRQRHPFLLLgtTANRTQSLNYGCI 155
Cdd:PRK14355  74 -LQE-EQLGTGHAVACAAPA-LDGFSGTVLIL----CGDVPllraetLQGMLAAHRATGAAVTVL--TARLENPFGYGRI 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  156 VENpQTHEVLHYVEK----PSTFISDIINCGIYLFspealkplrdvfqrnqqdgqleDSPGLWPGAGTIRLEQdvfsala 231
Cdd:PRK14355 145 VRD-ADGRVLRIVEEkdatPEERSIREVNSGIYCV----------------------EAAFLFDAIGRLGNDN------- 194

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  232 GQGQIYvhLTDgIWSQIKSAGSALYASRLYLS--------RYQDTHPERLAKHTPGGPWIRGNV--------YIHPTAKV 295
Cdd:PRK14355 195 AQGEYY--LTD-IVAMAAAEGLRCLAFPVADPdeimgvndRAQLAEAARVLRRRINRELMLAGVtlidpettYIDRGVVI 271

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 45447090  296 APSAVLGPNVSIGKGVTVGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVG 348
Cdd:PRK14355 272 GRDTTIYPGVCISGDTRIGEGCTIEQGVVIKGCRIGDDVTVKAGSVLEDSVVG 324
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 2-351 2.81e-11

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 64.85  E-value: 2.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090    2 LKAVILIGGpqKGTRFRPlsfEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLI---GFYQPDEPLTQFLEAAQQEfnl 78
Cdd:PRK14354   3 RYAIILAAG--KGTRMKS---KLPKVLHKVCGKPMVEHVVDSVKKA-GIDKIVTVvghGAEEVKEVLGDRSEFALQE--- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   79 pvrylqefAPLGTGGGLYHFRDqILAGSPEAFFVlnadVCSDFPL------SAMLEAHRRQR-HPFLLLGTTANRTqslN 151
Cdd:PRK14354  74 --------EQLGTGHAVMQAEE-FLADKEGTTLV----ICGDTPLitaetlKNLIDFHEEHKaAATILTAIAENPT---G 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  152 YGCIVENPQThEVLHYVEKP--STFISDI--INCGIYLFSPEAL-KPLRDVFQRNQQdgqledspglwpgagtirleqdv 226
Cdd:PRK14354 138 YGRIIRNENG-EVEKIVEQKdaTEEEKQIkeINTGTYCFDNKALfEALKKISNDNAQ----------------------- 193

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  227 fsalagqGQIYvhLTDGIwSQIKSAGSALYA-------------SRLYLSRYQDTHPER-LAKHTPGG-----PwirGNV 287
Cdd:PRK14354 194 -------GEYY--LTDVI-EILKNEGEKVGAyqtedfeeslgvnDRVALAEAEKVMRRRiNEKHMVNGvtiidP---EST 260

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  288 YIHPTAKVAPSAVLGPNV------SIGKGVTVGEGVRLRESIVLHGATLQeHTCVLHSIVGWGSTVGRWA 351
Cdd:PRK14354 261 YIDADVEIGSDTVIEPGVvikgntVIGEDCVIGPGSRIVDSTIGDGVTIT-NSVIEESKVGDNVTVGPFA 329
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 230-353 5.40e-11

UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope biogenesis]; UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 63.50  E-value: 5.40e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 230 LAGQGQIYVHltdGIwSQIKSAGS---ALYASRLYLSRYQDTH------PERLAKHTPGGPWIR-GNVY----------- 288
Cdd:COG1044  15 LVGDGDLEIT---GV-APLEEAGPgdlSFLANPKYAKQLATTKasavivPPDFAAALPGLALIVvDNPYlafakllqlfy 90

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45447090 289 --------IHPTAKVAPSAVLGPNVSIGKGVTVGEGVRLRESIVLHGatlqehtcvlHSIVGWGSTVGR----WARV 353
Cdd:COG1044  91 pppapapgIHPSAVIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGP----------GVVIGDGVVIGDdcvlHPNV 157
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 288-355 1.90e-10

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


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 56.87  E-value: 1.90e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45447090 288 YIHPTAKVAPSAVLGPNVsIGKGVTVGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVGRWARVEG 355
Cdd:cd03356   1 LIGESTVIGENAIIKNSV-IGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVN 67
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 289-353 1.16e-09

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 59.38  E-value: 1.16e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45447090  289 IHPTAKVAPSAVLGPNVSIGKGVTVGEGVRLRESIVLHGatlqehtcvlHSIVGWGSTVGR----WARV 353
Cdd:PRK00892 103 IHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGA----------GAVIGDGVKIGAdcrlHANV 161
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-352 1.47e-09

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 59.74  E-value: 1.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090    4 AVILIGGpqKGTRFRPlsfEVPKPLFPVAGVPMIQHHIEACAQVPGMQEILLIGFYQpdepltqflEAAQQEF-NLPVRY 82
Cdd:PRK14356   8 ALILAAG--KGTRMHS---DKPKVLQTLLGEPMLRFVYRALRPLFGDNVWTVVGHRA---------DMVRAAFpDEDARF 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   83 LQEFAPLGTGGGLYHFRDQILAGSPEAFFVLNAD--VCSDFPLSAMLEAHRRQRHPFLllgtTANRTQSLNYG------- 153
Cdd:PRK14356  74 VLQEQQLGTGHALQCAWPSLTAAGLDRVLVVNGDtpLVTTDTIDDFLKEAAGADLAFM----TLTLPDPGAYGrvvrrng 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  154 ---CIVENPQTHEVLHYVEkpstfiSDIINCGIYLFSPEALKPLRDVFQRNQQDGQ--LEDSPGLWPGAGtirleQDVFS 228
Cdd:PRK14356 150 hvaAIVEAKDYDEALHGPE------TGEVNAGIYYLRLDAVESLLPRLTNANKSGEyyITDLVGLAVAEG-----MNVLG 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  229 ALAGQGQIYVhltdGIwsqiksagsalyASRLYLSRYQDTHPERLA-KHTPGGPWIR--GNVYIHPTAKVAPSAVL-GP- 303
Cdd:PRK14356 219 VNCGEDPNLL----GV------------NTPAELVRSEELLRARIVeKHLESGVLIHapESVRIGPRATIEPGAEIyGPc 282

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 45447090  304 ----NVSIGKGVTVGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVGRWAR 352
Cdd:PRK14356 283 eiygASRIARGAVIHSHCWLRDAVVSSGATIHSFSHLEGAEVGDGCSVGPYAR 335
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 3-243 1.89e-09

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: 57.93  E-value: 1.89e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   3 KAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIG---------FYQPDEPLTQFLEAAQ 73
Cdd:cd02541   2 KAVIPAAG--LGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAA-GIEDIIIVTgrgkraiedHFDRSYELEETLEKKG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  74 QEFNL----------PVRYLQEFAPLGTGgglyhfrDQILAGSP----EAFFVLNADV---CSDFPLSAMLEAHRRQRHP 136
Cdd:cd02541  79 KTDLLeevriisdlaNIHYVRQKEPLGLG-------HAVLCAKPfigdEPFAVLLGDDlidSKEPCLKQLIEAYEKTGAS 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 137 FLLLGTTANRTQSlNYGCIV---ENPQTHEVLHYVEKPStfISD------IIncGIYLFSPEALKPLrdvfqRNQQdgql 207
Cdd:cd02541 152 VIAVEEVPPEDVS-KYGIVKgekIDGDVFKVKGLVEKPK--PEEapsnlaIV--GRYVLTPDIFDIL-----ENTK---- 217

                       250       260       270
                ....*....|....*....|....*....|....*..
gi 45447090 208 edspglwPGA-GTIRLeQDVFSALAGQGQIYVHLTDG 243
Cdd:cd02541 218 -------PGKgGEIQL-TDAIAKLLEEEPVYAYVFEG 246
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 2-191 4.50e-09

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: 56.08  E-value: 4.50e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   2 LKAVILigGPQKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQvPGMQEILLIGFYQPDEpLTQFLEAAQQEfnlpvr 81
Cdd:cd04197   1 LQAVVL--ADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLAL-NGVEEVFVFCCSHSDQ-IKEYIEKSKWS------ 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  82 ylqefaplgtgGGLYHFRDQILAGSPEAF------------------FVL-NADVCSDFPLSAMLEAHRRQR-------- 134
Cdd:cd04197  71 -----------KPKSSLMIVIIIMSEDCRslgdalrdldakglirgdFILvSGDVVSNIDLKEILEEHKERRkkdknaim 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 135 -------HPFLLlgtTANRTQSLNygcIVENPQTHEVLHYVEKP----STFIS----------------DIINCGIYLFS 187
Cdd:cd04197 140 tmvlkeaSPPHR---TRRTGEEFV---IAVDPKTSRLLHYEELPgskyRSITDlpsellgsnseveirhDLLDCHIDICS 213


                ....
gi 45447090 188 PEAL 191
Cdd:cd04197 214 PDVL 217
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 4-361 5.93e-09

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 57.39  E-value: 5.93e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   4 AVILIGGpqKGTRFRPLSFEVPKPLFPVAG------VP---MIQHhieacaqvpGMQEILLIGFYQPDE----------- 63
Cdd:COG0448   4 AIILAGG--RGSRLGPLTKDRAKPAVPFGGkyriidFPlsnCVNS---------GIRRVGVLTQYKSHSlndhigsgkpw 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  64 ---PLTQFLE--AAQQEFNLPVRYLqefaplGTGGGLYHFRDQILAGSPEAFFVLNAD-VCS-DFplSAMLEAHRRQRHP 136
Cdd:COG0448  73 dldRKRGGVFilPPYQQREGEDWYQ------GTADAVYQNLDFIERSDPDYVLILSGDhIYKmDY--RQMLDFHIESGAD 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 137 FLLLGTTANRTQSLNYGCIVENPQtHEVLHYVEKPSTFISDIINCGIYLFSPEAlkpLRDVFQRNQQDGQLEdspglwpg 216
Cdd:COG0448 145 ITVACIEVPREEASRFGVMEVDED-GRITEFEEKPKDPKSALASMGIYVFNKDV---LIELLEEDAPNSSHD-------- 212

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 217 agtirLEQDVFSALAGQGQIYVHLTDGIWSQIksaGS--ALYASRLYLsryqdTHPE-RLAKHTPGGPwIRGNVYIHPTA 293
Cdd:COG0448 213 -----FGKDIIPRLLDRGKVYAYEFDGYWRDV---GTidSYYEANMDL-----LDPEpEFNLYDPEWP-IYTKQKDLPPA 278

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 294 KVAPSA--------------------VLGPNVSIGKGVTVgegvrlRESIVLHGATLQEHTCVLHSIVGWGSTVGRWARV 353
Cdd:COG0448 279 KFVRGGkvknslvsngciisgtvensVLFRGVRVESGAVV------ENSVIMPGVVIGEGAVIENAIIDKNVVIPPGVVI 352


                ....*...
gi 45447090 354 EGTPSDPN 361
Cdd:COG0448 353 GEDPEEDR 360
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 282-353 3.15e-08

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: 53.19  E-value: 3.15e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45447090 282 WIRGNVYIHPTAKVAPSAVLGPNVSIGKGVTVGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVGRWARV 353
Cdd:cd03353  11 YIDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIKDSTIGDGVVIKASSVIEGAVIGNGATVGPFAHL 82
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 289-412 4.56e-08

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: 51.99  E-value: 4.56e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 289 IHPTAKVAPSAVLGPNVSIGKGVTVGEGVRLR---ESIVLH-GATLQEhTCVLHS------IVGWGSTVGRWARVEGTPS 358
Cdd:cd04745   3 VDPSSFVHPTAVLIGDVIIGKNCYIGPHASLRgdfGRIVIRdGANVQD-NCVIHGfpgqdtVLEENGHIGHGAILHGCTI 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 359 DPNpndprARMDSESLFKDGKLLPAITILGC------RVRIPAEVLILNSIVLPHKELSR 412
Cdd:cd04745  82 GRN-----ALVGMNAVVMDGAVIGEESIVGAmafvkaGTVIPPRSLIAGSPAKVIRELSD 136
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 280-348 6.78e-08

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 52.41  E-value: 6.78e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45447090 280 GPWIRGNVYIHPTAKVAPSAVLGPNVSIGKGVTVGEGVRLREsivlhGATLQEHT-----CVLHSivgwGSTVG 348
Cdd:cd03352   7 NVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHP-----NVTIYEGCiigdrVIIHS----GAVIG 71
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
289-329 9.47e-08

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 52.79  E-value: 9.47e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 45447090  289 IHPTAKVAPSAVLGPNVSIG------KGVTVGEGVRLRESIVLHGAT 329
Cdd:PRK05289   5 IHPTAIVEPGAKIGENVEIGpfcvigPNVVIGDGTVIGSHVVIDGHT 51
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 289-329 1.07e-07

UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this family catalyze the transfer of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to UDP-GlcNAc. It is the first enzyme in the lipid A biosynthetic pathway and is also referred to as LpxA. Lipid A is essential for the growth of Escherichia coli and related bacteria. It is also essential for maintaining the integrity of the outer membrane. UDP-GlcNAc acyltransferase is a homotrimer of left-handed parallel beta helix (LbH) subunits. Each subunit contains an N-terminal LbH region with 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal alpha-helical region.


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 52.82  E-value: 1.07e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 45447090 289 IHPTAKVAPSAVLGPNVSIG------KGVTVGEGVRLRESIVLHGAT 329
Cdd:cd03351   2 IHPTAIVDPGAKIGENVEIGpfcvigPNVEIGDGTVIGSHVVIDGPT 48
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 4-245 1.09e-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: 52.57  E-value: 1.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   4 AVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQE-ILLIGF-----------YQP---------D 62
Cdd:cd02524   1 VVILAGG--LGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHY-GHNDfILCLGYkghvikeyflnYFLhnsdvtidlG 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  63 EPLTQFLEAAQQEFNLpvrylqEFAPLG----TGGGLYHFRDQIlaGSPEAFFVLNADVCSDFPLSAMLEAHRRQRhpfl 138
Cdd:cd02524  78 TNRIELHNSDIEDWKV------TLVDTGlntmTGGRLKRVRRYL--GDDETFMLTYGDGVSDVNINALIEFHRSHG---- 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 139 LLGTTANRTQSLNYGCIVENPQtHEVLHYVEKPSTFISdIINCGIYLFSPEALKPLrdvfqrnqqdgqledspglwPGAG 218
Cdd:cd02524 146 KLATVTAVHPPGRFGELDLDDD-GQVTSFTEKPQGDGG-WINGGFFVLEPEVFDYI--------------------DGDD 203

                       250       260
                ....*....|....*....|....*..
gi 45447090 219 TIrLEQDVFSALAGQGQIYVHLTDGIW 245
Cdd:cd02524 204 TV-FEREPLERLAKDGELMAYKHTGFW 229
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 289-329 1.31e-07

Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane/envelope biogenesis]; Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 52.33  E-value: 1.31e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 45447090 289 IHPTAKVAPSAVLGPNVSIG------KGVTVGEGVRLRESIVLHGAT 329
Cdd:COG1043   4 IHPTAIVDPGAKLGENVEIGpfcvigPDVEIGDGTVIGSHVVIEGPT 50
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 4-117 2.51e-07

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


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 49.89  E-value: 2.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090     4 AVILIGGpqKGTRFRplsfeVPKPLFPVAGVPMIQHHIEACAQVPGmqEILLIGfyqPDEPLTQFLEAaqqefnLPVRYL 83
Cdd:pfam12804   1 AVILAGG--RSSRMG-----GDKALLPLGGKPLLERVLERLRPAGD--EVVVVA---NDEEVLAALAG------LGVPVV 62

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 45447090    84 -QEFAPLGTGGGLYHFRDQilAGSPEAFFVLNADV 117
Cdd:pfam12804  63 pDPDPGQGPLAGLLAALRA--APGADAVLVLACDM 95
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
3-245 5.04e-07

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 50.80  E-value: 5.04e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   3 KAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIG----------F-YQPDepLTQFLEA 71
Cdd:COG1210   5 KAVIPVAG--LGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAA-GIEEIIFVTgrgkraiedhFdRSYE--LEATLEA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  72 A--QQEFNLpVRYLQEFA---------PLGTGGGLYHFRDQIlagSPEAFFVLNAD--VCSDFP-LSAMLEAHRRQRHPF 137
Cdd:COG1210  80 KgkEELLEE-VRSISPLAnihyvrqkePLGLGHAVLCARPFV---GDEPFAVLLGDdlIDSEKPcLKQMIEVYEETGGSV 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 138 LLLGTTAnRTQSLNYGCIV---ENPQTHEVLHYVEKPS--TFISDIINCGIYLFSPEalkplrdVFQ--RNQQdgqleds 210
Cdd:COG1210 156 IAVQEVP-PEEVSKYGIVDgeeIEGGVYRVTGLVEKPApeEAPSNLAIVGRYILTPE-------IFDilEKTK------- 220

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 45447090 211 pglwPGA-GTIRLeQDVFSALAGQGQIYVHLTDGIW 245
Cdd:COG1210 221 ----PGAgGEIQL-TDAIAALAKEEPVYAYEFEGKR 251
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 3-219 5.95e-07

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: 50.27  E-value: 5.95e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   3 KAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIGFYQpDEPLTQFLEAAQQEFNLPVRY 82
Cdd:cd02538   2 KGIILAGG--SGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLA-GIREILIISTPE-DLPLFKELLGDGSDLGIRITY 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  83 LQEFAPlgtgGGLyhfrdqilagsPEAF-----FVLNADVC--------SDFPLSAMLEAHRRQRHPFLLLGTTANRTQs 149
Cdd:cd02538  78 AVQPKP----GGL-----------AQAFiigeeFIGDDPVClilgdnifYGQGLSPILQRAAAQKEGATVFGYEVNDPE- 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 150 lNYGcIVENPQTHEVLHYVEKPSTFISDIINCGIYLFSPEA------LKP-------LRDV----FQRNQQDGQLEDSPG 212
Cdd:cd02538 142 -RYG-VVEFDENGRVLSIEEKPKKPKSNYAVTGLYFYDNDVfeiakqLKPsargeleITDVnneyLEKGKLSVELLGRGF 219


                ....*..
gi 45447090 213 LWPGAGT 219
Cdd:cd02538 220 AWLDTGT 226
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 287-348 6.23e-07

Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is composed of mostly uncharacterized proteins containing an N-terminal helical subdomain followed by a LbH domain. The alignment contains 6 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity. A few members are identified as NeuD, a sialic acid (Sia) O-acetyltransferase that is required for Sia synthesis and surface polysaccharide sialylation.


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 49.41  E-value: 6.23e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45447090 287 VYIHPTAKVAPSAVLGPNVSIGKGVTVGEGVRL-RESIVLHGATLqEHTCVL--HSIVGWGSTVG 348
Cdd:cd03360  85 TLIHPSAVVSPSAVIGEGCVIMAGAVINPDARIgDNVIINTGAVI-GHDCVIgdFVHIAPGVVLS 148
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-169 6.44e-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: 6.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090    4 AVILIGGpqKGTRFRPlsfEVPKPLFPVAGVPMIQHHIEACAQVPGMQEILLIGFYQPDepltqfLEAAQQEFNLPVR-Y 82
Cdd:PRK14353   8 AIILAAG--EGTRMKS---SLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEA------VAAAAAKIAPDAEiF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   83 LQEfAPLGTGGGLYHFRDQiLAGSPEAFFVLNADV--CSDFPLSAMLEaHRRQRHPFLLLGT-TANRTQslnYGCIVEnp 159
Cdd:PRK14353  77 VQK-ERLGTAHAVLAAREA-LAGGYGDVLVLYGDTplITAETLARLRE-RLADGADVVVLGFrAADPTG---YGRLIV-- 148

                        170
                 ....*....|
gi 45447090  160 QTHEVLHYVE 169
Cdd:PRK14353 149 KGGRLVAIVE 158
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 288-339 8.34e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 50.52  E-value: 8.34e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  288 YIHPTAKVAPSAVLGPNVSIGKGVT------------VGEGVRLRESIVLH-GATLQEHT-----CVLHS 339
Cdd:PRK00892 108 VIDPSAKIGEGVSIGPNAVIGAGVVigdgvvigagavIGDGVKIGADCRLHaNVTIYHAVrignrVIIHS 177
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 280-348 2.86e-06

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


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 47.20  E-value: 2.86e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45447090 280 GPWIRGNVYIHPTAKVAPSAVLGPNVSIGKGVTVGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVG 348
Cdd:cd05636  29 GAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSIIMDGTKVPHLNYVGDSVLGENVNLG 97
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 289-349 3.32e-06

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 46.94  E-value: 3.32e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45447090 289 IHPTAKVAPSAVLGPNVSIGKGVTVGEGVRLR---ESIVL-HGATLQEHtCVLHSIVGWGSTVGR 349
Cdd:COG0663  13 IHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRgdvGPIRIgEGSNIQDG-VVLHVDPGYPLTIGD 76
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 283-348 1.71e-05

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


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 44.89  E-value: 1.71e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45447090 283 IRGNVYIHPTAKVAPSAVLGPNVSIGKGVTVGEGVRLRESIVLH-GATLQEHTCVLHSIVGWGSTVG 348
Cdd:cd05636  14 IKGPVWIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGdGCVVGNSVEVKNSIIMDGTKVP 80
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-353 1.75e-05

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 46.84  E-value: 1.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090    1 MLKAVILIGGpqKGTRFRPlsfEVPKPLFPVAGVPMIQHHIEACAQVPGMQEILLIGfYQPDE--------PLTQFLEAA 72
Cdd:PRK14360   1 MLAVAILAAG--KGTRMKS---SLPKVLHPLGGKSLVERVLDSCEELKPDRRLVIVG-HQAEEveqslahlPGLEFVEQQ 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   73 QQefnlpvrylqefapLGTGgglyHFRDQILA---GSPEAFFVLNADVcsdfPL------SAMLEAHRRQRHPFLLLgtT 143
Cdd:PRK14360  75 PQ--------------LGTG----HAVQQLLPvlkGFEGDLLVLNGDV----PLlrpetlEALLNTHRSSNADVTLL--T 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  144 ANRTQSLNYGCIVENPQTHeVLHYVEK----PSTFISDIINCGIYLFSPEALKPLRDVFQRNQQdgqledspglwpgagt 219
Cdd:PRK14360 131 ARLPNPKGYGRVFCDGNNL-VEQIVEDrdctPAQRQNNRINAGIYCFNWPALAEVLPKLSSNND---------------- 193

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  220 irleqdvfsalagQGQIYvhLTDGIwSQIKSAGSALYA---------SRLYLSRYQDTHPERLAKHtpggpWIRGNV-YI 289
Cdd:PRK14360 194 -------------QKEYY--LTDTV-SLLDPVMAVEVEdyqeinginDRKQLAQCEEILQNRIKEK-----WMLAGVtFI 252

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45447090  290 HP-------TAKVAPSAVLGPNVSIgKGVTV-GEGVRLRESIVLHGATLQEHTCVLHSIVgWGSTVGRWARV 353
Cdd:PRK14360 253 DPasctiseTVELGPDVIIEPQTHL-RGNTViGSGCRIGPGSLIENSQIGENVTVLYSVV-SDSQIGDGVKI 322
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 289-350 1.82e-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: 44.32  E-value: 1.82e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45447090 289 IHPTAKVAPSAVLGPNVSIGKGVTVGEGVRLR---ESIVL-HGATLQEHtCVLHSIVGWGSTVGRW 350
Cdd:cd04645   2 IDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRgdvNPIRIgERTNIQDG-SVLHVDPGYPTIIGDN 66
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 5-187 2.05e-05

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: 45.71  E-value: 2.05e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   5 VILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVPGMQEILLIGfyqpDEPLTQFLEAAQQEFNLPVRYLQ 84
Cdd:cd04183   2 IIPMAG--LGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFICR----DEHNTKFHLDESLKLLAPNATVV 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  85 EFAPLgTGGGL---YHFRDQIlaGSPEAFFVLNADVCSDFPLSAMLEAHRrqrhpflllgttanrtQSLNYGCIVENPQT 161
Cdd:cd04183  76 ELDGE-TLGAActvLLAADLI--DNDDPLLIFNCDQIVESDLLAFLAAFR----------------ERDLDGGVLTFFSS 136

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 45447090 162 HEVLHYVEKPS------TF----ISDIINCGIYLFS 187
Cdd:cd04183 137 HPRWSYVKLDEngrvieTAekepISDLATAGLYYFK 172
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 3-238 2.93e-05

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 45.44  E-value: 2.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090    3 KAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIeACAQVPGMQEILLIGFYQpDEPLTQFLEAAQQEFNLPVRY 82
Cdd:PRK15480   5 KGIILAGG--SGTRLYPVTMAVSKQLLPIYDKPMIYYPL-STLMLAGIRDILIISTPQ-DTPRFQQLLGDGSQWGLNLQY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   83 LQEFAPLGTGGGLYHFRDQIlaGSPEAFFVLNADVCSDFPLSAMLEAHRRQRHPFLLLGTTANRTQslNYGcIVENPQTH 162
Cdd:PRK15480  81 KVQPSPDGLAQAFIIGEEFI--GGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPE--RYG-VVEFDQNG 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45447090  163 EVLHYVEKPSTFISDIINCGIYLFSPEALKPLRDVfqRNQQDGQLEDSpglwpGAGTIRLEQDVFS-ALAGQGQIYV 238
Cdd:PRK15480 156 TAISLEEKPLQPKSNYAVTGLYFYDNDVVEMAKNL--KPSARGELEIT-----DINRIYMEQGRLSvAMMGRGYAWL 225
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 2-92 3.52e-05

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 45.79  E-value: 3.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090    2 LKAVILIGGpqKGTRfrpLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIgfYQ----------PDEPLTQFLEA 71
Cdd:PRK09451   6 MSVVILAAG--KGTR---MYSDLPKVLHTLAGKPMVQHVIDAANEL-GAQHVHLV--YGhggdllkqtlADEPLNWVLQA 77

                         90       100
                 ....*....|....*....|.
gi 45447090   72 AQqefnlpvrylqefapLGTG 92
Cdd:PRK09451  78 EQ---------------LGTG 83
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 2-215 4.13e-05

GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes.


Pssm-ID: 133003 [Multi-domain]  Cd Length: 274  Bit Score: 44.87  E-value: 4.13e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   2 LKAVILIGGpqKGTRFRPLSFE-VPKPLFPVAGV-PMIQHHIEACAQVPGMQEILLIgfyqpdeplT----QFLEAAQ-Q 74
Cdd:cd02509   1 IYPVILAGG--SGTRLWPLSREsYPKQFLKLFGDkSLLQQTLDRLKGLVPPDRILVV---------TneeyRFLVREQlP 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  75 EFNLPVRYLQEFAPLGTGG----GLYHFRDQilagSPEA-FFVLNAD-VCSDFP-----LSAMLEAHRRQRhpFLLLGTT 143
Cdd:cd02509  70 EGLPEENIILEPEGRNTAPaialAALYLAKR----DPDAvLLVLPSDhLIEDVEaflkaVKKAVEAAEEGY--LVTFGIK 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 144 ANRTQSlNYGCI----VENPQTHEVLHYVEKPST-----FISD---IINCGIYLFS------------PEALKPLRDVFQ 199
Cdd:cd02509 144 PTRPET-GYGYIeageKLGGGVYRVKRFVEKPDLetakeYLESgnyLWNSGIFLFRaktfleelkkhaPDIYEALEKALA 222

                       250
                ....*....|....*.
gi 45447090 200 RNQQDGQLEDSPGLWP 215
Cdd:cd02509 223 AAGTDDFLRLLEEAFA 238
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 295-349 4.99e-05

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: 41.41  E-value: 4.99e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 295 VAPSAVLGPNVSI-----GKGVTVGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVGR 349
Cdd:cd04652   2 VGENTQVGEKTSIkrsviGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGE 61
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 289-350 7.85e-05

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 43.86  E-value: 7.85e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45447090  289 IHPTAKVAPSAVL------GPNVSIGKGVTVGEGVRLRESIVLHGATLQEHTCVLHSivgwGSTVGRW 350
Cdd:PRK12461   2 IHPTAVIDPSAKLgsgveiGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQ----GAVVGDE 65
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 289-338 2.93e-04

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 41.72  E-value: 2.93e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 45447090  289 IHPTAKVAPSAVLGPNVSIGKGVTVGEGVRLRES----IVLHGATLQEhTCVLH 338
Cdd:PRK13627  13 VHPTAFVHPSAVLIGDVIVGAGVYIGPLASLRGDygrlIVQAGANLQD-GCIMH 65
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 4-55 3.01e-04

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: 41.74  E-value: 3.01e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 45447090   4 AVILIGGpqKGTRFrplSFEVPKPLFPVAGVPMIQHHIEACAQVPGMQEILL 55
Cdd:cd02516   3 AIILAAG--SGSRM---GADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVV 49
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
2-243 3.92e-04

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 42.18  E-value: 3.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090    2 LKAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAqVPGMQEILLIGFYQPDEPLTQFLEAAQQEFNLPVR 81
Cdd:PRK10122   4 LKAVIPVAG--LGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIV-AAGIKEIVLVTHASKNAVENHFDTSYELESLLEQR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090   82 Y-------LQEFAPLGTG---------GGLYHfrdQILAGSP----EAFFVLNADVCSD--------FPLSAML----EA 129
Cdd:PRK10122  81 VkrqllaeVQSICPPGVTimnvrqgqpLGLGH---SILCARPaigdNPFVVVLPDVVIDdasadplrYNLAAMIarfnET 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090  130 HRRQ----RHPFLLLGTTANRTQSlnygcIVENP-QTHEVLHYVEK---PSTFISDIINCGIYLFSPEALKPLRDVfqrn 201
Cdd:PRK10122 158 GRSQvlakRMPGDLSEYSVIQTKE-----PLDREgKVSRIVEFIEKpdqPQTLDSDLMAVGRYVLSADIWPELERT---- 228

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 45447090  202 qqdgqledSPGLWpgaGTIRLeQDVFSALAGQGQIYVHLTDG 243
Cdd:PRK10122 229 --------EPGAW---GRIQL-TDAIAELAKKQSVDAMLMTG 258
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 282-354 4.66e-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: 40.47  E-value: 4.66e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 282 WIRGNVYIHPTAKVAPSAVLGPNVS-------------------------------------IGKGVTVGEGVrlresiV 324
Cdd:cd04645   1 EIDPSAFIAPNATVIGDVTLGEGSSvwfgavlrgdvnpirigertniqdgsvlhvdpgyptiIGDNVTVGHGA------V 74

                        90       100       110
                ....*....|....*....|....*....|.
gi 45447090 325 LHGATLQEHTCV-LHSIVGWGSTVGRWARVE 354
Cdd:cd04645  75 LHGCTIGDNCLIgMGAIILDGAVIGKGSIVA 105
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 300-349 4.95e-04

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: 38.71  E-value: 4.95e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45447090 300 VLGPNVSIGK-----------GVTVGEGVRLRESIVLHGATLQEHtCVL--HSIVGWGSTVGR 349
Cdd:cd05787  18 VIGRNCKIGKnvvidnsyiwdDVTIEDGCTIHHSIVADGAVIGKG-CTIppGSLISFGVVIGD 79
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 281-354 5.20e-04

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 40.40  E-value: 5.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 281 PWIRGNVYIHPTAK------------VAPSAVL---------GPN----------------VSIGKGVTVGEGVrlresi 323
Cdd:COG0663  11 PQIHPSAFVAPTAVvigdvtigedvsVWPGAVLrgdvgpiriGEGsniqdgvvlhvdpgypLTIGDDVTIGHGA------ 84

                        90       100       110
                ....*....|....*....|....*....|.
gi 45447090 324 VLHGATLQEhtcvlHSIVGWGSTVGRWARVE 354
Cdd:COG0663  85 ILHGCTIGD-----NVLIGMGAIVLDGAVIG 110
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 2-57 7.87e-04

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: 40.18  E-value: 7.87e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 45447090   2 LKAVILIGGpqKGTRFRplsfeVPKPLFPVAGVPMIQHHIEACAQVPGmqEILLIG 57
Cdd:COG0746   5 ITGVILAGG--RSRRMG-----QDKALLPLGGRPLLERVLERLRPQVD--EVVIVA 51
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 300-354 1.50e-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: 37.17  E-value: 1.50e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45447090 300 VLGPNVSIGKGVTV-----------GEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVGRWARVE 354
Cdd:cd05787   1 VIGRGTSIGEGTTIknsvigrnckiGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIP 66
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 287-355 1.65e-03

Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 37.23  E-value: 1.65e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45447090 287 VYIHPTAKVAPSAVLGPNVSIGKGVTVGEGVRLResivlhgaTLQEHTCVLHSIVGWGSTVGRWARVEG 355
Cdd:cd00208   1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIG--------AATGPNEKNPTIIGDNVEIGANAVIHG 61
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 307-383 2.39e-03

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: 36.84  E-value: 2.39e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45447090 307 IGKGVTVGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVGRWARVEGTPSDPNPN-DPRARMDSESLFKDGKLLPA 383
Cdd:cd03356   2 IGESTVIGENAIIKNSVIGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAViGENVRVVNLCIIGDDVVVED 79
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-56 2.45e-03

Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 39.66  E-value: 2.45e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 45447090   1 MLKAVILIGGpqKGTRFRPLSFEV-PKPLFPVAG-VPMIQHHIEACAQVPGMQEILLI 56
Cdd:COG0836   2 MIYPVILAGG--SGTRLWPLSRESyPKQFLPLLGeKSLLQQTVERLAGLVPPENILVV 57
PRK13368 PRK13368
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 26-55 2.99e-03

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 184007  Cd Length: 238  Bit Score: 39.18  E-value: 2.99e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 45447090   26 KPLFPVAGVPMIQHHIEACAQVPGMQEILL 55
Cdd:PRK13368  19 KPLLDILGKPMIQHVYERAAQAAGVEEVYV 48
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 283-348 3.95e-03

Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity, however, some subfamilies in this hierarchy also show activities related to ion transport or translation initiation. Many are trimeric in their active forms.


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 36.07  E-value: 3.95e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45447090 283 IRGNVYIHPTAKVAPSAVLGPNVSIGKGVTVG---EGVRLRESIVLHGATLQEHTCVL-------HSIVGWGSTVG 348
Cdd:cd00208   3 IGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGaatGPNEKNPTIIGDNVEIGANAVIHggvkigdNAVIGAGAVVT 78
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
286-315 3.95e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 34.62  E-value: 3.95e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 45447090   286 NVYIHPTAKVAPSAVLGPNVSIGKGVTVGE 315
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 298-353 4.47e-03

UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of 3-hydroxymyristic acid or 3-hydroxy-arachidic acid, depending on the organism, from the acyl carrier protein (ACP) to UDP-3-O-acyl-glucosamine to produce UDP-2,3-diacyl-GlcNAc. This constitutes the third step in the lipid A biosynthetic pathway in Gram-negative bacteria. LpxD is a homotrimer, with each subunit consisting of a novel combination of an N-terminal uridine-binding domain, a core lipid-binding left-handed parallel beta helix (LbH) domain, and a C-terminal alpha-helical extension. The LbH domain contains 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X).


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 38.16  E-value: 4.47e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 298 SAVLGPNVSIGKGVTVGEGVRLRESIVLHGatlqehtcvlHSIVGWGSTVGR----WARV 353
Cdd:cd03352   1 SAKIGENVSIGPNAVIGEGVVIGDGVVIGP----------GVVIGDGVVIGDdcviHPNV 50
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 281-347 5.58e-03

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


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 37.61  E-value: 5.58e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45447090 281 PWIRGNVYIHPTAKVAPSAVLGPNVSIGKGV----------TVGEGVRLRESIVLHG-----ATLQEHTCVLH------- 338
Cdd:cd00710   3 PVIDPSAYVHPTAVVIGDVIIGDNVFVGPGAsiradegtpiIIGANVNIQDGVVIHAlegysVWIGKNVSIAHgaivhgp 82

                        90
                ....*....|....*
gi 45447090 339 ------SIVGWGSTV 347
Cdd:cd00710  83 ayigdnCFIGFRSVV 97
LbH_unknown cd05635
Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group ...
 283-343 6.05e-03

Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group are uncharacterized bacterial proteins containing a LbH domain with 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: 100059 [Multi-domain]  Cd Length: 101  Bit Score: 36.10  E-value: 6.05e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45447090 283 IRGNVYIHPTAKVAPSAVLGPNVSIGKGVTVGEGVrlrESIVLHGATLQEHTCVL-HSIVG-W 343
Cdd:cd05635  26 IEGPVYIGPGSRVKMGARIYGNTTIGPTCKIGGEV---EDSIIEGYSNKQHDGFLgHSYLGsW 85
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
280-308 6.86e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.85  E-value: 6.86e-03
                          10        20
                  ....*....|....*....|....*....
gi 45447090   280 GPWIRGNVYIHPTAKVAPSAVLGPNVSIG 308
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIG 29
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 5-55 9.23e-03

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: 37.42  E-value: 9.23e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 45447090   5 VILIGGpqKGTRFRPlsfEVPKPLFPVAGVPMIQHHIEACAQVPGMQEILL 55
Cdd:COG1211   1 IIPAAG--SGSRMGA---GIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVV 46
 
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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