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Conserved domains on  [gi|1985656924|emb|CAE5973377|]
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unnamed protein product [Arabidopsis arenosa]

Protein Classification

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 ...
 8-264 1.62e-157

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: 449.40  E-value: 1.62e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   8 AVIMVGGPTKGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKISNLAQIFLIGFYEEREFALYVSSISNELKIPVRYLK 87
Cdd:cd06428     1 AVILVGGPQKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  88 EDKPHGSAGALYYFRDRIMEEKPSHVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVSAEAASQFGELIADPDTKEL 167
Cdd:cd06428    81 EYKPLGTAGGLYHFRDQILAGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEASREQASNYGCIVEDPSTGEV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 168 LHYTEKPETFVSDLINCGVYVFTSDIFNAIEEVYSQIRDASSNYQSATRSVPADFVRLDQDILSPLAGKKQLYTYENKDF 247
Cdd:cd06428   161 LHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNREGRAEVIRLEQDVLTPLAGSGKLYVYKTDDF 240

                         250
                  ....*....|....*..
gi 1985656924 248 WEQIKTPGKSLKCSALY 264
Cdd:cd06428   241 WSQIKTAGSAIYANRLY 257
PLN00152 PLN00152
DNA-directed RNA polymerase; Provisional
 409-539 1.26e-67

DNA-directed RNA polymerase; Provisional


:

Pssm-ID: 177755  Cd Length: 130  Bit Score: 214.35  E-value: 1.26e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 409 DYNEVDdLGYEDEPVEPEIEEGVEEDADIKENDDVNGEPMETEDKVETEPVQRPRKTSKFMTKYERARILGTRALQISMN 488
Cdd:PLN00152    1 DYNDMD-MGYEDEPSEPEIEEGAEEDSESNNNDEVKGSIGENEDKEEQEPVQRPRKTTPYMTKYERARILGTRALQISMN 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1985656924 489 APVMVELEGETDPLEIAMKELRQRKIPFTIRRYLPDGSFEEWGVDELIVED 539
Cdd:PLN00152   80 APVMVELEGETDPLEIAMKELRERKIPFTIRRYLPDGSYEDWGVDELIVED 130
LbetaH super family cl00160
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 294-381 1.06e-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: 94.91  E-value: 1.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 294 IHPSVKLHPTAKIGPNVSISANVRVGPGVRLISCIILDDVEIKDNAVVINSIIGWKSSIGRWSRVQasgdynerlGITIL 373
Cdd:cd05824     2 IDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLE---------NVTVL 72


                  ....*...
gi 1985656924 374 GEAVTVED 381
Cdd:cd05824    73 GDDVTIKD 80
 
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 ...
 8-264 1.62e-157

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: 449.40  E-value: 1.62e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   8 AVIMVGGPTKGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKISNLAQIFLIGFYEEREFALYVSSISNELKIPVRYLK 87
Cdd:cd06428     1 AVILVGGPQKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  88 EDKPHGSAGALYYFRDRIMEEKPSHVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVSAEAASQFGELIADPDTKEL 167
Cdd:cd06428    81 EYKPLGTAGGLYHFRDQILAGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEASREQASNYGCIVEDPSTGEV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 168 LHYTEKPETFVSDLINCGVYVFTSDIFNAIEEVYSQIRDASSNYQSATRSVPADFVRLDQDILSPLAGKKQLYTYENKDF 247
Cdd:cd06428   161 LHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNREGRAEVIRLEQDVLTPLAGSGKLYVYKTDDF 240

                         250
                  ....*....|....*..
gi 1985656924 248 WEQIKTPGKSLKCSALY 264
Cdd:cd06428   241 WSQIKTAGSAIYANRLY 257
PLN00152 PLN00152
DNA-directed RNA polymerase; Provisional
 409-539 1.26e-67

DNA-directed RNA polymerase; Provisional


Pssm-ID: 177755  Cd Length: 130  Bit Score: 214.35  E-value: 1.26e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 409 DYNEVDdLGYEDEPVEPEIEEGVEEDADIKENDDVNGEPMETEDKVETEPVQRPRKTSKFMTKYERARILGTRALQISMN 488
Cdd:PLN00152    1 DYNDMD-MGYEDEPSEPEIEEGAEEDSESNNNDEVKGSIGENEDKEEQEPVQRPRKTTPYMTKYERARILGTRALQISMN 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1985656924 489 APVMVELEGETDPLEIAMKELRQRKIPFTIRRYLPDGSFEEWGVDELIVED 539
Cdd:PLN00152   80 APVMVELEGETDPLEIAMKELRERKIPFTIRRYLPDGSYEDWGVDELIVED 130
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 8-254 1.08e-38

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: 141.83  E-value: 1.08e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   8 AVIMVGGptKGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKiSNLAQIFLIGFYEEREFALYVSSISnELKIPVRYLK 87
Cdd:COG1208     2 AVILAGG--LGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAA-AGITEIVINVGYLAEQIEEYFGDGS-RFGVRITYVD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  88 EDKPHGSAGALYYFRDRIMEEkpsHVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVsaEAASQFGELIADPDTKeL 167
Cdd:COG1208    78 EGEPLGTGGALKRALPLLGDE---PFLVLNGDILTDLDLAALLAFHREKGADATLALVPV--PDPSRYGVVELDGDGR-V 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 168 LHYTEKPETFVSDLINCGVYVFTSDIFNAIEEvysqirdassnyqsatrSVPADFVrldqDILSPLAGKKQLYTYENKDF 247
Cdd:COG1208   152 TRFVEKPEEPPSNLINAGIYVLEPEIFDYIPE-----------------GEPFDLE----DLLPRLIAEGRVYGYVHDGY 210


                  ....*..
gi 1985656924 248 WEQIKTP 254
Cdd:COG1208   211 WLDIGTP 217
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 8-347 7.97e-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: 7.97e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   8 AVIMVGGptKGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKISNLAQIFLIGfYEEREFALYVSSISnELKIPVRYLK 87
Cdd:TIGR03992   3 AVILAAG--KGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVG-YGKEKVREYFGDGS-RGGVPIEYVV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  88 EDKPHGSAGALYYFRDRIMEEkpshVFLLNCDVCCSFP-LQGILDAHRryggiGTMLVIKVsaEAASQFGELIADPDT-K 165
Cdd:TIGR03992  79 QEEQLGTADALGSAKEYVDDE----FLVLNGDVLLDSDlLERLIRAEA-----PAIAVVEV--DDPSDYGVVETDGGRvT 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 166 ELLhytEKPETFVSDLINCGVYVFTSDIFNAIEEVYSQIRDassNYQSAtrsvpadfvrldqDILSPLAGKKQLYTYENK 245
Cdd:TIGR03992 148 GIV---EKPENPPSNLINAGIYLFSPEIFELLEKTKLSPRG---EYELT-------------DALQLLIDEGKVKAVELD 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 246 DFWEQIKTPGKSLKCSALYLSQFR-------QTSPHILAS---GDGTNRKPN--IIGDVYIHPSVKLHPTAKIGPNVSIS 313
Cdd:TIGR03992 209 GFWLDVGRPWDLLDANEALLDNLEpriegtvEENVTIKGPvviGEGAVIRSGtyIEGPVYIGKNCDIGPNAYIRPYTVIG 288

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1985656924 314 ANVRVGPGVRLISCIILDDVEIKDNAVVINSIIG 347
Cdd:TIGR03992 289 NNVHIGNAVEIKNSIIMEGTKIPHLSYVGDSVIG 322
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 7-202 1.45e-27

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: 111.19  E-value: 1.45e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   7 VAVIMVGGptKGTRFRPLSFNTPKPLIPLAGQ-PMIHHPISACKKISNLAQIFLIGFYEEREFALYVSSISnELKIPVRY 85
Cdd:pfam00483   1 KAIILAGG--SGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGS-KFGVQITY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  86 LKEDKPHGSAGALYYFRDRIMEEKpSHVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVSAEAASQFGELIADPDTK 165
Cdd:pfam00483  78 ALQPEGKGTAPAVALAADFLGDEK-SDVLVLGGDHIYRMDLEQAVKFHIEKAADATVTFGIVPVEPPTGYGVVEFDDNGR 156

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1985656924 166 eLLHYTEKPETFV-SDLINCGVYVFTSDIFNAIEEVYS 202
Cdd:pfam00483 157 -VIRFVEKPKLPKaSNYASMGIYIFNSGVLDFLAKYLE 193
LbH_M1P_guanylylT_C cd05824
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 294-381 1.06e-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: 94.91  E-value: 1.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 294 IHPSVKLHPTAKIGPNVSISANVRVGPGVRLISCIILDDVEIKDNAVVINSIIGWKSSIGRWSRVQasgdynerlGITIL 373
Cdd:cd05824     2 IDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLE---------NVTVL 72


                  ....*...
gi 1985656924 374 GEAVTVED 381
Cdd:cd05824    73 GDDVTIKD 80
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 5-383 4.02e-13

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 71.05  E-value: 4.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   5 KVVAVIMVGGptKGTRFRPLSFNTPKPLIPLAGQ-PMIHHPISACKKiSNLAQIFLIGFYEEREFALYVSS--------I 75
Cdd:PRK05293    3 EMLAMILAGG--QGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCAN-SGIDTVGVLTQYQPLELNNHIGIgspwdldrI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  76 SNELKIPVRYLKEDKPH---GSAGALYYFRDRIMEEKPSHVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVSAEAA 152
Cdd:PRK05293   80 NGGVTILPPYSESEGGKwykGTAHAIYQNIDYIDQYDPEYVLILSGDHIYKMDYDKMLDYHKEKEADVTIAVIEVPWEEA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 153 SQFGELIADPDTkELLHYTEKPETFVSDLINCGVYVFTSDIfnaIEEVYsqIRDASSNYQSatrsvpADFvrlDQDIL-S 231
Cdd:PRK05293  160 SRFGIMNTDENM-RIVEFEEKPKNPKSNLASMGIYIFNWKR---LKEYL--IEDEKNPNSS------HDF---GKNVIpL 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 232 PLAGKKQLYTYENKDFWEQIKT-------------PGKSLKcsaLYLSQFRQTS------PHILAsgDGTNRKPNIIGD- 291
Cdd:PRK05293  225 YLEEGEKLYAYPFKGYWKDVGTieslweanmellrPENPLN---LFDRNWRIYSvnpnlpPQYIA--ENAKVKNSLVVEg 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 292 VYIHPSVKlhptakigpNVSISANVRVGPGVRLISCIILDDVEIKDNAVVINSIIGWKSSIGRWSRVQASGDynerlGIT 371
Cdd:PRK05293  300 CVVYGTVE---------HSVLFQGVQVGEGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVIIGGGKE-----VIT 365

                         410
                  ....*....|..
gi 1985656924 372 ILGEAVTVEDEV 383
Cdd:PRK05293  366 VIGENEVIGVGT 377
RNA_pol_Rpb6 pfam01192
RNA polymerase Rpb6; Rpb6 is an essential subunit in the eukaryotic polymerases Pol I, II and ...
 463-515 2.17e-10

RNA polymerase Rpb6; Rpb6 is an essential subunit in the eukaryotic polymerases Pol I, II and III. This family also contains the bacterial equivalent to Rpb6, the omega subunit. Rpb6 and omega are structurally conserved and both function in polymerase assembly.


Pssm-ID: 426112  Cd Length: 52  Bit Score: 55.99  E-value: 2.17e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1985656924 463 RKTSKFMTKYERARILGTRALQISMNAPVMVELEGEtDPLEIAMKELRQRKIP 515
Cdd:pfam01192   1 DLLKKVDNRYELVVIAAKRARQLSMGAPPIKLDSFD-KPVVIALREIAEGKIP 52
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 293-347 8.39e-10

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: 60.42  E-value: 8.39e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1985656924 293 YIHPSVKLHPTAKIGPNVSISANVRVGPGVRLIS-CIILDDVEIKDNA-----VVI--NSIIG 347
Cdd:COG1044   104 VIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPgVVIGDGVVIGDDCvlhpnVTIyeRCVIG 166
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 294-388 1.16e-09

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 60.15  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 294 IHPSVKLHPTAKIGPNVSISANVRVGPGvrlisciilddVEIKDNaVVI--NSIIGWKSSIGRWSRVQAsgdynerlGIT 371
Cdd:PRK00892  103 IHPSAVIDPSAKIGEGVSIGPNAVIGAG-----------VVIGDG-VVIgaGAVIGDGVKIGADCRLHA--------NVT 162

                          90       100
                  ....*....|....*....|..
gi 1985656924 372 IlGEAVTVEDEV-----AVIGS 388
Cdd:PRK00892  163 I-YHAVRIGNRViihsgAVIGS 183
RpoZ COG1758
DNA-directed RNA polymerase, subunit K/omega [Transcription]; DNA-directed RNA polymerase, ...
 471-520 8.29e-04

DNA-directed RNA polymerase, subunit K/omega [Transcription]; DNA-directed RNA polymerase, subunit K/omega is part of the Pathway/BioSystem: RNA polymerase


Pssm-ID: 441364  Cd Length: 64  Bit Score: 37.85  E-value: 8.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1985656924 471 KYERARILGTRALQISMNAPVMVELEGEtDPLEIAMKELRQRKIPFTIRR 520
Cdd:COG1758    16 RYELVLLAAKRARQLAEGAEPLVEPDSD-KPVVIALREIAEGKITIEILE 64
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 301-358 2.50e-03

acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes LpxA, an enzyme for the biosynthesis of lipid A, a component oflipopolysaccharide (LPS) in the outer membrane outer leaflet of most Gram-negative bacteria. Some differences are found between lipid A of different species, but this protein represents the first step (from UDP-N-acetyl-D-glucosamine) and appears to be conserved in function. Proteins from this family contain many copies of the bacterial transferase hexapeptide repeat (pfam00132). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 39.94  E-value: 2.50e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 301 HPTAKIGPNVSISANVRVGPgvrliSCIILDDVEIKDNaVVINS--IIGWKSSIGRWSRV 358
Cdd:TIGR01852   2 HPTAIIEPGAEIGENVEIGP-----FCIVGPGVKIGDG-VELKShvVILGHTTIGEGTRI 55
 
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 ...
 8-264 1.62e-157

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: 449.40  E-value: 1.62e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   8 AVIMVGGPTKGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKISNLAQIFLIGFYEEREFALYVSSISNELKIPVRYLK 87
Cdd:cd06428     1 AVILVGGPQKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  88 EDKPHGSAGALYYFRDRIMEEKPSHVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVSAEAASQFGELIADPDTKEL 167
Cdd:cd06428    81 EYKPLGTAGGLYHFRDQILAGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEASREQASNYGCIVEDPSTGEV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 168 LHYTEKPETFVSDLINCGVYVFTSDIFNAIEEVYSQIRDASSNYQSATRSVPADFVRLDQDILSPLAGKKQLYTYENKDF 247
Cdd:cd06428   161 LHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNREGRAEVIRLEQDVLTPLAGSGKLYVYKTDDF 240

                         250
                  ....*....|....*..
gi 1985656924 248 WEQIKTPGKSLKCSALY 264
Cdd:cd06428   241 WSQIKTAGSAIYANRLY 257
PLN00152 PLN00152
DNA-directed RNA polymerase; Provisional
 409-539 1.26e-67

DNA-directed RNA polymerase; Provisional


Pssm-ID: 177755  Cd Length: 130  Bit Score: 214.35  E-value: 1.26e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 409 DYNEVDdLGYEDEPVEPEIEEGVEEDADIKENDDVNGEPMETEDKVETEPVQRPRKTSKFMTKYERARILGTRALQISMN 488
Cdd:PLN00152    1 DYNDMD-MGYEDEPSEPEIEEGAEEDSESNNNDEVKGSIGENEDKEEQEPVQRPRKTTPYMTKYERARILGTRALQISMN 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1985656924 489 APVMVELEGETDPLEIAMKELRQRKIPFTIRRYLPDGSFEEWGVDELIVED 539
Cdd:PLN00152   80 APVMVELEGETDPLEIAMKELRERKIPFTIRRYLPDGSYEDWGVDELIVED 130
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 8-265 2.51e-48

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: 167.39  E-value: 2.51e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   8 AVIMVGGptKGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKIsNLAQIFLIGFYEEREFALYVSSISNELKIPVRYLK 87
Cdd:cd06425     3 ALILVGG--YGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKA-GVKEIILAVNYRPEDMVPFLKEYEKKLGIKITFSI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  88 EDKPHGSAGALYYFRDRImeEKPSHVFL-LNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVsaEAASQFGELIADPDTKE 166
Cdd:cd06425    80 ETEPLGTAGPLALARDLL--GDDDEPFFvLNSDVICDFPLAELLDFHKKHGAEGTILVTKV--EDPSKYGVVVHDENTGR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 167 LLHYTEKPETFVSDLINCGVYVFTSDIFNAIEEvysqiRDASsnyqsatrsvpadfvrLDQDILSPLAGKKQLYTYENKD 246
Cdd:cd06425   156 IERFVEKPKVFVGNKINAGIYILNPSVLDRIPL-----RPTS----------------IEKEIFPKMASEGQLYAYELPG 214

                         250
                  ....*....|....*....
gi 1985656924 247 FWEQIKTPGKSLKCSALYL 265
Cdd:cd06425   215 FWMDIGQPKDFLKGMSLYL 233
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 8-251 4.77e-46

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: 160.82  E-value: 4.77e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   8 AVIMVGGptKGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKIsNLAQIFLIGFYEEREFALYVSSISNeLKIPVRYLK 87
Cdd:cd04181     1 AVILAAG--KGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARA-GIDEIILVVGYLGEQIEEYFGDGSK-FGVNIEYVV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  88 EDKPHGSAGALYYFRDRIMEEkpsHVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVsaEAASQFGELIADpDTKEL 167
Cdd:cd04181    77 QEEPLGTAGAVRNAEDFLGDD---DFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEV--EDPSRYGVVELD-DDGRV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 168 LHYTEKPETFVSDLINCGVYVFTSDIFNAIEEVYSQIRDASsnyqsatrsvpadfvrldQDILSPLAGKKQLYTYENKDF 247
Cdd:cd04181   151 TRFVEKPTLPESNLANAGIYIFEPEILDYIPEILPRGEDEL------------------TDAIPLLIEEGKVYGYPVDGY 212


                  ....
gi 1985656924 248 WEQI 251
Cdd:cd04181   213 WLDI 216
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 8-254 1.08e-38

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: 141.83  E-value: 1.08e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   8 AVIMVGGptKGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKiSNLAQIFLIGFYEEREFALYVSSISnELKIPVRYLK 87
Cdd:COG1208     2 AVILAGG--LGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAA-AGITEIVINVGYLAEQIEEYFGDGS-RFGVRITYVD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  88 EDKPHGSAGALYYFRDRIMEEkpsHVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVsaEAASQFGELIADPDTKeL 167
Cdd:COG1208    78 EGEPLGTGGALKRALPLLGDE---PFLVLNGDILTDLDLAALLAFHREKGADATLALVPV--PDPSRYGVVELDGDGR-V 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 168 LHYTEKPETFVSDLINCGVYVFTSDIFNAIEEvysqirdassnyqsatrSVPADFVrldqDILSPLAGKKQLYTYENKDF 247
Cdd:COG1208   152 TRFVEKPEEPPSNLINAGIYVLEPEIFDYIPE-----------------GEPFDLE----DLLPRLIAEGRVYGYVHDGY 210


                  ....*..
gi 1985656924 248 WEQIKTP 254
Cdd:COG1208   211 WLDIGTP 217
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 8-347 7.97e-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: 7.97e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   8 AVIMVGGptKGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKISNLAQIFLIGfYEEREFALYVSSISnELKIPVRYLK 87
Cdd:TIGR03992   3 AVILAAG--KGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVG-YGKEKVREYFGDGS-RGGVPIEYVV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  88 EDKPHGSAGALYYFRDRIMEEkpshVFLLNCDVCCSFP-LQGILDAHRryggiGTMLVIKVsaEAASQFGELIADPDT-K 165
Cdd:TIGR03992  79 QEEQLGTADALGSAKEYVDDE----FLVLNGDVLLDSDlLERLIRAEA-----PAIAVVEV--DDPSDYGVVETDGGRvT 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 166 ELLhytEKPETFVSDLINCGVYVFTSDIFNAIEEVYSQIRDassNYQSAtrsvpadfvrldqDILSPLAGKKQLYTYENK 245
Cdd:TIGR03992 148 GIV---EKPENPPSNLINAGIYLFSPEIFELLEKTKLSPRG---EYELT-------------DALQLLIDEGKVKAVELD 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 246 DFWEQIKTPGKSLKCSALYLSQFR-------QTSPHILAS---GDGTNRKPN--IIGDVYIHPSVKLHPTAKIGPNVSIS 313
Cdd:TIGR03992 209 GFWLDVGRPWDLLDANEALLDNLEpriegtvEENVTIKGPvviGEGAVIRSGtyIEGPVYIGKNCDIGPNAYIRPYTVIG 288

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1985656924 314 ANVRVGPGVRLISCIILDDVEIKDNAVVINSIIG 347
Cdd:TIGR03992 289 NNVHIGNAVEIKNSIIMEGTKIPHLSYVGDSVIG 322
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 7-202 1.45e-27

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: 111.19  E-value: 1.45e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   7 VAVIMVGGptKGTRFRPLSFNTPKPLIPLAGQ-PMIHHPISACKKISNLAQIFLIGFYEEREFALYVSSISnELKIPVRY 85
Cdd:pfam00483   1 KAIILAGG--SGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGS-KFGVQITY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  86 LKEDKPHGSAGALYYFRDRIMEEKpSHVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVSAEAASQFGELIADPDTK 165
Cdd:pfam00483  78 ALQPEGKGTAPAVALAADFLGDEK-SDVLVLGGDHIYRMDLEQAVKFHIEKAADATVTFGIVPVEPPTGYGVVEFDDNGR 156

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1985656924 166 eLLHYTEKPETFV-SDLINCGVYVFTSDIFNAIEEVYS 202
Cdd:pfam00483 157 -VIRFVEKPKLPKaSNYASMGIYIFNSGVLDFLAKYLE 193
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 8-254 1.94e-26

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: 107.25  E-value: 1.94e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   8 AVIMVGGptKGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKK--ISNLaqIFLIGF--------YEEREFALyvssisn 77
Cdd:cd06915     1 AVILAGG--LGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARqgISRI--VLSVGYlaeqieeyFGDGYRGG------- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  78 elkIPVRYLKEDKPHGSAGALYYFRDRIMEEkpsHVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVsaEAASQFGE 157
Cdd:cd06915    70 ---IRIYYVIEPEPLGTGGAIKNALPKLPED---QFLVLNGDTYFDVDLLALLAALRASGADATMALRRV--PDASRYGN 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 158 LIADPDtKELLHYTEKPETFVSDLINCGVYVFTSDIFNAIeevysqirdassnyqsatrsvPADFVRLDQDILSPLAGKK 237
Cdd:cd06915   142 VTVDGD-GRVIAFVEKGPGAAPGLINGGVYLLRKEILAEI---------------------PADAFSLEADVLPALVKRG 199

                         250
                  ....*....|....*..
gi 1985656924 238 QLYTYENKDFWEQIKTP 254
Cdd:cd06915   200 RLYGFEVDGYFIDIGIP 216
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 8-199 2.76e-24

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: 101.49  E-value: 2.76e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   8 AVIMVGGptKGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKK--ISNLAQIflIGFYEErEFALYVSSISNeLKIPVRY 85
Cdd:cd04189     3 GLILAGG--KGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREagIEDIGIV--VGPTGE-EIKEALGDGSR-FGVRITY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  86 LKEDKPHGSAGALYYFRDRImEEKPSHVFLlnCDVCCSFPLQGILDAHRRYGGIGTMLVIKVsaEAASQFGelIADPDTK 165
Cdd:cd04189    77 ILQEEPLGLAHAVLAARDFL-GDEPFVVYL--GDNLIQEGISPLVRDFLEEDADASILLAEV--EDPRRFG--VAVVDDG 149

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1985656924 166 ELLHYTEKPETFVSDLINCGVYVFTSDIFNAIEE 199
Cdd:cd04189   150 RIVRLVEKPKEPPSNLALVGVYAFTPAIFDAISR 183
rpoK PRK01099
DNA-directed RNA polymerase subunit K; Provisional
 470-524 1.05e-23

DNA-directed RNA polymerase subunit K; Provisional


Pssm-ID: 179220  Cd Length: 62  Bit Score: 94.23  E-value: 1.05e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1985656924 470 TKYERARILGTRALQISMNAPVMVELEGETDPLEIAMKELRQRKIPFTIRRYLPD 524
Cdd:PRK01099    8 TRFERARIIGARALQISMGAPVLIDIPESTDPLDIAEEEFKRGVLPITVKRPLPN 62
LbH_M1P_guanylylT_C cd05824
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 294-381 1.06e-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: 94.91  E-value: 1.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 294 IHPSVKLHPTAKIGPNVSISANVRVGPGVRLISCIILDDVEIKDNAVVINSIIGWKSSIGRWSRVQasgdynerlGITIL 373
Cdd:cd05824     2 IDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLE---------NVTVL 72


                  ....*...
gi 1985656924 374 GEAVTVED 381
Cdd:cd05824    73 GDDVTIKD 80
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 8-199 1.49e-22

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: 96.04  E-value: 1.49e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   8 AVIMVGGptKGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKisnlaqiflIGFyeeREFALYVSSISNELK------- 80
Cdd:cd06426     1 VVIMAGG--KGTRLRPLTENTPKPMLKVGGKPILETIIDRFIA---------QGF---RNFYISVNYLAEMIEdyfgdgs 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  81 ---IPVRYLKEDKPHGSAGALyyfrdRIMEEKPSH-VFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVSAEAAsqFG 156
Cdd:cd06426    67 kfgVNISYVREDKPLGTAGAL-----SLLPEKPTDpFLVMNGDILTNLNYEHLLDFHKENNADATVCVREYEVQVP--YG 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1985656924 157 ELiaDPDTKELLHYTEKPE-TFvsdLINCGVYVFTSDIFNAIEE 199
Cdd:cd06426   140 VV--ETEGGRITSIEEKPThSF---LVNAGIYVLEPEVLDLIPK 178
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 5-347 5.25e-21

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 94.76  E-value: 5.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   5 KVVAVIMVGGptKGTRFRPLSFNTPKPLIPLAGQ-PMIHHPISACkkI-SNLAQIFLIGFYEEREFALYVSS-------- 74
Cdd:COG0448     1 KVLAIILAGG--RGSRLGPLTKDRAKPAVPFGGKyRIIDFPLSNC--VnSGIRRVGVLTQYKSHSLNDHIGSgkpwdldr 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  75 ISNELKIPVRYLKEDKPH---GSAGALYYFRDRIMEEKPSHVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVSAEA 151
Cdd:COG0448    77 KRGGVFILPPYQQREGEDwyqGTADAVYQNLDFIERSDPDYVLILSGDHIYKMDYRQMLDFHIESGADITVACIEVPREE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 152 ASQFGELIADPDTKeLLHYTEKPETFVSDLINCGVYVFTSDIFnaIEEVysqIRDASSNYQsatrsvpaDFVRldqDILS 231
Cdd:COG0448   157 ASRFGVMEVDEDGR-ITEFEEKPKDPKSALASMGIYVFNKDVL--IELL---EEDAPNSSH--------DFGK---DIIP 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 232 PLAGKKQLYTYENKDFWEQIKTPgkslkcSALYlsqfrQTSPHILasgdgtnrKPNIIGDVY-----IHPSVKLHPTAKI 306
Cdd:COG0448   220 RLLDRGKVYAYEFDGYWRDVGTI------DSYY-----EANMDLL--------DPEPEFNLYdpewpIYTKQKDLPPAKF 280

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1985656924 307 GPN-------VS-------------ISANVRVGPGVRLISCIILDDVEIKDNAVVINSIIG 347
Cdd:COG0448   281 VRGgkvknslVSngciisgtvensvLFRGVRVESGAVVENSVIMPGVVIGEGAVIENAIID 341
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 8-194 5.51e-19

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: 85.77  E-value: 5.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   8 AVIMVGGptKGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKiSNLAQIFLI-GFYEEREFALYVSSISNELKIPVR-- 84
Cdd:cd02507     3 AVVLADG--FGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEK-AGVEEVFVVcCEHSQAIIEHLLKSKWSSLSSKMIvd 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  85 --YLKEDKPHGSAGALYYFRDRImeekPSHVFLLNCDVCCSFPLQGILDAHR--RYGGIGTMLVIKVSA---EAASQFGE 157
Cdd:cd02507    80 viTSDLCESAGDALRLRDIRGLI----RSDFLLLSCDLVSNIPLSELLEERRkkDKNAIATLTVLLASPpvsTEQSKKTE 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1985656924 158 ---LIADPDT---KELLHYTEKPE------------------TFVSDLINCGVYVFTSDIF 194
Cdd:cd02507   156 eedVIAVDSKtqrLLLLHYEEDLDedleliirksllskhpnvTIRTDLLDCHIYICSPDVL 216
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 8-194 2.26e-18

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: 83.86  E-value: 2.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   8 AVIMVGGptKGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKISNLAQIFLIGFYEEREFALYVSSISNELKIPVRYLK 87
Cdd:cd04198     3 AVILAGG--GGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSFPLNLKQKLDEVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  88 E--DKPHGSAGALYYFRDRImeekPSHVFLLNCDVCCSFPLQGILDAHRRYGGIGTML-------VIKVSAEAASQFGE- 157
Cdd:cd04198    81 IvlDEDMGTADSLRHIRKKI----KKDFLVLSCDLITDLPLIELVDLHRSHDASLTVLlypppvsSEQKGGKGKSKKADe 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1985656924 158 --LIADPDTKELLHYTEKPE-------------------TFVSDLINCGVYVFTSDIF 194
Cdd:cd04198   157 rdVIGLDEKTQRLLFITSEEdldedlelrksllkrhprvTITTKLLDAHVYIFKRWVL 214
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 8-366 3.64e-18

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: 85.92  E-value: 3.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   8 AVIMVGGptKGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKIsNLAQIFLIGFYEEREFALYVSSISNELKIPVRYLK 87
Cdd:TIGR01208   2 ALILAAG--KGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEA-GITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  88 EDKPHGSAGALYYFRDrimeekpshvFLLNCDVCCSFPLQGILDAHRRY-------GGIGTMLVIKVsaEAASQFGelIA 160
Cdd:TIGR01208  79 QGEPLGLAHAVYTARD----------FLGDDDFVVYLGDNLIQDGISRFvksfeekDYDALILLTKV--RDPTAFG--VA 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 161 D-PDTKELLHYTEKPETFVSDLINCGVYVFTSDIFNAIeevySQIRDASSNYQSATrsvpadfvrldqDILSPLAGKKQL 239
Cdd:TIGR01208 145 VlEDGKRILKLVEKPKEPPSNLAVVGLYMFRPLIFEAI----KNIKPSWRGELEIT------------DAIQWLIEKGYK 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 240 YTYEN-KDFWEQIKTPGKSLKCSALYLSqfrQTSPHILasgdGTNRKPNIIGDVYIHPSVKL-----HPTAKIGPNVSIS 313
Cdd:TIGR01208 209 VGGSKvTGWWKDTGKPEDLLDANRLILD---EVEREVQ----GVDDESKIRGRVVVGEGAKIvnsviRGPAVIGEDCIIE 281

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 314 aNVRVGP------GVRLIS-----CIILDDVEIKDN-AVVINSIIGWKSSIGRWSRVQAS-----GDYNE 366
Cdd:TIGR01208 282 -NSYIGPytsigeGVVIRDaevehSIVLDESVIEGVqARIVDSVIGKKVRIKGNRRRPGDlrltiGDYSQ 350
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
8-200 1.32e-17

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 83.22  E-value: 1.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   8 AVIMVGGptKGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKkisnLAQI----FLIGFYEEREFALYVSSISnELKIPV 83
Cdd:COG1209     3 GIILAGG--SGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLM----LAGIreilIISTPEDGPQFERLLGDGS-QLGIKI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  84 RYLKEDKPHGSAGALYyfrdrIMEEkpshvFLLNCDVCCSF--------PLQGILDAHRRYGGIGTMLVIKVsaEAASQF 155
Cdd:COG1209    76 SYAVQPEPLGLAHAFI-----IAED-----FIGGDPVALVLgdnifygdGLSELLREAAARESGATIFGYKV--EDPERY 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1985656924 156 G--ELiaDPDTKeLLHYTEKPETFVSDLINCGVYVFTSDIFNAIEEV 200
Cdd:COG1209   144 GvvEF--DEDGR-VVSLEEKPKEPKSNLAVTGLYFYDNDVVEIAKNL 187
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 293-381 4.09e-16

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: 73.04  E-value: 4.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 293 YIHPSVKLHPTAKIGPNVsISANVRVGPGVRLISCIILDDVEIKDNAVVINSIIGWKSSIGRWSRVqasgdynerLGITI 372
Cdd:cd03356     1 LIGESTVIGENAIIKNSV-IGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRV---------VNLCI 70


                  ....*....
gi 1985656924 373 LGEAVTVED 381
Cdd:cd03356    71 IGDDVVVED 79
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 5-383 4.02e-13

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 71.05  E-value: 4.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   5 KVVAVIMVGGptKGTRFRPLSFNTPKPLIPLAGQ-PMIHHPISACKKiSNLAQIFLIGFYEEREFALYVSS--------I 75
Cdd:PRK05293    3 EMLAMILAGG--QGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCAN-SGIDTVGVLTQYQPLELNNHIGIgspwdldrI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  76 SNELKIPVRYLKEDKPH---GSAGALYYFRDRIMEEKPSHVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVSAEAA 152
Cdd:PRK05293   80 NGGVTILPPYSESEGGKwykGTAHAIYQNIDYIDQYDPEYVLILSGDHIYKMDYDKMLDYHKEKEADVTIAVIEVPWEEA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 153 SQFGELIADPDTkELLHYTEKPETFVSDLINCGVYVFTSDIfnaIEEVYsqIRDASSNYQSatrsvpADFvrlDQDIL-S 231
Cdd:PRK05293  160 SRFGIMNTDENM-RIVEFEEKPKNPKSNLASMGIYIFNWKR---LKEYL--IEDEKNPNSS------HDF---GKNVIpL 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 232 PLAGKKQLYTYENKDFWEQIKT-------------PGKSLKcsaLYLSQFRQTS------PHILAsgDGTNRKPNIIGD- 291
Cdd:PRK05293  225 YLEEGEKLYAYPFKGYWKDVGTieslweanmellrPENPLN---LFDRNWRIYSvnpnlpPQYIA--ENAKVKNSLVVEg 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 292 VYIHPSVKlhptakigpNVSISANVRVGPGVRLISCIILDDVEIKDNAVVINSIIGWKSSIGRWSRVQASGDynerlGIT 371
Cdd:PRK05293  300 CVVYGTVE---------HSVLFQGVQVGEGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVIIGGGKE-----VIT 365

                         410
                  ....*....|..
gi 1985656924 372 ILGEAVTVEDEV 383
Cdd:PRK05293  366 VIGENEVIGVGT 377
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 8-253 4.19e-12

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: 66.44  E-value: 4.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   8 AVIMVGGptKGTRFRPLSFNTPKPLIPLAGQPMIHHpisackkISNLAQ-------IFLIGF-----------YEEREFA 69
Cdd:cd02524     1 VVILAGG--LGTRLSEETELKPKPMVEIGGRPILWH-------IMKIYShyghndfILCLGYkghvikeyflnYFLHNSD 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  70 LYVSSISNELKIpvrylkedkpHGSA------------------GALYYFRDRIMEEKPshvFLLN-CDVCCSFPLQGIL 130
Cdd:cd02524    72 VTIDLGTNRIEL----------HNSDiedwkvtlvdtglntmtgGRLKRVRRYLGDDET---FMLTyGDGVSDVNINALI 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 131 DAHRRYGGIGTMLVIKvsaeAASQFGELIADPDTKeLLHYTEKPETfVSDLINCGVYVFTSDIFNAIEEvysqirdassn 210
Cdd:cd02524   139 EFHRSHGKLATVTAVH----PPGRFGELDLDDDGQ-VTSFTEKPQG-DGGWINGGFFVLEPEVFDYIDG----------- 201

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1985656924 211 yqsatrsvpaDFVRLDQDILSPLAGKKQLYTYENKDFWEQIKT 253
Cdd:cd02524   202 ----------DDTVFEREPLERLAKDGELMAYKHTGFWQCMDT 234
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 5-387 7.26e-12

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: 67.36  E-value: 7.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   5 KVVAVIMVGGptKGTRFRplSfNTPKPLIPLAGQPMIHHPISACKKIsNLAQIFLI-GFyeEREfalyvsSISNELK-IP 82
Cdd:COG1207     2 PLAVVILAAG--KGTRMK--S-KLPKVLHPLAGKPMLEHVLDAARAL-GPDRIVVVvGH--GAE------QVRAALAdLD 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  83 VRYLKEDKPHGSAGALYYFRDRImEEKPSHVFLLNCDVccsfPL------QGILDAHRRYGGIGTMLvikvSAEAA---- 152
Cdd:COG1207    68 VEFVLQEEQLGTGHAVQQALPAL-PGDDGTVLVLYGDV----PLiraetlKALLAAHRAAGAAATVL----TAELDdptg 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 153 ------SQFGELI-------ADPDTKELlhyTEkpetfvsdlINCGVYVF-TSDIFNAIEEVysqirdASSNyqsatrsv 218
Cdd:COG1207   139 ygrivrDEDGRVLriveekdATEEQRAI---RE---------INTGIYAFdAAALREALPKL------SNDN-------- 192

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 219 padfvrlDQ------DILSPLAGK-KQLYTYENKDFWE--------QiktpgksL-KCSALYlsQFRQTSPHILAsgdG- 281
Cdd:COG1207   193 -------AQgeyyltDVIAIARADgLKVAAVQPEDPWEvlgvndrvQ-------LaEAERIL--QRRIAERLMRA---Gv 253

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 282 TNRKPN--------IIG-DVYIHPSVKLHptakiGpNVSISANVRVGPGVRLISCIILDDVEIKdNAVVINSIIGWKSSI 352
Cdd:COG1207   254 TIIDPAttyidgdvEIGrDVVIDPNVILE-----G-KTVIGEGVVIGPNCTLKDSTIGDGVVIK-YSVIEDAVVGAGATV 326

                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1985656924 353 GRWSRVqasgdyneRLGiTILGEAVTVED--EV--AVIG 387
Cdd:COG1207   327 GPFARL--------RPG-TVLGEGVKIGNfvEVknSTIG 356
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 8-200 1.13e-11

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


Pssm-ID: 133020 [Multi-domain]  Cd Length: 229  Bit Score: 64.46  E-value: 1.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   8 AVIMVGGptKGTRFRplsFNTPKPLIPLAGQPMIHHPISACKKIsNLAQIFLIGFYEEREFALYVSsisnelKIPVRYLK 87
Cdd:cd02540     1 AVILAAG--KGTRMK---SDLPKVLHPLAGKPMLEHVLDAARAL-GPDRIVVVVGHGAEQVKKALA------NPNVEFVL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  88 EDKPHGSAGALYYFRDRImEEKPSHVFLLNCDVccsfPL------QGILDAHRRYGGIGTMLvikvSAEAA--SQFGELI 159
Cdd:cd02540    69 QEEQLGTGHAVKQALPAL-KDFEGDVLVLYGDV----PLitpetlQRLLEAHREAGADVTVL----TAELEdpTGYGRII 139

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1985656924 160 ADpDTKELLHYTE----KPETFVSDLINCGVYVF-TSDIFNAIEEV 200
Cdd:cd02540   140 RD-GNGKVLRIVEekdaTEEEKAIREVNAGIYAFdAEFLFEALPKL 184
RNA_pol_Rpb6 pfam01192
RNA polymerase Rpb6; Rpb6 is an essential subunit in the eukaryotic polymerases Pol I, II and ...
 463-515 2.17e-10

RNA polymerase Rpb6; Rpb6 is an essential subunit in the eukaryotic polymerases Pol I, II and III. This family also contains the bacterial equivalent to Rpb6, the omega subunit. Rpb6 and omega are structurally conserved and both function in polymerase assembly.


Pssm-ID: 426112  Cd Length: 52  Bit Score: 55.99  E-value: 2.17e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1985656924 463 RKTSKFMTKYERARILGTRALQISMNAPVMVELEGEtDPLEIAMKELRQRKIP 515
Cdd:pfam01192   1 DLLKKVDNRYELVVIAAKRARQLSMGAPPIKLDSFD-KPVVIALREIAEGKIP 52
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 8-208 3.74e-10

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: 60.32  E-value: 3.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   8 AVIMVGGptKGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKIsNLAQIFLI-GFYEE--REFA---LYVSSISNElki 81
Cdd:cd02523     1 AIILAAG--RGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEA-GIDDIVIVtGYKKEqiEELLkkyPNIKFVYNP--- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  82 pvRYLKEdkphGSAGALYYFRDRIMEekpsHVFLLNCDVccsFPLQGILDAHRRYGGIGTMLVIKVSAEAASQFGELIAD 161
Cdd:cd02523    75 --DYAET----NNIYSLYLARDFLDE----DFLLLEGDV---VFDPSILERLLSSPADNAILVDKKTKEWEDEYVKDLDD 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1985656924 162 PDTkelLHYTEKPETFVSDL--INCGVYVFTSDIFNAIEEVYSQIRDAS 208
Cdd:cd02523   142 AGV---LLGIISKAKNLEEIqgEYVGISKFSPEDADRLAEALEELIEAG 187
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 18-199 3.83e-10

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: 59.89  E-value: 3.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  18 GTRFRPLSFNTPKPLIPLAGQPMIHHPISACK------KISNLA----QIflIGFYEEREFALYVsSISNElkiPVRYLk 87
Cdd:cd06422    10 GTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAaagirrIVVNTHhladQI--EAHLGDSRFGLRI-TISDE---PDELL- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  88 edkphGSAGALYYFRDRIMEEkPshVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVSAEAASQFGELIADPDtkel 167
Cdd:cd06422    83 -----ETGGGIKKALPLLGDE-P--FLVVNGDILWDGDLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFSLDAD---- 150

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1985656924 168 LHYTEKPETFVSDLINCGVYVFTSDIFNAIEE 199
Cdd:cd06422   151 GRLRRGGGGAVAPFTFTGIQILSPELFAGIPP 182
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 293-347 8.39e-10

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: 60.42  E-value: 8.39e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1985656924 293 YIHPSVKLHPTAKIGPNVSISANVRVGPGVRLIS-CIILDDVEIKDNA-----VVI--NSIIG 347
Cdd:COG1044   104 VIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPgVVIGDGVVIGDDCvlhpnVTIyeRCVIG 166
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 294-388 1.16e-09

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 60.15  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 294 IHPSVKLHPTAKIGPNVSISANVRVGPGvrlisciilddVEIKDNaVVI--NSIIGWKSSIGRWSRVQAsgdynerlGIT 371
Cdd:PRK00892  103 IHPSAVIDPSAKIGEGVSIGPNAVIGAG-----------VVIGDG-VVIgaGAVIGDGVKIGADCRLHA--------NVT 162

                          90       100
                  ....*....|....*....|..
gi 1985656924 372 IlGEAVTVEDEV-----AVIGS 388
Cdd:PRK00892  163 I-YHAVRIGNRViihsgAVIGS 183
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 6-200 2.72e-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: 57.23  E-value: 2.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   6 VVAVIMvgGPTKGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKiSNLAQIFligfyeerefaLYVSSISNELKIPVRY 85
Cdd:cd04197     1 LQAVVL--ADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLAL-NGVEEVF-----------VFCCSHSDQIKEYIEK 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  86 LKEDKPHG--------------SAG-ALYYFRDRIMEEkpSHVFLLNCDVCCSFPLQGILDAHRRY-----GGIGTMLVI 145
Cdd:cd04197    67 SKWSKPKSslmiviiimsedcrSLGdALRDLDAKGLIR--GDFILVSGDVVSNIDLKEILEEHKERrkkdkNAIMTMVLK 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1985656924 146 KVSAEAASQFGE---LIA-DPDTKELLHYTEKPETFvsdliNCGVYVFTSDIFNAIEEV 200
Cdd:cd04197   145 EASPPHRTRRTGeefVIAvDPKTSRLLHYEELPGSK-----YRSITDLPSELLGSNSEV 198
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 292-358 3.55e-09

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: 56.66  E-value: 3.55e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1985656924 292 VYIHPSVKLHPTAKIGPNV------SISANVRVGPGVRLISCIILDDVEIKDNAVVINSIIGWKSSIGRWSRV 358
Cdd:cd03353    10 TYIDGDVEIGVDVVIDPGVilegktVIGEDCVIGPNCVIKDSTIGDGVVIKASSVIEGAVIGNGATVGPFAHL 82
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 300-359 5.65e-09

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: 52.97  E-value: 5.65e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1985656924 300 LHPTAKIGPNVSI-----SANVRVGPGVRLISCIILDDVEIKDNAVVINSIIGWKSSIGRWSRVQ 359
Cdd:cd04652     2 VGENTQVGEKTSIkrsviGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLK 66
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-353 1.16e-08

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 57.45  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   4 EKVVAVIMVGGptKGTRFRPlsfNTPKPLIPLAGQPMIHHPISACKKiSNLAQIFLI-GFYEEREFALYVSsisnelKIP 82
Cdd:PRK14355    2 NNLAAIILAAG--KGTRMKS---DLVKVMHPLAGRPMVSWPVAAARE-AGAGRIVLVvGHQAEKVREHFAG------DGD 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  83 VRYLKEDKPHG-------SAGALYYFRDRimeekpshVFLLNCDVCCSFP--LQGILDAHRRYGGIGTMLVIKVsaEAAS 153
Cdd:PRK14355   70 VSFALQEEQLGtghavacAAPALDGFSGT--------VLILCGDVPLLRAetLQGMLAAHRATGAAVTVLTARL--ENPF 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 154 QFGELIADPDTKELLHYTEK---PETFVSDLINCGVYVFTSDIF----------NAIEEVY-SQIRDASSNYQSATRSVP 219
Cdd:PRK14355  140 GYGRIVRDADGRVLRIVEEKdatPEERSIREVNSGIYCVEAAFLfdaigrlgndNAQGEYYlTDIVAMAAAEGLRCLAFP 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 220 ADfvrlDQDILSPLAGKKQLytyenkdfweqiktpgkslkCSALYLSQFRQTSPHILAsgdGTNrkpnIIG--DVYIHPS 297
Cdd:PRK14355  220 VA----DPDEIMGVNDRAQL--------------------AEAARVLRRRINRELMLA---GVT----LIDpeTTYIDRG 268

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1985656924 298 VKLHPTAKIGPNVSISANVRVG------PGVRLISCIILDDVEIKDNAVVINSIIGWKSSIG 353
Cdd:PRK14355  269 VVIGRDTTIYPGVCISGDTRIGegctieQGVVIKGCRIGDDVTVKAGSVLEDSVVGDDVAIG 330
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 293-347 3.31e-08

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 55.53  E-value: 3.31e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1985656924 293 YIHPSVKLHPTAKIGPNVSISANVRVGPGVRLIS-CIILDDVEIKDNA-----VVI--NSIIG 347
Cdd:PRK00892  108 VIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAgAVIGDGVKIGADCrlhanVTIyhAVRIG 170
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 1-346 1.89e-07

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 53.29  E-value: 1.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   1 MSEEKVVAVIMVGGptKGTRFRPLSFNTPKPLIPLAGQPMIhhpisackkI----SNLA-----QIFLIGFYeeREFALY 71
Cdd:PRK00844    1 RAMPKVLAIVLAGG--EGKRLMPLTADRAKPAVPFGGSYRL---------IdfvlSNLVnsgylRIYVLTQY--KSHSLD 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  72 --------VSSISNELKIPVRYLKEDKPH---GSAGALYYFRDRIMEEKPSHVFLLNCDVCCSFPLQGILDAHRRYGGIG 140
Cdd:PRK00844   68 rhisqtwrLSGLLGNYITPVPAQQRLGKRwylGSADAIYQSLNLIEDEDPDYVVVFGADHVYRMDPRQMVDFHIESGAGV 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 141 TMLVIKVSAEAASQFGELIADPDTKeLLHYTEKP-----------ETFVSdlinCGVYVFTSDIFnaIEEVysqIRDAsS 209
Cdd:PRK00844  148 TVAAIRVPREEASAFGVIEVDPDGR-IRGFLEKPadppglpddpdEALAS----MGNYVFTTDAL--VDAL---RRDA-A 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 210 NYQSATrsvpaDFvrlDQDILSPLAGKKQLYTY------------ENKDFWEQIKTpgkslkCSALYLSQFRQTSPHilA 277
Cdd:PRK00844  217 DEDSSH-----DM---GGDIIPRLVERGRAYVYdfstnevpgateRDRGYWRDVGT------IDAYYDAHMDLLSVH--P 280

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 278 SGDGTNRK-PniigdvyIHPSVKLHPTAK---------------IGPNVSISA----------NVRVGPGVRLISCIILD 331
Cdd:PRK00844  281 VFNLYNREwP-------IYTSSPNLPPAKfvdgggrvgsaqdslVSAGSIISGatvrnsvlspNVVVESGAEVEDSVLMD 353

                         410
                  ....*....|....*
gi 1985656924 332 DVEIKDNAVVINSII 346
Cdd:PRK00844  354 GVRIGRGAVVRRAIL 368
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 293-347 1.95e-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: 1.95e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1985656924 293 YIHPSVKLHPTAKIGPNVSISANVRVGPGVRLIS-CIILDDVEI-KDNAVVINSIIG 347
Cdd:COG1043     9 IVDPGAKLGENVEIGPFCVIGPDVEIGDGTVIGShVVIEGPTTIgKNNRIFPFASIG 65
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
8-120 1.98e-07

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 52.17  E-value: 1.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   8 AVIMVGGptKGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKiSNLAQIFLIGFYEEREFALYVssisNELKIPVRYLK 87
Cdd:COG1213     2 AVILAAG--RGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAA-AGIKDIVVVTGYKAELIEEAL----ARPGPDVTFVY 74

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1985656924  88 EDKPH--GSAGALYYFRDRIMEEkpshVFLLNCDV 120
Cdd:COG1213    75 NPDYDetNNIYSLWLAREALDED----FLLLNGDV 105
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 295-388 3.25e-07

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: 52.33  E-value: 3.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 295 HPSVKLHPTAKIGPNVSISANVRVGPGVrliscIILDDVEIKDNaVVI--NSIIGWKSSIGRWSRVQAsgdynerlGITI 372
Cdd:COG1044    94 APAPGIHPSAVIDPSAKIGEGVSIGPFA-----VIGAGVVIGDG-VVIgpGVVIGDGVVIGDDCVLHP--------NVTI 159

                          90       100
                  ....*....|....*....|.
gi 1985656924 373 lGEAVTVEDEV-----AVIGS 388
Cdd:COG1044   160 -YERCVIGDRViihsgAVIGA 179
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 297-360 3.44e-07

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: 50.87  E-value: 3.44e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1985656924 297 SVKLHPTAKIGPNVSISANVRVGPGVRLIS-CIILDDVEIKDNAVVI-NSIIGWKSSIGRWSRVQA 360
Cdd:cd03352     1 SAKIGENVSIGPNAVIGEGVVIGDGVVIGPgVVIGDGVVIGDDCVIHpNVTIYEGCIIGDRVIIHS 66
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 8-207 5.75e-07

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


Pssm-ID: 133021 [Multi-domain]  Cd Length: 267  Bit Score: 50.99  E-value: 5.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   8 AVIMVGGptKGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKiSNLAQIFLIG---------------FYEER------ 66
Cdd:cd02541     3 AVIPAAG--LGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVA-AGIEDIIIVTgrgkraiedhfdrsyELEETlekkgk 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  67 -EFALYVSSISNELKIpvRYLKEDKPHGSAGALYYFRDRIMEEkPSHVfLLNCDVCCSFP--LQGILDAHRRYGGiGTML 143
Cdd:cd02541    80 tDLLEEVRIISDLANI--HYVRQKEPLGLGHAVLCAKPFIGDE-PFAV-LLGDDLIDSKEpcLKQLIEAYEKTGA-SVIA 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1985656924 144 VIKVSAEAASQFGelIADP-----DTKELLHYTEKP--ETFVSDLINCGVYVFTSDIFNAIEEVYS------QIRDA 207
Cdd:cd02541   155 VEEVPPEDVSKYG--IVKGekidgDVFKVKGLVEKPkpEEAPSNLAIVGRYVLTPDIFDILENTKPgkggeiQLTDA 229
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 287-398 6.61e-07

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: 50.10  E-value: 6.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 287 NIIG-DVYIHPSVKLHPTAKIGPNVSISANVRVGPGVR-----LIS--CIILDDVEIKDNaVVI--NSIIG-----WKSS 351
Cdd:cd03352     2 AKIGeNVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVigddcVIHpnVTIYEGCIIGDR-VIIhsGAVIGsdgfgFAPD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1985656924 352 IGRWSRVQASGdynerlgitilgeAVTVEDEVaVIGSivlqNKTLNR 398
Cdd:cd03352    81 GGGWVKIPQLG-------------GVIIGDDV-EIGA----NTTIDR 109
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 7-210 1.10e-06

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: 49.94  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   7 VAVIMVGgptKGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKISNLAQIFLIGFYEEREFALYVSSIsnELKIPVRYL 86
Cdd:cd04183     1 IIIPMAG---LGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFICRDEHNTKFHLDESLK--LLAPNATVV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  87 KEDKP-HGSAGALYYFRDRIMEEKPshVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVSAEAASqFGELIADPDTK 165
Cdd:cd04183    76 ELDGEtLGAACTVLLAADLIDNDDP--LLIFNCDQIVESDLLAFLAAFRERDLDGGVLTFFSSHPRWS-YVKLDENGRVI 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1985656924 166 EllhYTEKpeTFVSDLINCGVYVFTS--DIFNAIEEVysQIRDASSN 210
Cdd:cd04183   153 E---TAEK--EPISDLATAGLYYFKSgsLFVEAAKKM--IRKDDSVN 192
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 6-229 2.62e-06

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: 49.11  E-value: 2.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   6 VVAVIMVGGptKGTRFRPLSFNT-PKPLIPLAG-QPMIHHPISACKKISNLAQIFLIGFYEerefalYVSSISNELK--- 80
Cdd:cd02509     1 IYPVILAGG--SGTRLWPLSRESyPKQFLKLFGdKSLLQQTLDRLKGLVPPDRILVVTNEE------YRFLVREQLPegl 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  81 IPVRYLKEDKPHGSAGALYYFRDRIMEEKPSHVFLlncdVCCSFPLQGILDAHRRyggigtmlVIKVSAEAAS------- 153
Cdd:cd02509    73 PEENIILEPEGRNTAPAIALAALYLAKRDPDAVLL----VLPSDHLIEDVEAFLK--------AVKKAVEAAEegylvtf 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 154 --------------QFGELIADPdTKELLHYTEKP-----ETFVSD---LINCGVYVFTSDIFnaIEEVYSQIRDASSNY 211
Cdd:cd02509   141 gikptrpetgygyiEAGEKLGGG-VYRVKRFVEKPdletaKEYLESgnyLWNSGIFLFRAKTF--LEELKKHAPDIYEAL 217

                         250
                  ....*....|....*....
gi 1985656924 212 QSATRSV-PADFVRLDQDI 229
Cdd:cd02509   218 EKALAAAgTDDFLRLLEEA 236
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 279-353 6.21e-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: 46.43  E-value: 6.21e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1985656924 279 GDGTNRKPN--IIGDVYIHPSVKLHPTAKIGPNVSISANVRVGPGVRLISCIILDDVEIKDNAVVINSIIGWKSSIG 353
Cdd:cd05636    21 GEGAIVRSGayIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSIIMDGTKVPHLNYVGDSVLGENVNLG 97
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
297-358 1.44e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 46.63  E-value: 1.44e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1985656924 297 SVKLHPTAKIGPNVSISANVRVGPGvrlisCIILDDVEIKDNAVVIN--SIIGWkSSIGRWSRV 358
Cdd:PRK05289    2 MAKIHPTAIVEPGAKIGENVEIGPF-----CVIGPNVVIGDGTVIGShvVIDGH-TTIGKNNRI 59
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
294-347 1.65e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 46.63  E-value: 1.65e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1985656924 294 IHPSVKLHPTAKIGPNVS------ISANVRVGPGVRLIS-CIILDDVEI-KDNAVVINSIIG 347
Cdd:PRK05289    5 IHPTAIVEPGAKIGENVEigpfcvIGPNVVIGDGTVIGShVVIDGHTTIgKNNRIFPFASIG 66
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 292-396 1.67e-05

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: 45.94  E-value: 1.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 292 VYIHPSVKLHPTAKIGPNVSISANVRVGPGVRlisciilddveIKDNaVVINS--IIGWKSSIgrwsrvqasGDYNErL- 368
Cdd:cd03360    85 TLIHPSAVVSPSAVIGEGCVIMAGAVINPDAR-----------IGDN-VIINTgaVIGHDCVI---------GDFVH-Ia 142

                          90       100       110
                  ....*....|....*....|....*....|
gi 1985656924 369 -GITILGEaVTVEDEVAV-IGSIVLQNKTL 396
Cdd:cd03360   143 pGVVLSGG-VTIGEGAFIgAGATIIQGVTI 171
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 8-120 1.78e-05

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: 44.88  E-value: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   8 AVIMVGGptKGTRFrplsfNTPKPLIPLAGQPMIHHPISACKKISnlAQIFLIGFYEEREFALyvssisneLKIPVRYLK 87
Cdd:pfam12804   1 AVILAGG--RSSRM-----GGDKALLPLGGKPLLERVLERLRPAG--DEVVVVANDEEVLAAL--------AGLGVPVVP 63

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1985656924  88 EDKPH-GSAGALYyfrdRIMEEKPSH--VFLLNCDV 120
Cdd:pfam12804  64 DPDPGqGPLAGLL----AALRAAPGAdaVLVLACDM 95
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 299-358 2.12e-05

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: 46.27  E-value: 2.12e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1985656924 299 KLHPTAKIGPNVSISANVRVGPGvrlisCIILDDVEIKDNAVVIN--SIIGWkSSIGRWSRV 358
Cdd:cd03351     1 MIHPTAIVDPGAKIGENVEIGPF-----CVIGPNVEIGDGTVIGShvVIDGP-TTIGKNNRI 56
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-60 3.04e-05

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 46.56  E-value: 3.04e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   1 MSEEKVVAVIMVGGptKGTRfrpLSFNTPKPLIPLAGQPMIHHPISACKKISNlAQIFLI 60
Cdd:PRK09451    1 MLNSAMSVVILAAG--KGTR---MYSDLPKVLHTLAGKPMVQHVIDAANELGA-QHVHLV 54
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 293-352 3.58e-05

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: 44.15  E-value: 3.58e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1985656924 293 YIHPSVKLHPTAKIGPNVSISANVRVGPGVrLISC------IILDDVEIKDNaVVINS------IIGWKSSI 352
Cdd:cd00710     4 VIDPSAYVHPTAVVIGDVIIGDNVFVGPGA-SIRAdegtpiIIGANVNIQDG-VVIHAlegysvWIGKNVSI 73
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 292-390 3.97e-05

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 46.36  E-value: 3.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 292 VYIHPSVKLHPTAKIGPNVSISANVRVG------PGVRLISCIILDDVEIKdNAVVINSIIGWKSSIGRWSRVqasgdyn 365
Cdd:PRK14354  260 TYIDADVEIGSDTVIEPGVVIKGNTVIGedcvigPGSRIVDSTIGDGVTIT-NSVIEESKVGDNVTVGPFAHL------- 331

                          90       100
                  ....*....|....*....|....*
gi 1985656924 366 eRLGiTILGEAVTVEDEVAVIGSIV 390
Cdd:PRK14354  332 -RPG-SVIGEEVKIGNFVEIKKSTI 354
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 312-347 4.20e-05

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


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 42.84  E-value: 4.20e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1985656924 312 ISANVRVGPGVRLISCIILDDVEIKDNAVVINSIIG 347
Cdd:cd04651    31 LFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIID 66
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 293-347 6.02e-05

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: 44.73  E-value: 6.02e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1985656924 293 YIHPSVKLHPTAKIGPNVSISANVRVGPGVRLIS-CIILDDVEI-KDNAVVINSIIG 347
Cdd:cd03351     7 IVDPGAKIGENVEIGPFCVIGPNVEIGDGTVIGShVVIDGPTTIgKNNRIFPFASIG 63
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 9-201 7.30e-05

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 45.37  E-value: 7.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   9 VIMVGGptKGTRFRPlsfNTPKPLIPLAGQPMIHHPISACKKISNlaQIFLIGFYEEREFALYVSSISNelkiPVRYLKE 88
Cdd:PRK14359    6 IILAAG--KGTRMKS---SLPKVLHTICGKPMLFYILKEAFAISD--DVHVVLHHQKERIKEAVLEYFP----GVIFHTQ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  89 DKPH--GSAGALyyfrdriMEEKPSH--VFLLNCD--VCCSFPLQGILDAHRRYggigTMLVIKvsAEAASQFGELI--- 159
Cdd:PRK14359   75 DLENypGTGGAL-------MGIEPKHerVLILNGDmpLVEKDELEKLLENDADI----VMSVFH--LADPKGYGRVVien 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1985656924 160 ---------ADPDTKELLhytekpetfvSDLINCGVYVFTSDIF----------NAIEEVY 201
Cdd:PRK14359  142 gqvkkiveqKDANEEELK----------IKSVNAGVYLFDRKLLeeylpllknqNAQKEYY 192
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 288-377 1.20e-04

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: 42.58  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 288 IIGDVYIHPSVKLHPTAKIGPNVSISANVRVGPGVRLI-SCIILDDVEIKDNAVVINSIIGWKSSIGRWSRVqasGDyne 366
Cdd:cd05636    14 IKGPVWIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRgYTVLGDGCVVGNSVEVKNSIIMDGTKVPHLNYV---GD--- 87

                          90
                  ....*....|.
gi 1985656924 367 rlgiTILGEAV 377
Cdd:cd05636    88 ----SVLGENV 94
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 297-354 1.81e-04

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: 43.47  E-value: 1.81e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 297 SVKLHPTAKIGPNVSISANVRVGPGvrlisCIILDDVEIKDNAVVIN--SIIGWkSSIGR 354
Cdd:COG1043     1 MAMIHPTAIVDPGAKLGENVEIGPF-----CVIGPDVEIGDGTVIGShvVIEGP-TTIGK 54
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 292-353 2.04e-04

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: 39.92  E-value: 2.04e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1985656924 292 VYIHPSVKLHPTAKIGPNVSISANVRVGPGVRLISC---------IILDDVEIKDNAVV-------INSIIGWKSSIG 353
Cdd:cd00208     1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAAtgpneknptIIGDNVEIGANAVIhggvkigDNAVIGAGAVVT 78
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 309-357 2.22e-04

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 43.86  E-value: 2.22e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1985656924 309 NVSISANVRVGPGVRLISCIILDDVEIKDNAVVINSIIGWKSSIGRWSR 357
Cdd:PRK09451  283 NVTLGNRVKIGAGCVLKNCVIGDDCEISPYSVVEDANLGAACTIGPFAR 331
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 302-381 2.26e-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: 39.87  E-value: 2.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 302 PTAKIGPNVSIS-----ANVRVGPGVRLISCIILDDVEIKDNAVVINSIIGWKSSIGRWSRVQASgdynerlgiTILGEA 376
Cdd:cd05787     4 RGTSIGEGTTIKnsvigRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIPPG---------SLISFG 74


                  ....*
gi 1985656924 377 VTVED 381
Cdd:cd05787    75 VVIGD 79
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 6-83 3.79e-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: 42.13  E-value: 3.79e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1985656924   6 VVAVIMVGGptKGTRFrplSFNTPKPLIPLAGQPMIHHPISACKKISNLAQIFLIGFYEEREFALYVSSISNELKIPV 83
Cdd:cd02516     1 VAAIILAAG--SGSRM---GADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVVVVPPDDIDLAKELAKYGLSKVVKI 73
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 294-358 4.19e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 42.32  E-value: 4.19e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1985656924 294 IHPSVKLHPTAKIGPNVSIsanvrvGPGvrlisCIILDDVEIKDnavviNSIIGWKSSIGRWSRV 358
Cdd:PRK12461    2 IHPTAVIDPSAKLGSGVEI------GPF-----AVIGANVEIGD-----GTWIGPHAVILGPTRI 50
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 8-198 4.67e-04

G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is the short form of glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.


Pssm-ID: 133019 [Multi-domain]  Cd Length: 240  Bit Score: 41.79  E-value: 4.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   8 AVIMVGGptKGTRFRPLSFNTPKPLIPLAGQPMIHHPISACkKISNLAQIFLIGfyEEREFALYVSSISN--ELKIPVRY 85
Cdd:cd02538     3 GIILAGG--SGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTL-MLAGIREILIIS--TPEDLPLFKELLGDgsDLGIRITY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924  86 LKEDKPHGSAGALYYFRDRIMEEKpshvfllncdVCCsfplqgILDAHRRYGGIGTMLVIKVSA--EAASQFGELIADP- 162
Cdd:cd02538    78 AVQPKPGGLAQAFIIGEEFIGDDP----------VCL------ILGDNIFYGQGLSPILQRAAAqkEGATVFGYEVNDPe 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1985656924 163 --------DTKELLHYTEKPETFVSDLINCGVYVFTSDIFNAIE 198
Cdd:cd02538   142 rygvvefdENGRVLSIEEKPKKPKSNYAVTGLYFYDNDVFEIAK 185
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-48 6.24e-04

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 42.54  E-value: 6.24e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1985656924   1 MSEEKVVAVIMVGGptKGTRFRPlsfNTPKPLIPLAGQPMIHHPISAC 48
Cdd:PRK14353    1 MTDRTCLAIILAAG--EGTRMKS---SLPKVLHPVAGRPMLAHVLAAA 43
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 5-60 7.73e-04

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 42.18  E-value: 7.73e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1985656924   5 KVVAVIMVGGptKGTRFRPLSFNTPKPLIPLAGQ-PMIHHPISACkkI-SNLAQIFLI 60
Cdd:PRK02862    3 RVLAIILGGG--AGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNC--InSGINKIYVL 56
RpoZ COG1758
DNA-directed RNA polymerase, subunit K/omega [Transcription]; DNA-directed RNA polymerase, ...
 471-520 8.29e-04

DNA-directed RNA polymerase, subunit K/omega [Transcription]; DNA-directed RNA polymerase, subunit K/omega is part of the Pathway/BioSystem: RNA polymerase


Pssm-ID: 441364  Cd Length: 64  Bit Score: 37.85  E-value: 8.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1985656924 471 KYERARILGTRALQISMNAPVMVELEGEtDPLEIAMKELRQRKIPFTIRR 520
Cdd:COG1758    16 RYELVLLAAKRARQLAEGAEPLVEPDSD-KPVVIALREIAEGKITIEILE 64
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 294-391 1.27e-03

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 39.63  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 294 IHPSVKLHPTAK-IGpNVSISANVRVGPGVRLISciildDVeikdnavviNSIIgwkssIGRWSRVQ------ASGDYNe 366
Cdd:COG0663    13 IHPSAFVAPTAVvIG-DVTIGEDVSVWPGAVLRG-----DV---------GPIR-----IGEGSNIQdgvvlhVDPGYP- 71

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1985656924 367 rlgiTILGEAVTV-----------EDEVAV-IGSIVL 391
Cdd:COG0663    72 ----LTIGDDVTIghgailhgctiGDNVLIgMGAIVL 104
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 294-341 1.75e-03

paaY-like: This group is composed by uncharacterized proteins with similarity to the protein product of the E. coli paaY gene, which is part of the paa gene cluster responsible for phenylacetic acid degradation. Proteins in this group are expected to adopt the left-handed parallel beta-helix (LbH) structure. They contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Similarity to gamma carbonic anhydrase and Ferripyochelin Binding Protein (FBP) may suggest metal binding capacity.


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 39.27  E-value: 1.75e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1985656924 294 IHPSVKLHPTAKIGPNVSISANVRVGPGVRL---ISCIILDD-VEIKDNAVV 341
Cdd:cd04745     3 VDPSSFVHPTAVLIGDVIIGKNCYIGPHASLrgdFGRIVIRDgANVQDNCVI 54
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 8-119 1.91e-03

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


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 39.48  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   8 AVIMVGGptKGTRFrplsfNTPKPLIPLAGQPMIHHPISACKKIsnLAQIFLIGFYEEREFALYvssisnelkiPVRYLK 87
Cdd:cd02503     3 GVILAGG--KSRRM-----GGDKALLELGGKPLLEHVLERLKPL--VDEVVISANRDQERYALL----------GVPVIP 63

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1985656924  88 EDKPH-GSAGALYyfrdRIMEEKPS-HVFLLNCD 119
Cdd:cd02503    64 DEPPGkGPLAGIL----AALRAAPAdWVLVLACD 93
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
4-60 2.10e-03

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 40.43  E-value: 2.10e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1985656924   4 EKVVAVIMVGGptKGTRFRPLS-FNTPKPLIPLAG-QPMIHHPISACKKISNLAQIFLI 60
Cdd:COG0836     1 SMIYPVILAGG--SGTRLWPLSrESYPKQFLPLLGeKSLLQQTVERLAGLVPPENILVV 57
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-119 2.19e-03

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: 39.41  E-value: 2.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924   1 MSEeKVVAVIMVGGptKGTRFrplsfNTPKPLIPLAGQPMIHHPISACKKISnlAQIFLIGFYEEREFALyvssisnelk 80
Cdd:COG0746     1 MTM-PITGVILAGG--RSRRM-----GQDKALLPLGGRPLLERVLERLRPQV--DEVVIVANRPERYAAL---------- 60

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1985656924  81 iPVRYLKEDKPH-GSAGALYyfrdRIMEEKPS-HVFLLNCD 119
Cdd:COG0746    61 -GVPVVPDDPPGaGPLAGIL----AALEAAPAeWVLVLACD 96
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 328-397 2.30e-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: 37.22  E-value: 2.30e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 328 IILDDVEIKDNAVVINSIIGWKSSIGRWSRVQASgdynerlgitILGEAVTVEDEVAVIGSIVLQNKTLN 397
Cdd:cd03356     1 LIGESTVIGENAIIKNSVIGDNVRIGDGVTITNS----------ILMDNVTIGANSVIVDSIIGDNAVIG 60
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
5-61 2.39e-03

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 39.73  E-value: 2.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1985656924   5 KVVAVIMVGGptKGTRFRPlsfNTPKPLIPLAGQPMIHHPISACKKISNLAQIFLIG 61
Cdd:PRK00155    3 MVYAIIPAAG--KGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPRIDEIIVVV 54
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
126-200 2.47e-03

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 40.02  E-value: 2.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 126 LQGILDAHRRYGG--IGTMlviKVSAEAASQFGelIADPDTKELLHYT-----EKP--ETFVSDLINCGVYVFTSDIFNA 196
Cdd:COG1210   141 LKQMIEVYEETGGsvIAVQ---EVPPEEVSKYG--IVDGEEIEGGVYRvtglvEKPapEEAPSNLAIVGRYILTPEIFDI 215


                  ....
gi 1985656924 197 IEEV 200
Cdd:COG1210   216 LEKT 219
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 301-358 2.50e-03

acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes LpxA, an enzyme for the biosynthesis of lipid A, a component oflipopolysaccharide (LPS) in the outer membrane outer leaflet of most Gram-negative bacteria. Some differences are found between lipid A of different species, but this protein represents the first step (from UDP-N-acetyl-D-glucosamine) and appears to be conserved in function. Proteins from this family contain many copies of the bacterial transferase hexapeptide repeat (pfam00132). [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 39.94  E-value: 2.50e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 301 HPTAKIGPNVSISANVRVGPgvrliSCIILDDVEIKDNaVVINS--IIGWKSSIGRWSRV 358
Cdd:TIGR01852   2 HPTAIIEPGAEIGENVEIGP-----FCIVGPGVKIGDG-VELKShvVILGHTTIGEGTRI 55
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 292-360 3.38e-03

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


Pssm-ID: 100045 [Multi-domain]  Cd Length: 101  Bit Score: 37.03  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 292 VYIHPSVKL--------------HPTAKIGPNVSISANVRVGpGVRLISC----IILDDVEIKDNAVVINSIigwksSIG 353
Cdd:cd03354     3 IDIHPGAKIgpglfidhgtgiviGETAVIGDNCTIYQGVTLG-GKGKGGGkrhpTIGDNVVIGAGAKILGNI-----TIG 76


                  ....*..
gi 1985656924 354 RWSRVQA 360
Cdd:cd03354    77 DNVKIGA 83
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
5-66 3.59e-03

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 38.99  E-value: 3.59e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1985656924   5 KVVAVIMVGGptKGTRFrplsfNTPKPLIPLAGQPMIHHPISACKKiSNLAQIFLI-GFYEER 66
Cdd:COG2068     3 KVAAIILAAG--ASSRM-----GRPKLLLPLGGKPLLERAVEAALA-AGLDPVVVVlGADAEE 57
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 299-391 4.23e-03

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: 38.16  E-value: 4.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1985656924 299 KLHPTAKIGPNVSISANVRVGPGvrlisciilddVEIKDNAVV---INSI-IGWKSSIGRWSRVQASGDYNerlgiTILG 374
Cdd:cd04645     1 EIDPSAFIAPNATVIGDVTLGEG-----------SSVWFGAVLrgdVNPIrIGERTNIQDGSVLHVDPGYP-----TIIG 64

                          90       100
                  ....*....|....*....|....*....
gi 1985656924 375 EAVTV-----------EDEVAV-IGSIVL 391
Cdd:cd04645    65 DNVTVghgavlhgctiGDNCLIgMGAIIL 93
 
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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