NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1063700043|ref|NP_001324263|]
View 

ADP-glucose pyrophosphorylase family protein [Arabidopsis thaliana]

Protein Classification

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

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 6-252 1.52e-149

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: 423.20  E-value: 1.52e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043   6 GTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKISNLAQIFLIGFYEEREFALYVSSISNELKIPVRYLKEDKPHGSAGA 85
Cdd:cd06428    11 GTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQEYKPLGTAGG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  86 LYYFRDRIMEEKPSHVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVSAEAASQFGELIADPDTKELLHYTEKPETF 165
Cdd:cd06428    91 LYHFRDQILAGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEASREQASNYGCIVEDPSTGEVLHYVEKPETF 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 166 VSDLINCGVYVFTSDIFNAIEEVYSQIRDTSSNYQSATRSVPADFVRLDQDILSPLAGKKQLYTYENKDFWEQIKTPGKS 245
Cdd:cd06428   171 VSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNREGRAEVIRLEQDVLTPLAGSGKLYVYKTDDFWSQIKTAGSA 250


                  ....*..
gi 1063700043 246 LKCSALY 252
Cdd:cd06428   251 IYANRLY 257
LbetaH super family cl00160
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 282-369 4.34e-23

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


The actual alignment was detected with superfamily member cd05824:

Pssm-ID: 469633 [Multi-domain]  Cd Length: 80  Bit Score: 91.83  E-value: 4.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 282 IHPSVKLHPTAKIGPNVSISANVRVGPGVRLISCIILDDVEIKENAVVINSIIGWKSSIGRWSRVQasgdyndrlGITIL 361
Cdd:cd05824     2 IDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLE---------NVTVL 72


                  ....*...
gi 1063700043 362 GEAVTVED 369
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 ...
 6-252 1.52e-149

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: 423.20  E-value: 1.52e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043   6 GTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKISNLAQIFLIGFYEEREFALYVSSISNELKIPVRYLKEDKPHGSAGA 85
Cdd:cd06428    11 GTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQEYKPLGTAGG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  86 LYYFRDRIMEEKPSHVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVSAEAASQFGELIADPDTKELLHYTEKPETF 165
Cdd:cd06428    91 LYHFRDQILAGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEASREQASNYGCIVEDPSTGEVLHYVEKPETF 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 166 VSDLINCGVYVFTSDIFNAIEEVYSQIRDTSSNYQSATRSVPADFVRLDQDILSPLAGKKQLYTYENKDFWEQIKTPGKS 245
Cdd:cd06428   171 VSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNREGRAEVIRLEQDVLTPLAGSGKLYVYKTDDFWSQIKTAGSA 250


                  ....*..
gi 1063700043 246 LKCSALY 252
Cdd:cd06428   251 IYANRLY 257
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 4-242 1.03e-37

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: 136.05  E-value: 1.03e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043   4 GLGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKiSNLAQIFLIGFYEEREFALYVSSISnELKIPVRYLKEDKPHGSA 83
Cdd:COG1208     8 GLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAA-AGITEIVINVGYLAEQIEEYFGDGS-RFGVRITYVDEGEPLGTG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  84 GALYYFRDRIMEEkpsHVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVsaEAASQFGELIADPDTKeLLHYTEKPE 163
Cdd:COG1208    86 GALKRALPLLGDE---PFLVLNGDILTDLDLAALLAFHREKGADATLALVPV--PDPSRYGVVELDGDGR-VTRFVEKPE 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063700043 164 TFVSDLINCGVYVFTSDIFNAIEEvysqirdtssnyqsatrSVPADFVrldqDILSPLAGKKQLYTYENKDFWEQIKTP 242
Cdd:COG1208   160 EPPSNLINAGIYVLEPEIFDYIPE-----------------GEPFDLE----DLLPRLIAEGRVYGYVHDGYWLDIGTP 217
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 4-335 3.00e-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: 128.10  E-value: 3.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043   4 GLGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKISNLAQIFLIGfYEEREFALYVSSISnELKIPVRYLKEDKPHGSA 83
Cdd:TIGR03992   9 GKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVG-YGKEKVREYFGDGS-RGGVPIEYVVQEEQLGTA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  84 GALYYFRDRIMEEkpshVFLLNCDVCCSFP-LQGILDAHRryggiGTMLVIKVsaEAASQFGELIADPDT-KELLhytEK 161
Cdd:TIGR03992  87 DALGSAKEYVDDE----FLVLNGDVLLDSDlLERLIRAEA-----PAIAVVEV--DDPSDYGVVETDGGRvTGIV---EK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 162 PETFVSDLINCGVYVFTSDIFNAIEEVYSQIRD----TssnyqsatrsvpadfvrldqDILSPLAGKKQLYTYENKDFWE 237
Cdd:TIGR03992 153 PENPPSNLINAGIYLFSPEIFELLEKTKLSPRGeyelT--------------------DALQLLIDEGKVKAVELDGFWL 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 238 QIKTPGKSLKCSALYLSQFR-------ETSPHILAS---GDGTNRKP--TIIGDVYIHPSVKLHPTAKIGPNVSISANVR 305
Cdd:TIGR03992 213 DVGRPWDLLDANEALLDNLEpriegtvEENVTIKGPvviGEGAVIRSgtYIEGPVYIGKNCDIGPNAYIRPYTVIGNNVH 292

                         330       340       350
                  ....*....|....*....|....*....|
gi 1063700043 306 VGPGVRLISCIILDDVEIKENAVVINSIIG 335
Cdd:TIGR03992 293 IGNAVEIKNSIIMEGTKIPHLSYVGDSVIG 322
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 4-190 6.90e-25

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: 101.95  E-value: 6.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043   4 GLGTRFRPLSFNTPKPLIPLAGQ-PMIHHPISACKKISNLAQIFLIGFYEEREFALYVSSISnELKIPVRYLKEDKPHGS 82
Cdd:pfam00483   8 GSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGS-KFGVQITYALQPEGKGT 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  83 AGALYYFRDRIMEEKpSHVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVSAEAASQFGELIADPDTKeLLHYTEKP 162
Cdd:pfam00483  87 APAVALAADFLGDEK-SDVLVLGGDHIYRMDLEQAVKFHIEKAADATVTFGIVPVEPPTGYGVVEFDDNGR-VIRFVEKP 164

                         170       180
                  ....*....|....*....|....*....
gi 1063700043 163 ETFV-SDLINCGVYVFTSDIFNAIEEVYS 190
Cdd:pfam00483 165 KLPKaSNYASMGIYIFNSGVLDFLAKYLE 193
LbH_M1P_guanylylT_C cd05824
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 282-369 4.34e-23

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


Pssm-ID: 100062 [Multi-domain]  Cd Length: 80  Bit Score: 91.83  E-value: 4.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 282 IHPSVKLHPTAKIGPNVSISANVRVGPGVRLISCIILDDVEIKENAVVINSIIGWKSSIGRWSRVQasgdyndrlGITIL 361
Cdd:cd05824     2 IDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLE---------NVTVL 72


                  ....*...
gi 1063700043 362 GEAVTVED 369
Cdd:cd05824    73 GDDVTIKD 80
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 81-371 6.24e-12

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 66.43  E-value: 6.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  81 GSAGALYYFRDRIMEEKPSHVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVSAEAASQFGELIADPDTkELLHYTE 160
Cdd:PRK05293  100 GTAHAIYQNIDYIDQYDPEYVLILSGDHIYKMDYDKMLDYHKEKEADVTIAVIEVPWEEASRFGIMNTDENM-RIVEFEE 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 161 KPETFVSDLINCGVYVFTSDIfnaIEEVYsqIRDTSSNYQSatrsvpADFvrlDQDIL-SPLAGKKQLYTYENKDFWEQI 239
Cdd:PRK05293  179 KPKNPKSNLASMGIYIFNWKR---LKEYL--IEDEKNPNSS------HDF---GKNVIpLYLEEGEKLYAYPFKGYWKDV 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 240 KTPgKSLKCSALYL-----------------SQFRETSPHILAsgDGTNRKPTIIGD-VYIHPSVKlhptakigpNVSIS 301
Cdd:PRK05293  245 GTI-ESLWEANMELlrpenplnlfdrnwriySVNPNLPPQYIA--ENAKVKNSLVVEgCVVYGTVE---------HSVLF 312

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 302 ANVRVGPGVRLISCIILDDVEIKENAVVINSIIGWKSSIGRWSRVQASGDyndrlGITILGEAVTVEDEV 371
Cdd:PRK05293  313 QGVQVGEGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVIIGGGKE-----VITVIGENEVIGVGT 377
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 281-335 1.82e-09

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: 58.49  E-value: 1.82e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063700043 281 YIHPSVKLHPTAKIGPNVSISANVRVGPGVRLIS-CIILDDVEIKENA-----VVI--NSIIG 335
Cdd:COG1044   104 VIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPgVVIGDGVVIGDDCvlhpnVTIyeRCVIG 166
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 282-376 2.36e-09

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 58.23  E-value: 2.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 282 IHPSVKLHPTAKIGPNVSISANVRVGPGVRlisciILDDVEIKENAVvinsiIGWKSSIGRWSRVQAsgdyndrlGITIl 361
Cdd:PRK00892  103 IHPSAVIDPSAKIGEGVSIGPNAVIGAGVV-----IGDGVVIGAGAV-----IGDGVKIGADCRLHA--------NVTI- 163

                          90       100
                  ....*....|....*....|
gi 1063700043 362 GEAVTVEDEV-----AVIGS 376
Cdd:PRK00892  164 YHAVRIGNRViihsgAVIGS 183
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 289-346 4.27e-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: 38.40  E-value: 4.27e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 289 HPTAKIGPNVSISANVRVGPgvrliSCIILDDVEIKENaVVINS--IIGWKSSIGRWSRV 346
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 ...
 6-252 1.52e-149

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: 423.20  E-value: 1.52e-149
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043   6 GTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKISNLAQIFLIGFYEEREFALYVSSISNELKIPVRYLKEDKPHGSAGA 85
Cdd:cd06428    11 GTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQEYKPLGTAGG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  86 LYYFRDRIMEEKPSHVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVSAEAASQFGELIADPDTKELLHYTEKPETF 165
Cdd:cd06428    91 LYHFRDQILAGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEASREQASNYGCIVEDPSTGEVLHYVEKPETF 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 166 VSDLINCGVYVFTSDIFNAIEEVYSQIRDTSSNYQSATRSVPADFVRLDQDILSPLAGKKQLYTYENKDFWEQIKTPGKS 245
Cdd:cd06428   171 VSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNREGRAEVIRLEQDVLTPLAGSGKLYVYKTDDFWSQIKTAGSA 250


                  ....*..
gi 1063700043 246 LKCSALY 252
Cdd:cd06428   251 IYANRLY 257
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 4-253 2.16e-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: 163.92  E-value: 2.16e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043   4 GLGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKIsNLAQIFLIGFYEEREFALYVSSISNELKIPVRYLKEDKPHGSA 83
Cdd:cd06425     9 GYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKA-GVKEIILAVNYRPEDMVPFLKEYEKKLGIKITFSIETEPLGTA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  84 GALYYFRDrIMEEKPSHVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVsaEAASQFGELIADPDTKELLHYTEKPE 163
Cdd:cd06425    88 GPLALARD-LLGDDDEPFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKV--EDPSKYGVVVHDENTGRIERFVEKPK 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 164 TFVSDLINCGVYVFTSDIFNAIEEvysqiRDTSsnyqsatrsvpadfvrLDQDILSPLAGKKQLYTYENKDFWEQIKTPG 243
Cdd:cd06425   165 VFVGNKINAGIYILNPSVLDRIPL-----RPTS----------------IEKEIFPKMASEGQLYAYELPGFWMDIGQPK 223

                         250
                  ....*....|
gi 1063700043 244 KSLKCSALYL 253
Cdd:cd06425   224 DFLKGMSLYL 233
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 4-239 1.70e-44

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: 153.12  E-value: 1.70e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043   4 GLGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKIsNLAQIFLIGFYEEREFALYVSSISNeLKIPVRYLKEDKPHGSA 83
Cdd:cd04181     7 GKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARA-GIDEIILVVGYLGEQIEEYFGDGSK-FGVNIEYVVQEEPLGTA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  84 GALYYFRDRIMEEkpsHVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVsaEAASQFGELIADpDTKELLHYTEKPE 163
Cdd:cd04181    85 GAVRNAEDFLGDD---DFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEV--EDPSRYGVVELD-DDGRVTRFVEKPT 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063700043 164 TFVSDLINCGVYVFTSDIFNAIEEvysqirdtssnyqsaTRSVPADFvrlDQDILSPLAGKKQLYTYENKDFWEQI 239
Cdd:cd04181   159 LPESNLANAGIYIFEPEILDYIPE---------------ILPRGEDE---LTDAIPLLIEEGKVYGYPVDGYWLDI 216
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 4-242 1.03e-37

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: 136.05  E-value: 1.03e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043   4 GLGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKiSNLAQIFLIGFYEEREFALYVSSISnELKIPVRYLKEDKPHGSA 83
Cdd:COG1208     8 GLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAA-AGITEIVINVGYLAEQIEEYFGDGS-RFGVRITYVDEGEPLGTG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  84 GALYYFRDRIMEEkpsHVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVsaEAASQFGELIADPDTKeLLHYTEKPE 163
Cdd:COG1208    86 GALKRALPLLGDE---PFLVLNGDILTDLDLAALLAFHREKGADATLALVPV--PDPSRYGVVELDGDGR-VTRFVEKPE 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063700043 164 TFVSDLINCGVYVFTSDIFNAIEEvysqirdtssnyqsatrSVPADFVrldqDILSPLAGKKQLYTYENKDFWEQIKTP 242
Cdd:COG1208   160 EPPSNLINAGIYVLEPEIFDYIPE-----------------GEPFDLE----DLLPRLIAEGRVYGYVHDGYWLDIGTP 217
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 4-335 3.00e-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: 128.10  E-value: 3.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043   4 GLGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKISNLAQIFLIGfYEEREFALYVSSISnELKIPVRYLKEDKPHGSA 83
Cdd:TIGR03992   9 GKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVG-YGKEKVREYFGDGS-RGGVPIEYVVQEEQLGTA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  84 GALYYFRDRIMEEkpshVFLLNCDVCCSFP-LQGILDAHRryggiGTMLVIKVsaEAASQFGELIADPDT-KELLhytEK 161
Cdd:TIGR03992  87 DALGSAKEYVDDE----FLVLNGDVLLDSDlLERLIRAEA-----PAIAVVEV--DDPSDYGVVETDGGRvTGIV---EK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 162 PETFVSDLINCGVYVFTSDIFNAIEEVYSQIRD----TssnyqsatrsvpadfvrldqDILSPLAGKKQLYTYENKDFWE 237
Cdd:TIGR03992 153 PENPPSNLINAGIYLFSPEIFELLEKTKLSPRGeyelT--------------------DALQLLIDEGKVKAVELDGFWL 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 238 QIKTPGKSLKCSALYLSQFR-------ETSPHILAS---GDGTNRKP--TIIGDVYIHPSVKLHPTAKIGPNVSISANVR 305
Cdd:TIGR03992 213 DVGRPWDLLDANEALLDNLEpriegtvEENVTIKGPvviGEGAVIRSgtYIEGPVYIGKNCDIGPNAYIRPYTVIGNNVH 292

                         330       340       350
                  ....*....|....*....|....*....|
gi 1063700043 306 VGPGVRLISCIILDDVEIKENAVVINSIIG 335
Cdd:TIGR03992 293 IGNAVEIKNSIIMEGTKIPHLSYVGDSVIG 322
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 4-242 8.45e-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: 103.79  E-value: 8.45e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043   4 GLGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKK--ISNLaqIFLIGF--------YEEREFALyvssisnelkIPVRY 73
Cdd:cd06915     7 GLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARqgISRI--VLSVGYlaeqieeyFGDGYRGG----------IRIYY 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  74 LKEDKPHGSAGALYYFRDRIMEEkpsHVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVsaEAASQFGELIADPDtK 153
Cdd:cd06915    75 VIEPEPLGTGGAIKNALPKLPED---QFLVLNGDTYFDVDLLALLAALRASGADATMALRRV--PDASRYGNVTVDGD-G 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 154 ELLHYTEKPETFVSDLINCGVYVFTSDIFNAIeevysqirdtssnyqsatrsvPADFVRLDQDILSPLAGKKQLYTYENK 233
Cdd:cd06915   149 RVIAFVEKGPGAAPGLINGGVYLLRKEILAEI---------------------PADAFSLEADVLPALVKRGRLYGFEVD 207


                  ....*....
gi 1063700043 234 DFWEQIKTP 242
Cdd:cd06915   208 GYFIDIGIP 216
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 4-190 6.90e-25

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: 101.95  E-value: 6.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043   4 GLGTRFRPLSFNTPKPLIPLAGQ-PMIHHPISACKKISNLAQIFLIGFYEEREFALYVSSISnELKIPVRYLKEDKPHGS 82
Cdd:pfam00483   8 GSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGS-KFGVQITYALQPEGKGT 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  83 AGALYYFRDRIMEEKpSHVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVSAEAASQFGELIADPDTKeLLHYTEKP 162
Cdd:pfam00483  87 APAVALAADFLGDEK-SDVLVLGGDHIYRMDLEQAVKFHIEKAADATVTFGIVPVEPPTGYGVVEFDDNGR-VIRFVEKP 164

                         170       180
                  ....*....|....*....|....*....
gi 1063700043 163 ETFV-SDLINCGVYVFTSDIFNAIEEVYS 190
Cdd:pfam00483 165 KLPKaSNYASMGIYIFNSGVLDFLAKYLE 193
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 4-187 1.34e-23

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: 98.02  E-value: 1.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043   4 GLGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKK--ISNLAQIflIGFYEErEFALYVSSISNeLKIPVRYLKEDKPHG 81
Cdd:cd04189     9 GKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREagIEDIGIV--VGPTGE-EIKEALGDGSR-FGVRITYILQEEPLG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  82 SAGALYYFRDRImEEKPSHVFLlnCDVCCSFPLQGILDAHRRYGGIGTMLVIKVsaEAASQFGelIADPDTKELLHYTEK 161
Cdd:cd04189    85 LAHAVLAARDFL-GDEPFVVYL--GDNLIQEGISPLVRDFLEEDADASILLAEV--EDPRRFG--VAVVDDGRIVRLVEK 157

                         170       180
                  ....*....|....*....|....*.
gi 1063700043 162 PETFVSDLINCGVYVFTSDIFNAIEE 187
Cdd:cd04189   158 PKEPPSNLALVGVYAFTPAIFDAISR 183
LbH_M1P_guanylylT_C cd05824
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 282-369 4.34e-23

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


Pssm-ID: 100062 [Multi-domain]  Cd Length: 80  Bit Score: 91.83  E-value: 4.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 282 IHPSVKLHPTAKIGPNVSISANVRVGPGVRLISCIILDDVEIKENAVVINSIIGWKSSIGRWSRVQasgdyndrlGITIL 361
Cdd:cd05824     2 IDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLE---------NVTVL 72


                  ....*...
gi 1063700043 362 GEAVTVED 369
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 ...
 4-187 1.41e-20

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: 89.11  E-value: 1.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043   4 GLGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKisnlaqiflIGFyeeREFALYVSSISNELK----------IPVRY 73
Cdd:cd06426     7 GKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIA---------QGF---RNFYISVNYLAEMIEdyfgdgskfgVNISY 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  74 LKEDKPHGSAGALyyfrdRIMEEKPSH-VFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVSAEAAsqFGELiaDPDT 152
Cdd:cd06426    75 VREDKPLGTAGAL-----SLLPEKPTDpFLVMNGDILTNLNYEHLLDFHKENNADATVCVREYEVQVP--YGVV--ETEG 145

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1063700043 153 KELLHYTEKPE-TFvsdLINCGVYVFTSDIFNAIEE 187
Cdd:cd06426   146 GRITSIEEKPThSF---LVNAGIYVLEPEVLDLIPK 178
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 81-335 1.08e-18

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 86.67  E-value: 1.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  81 GSAGALYYFRDRIMEEKPSHVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVSAEAASQFGELIADPDTKeLLHYTE 160
Cdd:COG0448    98 GTADAVYQNLDFIERSDPDYVLILSGDHIYKMDYRQMLDFHIESGADITVACIEVPREEASRFGVMEVDEDGR-ITEFEE 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 161 KPETFVSDLINCGVYVFTSDIFnaIEEVYSQIRDTSSnyqsatrsvpaDFVRldqDILSPLAGKKQLYTYENKDFWEQIK 240
Cdd:COG0448   177 KPKDPKSALASMGIYVFNKDVL--IELLEEDAPNSSH-----------DFGK---DIIPRLLDRGKVYAYEFDGYWRDVG 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 241 TPgkslkcSALYlsqfrETSPHILasgdgtnrKPTIIGDVY-----IHPSVKLHPTAKIGPN-------VS--------- 299
Cdd:COG0448   241 TI------DSYY-----EANMDLL--------DPEPEFNLYdpewpIYTKQKDLPPAKFVRGgkvknslVSngciisgtv 301

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1063700043 300 ----ISANVRVGPGVRLISCIILDDVEIKENAVVINSIIG 335
Cdd:COG0448   302 ensvLFRGVRVESGAVVENSVIMPGVVIGEGAVIENAIID 341
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 4-340 5.57e-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: 84.38  E-value: 5.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043   4 GLGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKIsNLAQIFLIGFYEEREFALYVSSISNELKIPVRYLKEDKPHGSA 83
Cdd:TIGR01208   8 GKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEA-GITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQGEPLGLA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  84 GALYYFRDrimeekpshvFLLNCDVCCSFPLQGILDAHRRY-------GGIGTMLVIKVsaEAASQFGelIAD-PDTKEL 155
Cdd:TIGR01208  87 HAVYTARD----------FLGDDDFVVYLGDNLIQDGISRFvksfeekDYDALILLTKV--RDPTAFG--VAVlEDGKRI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 156 LHYTEKPETFVSDLINCGVYVFTSDIFNAIeevySQIRDTSSNYQSATrsvpadfvrldqDILSPLAGKKQLYTYEN-KD 234
Cdd:TIGR01208 153 LKLVEKPKEPPSNLAVVGLYMFRPLIFEAI----KNIKPSWRGELEIT------------DAIQWLIEKGYKVGGSKvTG 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 235 FWEQIKTPGKSLKCSALYLSqfrETSPHILasgdGTNRKPTIIGDVYIHPSVKL-----HPTAKIGPNVSISaNVRVGP- 308
Cdd:TIGR01208 217 WWKDTGKPEDLLDANRLILD---EVEREVQ----GVDDESKIRGRVVVGEGAKIvnsviRGPAVIGEDCIIE-NSYIGPy 288

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1063700043 309 -----GVRLIS-----CIILDDVEIKEN-AVVINSIIGWKSSI 340
Cdd:TIGR01208 289 tsigeGVVIRDaevehSIVLDESVIEGVqARIVDSVIGKKVRI 331
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
4-188 7.14e-17

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 80.13  E-value: 7.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043   4 GLGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKkisnLAQI----FLIGFYEEREFALYVSSISnELKIPVRYLKEDKP 79
Cdd:COG1209     9 GSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLM----LAGIreilIISTPEDGPQFERLLGDGS-QLGIKISYAVQPEP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  80 HGSAGALYyfrdrIMEEkpshvFLLNCDVCCSF--------PLQGILDAHRRYGGIGTMLVIKVsaEAASQFG--ELiaD 149
Cdd:COG1209    84 LGLAHAFI-----IAED-----FIGGDPVALVLgdnifygdGLSELLREAAARESGATIFGYKV--EDPERYGvvEF--D 149

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1063700043 150 PDTKeLLHYTEKPETFVSDLINCGVYVFTSDIFNAIEEV 188
Cdd:COG1209   150 EDGR-VVSLEEKPKEPKSNLAVTGLYFYDNDVVEIAKNL 187
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 4-182 1.45e-16

The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; N-terminal domain of eEIF-2B epsilon and gamma, subunits of eukaryotic translation initiators, is a subfamily of glycosyltranferase 2 and is predicted to have glycosyltranferase activity. eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133001 [Multi-domain]  Cd Length: 216  Bit Score: 77.68  E-value: 1.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043   4 GLGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKiSNLAQIFLI-GFYEEREFALYVSSISNELKIPVR----YLKEDK 78
Cdd:cd02507     9 GFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEK-AGVEEVFVVcCEHSQAIIEHLLKSKWSSLSSKMIvdviTSDLCE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  79 PHGSAGALYYFRDRImeekPSHVFLLNCDVCCSFPLQGILDAHR--RYGGIGTMLVIKVSA---EAASQFGE---LIADP 150
Cdd:cd02507    88 SAGDALRLRDIRGLI----RSDFLLLSCDLVSNIPLSELLEERRkkDKNAIATLTVLLASPpvsTEQSKKTEeedVIAVD 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063700043 151 DT---KELLHYTEKPE------------------TFVSDLINCGVYVFTSDIF 182
Cdd:cd02507   164 SKtqrLLLLHYEEDLDedleliirksllskhpnvTIRTDLLDCHIYICSPDVL 216
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 4-182 1.07e-15

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: 75.39  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043   4 GLGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKISNLAQIFLIGFYEEREFALYVSSISNELKIPVRYLKE--DKPHG 81
Cdd:cd04198     9 GGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSFPLNLKQKLDEVTIvlDEDMG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  82 SAGALYYFRDRImeekPSHVFLLNCDVCCSFPLQGILDAHRRYGGIGTML-------VIKVSAEAASQFGE---LIADPD 151
Cdd:cd04198    89 TADSLRHIRKKI----KKDFLVLSCDLITDLPLIELVDLHRSHDASLTVLlypppvsSEQKGGKGKSKKADerdVIGLDE 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1063700043 152 TKELLHYTEKPE-------------------TFVSDLINCGVYVFTSDIF 182
Cdd:cd04198   165 KTQRLLFITSEEdldedlelrksllkrhprvTITTKLLDAHVYIFKRWVL 214
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 281-369 2.75e-15

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: 70.35  E-value: 2.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 281 YIHPSVKLHPTAKIGPNVsISANVRVGPGVRLISCIILDDVEIKENAVVINSIIGWKSSIGRWSRVqasgdyndrLGITI 360
Cdd:cd03356     1 LIGESTVIGENAIIKNSV-IGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRV---------VNLCI 70


                  ....*....
gi 1063700043 361 LGEAVTVED 369
Cdd:cd03356    71 IGDDVVVED 79
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 4-241 9.87e-13

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: 67.60  E-value: 9.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043   4 GLGTRFRPLSFNTPKPLIPLAGQPMIHHpisackkISNLAQ-------IFLIGF-----------YEEREFALYVSSISN 65
Cdd:cd02524     7 GLGTRLSEETELKPKPMVEIGGRPILWH-------IMKIYShyghndfILCLGYkghvikeyflnYFLHNSDVTIDLGTN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  66 ELKIpvrylkedkpHGSA------------------GALYYFRDRIMEEKPshvFLLN-CDVCCSFPLQGILDAHRRYGG 126
Cdd:cd02524    80 RIEL----------HNSDiedwkvtlvdtglntmtgGRLKRVRRYLGDDET---FMLTyGDGVSDVNINALIEFHRSHGK 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 127 IGTMLVIKvsaeAASQFGELIADPDTKeLLHYTEKPETfVSDLINCGVYVFTSDIFNAIEEvysqiRDTSsnyqsatrsv 206
Cdd:cd02524   147 LATVTAVH----PPGRFGELDLDDDGQ-VTSFTEKPQG-DGGWINGGFFVLEPEVFDYIDG-----DDTV---------- 205

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1063700043 207 padfvrLDQDILSPLAGKKQLYTYENKDFWEQIKT 241
Cdd:cd02524   206 ------FEREPLERLAKDGELMAYKHTGFWQCMDT 234
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 4-375 2.43e-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: 68.13  E-value: 2.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043   4 GLGTRFRplSfNTPKPLIPLAGQPMIHHPISACKKIsNLAQIFLI-GFyeEREfalyvsSISNELK-IPVRYLKEDKPHG 81
Cdd:COG1207    11 GKGTRMK--S-KLPKVLHPLAGKPMLEHVLDAARAL-GPDRIVVVvGH--GAE------QVRAALAdLDVEFVLQEEQLG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  82 SAGALYYFRDRImEEKPSHVFLLNCDVccsfPL------QGILDAHRRYGGIGTMLvikvSAEAA----------SQFGE 145
Cdd:COG1207    79 TGHAVQQALPAL-PGDDGTVLVLYGDV----PLiraetlKALLAAHRAAGAAATVL----TAELDdptgygrivrDEDGR 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 146 LI-------ADPDTKELlhyTEkpetfvsdlINCGVYVF-TSDIFNAIEEVysqirdTSSNyqsatrsvpadfvrlDQ-- 215
Cdd:COG1207   150 VLriveekdATEEQRAI---RE---------INTGIYAFdAAALREALPKL------SNDN---------------AQge 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 216 ----DILSPLAGK-KQLYTYENKDFWE--------QIKTPGKSLKcsalylsqfRETSPHILASGdgtnrkPTIIgD--- 279
Cdd:COG1207   197 yyltDVIAIARADgLKVAAVQPEDPWEvlgvndrvQLAEAERILQ---------RRIAERLMRAG------VTII-Dpat 260

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 280 VYIHPSVKLHPTAKIGPNV------SISANVRVGPGVRLISCIILDDVEIKeNAVVINSIIGWKSSIGRWSRVqasgdyn 353
Cdd:COG1207   261 TYIDGDVEIGRDVVIDPNVilegktVIGEGVVIGPNCTLKDSTIGDGVVIK-YSVIEDAVVGAGATVGPFARL------- 332

                         410       420
                  ....*....|....*....|....*.
gi 1063700043 354 dRLGiTILGEAVTVED--EV--AVIG 375
Cdd:COG1207   333 -RPG-TVLGEGVKIGNfvEVknSTIG 356
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 4-187 5.54e-12

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


Pssm-ID: 133044 [Multi-domain]  Cd Length: 221  Bit Score: 64.90  E-value: 5.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043   4 GLGTRFRPLSFNTPKPLIPLAGQPMIHHPISACK------KISNLA----QIflIGFYEEREFALYVsSISNElkiPVRY 73
Cdd:cd06422     8 GLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAaagirrIVVNTHhladQI--EAHLGDSRFGLRI-TISDE---PDEL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  74 LkedkphGSAGALYYFRDRIMEEkPshVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVSAEAASQFGELIADPDtk 153
Cdd:cd06422    82 L------ETGGGIKKALPLLGDE-P--FLVVNGDILWDGDLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFSLDAD-- 150

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1063700043 154 elLHYTEKPETFVSDLINCGVYVFTSDIFNAIEE 187
Cdd:cd06422   151 --GRLRRGGGGAVAPFTFTGIQILSPELFAGIPP 182
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 81-371 6.24e-12

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 66.43  E-value: 6.24e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  81 GSAGALYYFRDRIMEEKPSHVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVSAEAASQFGELIADPDTkELLHYTE 160
Cdd:PRK05293  100 GTAHAIYQNIDYIDQYDPEYVLILSGDHIYKMDYDKMLDYHKEKEADVTIAVIEVPWEEASRFGIMNTDENM-RIVEFEE 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 161 KPETFVSDLINCGVYVFTSDIfnaIEEVYsqIRDTSSNYQSatrsvpADFvrlDQDIL-SPLAGKKQLYTYENKDFWEQI 239
Cdd:PRK05293  179 KPKNPKSNLASMGIYIFNWKR---LKEYL--IEDEKNPNSS------HDF---GKNVIpLYLEEGEKLYAYPFKGYWKDV 244

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 240 KTPgKSLKCSALYL-----------------SQFRETSPHILAsgDGTNRKPTIIGD-VYIHPSVKlhptakigpNVSIS 301
Cdd:PRK05293  245 GTI-ESLWEANMELlrpenplnlfdrnwriySVNPNLPPQYIA--ENAKVKNSLVVEgCVVYGTVE---------HSVLF 312

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 302 ANVRVGPGVRLISCIILDDVEIKENAVVINSIIGWKSSIGRWSRVQASGDyndrlGITILGEAVTVEDEV 371
Cdd:PRK05293  313 QGVQVGEGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVIIGGGKE-----VITVIGENEVIGVGT 377
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 4-188 5.07e-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: 62.15  E-value: 5.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043   4 GLGTRFRplsFNTPKPLIPLAGQPMIHHPISACKKIsNLAQIFLIGFYEEREFALYVSsisnelKIPVRYLKEDKPHGSA 83
Cdd:cd02540     7 GKGTRMK---SDLPKVLHPLAGKPMLEHVLDAARAL-GPDRIVVVVGHGAEQVKKALA------NPNVEFVLQEEQLGTG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  84 GALYYFRDRImEEKPSHVFLLNCDVccsfPL------QGILDAHRRYGGIGTMLvikvSAEAA--SQFGELIADpDTKEL 155
Cdd:cd02540    77 HAVKQALPAL-KDFEGDVLVLYGDV----PLitpetlQRLLEAHREAGADVTVL----TAELEdpTGYGRIIRD-GNGKV 146

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1063700043 156 LHYTE----KPETFVSDLINCGVYVF-TSDIFNAIEEV 188
Cdd:cd02540   147 LRIVEekdaTEEEKAIREVNAGIYAFdAEFLFEALPKL 184
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 4-196 4.35e-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: 59.17  E-value: 4.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043   4 GLGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKIsNLAQIFLI-GFYEE--REFA---LYVSSISNElkipvRYLKEd 77
Cdd:cd02523     7 GRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEA-GIDDIVIVtGYKKEqiEELLkkyPNIKFVYNP-----DYAET- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  78 kphGSAGALYYFRDRIMEekpsHVFLLNCDVccsFPLQGILDAHRRYGGIGTMLVIKVSAEAASQFGELIADPDTkelLH 157
Cdd:cd02523    80 ---NNIYSLYLARDFLDE----DFLLLEGDV---VFDPSILERLLSSPADNAILVDKKTKEWEDEYVKDLDDAGV---LL 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1063700043 158 YTEKPETFVSDL--INCGVYVFTSDIFNAIEEVYSQIRDTS 196
Cdd:cd02523   147 GIISKAKNLEEIqgEYVGISKFSPEDADRLAEALEELIEAG 187
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 281-335 1.82e-09

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: 58.49  E-value: 1.82e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063700043 281 YIHPSVKLHPTAKIGPNVSISANVRVGPGVRLIS-CIILDDVEIKENA-----VVI--NSIIG 335
Cdd:COG1044   104 VIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPgVVIGDGVVIGDDCvlhpnVTIyeRCVIG 166
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 282-376 2.36e-09

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 58.23  E-value: 2.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 282 IHPSVKLHPTAKIGPNVSISANVRVGPGVRlisciILDDVEIKENAVvinsiIGWKSSIGRWSRVQAsgdyndrlGITIl 361
Cdd:PRK00892  103 IHPSAVIDPSAKIGEGVSIGPNAVIGAGVV-----IGDGVVIGAGAV-----IGDGVKIGADCRLHA--------NVTI- 163

                          90       100
                  ....*....|....*....|
gi 1063700043 362 GEAVTVEDEV-----AVIGS 376
Cdd:PRK00892  164 YHAVRIGNRViihsgAVIGS 183
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 280-346 4.90e-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: 55.50  E-value: 4.90e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063700043 280 VYIHPSVKLHPTAKIGPNV------SISANVRVGPGVRLISCIILDDVEIKENAVVINSIIGWKSSIGRWSRV 346
Cdd:cd03353    10 TYIDGDVEIGVDVVIDPGVilegktVIGEDCVIGPNCVIKDSTIGDGVVIKASSVIEGAVIGNGATVGPFAHL 82
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 6-188 6.71e-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: 55.69  E-value: 6.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043   6 GTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKiSNLAQIFligfyeerefaLYVSSISNELKIPVRYLKEDKPHG---- 81
Cdd:cd04197    11 NRRFRPLTKEKPRCLLPLANVPLIDYTLEFLAL-NGVEEVF-----------VFCCSHSDQIKEYIEKSKWSKPKSslmi 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  82 ----------SAG-ALYYFRDRIMEEkpSHVFLLNCDVCCSFPLQGILDAHRRY-----GGIGTMLVIKVSAEAASQFGE 145
Cdd:cd04197    79 viiimsedcrSLGdALRDLDAKGLIR--GDFILVSGDVVSNIDLKEILEEHKERrkkdkNAIMTMVLKEASPPHRTRRTG 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1063700043 146 ---LIA-DPDTKELLHYTEKPETFvsdliNCGVYVFTSDIFNAIEEV 188
Cdd:cd04197   157 eefVIAvDPKTSRLLHYEELPGSK-----YRSITDLPSELLGSNSEV 198
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 288-347 1.33e-08

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: 51.42  E-value: 1.33e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063700043 288 LHPTAKIGPNVSI-----SANVRVGPGVRLISCIILDDVEIKENAVVINSIIGWKSSIGRWSRVQ 347
Cdd:cd04652     2 VGENTQVGEKTSIkrsviGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLK 66
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 4-188 3.05e-08

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: 54.46  E-value: 3.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043   4 GLGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKiSNLAQIFLIG---------------FYEER-------EFALYVS 61
Cdd:cd02541     9 GLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVA-AGIEDIIIVTgrgkraiedhfdrsyELEETlekkgktDLLEEVR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  62 SISNELKIpvRYLKEDKPHGSAGALYYFRDRIMEEkPSHVfLLNCDVCCSFP--LQGILDAHRRYGGiGTMLVIKVSAEA 139
Cdd:cd02541    88 IISDLANI--HYVRQKEPLGLGHAVLCAKPFIGDE-PFAV-LLGDDLIDSKEpcLKQLIEAYEKTGA-SVIAVEEVPPED 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063700043 140 ASQFGelIADP-----DTKELLHYTEKP--ETFVSDLINCGVYVFTSDIFNAIEEV 188
Cdd:cd02541   163 VSKYG--IVKGekidgDVFKVKGLVEKPkpEEAPSNLAIVGRYVLTPDIFDILENT 216
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 281-335 6.59e-08

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 53.99  E-value: 6.59e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063700043 281 YIHPSVKLHPTAKIGPNVSISANVRVGPGVRLIS-CIILDDVEIKENA-----VVI--NSIIG 335
Cdd:PRK00892  108 VIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAgAVIGDGVKIGADCrlhanVTIyhAVRIG 170
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-341 6.69e-08

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 54.36  E-value: 6.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043   4 GLGTRFRPlsfNTPKPLIPLAGQPMIHHPISACKKiSNLAQIFLI-GFYEEREFALYVSsisnelKIPVRYLKEDKPHG- 81
Cdd:PRK14355   12 GKGTRMKS---DLVKVMHPLAGRPMVSWPVAAARE-AGAGRIVLVvGHQAEKVREHFAG------DGDVSFALQEEQLGt 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  82 ------SAGALYYFRDRimeekpshVFLLNCDVCCSFP--LQGILDAHRRYGGIGTMLVIKVsaEAASQFGELIADPDTK 153
Cdd:PRK14355   82 ghavacAAPALDGFSGT--------VLILCGDVPLLRAetLQGMLAAHRATGAAVTVLTARL--ENPFGYGRIVRDADGR 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 154 ELLHYTEK---PETFVSDLINCGVYVFTSDIF----------NAIEEVY-SQIRDTSSNYQSATRSVPADfvrlDQDILS 219
Cdd:PRK14355  152 VLRIVEEKdatPEERSIREVNSGIYCVEAAFLfdaigrlgndNAQGEYYlTDIVAMAAAEGLRCLAFPVA----DPDEIM 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 220 PLAGKKQLytyenkdfweqiktpgkslkCSALYLSQFRETSPHILAsgdGTnrkpTIIG--DVYIHPSVKLHPTAKIGPN 297
Cdd:PRK14355  228 GVNDRAQL--------------------AEAARVLRRRINRELMLA---GV----TLIDpeTTYIDRGVVIGRDTTIYPG 280

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1063700043 298 VSISANVRVG------PGVRLISCIILDDVEIKENAVVINSIIGWKSSIG 341
Cdd:PRK14355  281 VCISGDTRIGegctieQGVVIKGCRIGDDVTVKAGSVLEDSVVGDDVAIG 330
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 4-198 1.25e-07

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


Pssm-ID: 133026 [Multi-domain]  Cd Length: 231  Bit Score: 51.87  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043   4 GLGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKISNLAQIFLIGFYEEREFALYVSSIsnELKIPVRYLKEDKP-HGS 82
Cdd:cd04183     7 GLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFICRDEHNTKFHLDESLK--LLAPNATVVELDGEtLGA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  83 AGALYYFRDRIMEEKPshVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVSAEAASqFGELIADPDTKEllhYTEKp 162
Cdd:cd04183    85 ACTVLLAADLIDNDDP--LLIFNCDQIVESDLLAFLAAFRERDLDGGVLTFFSSHPRWS-YVKLDENGRVIE---TAEK- 157

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1063700043 163 eTFVSDLINCGVYVFTS--DIFNAIEEVysQIRDTSSN 198
Cdd:cd04183   158 -EPISDLATAGLYYFKSgsLFVEAAKKM--IRKDDSVN 192
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
4-108 1.49e-07

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 51.78  E-value: 1.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043   4 GLGTRFRPLSFNTPKPLIPLAGQPMIHHPISACKKiSNLAQIFLIGFYEEREFALYVssisNELKIPVRYLKEDKPH--G 81
Cdd:COG1213     8 GRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAA-AGIKDIVVVTGYKAELIEEAL----ARPGPDVTFVYNPDYDetN 82

                          90       100
                  ....*....|....*....|....*..
gi 1063700043  82 SAGALYYFRDRIMEEkpshVFLLNCDV 108
Cdd:COG1213    83 NIYSLWLAREALDED----FLLLNGDV 105
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 281-329 2.66e-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: 51.17  E-value: 2.66e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1063700043 281 YIHPSVKLHPTAKIGPNVSISANVRVGPGVRLIS-CIILDDVEIKENAVV 329
Cdd:COG1043     9 IVDPGAKLGENVEIGPFCVIGPDVEIGDGTVIGShVVIEGPTTIGKNNRI 58
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 81-334 7.92e-07

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 50.60  E-value: 7.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  81 GSAGALYYFRDRIMEEKPSHVFLLNCDVCCSFPLQGILDAHRRYGGIGTMLVIKVSAEAASQFGELIADPDTKeLLHYTE 160
Cdd:PRK00844  100 GSADAIYQSLNLIEDEDPDYVVVFGADHVYRMDPRQMVDFHIESGAGVTVAAIRVPREEASAFGVIEVDPDGR-IRGFLE 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 161 KP-----------ETFVSdlinCGVYVFTSDIFnaIEEVYSQIRDTSSNYqsatrsvpaDFvrlDQDILSPLAGKKQLYT 229
Cdd:PRK00844  179 KPadppglpddpdEALAS----MGNYVFTTDAL--VDALRRDAADEDSSH---------DM---GGDIIPRLVERGRAYV 240

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 230 Y------------ENKDFWEQIKTpgkslkCSALYLSQFRETSPHilASGDGTNRK-PtiigdvyIHPSVKLHPTAK--- 293
Cdd:PRK00844  241 YdfstnevpgateRDRGYWRDVGT------IDAYYDAHMDLLSVH--PVFNLYNREwP-------IYTSSPNLPPAKfvd 305

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063700043 294 ------------IGPNVSISA----------NVRVGPGVRLISCIILDDVEIKENAVVINSII 334
Cdd:PRK00844  306 gggrvgsaqdslVSAGSIISGatvrnsvlspNVVVESGAEVEDSVLMDGVRIGRGAVVRRAIL 368
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 283-376 1.04e-06

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: 50.02  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 283 HPSVKLHPTAKIGPNVSISANVRVGPGVrliscIILDDVEIKENaVVI--NSIIGWKSSIGRWSRVQAsgdyndrlGITI 360
Cdd:COG1044    94 APAPGIHPSAVIDPSAKIGEGVSIGPFA-----VIGAGVVIGDG-VVIgpGVVIGDGVVIGDDCVLHP--------NVTI 159

                          90       100
                  ....*....|....*....|.
gi 1063700043 361 lGEAVTVEDEV-----AVIGS 376
Cdd:COG1044   160 -YERCVIGDRViihsgAVIGA 179
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 285-348 1.23e-06

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: 48.56  E-value: 1.23e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063700043 285 SVKLHPTAKIGPNVSISANVRVGPGVRLIS-CIILDDVEIKENAVVI-NSIIGWKSSIGRWSRVQA 348
Cdd:cd03352     1 SAKIGENVSIGPNAVIGEGVVIGDGVVIGPgVVIGDGVVIGDDCVIHpNVTIYEGCIIGDRVIIHS 66
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 276-335 2.03e-06

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: 48.17  E-value: 2.03e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063700043 276 IIG-DVYIHPSVKLHPTAKIGPNVSISANVRVGPGVRlisciILDDVEIKENAVVI-NSIIG 335
Cdd:cd03352     3 KIGeNVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVV-----IGDDCVIHPNVTIYeGCIIG 59
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 267-341 3.28e-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: 46.81  E-value: 3.28e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063700043 267 GDGTNRKPT--IIGDVYIHPSVKLHPTAKIGPNVSISANVRVGPGVRLISCIILDDVEIKENAVVINSIIGWKSSIG 341
Cdd:cd05636    21 GEGAIVRSGayIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSIIMDGTKVPHLNYVGDSVLGENVNLG 97
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 275-378 1.48e-05

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 46.75  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 275 TIIG--DVYIHPSVKLHPTAKIGPNVSISANVRVG------PGVRLISCIILDDVEIKeNAVVINSIIGWKSSIGRWSRV 346
Cdd:PRK14354  253 TIIDpeSTYIDADVEIGSDTVIEPGVVIKGNTVIGedcvigPGSRIVDSTIGDGVTIT-NSVIEESKVGDNVTVGPFAHL 331

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1063700043 347 qasgdyndRLGiTILGEAVTVEDEVAVIGSIV 378
Cdd:PRK14354  332 --------RPG-SVIGEEVKIGNFVEIKKSTI 354
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 300-335 1.56e-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: 43.61  E-value: 1.56e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1063700043 300 ISANVRVGPGVRLISCIILDDVEIKENAVVINSIIG 335
Cdd:cd04651    31 LFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIID 66
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
282-326 2.06e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 45.47  E-value: 2.06e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1063700043 282 IHPSVKLHPTAKIGPNVS------ISANVRVGPGVRLIS-CIILDDVEIKEN 326
Cdd:PRK05289    5 IHPTAIVEPGAKIGENVEigpfcvIGPNVVIGDGTVIGShVVIDGHTTIGKN 56
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
285-346 2.75e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 45.09  E-value: 2.75e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063700043 285 SVKLHPTAKIGPNVSISANVRVGPGvrlisCIILDDVEIKENAVVIN--SIIGWkSSIGRWSRV 346
Cdd:PRK05289    2 MAKIHPTAIVEPGAKIGENVEIGPF-----CVIGPNVVIGDGTVIGShvVIDGH-TTIGKNNRI 59
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 282-346 3.12e-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: 45.12  E-value: 3.12e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063700043 282 IHPSVKLHPTAKIGPNVSISANVRVGPGVRlisciILDDVEIKENAVvinsIIGWkSSIGRWSRV 346
Cdd:cd03351     2 IHPTAIVDPGAKIGENVEIGPFCVIGPNVE-----IGDGTVIGSHVV----IDGP-TTIGKNNRI 56
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-189 5.50e-05

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 44.98  E-value: 5.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043   4 GLGTRFRPlsfNTPKPLIPLAGQPMIHHPISACKKISNlaQIFLIGFYEEREFALYVSSISNelkiPVRYLKEDKPH--G 81
Cdd:PRK14359   11 GKGTRMKS---SLPKVLHTICGKPMLFYILKEAFAISD--DVHVVLHHQKERIKEAVLEYFP----GVIFHTQDLENypG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  82 SAGALyyfrdriMEEKPSH--VFLLNCD--VCCSFPLQGILDAHRRYggigTMLVIKvsAEAASQFGELI---------- 147
Cdd:PRK14359   82 TGGAL-------MGIEPKHerVLILNGDmpLVEKDELEKLLENDADI----VMSVFH--LADPKGYGRVViengqvkkiv 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1063700043 148 --ADPDTKELLhytekpetfvSDLINCGVYVFTSDIF----------NAIEEVY 189
Cdd:PRK14359  149 eqKDANEEELK----------IKSVNAGVYLFDRKLLeeylpllknqNAQKEYY 192
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 281-335 9.37e-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: 43.57  E-value: 9.37e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1063700043 281 YIHPSVKLHPTAKIGPNVSISANVRVGPGVRLIS-CIILDDVEIKENAVVIN-SIIG 335
Cdd:cd03351     7 IVDPGAKIGENVEIGPFCVIGPNVEIGDGTVIGShVVIDGPTTIGKNNRIFPfASIG 63
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 297-345 1.20e-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: 1.20e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1063700043 297 NVSISANVRVGPGVRLISCIILDDVEIKENAVVINSIIGWKSSIGRWSR 345
Cdd:PRK09451  283 NVTLGNRVKIGAGCVLKNCVIGDDCEISPYSVVEDANLGAACTIGPFAR 331
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 280-384 1.57e-04

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: 42.47  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 280 VYIHPSVKLHPTAKIGPNVSISANVRVGPGVRLisciilddveikENAVVINS--IIGWKSSIGRWSRVqASGdyndrlg 357
Cdd:cd03360    85 TLIHPSAVVSPSAVIGEGCVIMAGAVINPDARI------------GDNVIINTgaVIGHDCVIGDFVHI-APG------- 144

                          90       100
                  ....*....|....*....|....*...
gi 1063700043 358 iTILGEAVTVEDEVAV-IGSIVLQNKTL 384
Cdd:cd03360   145 -VVLSGGVTIGEGAFIgAGATIIQGVTI 171
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 280-341 1.76e-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: 1.76e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063700043 280 VYIHPSVKLHPTAKIGPNVSISANVRVGPGVRLISC---------IILDDVEIKENAVV-------INSIIGWKSSIG 341
Cdd:cd00208     1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAAtgpneknptIIGDNVEIGANAVIhggvkigDNAVIGAGAVVT 78
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 285-342 3.26e-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: 41.93  E-value: 3.26e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 285 SVKLHPTAKIGPNVSISANVRVGPGvrlisCIILDDVEIKENAVVIN--SIIGWkSSIGR 342
Cdd:COG1043     1 MAMIHPTAIVDPGAKLGENVEIGPF-----CVIGPDVEIGDGTVIGShvVIEGP-TTIGK 54
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 281-341 3.70e-04

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: 40.69  E-value: 3.70e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063700043 281 YIHPSVKLHPTAKIGPNVSISANVRVGPGVrLISC------IILDDVEIKENaVVINSIIGWKSSIG 341
Cdd:cd00710     4 VIDPSAYVHPTAVVIGDVIIGDNVFVGPGA-SIRAdegtpiIIGANVNIQDG-VVIHALEGYSVWIG 68
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
4-188 4.54e-04

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 41.56  E-value: 4.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043   4 GLGTRFRPLSFNTPKPLIPLAGQPMIHHPI-----SACKKIsnlaqIFLIG---------F---YE-EREF------ALY 59
Cdd:COG1210    12 GLGTRFLPATKAIPKEMLPIVDKPLIQYVVeeavaAGIEEI-----IFVTGrgkraiedhFdrsYElEATLeakgkeELL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  60 --VSSISNELKIpvRYLKEDKPHGSAGALYYFRDRIMEEkPshvF--LLNCDVCCSFP--LQGILDAHRRYGG--IGTMl 131
Cdd:COG1210    87 eeVRSISPLANI--HYVRQKEPLGLGHAVLCARPFVGDE-P---FavLLGDDLIDSEKpcLKQMIEVYEETGGsvIAVQ- 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063700043 132 viKVSAEAASQFGelIADPDTKELLHYT-----EKP--ETFVSDLINCGVYVFTSDIFNAIEEV 188
Cdd:COG1210   160 --EVPPEEVSKYG--IVDGEEIEGGVYRvtglvEKPapEEAPSNLAIVGRYILTPEIFDILEKT 219
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 4-108 5.58e-04

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: 40.26  E-value: 5.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043   4 GLGTRFrplsfNTPKPLIPLAGQPMIHHPISACKKISnlAQIFLIGFYEEREFALyvssisneLKIPVRYLKEDKPH-GS 82
Cdd:pfam12804   7 GRSSRM-----GGDKALLPLGGKPLLERVLERLRPAG--DEVVVVANDEEVLAAL--------AGLGVPVVPDPDPGqGP 71

                          90       100
                  ....*....|....*....|....*...
gi 1063700043  83 AGALYyfrdRIMEEKPSH--VFLLNCDV 108
Cdd:pfam12804  72 LAGLL----AALRAAPGAdaVLVLACDM 95
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 282-346 9.32e-04

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 40.39  E-value: 9.32e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063700043 282 IHPSVKLHPTAKIGPNVSIsanvrvGPGvrlisCIILDDVEIKEnavviNSIIGWKSSIGRWSRV 346
Cdd:PRK12461    2 IHPTAVIDPSAKLGSGVEI------GPF-----AVIGANVEIGD-----GTWIGPHAVILGPTRI 50
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 316-394 1.89e-03

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


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 36.84  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 316 IILDDVEIKENAVVINSIIGWKSSIGRWSRVQASgdyndrlgitILGEAVTVEDEVAVIGSIVLQNKTL--NVSVQDDII 393
Cdd:cd03356     1 LIGESTVIGENAIIKNSVIGDNVRIGDGVTITNS----------ILMDNVTIGANSVIVDSIIGDNAVIgeNVRVVNLCI 70


                  .
gi 1063700043 394 L 394
Cdd:cd03356    71 I 71
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 282-379 1.91e-03

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 38.85  E-value: 1.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 282 IHPSVKLHPTAK-IGpNVSISANVRVGPGVRLISciildDVeikenavviNSIIgwkssIGRWSRVQ------ASGDYNd 354
Cdd:COG0663    13 IHPSAFVAPTAVvIG-DVTIGEDVSVWPGAVLRG-----DV---------GPIR-----IGEGSNIQdgvvlhVDPGYP- 71

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1063700043 355 rlgiTILGEAVTV-----------EDEVAV-IGSIVL 379
Cdd:COG0663    72 ----LTIGDDVTIghgailhgctiGDNVLIgMGAIVL 104
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 267-335 3.18e-03

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: 36.40  E-value: 3.18e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063700043 267 GDGTNRKPTIIGdvyihpsvklhPTAKIGPNVSISA-----NVRVGPGVRLISCIILDDVEIKENAVVINSIIG 335
Cdd:cd04652     9 GEKTSIKRSVIG-----------ANCKIGKRVKITNcvimdNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLVG 71
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 290-369 3.55e-03

eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 36.02  E-value: 3.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 290 PTAKIGPNVSIS-----ANVRVGPGVRLISCIILDDVEIKENAVVINSIIGWKSSIGRWSRVQASgdyndrlgiTILGEA 364
Cdd:cd05787     4 RGTSIGEGTTIKnsvigRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIPPG---------SLISFG 74


                  ....*
gi 1063700043 365 VTVED 369
Cdd:cd05787    75 VVIGD 79
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 289-346 4.27e-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: 38.40  E-value: 4.27e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 289 HPTAKIGPNVSISANVRVGPgvrliSCIILDDVEIKENaVVINS--IIGWKSSIGRWSRV 346
Cdd:TIGR01852   2 HPTAIIEPGAEIGENVEIGP-----FCIVGPGVKIGDG-VELKShvVILGHTTIGEGTRI 55
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 4-186 5.71e-03

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: 37.94  E-value: 5.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043   4 GLGTRFRPLSFNTPKPLIPLAGQPMIHHPISACkKISNLAQIFLIGfyEEREFALYVSSISN--ELKIPVRYLKEDKPHG 81
Cdd:cd02538     9 GSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTL-MLAGIREILIIS--TPEDLPLFKELLGDgsDLGIRITYAVQPKPGG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043  82 SAGALYYFRDRIMEEKpshvfllncdVCCsfplqgILDAHRRYGGIGTMLVIKVSA--EAASQFGELIADP--------- 150
Cdd:cd02538    86 LAQAFIIGEEFIGDDP----------VCL------ILGDNIFYGQGLSPILQRAAAqkEGATVFGYEVNDPerygvvefd 149

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1063700043 151 DTKELLHYTEKPETFVSDLINCGVYVFTSDIFNAIE 186
Cdd:cd02538   150 ENGRVLSIEEKPKKPKSNYAVTGLYFYDNDVFEIAK 185
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-48 5.86e-03

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 38.47  E-value: 5.86e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1063700043   4 GLGTRfrpLSFNTPKPLIPLAGQPMIHHPISACKKISNlAQIFLI 48
Cdd:PRK09451   14 GKGTR---MYSDLPKVLHTLAGKPMVQHVIDAANELGA-QHVHLV 54
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-36 6.34e-03

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 38.69  E-value: 6.34e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1063700043   4 GLGTRFRPlsfNTPKPLIPLAGQPMIHHPISAC 36
Cdd:PRK14353   14 GEGTRMKS---SLPKVLHPVAGRPMLAHVLAAA 43
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 282-329 7.78e-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: 36.96  E-value: 7.78e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1063700043 282 IHPSVKLHPTAKIGPNVSISANVRVGPGVRL---ISCIILDD-VEIKENAVV 329
Cdd:cd04745     3 VDPSSFVHPTAVLIGDVIIGKNCYIGPHASLrgdFGRIVIRDgANVQDNCVI 54
LbH_SAT cd03354
Serine acetyltransferase (SAT): SAT catalyzes the CoA-dependent acetylation of the side chain ...
 280-348 9.23e-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: 35.49  E-value: 9.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063700043 280 VYIHPSVKL--------------HPTAKIGPNVSISANVRVGpGVRLISC----IILDDVEIKENAVVINSIigwksSIG 341
Cdd:cd03354     3 IDIHPGAKIgpglfidhgtgiviGETAVIGDNCTIYQGVTLG-GKGKGGGkrhpTIGDNVVIGAGAKILGNI-----TIG 76


                  ....*..
gi 1063700043 342 RWSRVQA 348
Cdd:cd03354    77 DNVKIGA 83
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH