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Conserved domains on  [gi|564365550|ref|XP_006243873|]
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mannose-1-phosphate guanyltransferase beta isoform X1 [Rattus norvegicus]

Protein Classification

mannose-1-phosphate guanyltransferase( domain architecture ID 10157656)

mannose-1-phosphate guanyltransferase catalyzes the formation of GDP-mannose, an essential precursor of glycan moieties of glycoproteins and glycolipids; similar to Homo sapiens mannose-1-phosphate guanyltransferase beta

EC:  2.7.7.13
Gene Ontology:  GO:0004475|GO:0009298|GO:0006486|GO:0005525

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 34-266 1.03e-171

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: 478.24  E-value: 1.03e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  34 MKALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQEQRLGIRISMSHE 113
Cdd:cd06425    1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKKLGIKITFSIE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 114 EEPLGTAGPLALARDLLSETADPFFVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADTGRIHRFV 193
Cdd:cd06425   81 TEPLGTAGPLALARDLLGDDDEPFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDENTGRIERFV 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564365550 194 EKPQVFVSNKINAGMYILSPAVLQRIQLKPTSIEKEIFPVMAKEGQLYAMELQGFWMDIGQPKDFLTGMCLFL 266
Cdd:cd06425  161 EKPKVFVGNKINAGIYILNPSVLDRIPLRPTSIEKEIFPKMASEGQLYAYELPGFWMDIGQPKDFLKGMSLYL 233
LbetaH super family cl00160
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 288-367 8.54e-33

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: 118.02  E-value: 8.54e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 288 LVDPSARIGQNCSIGPNVSLGPGVVVEDGVCIRRCTVLRDAHIRSHSWLESCIVGWRCRVGQWVRMENVTVLGEDVIVND 367
Cdd:cd05824    1 LIDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLENVTVLGDDVTIKD 80
 
Name Accession Description Interval E-value
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 34-266 1.03e-171

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: 478.24  E-value: 1.03e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  34 MKALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQEQRLGIRISMSHE 113
Cdd:cd06425    1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKKLGIKITFSIE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 114 EEPLGTAGPLALARDLLSETADPFFVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADTGRIHRFV 193
Cdd:cd06425   81 TEPLGTAGPLALARDLLGDDDEPFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDENTGRIERFV 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564365550 194 EKPQVFVSNKINAGMYILSPAVLQRIQLKPTSIEKEIFPVMAKEGQLYAMELQGFWMDIGQPKDFLTGMCLFL 266
Cdd:cd06425  161 EKPKVFVGNKINAGIYILNPSVLDRIPLRPTSIEKEIFPKMASEGQLYAYELPGFWMDIGQPKDFLKGMSLYL 233
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 35-267 8.77e-88

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: 265.48  E-value: 8.77e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  35 KALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQEqRLGIRISMSHEE 114
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGS-RFGVRITYVDEG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 115 EPLGTAGPLALARDLLSEtaDPFFVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADtGRIHRFVE 194
Cdd:COG1208   80 EPLGTGGALKRALPLLGD--EPFLVLNGDILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGD-GRVTRFVE 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564365550 195 KPQVFVSNKINAGMYILSPAVLQRIQLKPT-SIEkEIFPVMAKEGQLYAMELQGFWMDIGQPKDFLTGMCLFLQ 267
Cdd:COG1208  157 KPEEPPSNLINAGIYVLEPEIFDYIPEGEPfDLE-DLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLS 229
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 35-263 9.06e-64

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: 204.02  E-value: 9.06e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550   35 KALILVGGYGTRLRPLTLSTPKPLVDFCNK-PILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQEQRLGIRISMSHE 113
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  114 EEPLGTAGPLALARDLLSETADPFFVLNSDVICDFPFQAMVQFHRHHGQE--GSILVTKVEEPSKYGVVVCEaDTGRIHR 191
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSDVLVLGGDHIYRMDLEQAVKFHIEKAADatVTFGIVPVEPPTGYGVVEFD-DNGRVIR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  192 FVEKPQVFV-SNKINAGMYILSPAVLQRI--QLKP----TSIEKEIFPVMAKEGQL-YAMELQGF-WMDIGQPKDFLTGM 262
Cdd:pfam00483 160 FVEKPKLPKaSNYASMGIYIFNSGVLDFLakYLEElkrgEDEITDILPKALEDGKLaYAFIFKGYaWLDVGTWDSLWEAN 239


                  .
gi 564365550  263 C 263
Cdd:pfam00483 240 L 240
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 34-348 6.07e-61

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: 201.67  E-value: 6.07e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550   34 MKALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAqEQRLGIRISMSHE 113
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGD-GSRGGVPIEYVVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  114 EEPLGTAGPLALARDLLSetaDPFFVLNSDVICDFP-FQAMVqfhrhHGQEGSILVTKVEEPSKYGVVvcEADTGRIHRF 192
Cdd:TIGR03992  80 EEQLGTADALGSAKEYVD---DEFLVLNGDVLLDSDlLERLI-----RAEAPAIAVVEVDDPSDYGVV--ETDGGRVTGI 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  193 VEKPQVFVSNKINAGMYILSPAV---LQRIQLKPTSiEKEIFPV---MAKEGQLYAMELQGFWMDIGQPKDFLTGMCLFL 266
Cdd:TIGR03992 150 VEKPENPPSNLINAGIYLFSPEIfelLEKTKLSPRG-EYELTDAlqlLIDEGKVKAVELDGFWLDVGRPWDLLDANEALL 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  267 QSLRQKHPERLYSGPGVVGNVLVDPSAR------------IGQNCSIGPN------VSLGPGVVVEDGVCIRRCTVLRDA 328
Cdd:TIGR03992 229 DNLEPRIEGTVEENVTIKGPVVIGEGAVirsgtyiegpvyIGKNCDIGPNayirpyTVIGNNVHIGNAVEIKNSIIMEGT 308

                         330       340
                  ....*....|....*....|
gi 564365550  329 HIRSHSWLESCIVGWRCRVG 348
Cdd:TIGR03992 309 KIPHLSYVGDSVIGENCNFG 328
LbH_M1P_guanylylT_C cd05824
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 288-367 8.54e-33

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: 118.02  E-value: 8.54e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 288 LVDPSARIGQNCSIGPNVSLGPGVVVEDGVCIRRCTVLRDAHIRSHSWLESCIVGWRCRVGQWVRMENVTVLGEDVIVND 367
Cdd:cd05824    1 LIDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLENVTVLGDDVTIKD 80
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 32-363 1.07e-20

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 93.27  E-value: 1.07e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  32 DAMKALILVGGYGTRLRPltlSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQEQrlgirISMS 111
Cdd:PRK14355   2 NNLAAIILAAGKGTRMKS---DLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDGD-----VSFA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 112 HEEEPLGTAGPLALARDLLSETADPFFVLNSDV--ICDFPFQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADtGRI 189
Cdd:PRK14355  74 LQEEQLGTGHAVACAAPALDGFSGTVLILCGDVplLRAETLQGMLAAHRATGAAVTVLTARLENPFGYGRIVRDAD-GRV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 190 HRFVEK----PQVFVSNKINAGMYILSPAVLQRI--QLKPTSIEKE-----IFPVMAKEGQLY-------AMELQGF--W 249
Cdd:PRK14355 153 LRIVEEkdatPEERSIREVNSGIYCVEAAFLFDAigRLGNDNAQGEyyltdIVAMAAAEGLRClafpvadPDEIMGVndR 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 250 MDIGQPKDFLTGMC---LFLQSLRQKHPERLYSGPGVVgnvlVDPSARIGQNCSIGPNVSLGPGVVVEDGVCIRRCTVLR 326
Cdd:PRK14355 233 AQLAEAARVLRRRInreLMLAGVTLIDPETTYIDRGVV----IGRDTTIYPGVCISGDTRIGEGCTIEQGVVIKGCRIGD 308

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 564365550 327 DAHIRSHSWLESCIVGWRCRVGQWVRMENVTVLGEDV 363
Cdd:PRK14355 309 DVTVKAGSVLEDSVVGDDVAIGPMAHLRPGTELSAHV 345
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 289-363 2.09e-11

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 64.65  E-value: 2.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 289 VDPSARIGQNCSIGPNVSLGPGVVVEDGVCIR-RCTVLRDAHIRSHSWL-------ESCIVGWRCRV------------- 347
Cdd:COG1044  105 IDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGpGVVIGDGVVIGDDCVLhpnvtiyERCVIGDRVIIhsgavigadgfgf 184

                         90       100
                 ....*....|....*....|....
gi 564365550 348 -----GQWVRME---NVtVLGEDV 363
Cdd:COG1044  185 apdedGGWVKIPqlgRV-VIGDDV 207
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 289-363 1.21e-10

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 62.08  E-value: 1.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 289 VDPSARIGQNCSIGPNVSLGPGVVVEDGVCI-------RRCTVLRDAHIRSH-SWLESCIVGWRCRV------------- 347
Cdd:PRK00892 109 IDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIgagavigDGVKIGADCRLHANvTIYHAVRIGNRVIIhsgavigsdgfgf 188

                         90       100
                 ....*....|....*....|...
gi 564365550 348 ----GQWVRME---NVtVLGEDV 363
Cdd:PRK00892 189 andrGGWVKIPqlgRV-IIGDDV 210
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
292-320 3.97e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 40.01  E-value: 3.97e-05
                          10        20
                  ....*....|....*....|....*....
gi 564365550  292 SARIGQNCSIGPNVSLGPGVVVEDGVCIR 320
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIG 29
 
Name Accession Description Interval E-value
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 34-266 1.03e-171

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: 478.24  E-value: 1.03e-171
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  34 MKALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQEQRLGIRISMSHE 113
Cdd:cd06425    1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKKLGIKITFSIE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 114 EEPLGTAGPLALARDLLSETADPFFVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADTGRIHRFV 193
Cdd:cd06425   81 TEPLGTAGPLALARDLLGDDDEPFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDENTGRIERFV 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564365550 194 EKPQVFVSNKINAGMYILSPAVLQRIQLKPTSIEKEIFPVMAKEGQLYAMELQGFWMDIGQPKDFLTGMCLFL 266
Cdd:cd06425  161 EKPKVFVGNKINAGIYILNPSVLDRIPLRPTSIEKEIFPKMASEGQLYAYELPGFWMDIGQPKDFLKGMSLYL 233
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 35-267 8.77e-88

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: 265.48  E-value: 8.77e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  35 KALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQEqRLGIRISMSHEE 114
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGS-RFGVRITYVDEG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 115 EPLGTAGPLALARDLLSEtaDPFFVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADtGRIHRFVE 194
Cdd:COG1208   80 EPLGTGGALKRALPLLGD--EPFLVLNGDILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGD-GRVTRFVE 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564365550 195 KPQVFVSNKINAGMYILSPAVLQRIQLKPT-SIEkEIFPVMAKEGQLYAMELQGFWMDIGQPKDFLTGMCLFLQ 267
Cdd:COG1208  157 KPEEPPSNLINAGIYVLEPEIFDYIPEGEPfDLE-DLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLS 229
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 36-253 1.17e-84

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: 256.74  E-value: 1.17e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  36 ALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQEqRLGIRISMSHEEE 115
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGS-KFGVNIEYVVQEE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 116 PLGTAGPLALARDLLSEtaDPFFVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEaDTGRIHRFVEK 195
Cdd:cd04181   80 PLGTAGAVRNAEDFLGD--DDFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEVEDPSRYGVVELD-DDGRVTRFVEK 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564365550 196 PQVFVSNKINAGMYILSPAVLQRIQLKPTS---IEKEIFPVMAKEGQLYAMELQGFWMDIG 253
Cdd:cd04181  157 PTLPESNLANAGIYIFEPEILDYIPEILPRgedELTDAIPLLIEEGKVYGYPVDGYWLDIG 217
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 35-263 9.06e-64

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: 204.02  E-value: 9.06e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550   35 KALILVGGYGTRLRPLTLSTPKPLVDFCNK-PILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQEQRLGIRISMSHE 113
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  114 EEPLGTAGPLALARDLLSETADPFFVLNSDVICDFPFQAMVQFHRHHGQE--GSILVTKVEEPSKYGVVVCEaDTGRIHR 191
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSDVLVLGGDHIYRMDLEQAVKFHIEKAADatVTFGIVPVEPPTGYGVVEFD-DNGRVIR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  192 FVEKPQVFV-SNKINAGMYILSPAVLQRI--QLKP----TSIEKEIFPVMAKEGQL-YAMELQGF-WMDIGQPKDFLTGM 262
Cdd:pfam00483 160 FVEKPKLPKaSNYASMGIYIFNSGVLDFLakYLEElkrgEDEITDILPKALEDGKLaYAFIFKGYaWLDVGTWDSLWEAN 239


                  .
gi 564365550  263 C 263
Cdd:pfam00483 240 L 240
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 34-348 6.07e-61

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: 201.67  E-value: 6.07e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550   34 MKALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAqEQRLGIRISMSHE 113
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGD-GSRGGVPIEYVVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  114 EEPLGTAGPLALARDLLSetaDPFFVLNSDVICDFP-FQAMVqfhrhHGQEGSILVTKVEEPSKYGVVvcEADTGRIHRF 192
Cdd:TIGR03992  80 EEQLGTADALGSAKEYVD---DEFLVLNGDVLLDSDlLERLI-----RAEAPAIAVVEVDDPSDYGVV--ETDGGRVTGI 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  193 VEKPQVFVSNKINAGMYILSPAV---LQRIQLKPTSiEKEIFPV---MAKEGQLYAMELQGFWMDIGQPKDFLTGMCLFL 266
Cdd:TIGR03992 150 VEKPENPPSNLINAGIYLFSPEIfelLEKTKLSPRG-EYELTDAlqlLIDEGKVKAVELDGFWLDVGRPWDLLDANEALL 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  267 QSLRQKHPERLYSGPGVVGNVLVDPSAR------------IGQNCSIGPN------VSLGPGVVVEDGVCIRRCTVLRDA 328
Cdd:TIGR03992 229 DNLEPRIEGTVEENVTIKGPVVIGEGAVirsgtyiegpvyIGKNCDIGPNayirpyTVIGNNVHIGNAVEIKNSIIMEGT 308

                         330       340
                  ....*....|....*....|
gi 564365550  329 HIRSHSWLESCIVGWRCRVG 348
Cdd:TIGR03992 309 KIPHLSYVGDSVIGENCNFG 328
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 36-258 8.33e-61

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: 195.85  E-value: 8.33e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  36 ALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMkAQEQRLGIRISMSHEEE 115
Cdd:cd06915    1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYF-GDGYRGGIRIYYVIEPE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 116 PLGTAGPLALARDLLSEtaDPFFVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADtGRIHRFVEK 195
Cdd:cd06915   80 PLGTGGAIKNALPKLPE--DQFLVLNGDTYFDVDLLALLAALRASGADATMALRRVPDASRYGNVTVDGD-GRVIAFVEK 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564365550 196 PQVFVSNKINAGMYILSPAVLQRIQLKPTSIEKEIFPVMAKEGQLYAMELQGFWMDIGQPKDF 258
Cdd:cd06915  157 GPGAAPGLINGGVYLLRKEILAEIPADAFSLEADVLPALVKRGRLYGFEVDGYFIDIGIPEDY 219
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 36-252 2.44e-58

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: 190.54  E-value: 2.44e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  36 ALILVGG--YGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAA-AGVDHVILAVSYMSQMLEKEMKAQEQRLGIRISMSH 112
Cdd:cd06428    1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKvPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 113 EEEPLGTAGPLALARD-LLSETADPFFVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKV--EEPSKYGVVVCEADTGRI 189
Cdd:cd06428   81 EYKPLGTAGGLYHFRDqILAGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEAsrEQASNYGCIVEDPSTGEV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 190 HRFVEKPQVFVSNKINAGMYILSPAVLQRIQL---------------------KPTSIEKEIFPVMAKEGQLYAMELQGF 248
Cdd:cd06428  161 LHYVEKPETFVSDLINCGVYLFSPEIFDTIKKafqsrqqeaqlgddnnregraEVIRLEQDVLTPLAGSGKLYVYKTDDF 240


                 ....
gi 564365550 249 WMDI 252
Cdd:cd06428  241 WSQI 244
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 35-260 2.21e-54

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: 179.30  E-value: 2.21e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  35 KALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMkaQEQRLGIRISMSHEE 114
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHL--GDSRFGLRITISDEP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 115 -EPLGTAGPLALARDLLSEtaDPFFVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKVEEPSK--YGVVVCEADtGRIHR 191
Cdd:cd06422   79 dELLETGGGIKKALPLLGD--EPFLVVNGDILWDGDLAPLLLLHAWRMDALLLLLPLVRNPGHngVGDFSLDAD-GRLRR 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564365550 192 FVEKpqvFVSNKINAGMYILSPAVLQRIQLKPTSIeKEIFPVMAKEGQLYAMELQGFWMDIGQPKDFLT 260
Cdd:cd06422  156 GGGG---AVAPFTFTGIQILSPELFAGIPPGKFSL-NPLWDRAIAAGRLFGLVYDGLWFDVGTPERLLA 220
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 36-258 1.78e-52

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: 174.24  E-value: 1.78e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  36 ALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKaQEQRLGIRISMSHEEE 115
Cdd:cd06426    1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFG-DGSKFGVNISYVREDK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 116 PLGTAGPLALARDLLSetaDPFFVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKVEEPSKYGVVvcEADTGRIHRFVEK 195
Cdd:cd06426   80 PLGTAGALSLLPEKPT---DPFLVMNGDILTNLNYEHLLDFHKENNADATVCVREYEVQVPYGVV--ETEGGRITSIEEK 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 196 P-QVFvsnKINAGMYILSPAVL------QRIQLkPTSIEKEIfpvmAKEGQLYAMELQGFWMDIGQPKDF 258
Cdd:cd06426  155 PtHSF---LVNAGIYVLEPEVLdlipknEFFDM-PDLIEKLI----KEGKKVGVFPIHEYWLDIGRPEDY 216
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 34-266 1.00e-50

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: 170.06  E-value: 1.00e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  34 MKALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLeKEMKAQEQRLGIRISMSHE 113
Cdd:cd04189    1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEI-KEALGDGSRFGVRITYILQ 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 114 EEPLGTAGPLALARDLLSEtaDPFFVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEAdtGRIHRFV 193
Cdd:cd04189   80 EEPLGLAHAVLAARDFLGD--EPFVVYLGDNLIQEGISPLVRDFLEEDADASILLAEVEDPRRFGVAVVDD--GRIVRLV 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564365550 194 EKPQVFVSNKINAGMYILSPAVLQRI-QLKPTS-----IEKEIFPVMAKEGQLYAMELQGFWMDIGQPKDFLTGMCLFL 266
Cdd:cd04189  156 EKPKEPPSNLALVGVYAFTPAIFDAIsRLKPSWrgeleITDAIQWLIDRGRRVGYSIVTGWWKDTGTPEDLLEANRLLL 234
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 35-347 1.67e-48

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: 167.96  E-value: 1.67e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550   35 KALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQEQRLGIRISMSHEE 114
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  115 EPLGTAGPLALARDLLSEtaDPFFVLNSDVICDFpfqAMVQFHRHHGQEG---SILVTKVEEPSKYGVVVCEaDTGRIHR 191
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGD--DDFVVYLGDNLIQD---GISRFVKSFEEKDydaLILLTKVRDPTAFGVAVLE-DGKRILK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  192 FVEKPQVFVSNKINAGMYILSPAVLQRIQ-LKPT-----SIEKEIFPVMAKEGQLYAMELQGFWMDIGQPKDFLTGMCLF 265
Cdd:TIGR01208 155 LVEKPKEPPSNLAVVGLYMFRPLIFEAIKnIKPSwrgelEITDAIQWLIEKGYKVGGSKVTGWWKDTGKPEDLLDANRLI 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  266 LQSLrQKHPERLYSGPGVVGNVLVDPSAR-----------IGQNCSI-----GPNVSLGPGVVVEDGVcIRRCTVLRDAH 329
Cdd:TIGR01208 235 LDEV-EREVQGVDDESKIRGRVVVGEGAKivnsvirgpavIGEDCIIensyiGPYTSIGEGVVIRDAE-VEHSIVLDESV 312

                         330
                  ....*....|....*....
gi 564365550  330 IRS-HSWLESCIVGWRCRV 347
Cdd:TIGR01208 313 IEGvQARIVDSVIGKKVRI 331
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
34-306 1.29e-44

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 156.02  E-value: 1.29e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  34 MKALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVS-YMSQMLEKEMKAQEQrLGIRISMSH 112
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTpEDGPQFERLLGDGSQ-LGIKISYAV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 113 EEEPLGTAGPLALARDLLSEtaDPFFVLNSDVICDFP-FQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADtGRIHR 191
Cdd:COG1209   80 QPEPLGLAHAFIIAEDFIGG--DPVALVLGDNIFYGDgLSELLREAAARESGATIFGYKVEDPERYGVVEFDED-GRVVS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 192 FVEKPQVFVSNKINAGMYILSPAVLQRIQ-LKP--------TSIEKEifpvMAKEGQLY-AMELQGF-WMDIGQPKDFL- 259
Cdd:COG1209  157 LEEKPKEPKSNLAVTGLYFYDNDVVEIAKnLKPsargeleiTDANQA----YLERGKLVvELLGRGFaWLDTGTHESLLe 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564365550 260 TGMclFLQSLrQKHPERLYSGPGVV----GNVLVDPSARIGQ---NCSIGPNVS 306
Cdd:COG1209  233 ANR--FVLTI-EKRQGLKIACPEEIayrmGWIDAEQLAKLANsleKSGYGPYLL 283
LbH_M1P_guanylylT_C cd05824
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 288-367 8.54e-33

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: 118.02  E-value: 8.54e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 288 LVDPSARIGQNCSIGPNVSLGPGVVVEDGVCIRRCTVLRDAHIRSHSWLESCIVGWRCRVGQWVRMENVTVLGEDVIVND 367
Cdd:cd05824    1 LIDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLENVTVLGDDVTIKD 80
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 36-263 1.93e-31

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: 119.98  E-value: 1.93e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  36 ALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLeKE--MKAQEQRLGIRISMS-- 111
Cdd:cd02524    1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYKGHVI-KEyfLNYFLHNSDVTIDLGtn 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 112 ----HEEEPLG-------------TAGPLALARDLLsETADPFFVLNSDVICDFPFQAMVQFHRHHGqeGSILVTKVEEP 174
Cdd:cd02524   80 rielHNSDIEDwkvtlvdtglntmTGGRLKRVRRYL-GDDETFMLTYGDGVSDVNINALIEFHRSHG--KLATVTAVHPP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 175 SKYGVVVCEaDTGRIHRFVEKPQVfVSNKINAGMYILSPAVLQRIQLKPTSIEKEIFPVMAKEGQLYAMELQGFW--MDI 252
Cdd:cd02524  157 GRFGELDLD-DDGQVTSFTEKPQG-DGGWINGGFFVLEPEVFDYIDGDDTVFEREPLERLAKDGELMAYKHTGFWqcMDT 234

                        250
                 ....*....|.
gi 564365550 253 GQPKDFLTGMC 263
Cdd:cd02524  235 LRDKQTLEELW 245
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 36-362 2.73e-31

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 122.49  E-value: 2.73e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  36 ALILVGGYGTRLRPLTLSTPKP---------LVDFcnkPI--LLHqvealaaAGVDHVILAVSYMSQMLEKEM-KAQEQR 103
Cdd:COG0448    4 AIILAGGRGSRLGPLTKDRAKPavpfggkyrIIDF---PLsnCVN-------SGIRRVGVLTQYKSHSLNDHIgSGKPWD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 104 L-----GIRI-----SMSHEEEPLGTAGPLALARDLL-SETADPFFVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKV- 171
Cdd:COG0448   74 LdrkrgGVFIlppyqQREGEDWYQGTADAVYQNLDFIeRSDPDYVLILSGDHIYKMDYRQMLDFHIESGADITVACIEVp 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 172 -EEPSKYGVVVCEADtGRIHRFVEKPQVFVSNKINAGMYILSPAVLQRI--QLKPTSIE---KEIFPVMAKEGQLYAMEL 245
Cdd:COG0448  154 rEEASRFGVMEVDED-GRITEFEEKPKDPKSALASMGIYVFNKDVLIELleEDAPNSSHdfgKDIIPRLLDRGKVYAYEF 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 246 QGFWMDIGQPKDFL-TGMCLflqsLRQKHPERLY--SGPgVVGNVLVDPSARIGQN-----------CSIGPNVS---LG 308
Cdd:COG0448  233 DGYWRDVGTIDSYYeANMDL----LDPEPEFNLYdpEWP-IYTKQKDLPPAKFVRGgkvknslvsngCIISGTVEnsvLF 307

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564365550 309 PGVVVEDGVCIRRCTVLRDAHIRSHSWLESCIVGWRCRVGqwvrmENVtVLGED 362
Cdd:COG0448  308 RGVRVESGAVVENSVIMPGVVIGEGAVIENAIIDKNVVIP-----PGV-VIGED 355
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 34-363 9.35e-31

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: 122.06  E-value: 9.35e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  34 MKALILVGGYGTRLRPltlSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQeqrlgiRISMSHE 113
Cdd:COG1207    3 LAVVILAAGKGTRMKS---KLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALADL------DVEFVLQ 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 114 EEPLGTAGPLALARDLLSETADPFFVLNSDVicdfPF------QAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADtG 187
Cdd:COG1207   74 EEQLGTGHAVQQALPALPGDDGTVLVLYGDV----PLiraetlKALLAAHRAAGAAATVLTAELDDPTGYGRIVRDED-G 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 188 RIHRFVE----KPQVFVSNKINAGMYILSPAVLQRI--QLKPTSIEKE-----IFPVMAKEG------------------ 238
Cdd:COG1207  149 RVLRIVEekdaTEEQRAIREINTGIYAFDAAALREAlpKLSNDNAQGEyyltdVIAIARADGlkvaavqpedpwevlgvn 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 239 ---QLYAME--LQG----FWMDIGqpkdfLTgmclflqsLRQkhPERLYsgpgvvgnvlVDPSARIGQNCSIGPNV---- 305
Cdd:COG1207  229 drvQLAEAEriLQRriaeRLMRAG-----VT--------IID--PATTY----------IDGDVEIGRDVVIDPNVileg 283

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 306 --SLGPGVVVEDGVCIRRCTVLRDAHIRsHSWLESCIVGWRCRVGQWVRMENVTVLGEDV 363
Cdd:COG1207  284 ktVIGEGVVIGPNCTLKDSTIGDGVVIK-YSVIEDAVVGAGATVGPFARLRPGTVLGEGV 342
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 34-259 3.23e-30

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: 116.86  E-value: 3.23e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  34 MKALILVGGYGTRLRPLTLSTPK---PLVDfcnKPILLHQVEALAAAGVDHVILAVSYMSQMLEK------------EMK 98
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKemlPIVD---KPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDhfdrsyeleetlEKK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  99 AQEQRL--------GIRISMSHEEEPLGTAGPLALARDLLSEtaDPFFVLNSDVICD---FPFQAMVQFHRHHGqeGSIL 167
Cdd:cd02541   78 GKTDLLeevriisdLANIHYVRQKEPLGLGHAVLCAKPFIGD--EPFAVLLGDDLIDskePCLKQLIEAYEKTG--ASVI 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 168 -VTKV--EEPSKYGVVVCEA---DTGRIHRFVEKPQVFV--SNKINAGMYILSPAVLQRIQLKPTSIEKEI-----FPVM 234
Cdd:cd02541  154 aVEEVppEDVSKYGIVKGEKidgDVFKVKGLVEKPKPEEapSNLAIVGRYVLTPDIFDILENTKPGKGGEIqltdaIAKL 233

                        250       260
                 ....*....|....*....|....*
gi 564365550 235 AKEGQLYAMELQGFWMDIGQPKDFL 259
Cdd:cd02541  234 LEEEPVYAYVFEGKRYDCGNKLGYL 258
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
35-259 3.12e-28

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 112.05  E-value: 3.12e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  35 KALILVGGYGTRLRPLTLSTPK---PLVDfcnKPILLHQVEALAAAGVDHVILAVSY----------MSQMLEKEMKAQ- 100
Cdd:COG1210    5 KAVIPVAGLGTRFLPATKAIPKemlPIVD---KPLIQYVVEEAVAAGIEEIIFVTGRgkraiedhfdRSYELEATLEAKg 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 101 -EQRLGI--RISMSHE------EEPLGTAGPLALARDLLSEtaDPFFVLNSDVICD--FP-FQAMVQFHRHHGqeGSIL- 167
Cdd:COG1210   82 kEELLEEvrSISPLANihyvrqKEPLGLGHAVLCARPFVGD--EPFAVLLGDDLIDseKPcLKQMIEVYEETG--GSVIa 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 168 VTKV--EEPSKYGVVVCEADTGRIHR---FVEKPQV--FVSNKINAGMYILSPAV---LQR--------IQLkpT-SIEK 228
Cdd:COG1210  158 VQEVppEEVSKYGIVDGEEIEGGVYRvtgLVEKPAPeeAPSNLAIVGRYILTPEIfdiLEKtkpgaggeIQL--TdAIAA 235

                        250       260       270
                 ....*....|....*....|....*....|.
gi 564365550 229 eifpvMAKEGQLYAMELQGFWMDIGQPKDFL 259
Cdd:COG1210  236 -----LAKEEPVYAYEFEGKRYDCGDKLGYL 261
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 36-258 3.13e-28

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: 110.40  E-value: 3.13e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  36 ALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAqeqRLGIRISMSHEEE 115
Cdd:cd02523    1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKK---YPNIKFVYNPDYA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 116 PLGTAGPLALARDLLSEtadPFFVLNSDVICDfpfQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADTGRIHRFVEK 195
Cdd:cd02523   78 ETNNIYSLYLARDFLDE---DFLLLEGDVVFD---PSILERLLSSPADNAILVDKKTKEWEDEYVKDLDDAGVLLGIISK 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564365550 196 PQvfVSNKINA---GMYILSPAVLQRI-----QLKPTSIEK----EIFPVMAKEGQLYAMELQ-GFWMDIGQPKDF 258
Cdd:cd02523  152 AK--NLEEIQGeyvGISKFSPEDADRLaealeELIEAGRVNlyyeDALQRLISEEGVKVKDISdGFWYEIDDLEDL 225
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
35-258 5.85e-27

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 107.25  E-value: 5.85e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  35 KALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEmkAQEQRLGIRISMSHEE 114
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEA--LARPGPDVTFVYNPDY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 115 EPLGTAGPLALARDLLSEtadPFFVLNSDVICDfP--FQAMVQfhrhHGQEGSILV-TKVEEPSKYGVVVCEADTGRIHR 191
Cdd:COG1213   79 DETNNIYSLWLAREALDE---DFLLLNGDVVFD-PaiLKRLLA----SDGDIVLLVdRKWEKPLDEEVKVRVDEDGRIVE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 192 FVEKPQvfvSNKINA---GMYILSPAVLQRI--QLKPTSIEK-------EIFPVMAKEG-QLYAMELQG-FWMDIGQPKD 257
Cdd:COG1213  151 IGKKLP---PEEADGeyiGIFKFSAEGAAALreALEALIDEGgpnlyyeDALQELIDEGgPVKAVDIGGlPWVEIDTPED 227


                 .
gi 564365550 258 F 258
Cdd:COG1213  228 L 228
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 36-218 1.01e-20

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: 89.88  E-value: 1.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  36 ALILVGGYGTRLRPltlSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKaqeqrlGIRISMSHEEE 115
Cdd:cd02540    1 AVILAAGKGTRMKS---DLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALA------NPNVEFVLQEE 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 116 PLGTAGPLALARDLLSETADPFFVLNSDVicdfPF------QAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEaDTGRI 189
Cdd:cd02540   72 QLGTGHAVKQALPALKDFEGDVLVLYGDV----PLitpetlQRLLEAHREAGADVTVLTAELEDPTGYGRIIRD-GNGKV 146

                        170       180       190
                 ....*....|....*....|....*....|...
gi 564365550 190 HRFVE----KPQVFVSNKINAGMYILSPAVLQR 218
Cdd:cd02540  147 LRIVEekdaTEEEKAIREVNAGIYAFDAEFLFE 179
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 32-363 1.07e-20

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 93.27  E-value: 1.07e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  32 DAMKALILVGGYGTRLRPltlSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQEQrlgirISMS 111
Cdd:PRK14355   2 NNLAAIILAAGKGTRMKS---DLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDGD-----VSFA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 112 HEEEPLGTAGPLALARDLLSETADPFFVLNSDV--ICDFPFQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADtGRI 189
Cdd:PRK14355  74 LQEEQLGTGHAVACAAPALDGFSGTVLILCGDVplLRAETLQGMLAAHRATGAAVTVLTARLENPFGYGRIVRDAD-GRV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 190 HRFVEK----PQVFVSNKINAGMYILSPAVLQRI--QLKPTSIEKE-----IFPVMAKEGQLY-------AMELQGF--W 249
Cdd:PRK14355 153 LRIVEEkdatPEERSIREVNSGIYCVEAAFLFDAigRLGNDNAQGEyyltdIVAMAAAEGLRClafpvadPDEIMGVndR 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 250 MDIGQPKDFLTGMC---LFLQSLRQKHPERLYSGPGVVgnvlVDPSARIGQNCSIGPNVSLGPGVVVEDGVCIRRCTVLR 326
Cdd:PRK14355 233 AQLAEAARVLRRRInreLMLAGVTLIDPETTYIDRGVV----IGRDTTIYPGVCISGDTRIGEGCTIEQGVVIKGCRIGD 308

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 564365550 327 DAHIRSHSWLESCIVGWRCRVGQWVRMENVTVLGEDV 363
Cdd:PRK14355 309 DVTVKAGSVLEDSVVGDDVAIGPMAHLRPGTELSAHV 345
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 34-259 1.68e-19

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: 86.86  E-value: 1.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  34 MKALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVdHVILAVSYMSQM-LEKEMKAQEQRLGIRISMSH 112
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGI-REILIISTPEDLpLFKELLGDGSDLGIRITYAV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 113 EEEPLGTAGPLALARDLLSEtaDPF-FVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADtGRIHR 191
Cdd:cd02538   80 QPKPGGLAQAFIIGEEFIGD--DPVcLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDEN-GRVLS 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564365550 192 FVEKPQVFVSNKINAGMYILSPAVLQRI-QLKPTSI-EKEIFPV---MAKEGQLYA--MELQGFWMDIGQPKDFL 259
Cdd:cd02538  157 IEEKPKKPKSNYAVTGLYFYDNDVFEIAkQLKPSARgELEITDVnneYLEKGKLSVelLGRGFAWLDTGTHESLL 231
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 36-386 6.07e-19

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 87.96  E-value: 6.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  36 ALILVGGYGTRLRPltlSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKemkaqeqRLGIRISMSHEEE 115
Cdd:PRK14354   5 AIILAAGKGTRMKS---KLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKE-------VLGDRSEFALQEE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 116 PLGTAGPLALARDLLSETADPFFVLNSDV--ICDFPFQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADtGRIHRFV 193
Cdd:PRK14354  75 QLGTGHAVMQAEEFLADKEGTTLVICGDTplITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNEN-GEVEKIV 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 194 E----KPQVFVSNKINAGMYILSPAVLQRI--QLKPTSIEKE-----IFPVMAKEGQL---YAMElqgfwmdigqpkDFL 259
Cdd:PRK14354 154 EqkdaTEEEKQIKEINTGTYCFDNKALFEAlkKISNDNAQGEyyltdVIEILKNEGEKvgaYQTE------------DFE 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 260 TGM------CLFL--QSLRQ----KHPERlysgpGVvgnVLVDPSarigqNCSIGPNVSLGPGVVVEDGVCIRRCTVL-R 326
Cdd:PRK14354 222 ESLgvndrvALAEaeKVMRRrineKHMVN-----GV---TIIDPE-----STYIDADVEIGSDTVIEPGVVIKGNTVIgE 288

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 327 DAHIRSHSWLESCIVGWRCRVGQWVRMEnvTVLGEDVIVNDELYLNgasvlPHKSIGESV 386
Cdd:PRK14354 289 DCVIGPGSRIVDSTIGDGVTITNSVIEE--SKVGDNVTVGPFAHLR-----PGSVIGEEV 341
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 34-216 1.14e-18

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: 83.84  E-value: 1.14e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  34 MKALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLE---KEMKAQEQRLGIRIS- 109
Cdd:cd02507    1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIehlLKSKWSSLSSKMIVDv 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 110 -MSHEEEPLGTAgpLALaRDLLSETADPFFVLNSDVICDFPFQAMVQFHRHH--GQEGSILVTKVEEPS---------KY 177
Cdd:cd02507   81 iTSDLCESAGDA--LRL-RDIRGLIRSDFLLLSCDLVSNIPLSELLEERRKKdkNAIATLTVLLASPPVsteqskkteEE 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 178 GVVVCEADTGRIhRFVEK--------------------PQVFVSNK-INAGMYILSPAVL 216
Cdd:cd02507  158 DVIAVDSKTQRL-LLLHYeedldedleliirksllskhPNVTIRTDlLDCHIYICSPDVL 216
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 34-365 1.79e-18

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 86.08  E-value: 1.79e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  34 MKALILVGGYGTRLRPLTLSTPKPLVDFCNK-PILLHQVEALAAAGVDHVILAVSYMSQMLEKEmkaqeqrLGI------ 106
Cdd:PRK05293   4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCANSGIDTVGVLTQYQPLELNNH-------IGIgspwdl 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 107 -RIS---------MSHEEEP--LGTAGPLALARDLLsETADPFFV--LNSDVICDFPFQAMVQFHRHHGQEGSILVTKV- 171
Cdd:PRK05293  77 dRINggvtilppySESEGGKwyKGTAHAIYQNIDYI-DQYDPEYVliLSGDHIYKMDYDKMLDYHKEKEADVTIAVIEVp 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 172 -EEPSKYGVVVCEADtGRIHRFVEKPQVFVSNKINAGMYILSPAVLQRI----QLKPTSIE---KEIFPVMAKEG-QLYA 242
Cdd:PRK05293 156 wEEASRFGIMNTDEN-MRIVEFEEKPKNPKSNLASMGIYIFNWKRLKEYliedEKNPNSSHdfgKNVIPLYLEEGeKLYA 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 243 MELQGFWMDIGQpkdfltgmclfLQSLRQ-------KHPE--------RLYS----------GPGV-VGNVLVDPSARI- 295
Cdd:PRK05293 235 YPFKGYWKDVGT-----------IESLWEanmellrPENPlnlfdrnwRIYSvnpnlppqyiAENAkVKNSLVVEGCVVy 303

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564365550 296 G--QNCSIGPNVSLGPGVVVEDGVcirrctVLRDAHIRSHSWLESCIVGWRCRVGQWVRM----ENVTVLGEDVIV 365
Cdd:PRK05293 304 GtvEHSVLFQGVQVGEGSVVKDSV------IMPGAKIGENVVIERAIIGENAVIGDGVIIgggkEVITVIGENEVI 373
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 38-383 3.55e-17

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 82.67  E-value: 3.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  38 ILVGGYGTRLRPltlSTPKPLVDFCNKPIL---LHQVEALAaagVDHVILAVSYMSQMLEKEMKA--------QEQRLG- 105
Cdd:PRK14360   6 ILAAGKGTRMKS---SLPKVLHPLGGKSLVervLDSCEELK---PDRRLVIVGHQAEEVEQSLAHlpglefveQQPQLGt 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 106 ---IRISMSHEEEPLGtagplalarDLLsetadpffVLNSDVicdfPF------QAMVQFHRHHGQEGSILVTKVEEPSK 176
Cdd:PRK14360  80 ghaVQQLLPVLKGFEG---------DLL--------VLNGDV----PLlrpetlEALLNTHRSSNADVTLLTARLPNPKG 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 177 YGVVVCEADtGRIHRFVEK----PQVFVSNKINAGMYILSPAVLQRI--QLKPTSIEKEIF---------PVMAKEGQLY 241
Cdd:PRK14360 139 YGRVFCDGN-NLVEQIVEDrdctPAQRQNNRINAGIYCFNWPALAEVlpKLSSNNDQKEYYltdtvslldPVMAVEVEDY 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 242 aMELQGfwmdIGQPKDFLTGMCLFLQSLRQKH---------P------ERLYSGPGVVgnvlVDPSARIGQNCSIGPNVS 306
Cdd:PRK14360 218 -QEING----INDRKQLAQCEEILQNRIKEKWmlagvtfidPasctisETVELGPDVI----IEPQTHLRGNTVIGSGCR 288

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 307 LGPGVVVEDGVCIRRCTVL----RDAHIRSHSWL-------ESCIVGWRCRVGQWVRMENvTVLGEDVIVNDELYLNGAS 375
Cdd:PRK14360 289 IGPGSLIENSQIGENVTVLysvvSDSQIGDGVKIgpyahlrPEAQIGSNCRIGNFVEIKK-SQLGEGSKVNHLSYIGDAT 367


                 ....*...
gi 564365550 376 VLPHKSIG 383
Cdd:PRK14360 368 LGEQVNIG 375
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 288-367 5.55e-17

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: 74.97  E-value: 5.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 288 LVDPSARIGQNCSIGPNVsLGPGVVVEDGVCIRRCTVLRDAHIRSHSWLESCIVGWRCRVGQWVRMENVTVLGEDVIVND 367
Cdd:cd03356    1 LIGESTVIGENAIIKNSV-IGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVNLCIIGDDVVVED 79
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 34-363 9.88e-17

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 81.56  E-value: 9.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  34 MKALILVGGYGTRLRPltlSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKaqeqrlGIRISMSHE 113
Cdd:PRK14358   8 LDVVILAAGQGTRMKS---ALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQ------GSGVAFARQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 114 EEPLGTAGPLALARDLLSETADPFFVLNSDVICDFP--FQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADtGRIHR 191
Cdd:PRK14358  79 EQQLGTGDAFLSGASALTEGDADILVLYGDTPLLRPdtLRALVADHRAQGSAMTILTGELPDATGYGRIVRGAD-GAVER 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 192 FVEKPQVFVSNK----INAGMYIL---SPAVLQRIQLKptsiekeifpvmAKEGQLYAMELQGFWMDIG---------QP 255
Cdd:PRK14358 158 IVEQKDATDAEKaigeFNSGVYVFdarAPELARRIGND------------NKAGEYYLTDLLGLYRAGGaqvrafklsDP 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 256 KDFL-----TGMCLFLQSLRQkhpeRLYSGPGVVGNVLVDPSA-RIGQNCSIGPNVSLGPGVV------VEDGVCIRRCT 323
Cdd:PRK14358 226 DEVLgandrAGLAQLEATLRR----RINEAHMKAGVTLQDPGTiLIEDTVTLGRDVTIEPGVLlrgqtrVADGVTIGAYS 301

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 564365550 324 VLRD------AHIRSHSWLESCIVGWRCRVGQWVRMENVTVLGEDV 363
Cdd:PRK14358 302 VVTDsvlhegAVIKPHSVLEGAEVGAGSDVGPFARLRPGTVLGEGV 347
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 36-365 4.52e-16

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 79.38  E-value: 4.52e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  36 ALILVGGYGTRLRPltlSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQEQRLGIrismshEEE 115
Cdd:PRK14356   8 ALILAAGKGTRMHS---DKPKVLQTLLGEPMLRFVYRALRPLFGDNVWTVVGHRADMVRAAFPDEDARFVL------QEQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 116 PLGTAGPLALARDLLSET-ADPFFVLNSD-------VICDFPFQAMvqfhrhhGQEGSILVTKVEEPSKYGVVVCEadTG 187
Cdd:PRK14356  79 QLGTGHALQCAWPSLTAAgLDRVLVVNGDtplvttdTIDDFLKEAA-------GADLAFMTLTLPDPGAYGRVVRR--NG 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 188 RIHRFVE----KPQVF--VSNKINAGMYILSPAVLQRIQLKPTSIEK-------EIFPVMAKEGQ----LYAMELQGFwM 250
Cdd:PRK14356 150 HVAAIVEakdyDEALHgpETGEVNAGIYYLRLDAVESLLPRLTNANKsgeyyitDLVGLAVAEGMnvlgVNCGEDPNL-L 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 251 DIGQPKDFLTGMCLFLQSLRQKH---------PERLYSGPGVVgnvlVDPSARIGQNCSIGPNVSLGPGVVVEDGVCIRR 321
Cdd:PRK14356 229 GVNTPAELVRSEELLRARIVEKHlesgvlihaPESVRIGPRAT----IEPGAEIYGPCEIYGASRIARGAVIHSHCWLRD 304

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 564365550 322 CTVLRDAHIRSHSWLESCIVGWRCRVGQWVRMENVTVLGEDVIV 365
Cdd:PRK14356 305 AVVSSGATIHSFSHLEGAEVGDGCSVGPYARLRPGAVLEEGARV 348
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 36-365 2.04e-15

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 77.21  E-value: 2.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  36 ALILVGGYGTRLRPltlSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMkaqeQRLGIRISMSHEEE 115
Cdd:PRK14353   8 AIILAAGEGTRMKS---SLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVAAAA----AKIAPDAEIFVQKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 116 PLGTAGPLALARDLLSETADPFFVLNSDV--ICDFPFQAMVQfHRHHGQEGSILVTKVEEPSKYGVVVceADTGRIHRFV 193
Cdd:PRK14353  81 RLGTAHAVLAAREALAGGYGDVLVLYGDTplITAETLARLRE-RLADGADVVVLGFRAADPTGYGRLI--VKGGRLVAIV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 194 E-KPQVFVSNKI---NAGMYILSPAVLQRI--QLKPTSIEKE-----IFPVMAKEGQLYAMelqgfwmdIGQPKDFLTGM 262
Cdd:PRK14353 158 EeKDASDEERAItlcNSGVMAADGADALALldRVGNDNAKGEyyltdIVAIARAEGLRVAV--------VEAPEDEVRGI 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 263 ----------CLFLQSLRQkhpERLYSGpgvVGnvLVDP-----SA--RIGQNCSIGPNVSLGPGVVVEDGvcirrctvl 325
Cdd:PRK14353 230 nsraelaeaeAVWQARRRR---AAMLAG---VT--LIAPetvffSYdtVIGRDVVIEPNVVFGPGVTVASG--------- 292

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 564365550 326 rdAHIRSHSWLESCIVGWRCRVGQWVRMENVTVLGEDVIV 365
Cdd:PRK14353 293 --AVIHAFSHLEGAHVGEGAEVGPYARLRPGAELGEGAKV 330
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 34-176 1.42e-14

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


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 72.31  E-value: 1.42e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  34 MKALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVS-----YMSQMLEKEMKAQEQRLGIRI 108
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPeeeqaEISTYLRSFPLNLKQKLDEVT 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564365550 109 SMSheEEPLGTAGPLalaRDLLSETADPFFVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKVEEPSK 176
Cdd:cd04198   81 IVL--DEDMGTADSL---RHIRKKIKKDFLVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVSSE 143
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 36-367 6.26e-14

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 72.55  E-value: 6.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  36 ALILVGGYGTRLRPLTLSTPKP---------LVDFC--NkpillhqveaLAAAGVDHVILAVSYMSQMLEKEMK------ 98
Cdd:PRK00844   8 AIVLAGGEGKRLMPLTADRAKPavpfggsyrLIDFVlsN----------LVNSGYLRIYVLTQYKSHSLDRHISqtwrls 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  99 -----------AQeQRLGirismshEEEPLGTAGP----LALARDllsETADPFFVLNSDVICDFPFQAMVQFHRHHGQE 163
Cdd:PRK00844  78 gllgnyitpvpAQ-QRLG-------KRWYLGSADAiyqsLNLIED---EDPDYVVVFGADHVYRMDPRQMVDFHIESGAG 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 164 GSI--LVTKVEEPSKYGVVVCEADtGRIHRFVEKPQ-----------VFVSnkinAGMYILSPAVL----QRIQLKPTSI 226
Cdd:PRK00844 147 VTVaaIRVPREEASAFGVIEVDPD-GRIRGFLEKPAdppglpddpdeALAS----MGNYVFTTDALvdalRRDAADEDSS 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 227 E---KEIFPVMAKEGQLYAM------------ELQGFWMDIGQ-------PKDFLTGMCLFlqSLRQKH-PERLYSGPGv 283
Cdd:PRK00844 222 HdmgGDIIPRLVERGRAYVYdfstnevpgateRDRGYWRDVGTidayydaHMDLLSVHPVF--NLYNREwPIYTSSPNL- 298

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 284 vgnvlvdPSARI---GQNCSIGPNVSLGPGVVVEDGVcIRRCTVLRDAHIRSHSWLESCIVGWRCRVGQWVRMENVtVLG 360
Cdd:PRK00844 299 -------PPAKFvdgGGRVGSAQDSLVSAGSIISGAT-VRNSVLSPNVVVESGAEVEDSVLMDGVRIGRGAVVRRA-ILD 369


                 ....*..
gi 564365550 361 EDVIVND 367
Cdd:PRK00844 370 KNVVVPP 376
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 36-197 1.95e-12

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: 66.09  E-value: 1.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  36 ALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQEQRLG------IRIS 109
Cdd:cd04197    3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKSKWSKPksslmiVIII 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 110 MSHEEEPLGTAgplalARDLLSE--TADPFFVLNSDVICDFPFQAMVQFH--RHHGQEGSILVTKVEEPSKYG------- 178
Cdd:cd04197   83 MSEDCRSLGDA-----LRDLDAKglIRGDFILVSGDVVSNIDLKEILEEHkeRRKKDKNAIMTMVLKEASPPHrtrrtge 157

                        170       180
                 ....*....|....*....|.
gi 564365550 179 --VVVCEADTGRIHRFVEKPQ 197
Cdd:cd04197  158 efVIAVDPKTSRLLHYEELPG 178
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
34-254 4.47e-12

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 66.07  E-value: 4.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  34 MKALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVIL-------AV------SY-MSQMLEKEMK- 98
Cdd:PRK10122   4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLvthasknAVenhfdtSYeLESLLEQRVKr 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  99 ---AQEQRL---GIRISMSHEEEPLGTAGPLALARDLLSEtaDPFFVLNSDVICD--------FPFQAMVQFHRHHGQEG 164
Cdd:PRK10122  84 qllAEVQSIcppGVTIMNVRQGQPLGLGHSILCARPAIGD--NPFVVVLPDVVIDdasadplrYNLAAMIARFNETGRSQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 165 SILVTKVEEPSKYGVV------VCEADTGRIHRFVEK---PQVFVSNKINAGMYILS-----------PAVLQRIQLKPT 224
Cdd:PRK10122 162 VLAKRMPGDLSEYSVIqtkeplDREGKVSRIVEFIEKpdqPQTLDSDLMAVGRYVLSadiwpelertePGAWGRIQLTDA 241

                        250       260       270
                 ....*....|....*....|....*....|
gi 564365550 225 SIEkeifpvMAKEGQLYAMELQGFWMDIGQ 254
Cdd:PRK10122 242 IAE------LAKKQSVDAMLMTGDSYDCGK 265
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 289-363 2.09e-11

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 64.65  E-value: 2.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 289 VDPSARIGQNCSIGPNVSLGPGVVVEDGVCIR-RCTVLRDAHIRSHSWL-------ESCIVGWRCRV------------- 347
Cdd:COG1044  105 IDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGpGVVIGDGVVIGDDCVLhpnvtiyERCVIGDRVIIhsgavigadgfgf 184

                         90       100
                 ....*....|....*....|....
gi 564365550 348 -----GQWVRME---NVtVLGEDV 363
Cdd:COG1044  185 apdedGGWVKIPqlgRV-VIGDDV 207
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 34-303 3.93e-11

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 64.40  E-value: 3.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  34 MKALILVGGYGTRLRPltlSTPKPLVDFCNKPILLHQVEaLAAAGVDHVILAVSYMSQMLEKEMKAQeqrlgirISMSHE 113
Cdd:PRK14357   1 MRALVLAAGKGTRMKS---KIPKVLHKISGKPMINWVID-TAKKVAQKVGVVLGHEAELVKKLLPEW-------VKIFLQ 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 114 EEPLGTAGPLALARDLLSEtADPFFVLNSDV--ICDFPFQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADTGRIHR 191
Cdd:PRK14357  70 EEQLGTAHAVMCARDFIEP-GDDLLILYGDVplISENTLKRLIEEHNRKGADVTILVADLEDPTGYGRIIRDGGKYRIVE 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 192 FVEKPQVFVSNK-INAGMYILSPAVLQRI--QLKPTSIEKEIFPV----MAKEGQLYAME-----------LQGFWMDIG 253
Cdd:PRK14357 149 DKDAPEEEKKIKeINTGIYVFSGDFLLEVlpKIKNENAKGEYYLTdavnFAEKVRVVKTEdlleitgvntrIQLAWLEKQ 228

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564365550 254 QPKDFLTGmcLFLQSLRQKHPERLYSGPGV-VG-NVLVDP------SARIGQNCSIGP 303
Cdd:PRK14357 229 LRMRILEE--LMENGVTILDPNTTYIHYDVeIGmDTIIYPmtfiegKTRIGEDCEIGP 284
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 274-363 4.89e-11

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: 61.28  E-value: 4.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 274 PERLYSGPGV-VG-NVLVDPSARIGQNCSIGPNVSLGPGVVVEDgvcirrCTVLRDAHIRSHSWLESCIVGWRCRVGQWV 351
Cdd:cd03353    7 PETTYIDGDVeIGvDVVIDPGVILEGKTVIGEDCVIGPNCVIKD------STIGDGVVIKASSVIEGAVIGNGATVGPFA 80

                         90
                 ....*....|..
gi 564365550 352 RMENVTVLGEDV 363
Cdd:cd03353   81 HLRPGTVLGEGV 92
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 35-253 4.91e-11

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 63.15  E-value: 4.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  35 KALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQEQRLGIRISMSHEE 114
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 115 EPLGTAGPLALARDLLSETaDPFFVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEaDTGRIHRFVE 194
Cdd:PRK15480  85 SPDGLAQAFIIGEEFIGGD-DCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFD-QNGTAISLEE 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564365550 195 KPQVFVSNKINAGMYILSPAVLQRIQ-LKPTS---IE-KEIFPVMAKEGQL-YAMELQGF-WMDIG 253
Cdd:PRK15480 163 KPLQPKSNYAVTGLYFYDNDVVEMAKnLKPSArgeLEiTDINRIYMEQGRLsVAMMGRGYaWLDTG 228
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 289-363 1.21e-10

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 62.08  E-value: 1.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 289 VDPSARIGQNCSIGPNVSLGPGVVVEDGVCI-------RRCTVLRDAHIRSH-SWLESCIVGWRCRV------------- 347
Cdd:PRK00892 109 IDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIgagavigDGVKIGADCRLHANvTIYHAVRIGNRVIIhsgavigsdgfgf 188

                         90       100
                 ....*....|....*....|...
gi 564365550 348 ----GQWVRME---NVtVLGEDV 363
Cdd:PRK00892 189 andrGGWVKIPqlgRV-IIGDDV 210
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 36-252 3.01e-10

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


Pssm-ID: 133002 [Multi-domain]  Cd Length: 200  Bit Score: 59.09  E-value: 3.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  36 ALILVGGYGTRLRPLTLSTPKPLV---------DFC--NkpillhqveaLAAAGVDHVILAVSYMSQMLE------KEMK 98
Cdd:cd02508    1 AIILAGGEGTRLSPLTKKRAKPAVpfggryrliDFPlsN----------MVNSGIRNVGVLTQYKSRSLNdhlgsgKEWD 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  99 AQEQRLGIRI---SMSHEEEPL-GTAGplALARDL---LSETADPFFVLNSDVICDFPFQAMVQFHRHHGqegsilvtkv 171
Cdd:cd02508   71 LDRKNGGLFIlppQQRKGGDWYrGTAD--AIYQNLdyiERSDPEYVLILSGDHIYNMDYREMLDFHIESG---------- 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 172 eepskygvvvceADtgrihrfvekpqVFVSNKINAGMYILSPAVLqrIQL-----KPTSIE--KEIFPVMAKEGQLYAME 244
Cdd:cd02508  139 ------------AD------------ITVVYKASMGIYIFSKDLL--IELleedaADGSHDfgKDIIPAMLKKLKIYAYE 192


                 ....*...
gi 564365550 245 LQGFWMDI 252
Cdd:cd02508  193 FNGYWADI 200
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 34-253 5.79e-10

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


Pssm-ID: 133003 [Multi-domain]  Cd Length: 274  Bit Score: 59.51  E-value: 5.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  34 MKALILVGGYGTRLRPL-TLSTPKPLVDFCNKPILLHQ-VE-ALAAAGVDHVILAVS--YMSQMLEkemKAQEQRLGIRI 108
Cdd:cd02509    1 IYPVILAGGSGTRLWPLsRESYPKQFLKLFGDKSLLQQtLDrLKGLVPPDRILVVTNeeYRFLVRE---QLPEGLPEENI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 109 SMsheeEPLG--TAGPLALARDLLSETA--DPFFVLNSD-VICDFP-FQAMVQFHRHHGQEGSIlVT---KVEEPS-KYG 178
Cdd:cd02509   78 IL----EPEGrnTAPAIALAALYLAKRDpdAVLLVLPSDhLIEDVEaFLKAVKKAVEAAEEGYL-VTfgiKPTRPEtGYG 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 179 VVVCEADTG----RIHRFVEKP-----QVFVSNK---INAGMYILSPAVLQRI--QLKPT------------------SI 226
Cdd:cd02509  153 YIEAGEKLGggvyRVKRFVEKPdletaKEYLESGnylWNSGIFLFRAKTFLEElkKHAPDiyealekalaaagtddflRL 232

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 564365550 227 EKEIFP----------VMAKEGQLYAMELQGFWMDIG 253
Cdd:cd02509  233 LEEAFAkipsisidyaVMEKTKKVAVVPADFGWSDLG 269
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 292-362 6.60e-10

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: 58.19  E-value: 6.60e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564365550 292 SARIGQNCSIGPNVSLGPGVVVEDGVCIR-RCTVLRDAHIRSHSWLES-CIVGWRCRVGQWVRMENVTVLGED 362
Cdd:cd03352    1 SAKIGENVSIGPNAVIGEGVVIGDGVVIGpGVVIGDGVVIGDDCVIHPnVTIYEGCIIGDRVIIHSGAVIGSD 73
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 37-209 5.63e-09

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: 56.11  E-value: 5.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  37 LILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSymsqmleKEMKAQEQrLGIRISMSH---- 112
Cdd:cd04183    2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFICR-------DEHNTKFH-LDESLKLLApnat 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 113 ----EEEPLGTAGPLALARDLLsETADPFFVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKVEEPsKYGVVVCEADtGR 188
Cdd:cd04183   74 vvelDGETLGAACTVLLAADLI-DNDDPLLIFNCDQIVESDLLAFLAAFRERDLDGGVLTFFSSHP-RWSYVKLDEN-GR 150

                        170       180
                 ....*....|....*....|.
gi 564365550 189 IHRFVEKpqVFVSNKINAGMY 209
Cdd:cd04183  151 VIETAEK--EPISDLATAGLY 169
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 34-362 1.24e-08

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 56.43  E-value: 1.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  34 MK---ALILVGGYGTRLRPLTLSTPKPLVDFCNK------PI------------LLHQ---------------------- 70
Cdd:PRK02862   1 MKrvlAIILGGGAGTRLYPLTKLRAKPAVPLAGKyrlidiPIsncinsginkiyVLTQfnsaslnrhisqtynfdgfsgg 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  71 -VEALAAagvdhvilavsymSQMLEKEMKAQEQRLGIRISMSHEEEPlgtagplalardllseTADPFFVLNSDVICDFP 149
Cdd:PRK02862  81 fVEVLAA-------------QQTPENPSWFQGTADAVRKYLWHFQEW----------------DVDEYLILSGDQLYRMD 131

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 150 FQAMVQFHRHHGQEGSILVTKVEE--PSKYGVVVCEaDTGRIHRFVEKPQ------------VFVSNKINA--------- 206
Cdd:PRK02862 132 YRLFVQHHRETGADITLAVLPVDEkdASGFGLMKTD-DDGRITEFSEKPKgdelkamavdtsRLGLSPEEAkgkpylasm 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 207 GMYILSPAVLQRI---QLKPTSIEKEIFPVMAKEGQLYAMELQGFWMDIGQPKDF------LTgmclflqslRQKHPE-R 276
Cdd:PRK02862 211 GIYVFSRDVLFDLlnkNPEYTDFGKEIIPEAIRDYKVQSYLFDGYWEDIGTIEAFyeanlaLT---------QQPNPPfS 281

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 277 LYsgpgvvgnvlvDPSARIG-----------QNCSIgpnvslgPGVVVEDGVCIRRCTVlrdahirshswlESCIVGWRC 345
Cdd:PRK02862 282 FY-----------DEKAPIYtrarylppsklLDATI-------TESIIAEGCIIKNCSI------------HHSVLGIRS 331

                        410
                 ....*....|....*..
gi 564365550 346 RVGQWVRMENVTVLGED 362
Cdd:PRK02862 332 RIESGCTIEDTLVMGAD 348
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 36-190 1.52e-08

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: 53.35  E-value: 1.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550   36 ALILVGGYGTRLRpltlsTPKPLVDFCNKPILLHQVEALAAAGvDHVILAVSYmsqmleKEMKAQEQRLGIRISmsheEE 115
Cdd:pfam12804   1 AVILAGGRSSRMG-----GDKALLPLGGKPLLERVLERLRPAG-DEVVVVAND------EEVLAALAGLGVPVV----PD 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  116 PLGTAGPL-----ALARdllSETADPFFVLNsdviCDFPF--QAMVQFHRHHGqegsilvtkveEPSKYGVVVCEADTGR 188
Cdd:pfam12804  65 PDPGQGPLagllaALRA---APGADAVLVLA----CDMPFltPELLRRLLAAA-----------EESGADIVVPVYDGGR 126


                  ..
gi 564365550  189 IH 190
Cdd:pfam12804 127 GH 128
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
35-230 1.59e-07

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 52.60  E-value: 1.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  35 KALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILaVSYMSQ---------------MLEKEMKA 99
Cdd:PRK13389  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVL-VTHSSKnsienhfdtsfeleaMLEKRVKR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 100 Q----EQRL---GIRISMSHEEEPLGTAGPLALARDLLSEtaDPFFVLNSDVICDF--------PFQAMVQFHRHHGQEg 164
Cdd:PRK13389  89 QlldeVQSIcppHVTIMQVRQGLAKGLGHAVLCAHPVVGD--EPVAVILPDVILDEyesdlsqdNLAEMIRRFDETGHS- 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564365550 165 SILVTKVEEPSKYGVVVCE------ADTGRIHRFVEKPQVFV--SNKINAGMYILSPAVLQRIQLKPTSIEKEI 230
Cdd:PRK13389 166 QIMVEPVADVTAYGVVDCKgvelapGESVPMVGVVEKPKADVapSNLAIVGRYVLSADIWPLLAKTPPGAGDEI 239
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 37-341 1.60e-07

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 53.07  E-value: 1.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  37 LILVGGYGTRLRPltlSTPKPLVDFCNKPILLHQV-EALAAAGVDHVILavSYMSQMLEKEMkaQEQRLGIRI-SMSHEE 114
Cdd:PRK14359   6 IILAAGKGTRMKS---SLPKVLHTICGKPMLFYILkEAFAISDDVHVVL--HHQKERIKEAV--LEYFPGVIFhTQDLEN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 115 EPlGTAGplALARDLLSetADPFFVLNSDVicdfPF---QAMVQFHRHHGQEgSILVTKVEEPSKYGVVVCEadTGRIHR 191
Cdd:PRK14359  79 YP-GTGG--ALMGIEPK--HERVLILNGDM----PLvekDELEKLLENDADI-VMSVFHLADPKGYGRVVIE--NGQVKK 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 192 FVE----KPQVFVSNKINAGMYILSPAVLQRI--QLKPTSIEKEIFPV----MAKEGQL--YAMEL-QGFWMDIGQPKDF 258
Cdd:PRK14359 147 IVEqkdaNEEELKIKSVNAGVYLFDRKLLEEYlpLLKNQNAQKEYYLTdiiaLAIEKGEtiKAVFVdEENFMGVNSKFEL 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 259 LTGMCLFLQSLRQKHPERlysgpGVVgnvlvdpsARIGQNCSIGPNVSLGPGVVVEDGVCIRRCTVLRDAHIRSHSWLES 338
Cdd:PRK14359 227 AKAEEIMQERIKKNAMKQ-----GVI--------MRLPETIYIESGVEFEGECELEEGVRILGKSKIENSHIKAHSVIEE 293


                 ...
gi 564365550 339 CIV 341
Cdd:PRK14359 294 SII 296
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 295-349 4.07e-07

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: 47.19  E-value: 4.07e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564365550 295 IGQNCSIGPNVSLG-----PGVVVEDGVCIRRCTVLRDAHIRSHSWLE-SCIVGWRCRVGQ 349
Cdd:cd05787   19 IGRNCKIGKNVVIDnsyiwDDVTIEDGCTIHHSIVADGAVIGKGCTIPpGSLISFGVVIGD 79
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 31-253 5.47e-07

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 51.38  E-value: 5.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  31 QDAMkALILVGGYGTRLRPLTLSTPKPLV---------DFcnkpillhqveALAAA---GVDHVILAVSYMSQMLEKEMk 98
Cdd:PRK00725  14 RDTL-ALILAGGRGSRLKELTDKRAKPAVyfggkfriiDF-----------ALSNCinsGIRRIGVLTQYKAHSLIRHI- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  99 aQE------QRLG--IRI---SMSHEEEP--LGTAGPLALARDLLsETADPFFV--LNSDVICDFPFQAMVQFHRHHGQE 163
Cdd:PRK00725  81 -QRgwsffrEELGefVDLlpaQQRVDEENwyRGTADAVYQNLDII-RRYDPKYVviLAGDHIYKMDYSRMLADHVESGAD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 164 ---GSILVTkVEEPSKYGVVvCEADTGRIHRFVEKPQ-----------VFVSnkinAGMYILSPAVLQRiQLK-----PT 224
Cdd:PRK00725 159 ctvACLEVP-REEASAFGVM-AVDENDRITAFVEKPAnppampgdpdkSLAS----MGIYVFNADYLYE-LLEedaedPN 231

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 564365550 225 S---IEKEIFPVMAKEGQLYA-----------MELQGFWMDIG 253
Cdd:PRK00725 232 SshdFGKDIIPKIVEEGKVYAhpfsdscvrsdPEEEPYWRDVG 274
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 41-87 7.33e-07

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


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 49.12  E-value: 7.33e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 564365550  41 GGYGTRLRpltlSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVS 87
Cdd:COG2266    3 GGKGTRLG----GGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVS 45
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 36-217 1.55e-06

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 49.94  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  36 ALILVGGYGTRLRPltlSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQEQRLGIRIsmshEEE 115
Cdd:PRK14352   7 VIVLAAGAGTRMRS---DTPKVLHTLAGRSMLGHVLHAAAGLAPQHLVVVVGHDRERVAPAVAELAPEVDIAV----QDE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 116 PLGT--AGPLALArDLLSETADPFFVLNSDVicdfPF------QAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADtG 187
Cdd:PRK14352  80 QPGTghAVQCALE-ALPADFDGTVVVTAGDV----PLldgetlADLVATHTAEGNAVTVLTTTLDDPTGYGRILRDQD-G 153

                        170       180       190
                 ....*....|....*....|....*....|....
gi 564365550 188 RIHRFVEK----PQVFVSNKINAGMYILSPAVLQ 217
Cdd:PRK14352 154 EVTAIVEQkdatPSQRAIREVNSGVYAFDAAVLR 187
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 34-150 2.59e-06

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


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 47.57  E-value: 2.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  34 MKALILVGGYGTRlrpltLSTPKPLVDFCNKPILLHQVEALAAAgVDHVILAVsymsqmleKEMKAQEQRLGIRISmshe 113
Cdd:cd02503    1 ITGVILAGGKSRR-----MGGDKALLELGGKPLLEHVLERLKPL-VDEVVISA--------NRDQERYALLGVPVI---- 62

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 564365550 114 EEPLGTAGPLA-LARDLLSETADPFFVLNsdviCDFPF 150
Cdd:cd02503   63 PDEPPGKGPLAgILAALRAAPADWVLVLA----CDMPF 96
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 32-150 3.35e-06

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


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 47.11  E-value: 3.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  32 DAMKALILVGGYGTRLRpltlsTPKPLVDFCNKPILLHQVEALAAAgVDHVILAVSYmsqmlekemKAQEQRLGIRIsms 111
Cdd:COG0746    3 MPITGVILAGGRSRRMG-----QDKALLPLGGRPLLERVLERLRPQ-VDEVVIVANR---------PERYAALGVPV--- 64

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 564365550 112 HEEEPLGtAGPLA--LArdLLSETADPFFVLnsdVICDFPF 150
Cdd:COG0746   65 VPDDPPG-AGPLAgiLA--ALEAAPAEWVLV---LACDMPF 99
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 36-161 9.85e-06

GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 45.63  E-value: 9.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550  36 ALILVGGYGTRLRpltlsTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQEQRLgirISMSHEEE 115
Cdd:cd04182    3 AIILAAGRSSRMG-----GNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVV---VINPDWEE 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564365550 116 PLGTAgpLALARDLLSETADPFFVLNsdviCDFPF------QAMVQFHRHHG 161
Cdd:cd04182   75 GMSSS--LAAGLEALPADADAVLILL----ADQPLvtaetlRALIDAFREDG 120
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 295-342 2.00e-05

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


Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 42.56  E-value: 2.00e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564365550 295 IGQNCSIGPNVSLG-----PGVVVEDGVCIRRCTVLRDAHIRSHSWLESCIVG 342
Cdd:cd04652   19 IGANCKIGKRVKITncvimDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLVG 71
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 272-363 2.12e-05

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 45.09  E-value: 2.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 272 KHPERLYSGPGVVG--------NVLVDPSARIGQNCSIGPNVSLGPGVVVEDGVCI-RRCTVlrdahirsHSwleSCIVG 342
Cdd:cd03352    3 KIGENVSIGPNAVIgegvvigdGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIgDRVII--------HS---GAVIG 71

                         90       100
                 ....*....|....*....|....*...
gi 564365550 343 -----WRCRVGQWVRMENV--TVLGEDV 363
Cdd:cd03352   72 sdgfgFAPDGGGWVKIPQLggVIIGDDV 99
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 288-330 2.20e-05

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: 45.39  E-value: 2.20e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 564365550 288 LVDPSARIGQNCSIGP------NVSLGPGVVVEDGVCIRRCTVL-RDAHI 330
Cdd:COG1043    9 IVDPGAKLGENVEIGPfcvigpDVEIGDGTVIGSHVVIEGPTTIgKNNRI 58
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 36-87 2.48e-05

CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 44.82  E-value: 2.48e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564365550  36 ALILVGGYGTRLRpltLSTPKPLVDFCNKPILLHQVEALAAAG-VDHVILAVS 87
Cdd:cd02516    3 AIILAAGSGSRMG---ADIPKQFLELGGKPVLEHTLEAFLAHPaIDEIVVVVP 52
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 288-319 2.69e-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: 2.69e-05
                         10        20        30
                 ....*....|....*....|....*....|..
gi 564365550 288 LVDPSARIGQNCSIGPNVSLGPGVVVEDGVCI 319
Cdd:cd03351    7 IVDPGAKIGENVEIGPFCVIGPNVEIGDGTVI 38
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
292-320 3.97e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 40.01  E-value: 3.97e-05
                          10        20
                  ....*....|....*....|....*....
gi 564365550  292 SARIGQNCSIGPNVSLGPGVVVEDGVCIR 320
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIG 29
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 286-365 5.65e-05

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


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 42.10  E-value: 5.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 286 NVLVDPSARIGQNCSIGPNVSLGPGVVVEDGVCIRRCTVL-RDAHIRSH----SWLESCIVGWRCRVGQwvrmeNVTVL- 359
Cdd:cd03358   10 NVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFtNDLYPRSKiyrkWELKGTTVKRGASIGA-----NATILp 84

                         90
                 ....*....|
gi 564365550 360 ----GEDVIV 365
Cdd:cd03358   85 gvtiGEYALV 94
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
36-87 6.29e-05

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 43.97  E-value: 6.29e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564365550  36 ALILVGGYGTRLRPltlSTPKPLVDFCNKPILLHQVEALAAAG-VDHVILAVS 87
Cdd:PRK00155   6 AIIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVP 55
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 287-384 7.08e-05

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


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 43.24  E-value: 7.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 287 VLVDPSARIGQNCSIG------PNVSLGPGVVVEDGVCI-RRCTVLRDAHIRSHswlesCIVGWrcrvgqwvrmeNVTVL 359
Cdd:cd03360   85 TLIHPSAVVSPSAVIGegcvimAGAVINPDARIGDNVIInTGAVIGHDCVIGDF-----VHIAP-----------GVVLS 148

                         90       100
                 ....*....|....*....|....*.
gi 564365550 360 GeDVIVNDELYLN-GASVLPHKSIGE 384
Cdd:cd03360  149 G-GVTIGEGAFIGaGATIIQGVTIGA 173
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 288-366 9.12e-05

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


Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 40.64  E-value: 9.12e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564365550 288 LVDPSARIGQNCSIGPNVsLGPGVVVEDGVCIRRCTVLRDAHIRSHSWLESCIVGWRCRVGQWVRMENVTVlGEDVIVN 366
Cdd:cd04652    1 LVGENTQVGEKTSIKRSV-IGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLV-GSGYRVE 77
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 280-330 1.38e-04

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 43.59  E-value: 1.38e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564365550 280 GPGVV-G-NVLVDPSARIGQNCSIGPNVSLGPGVVVEDGVCI-RRCTVLRDAHI 330
Cdd:PRK00892 128 GAGVViGdGVVIGAGAVIGDGVKIGADCRLHANVTIYHAVRIgNRVIIHSGAVI 181
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 279-348 2.20e-04

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


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 41.42  E-value: 2.20e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 279 SGPGVVGNVLVDPSARIGQNCSIGPNVSLGPGVVVEDGVCIRRCTVLRDAHIRSHSWLESCIVGWRCRVG 348
Cdd:cd05636   28 SGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSIIMDGTKVPHLNYVGDSVLGENVNLG 97
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 37-95 2.38e-04

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440824  Cd Length: 224  Bit Score: 42.04  E-value: 2.38e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564365550  37 LILVGGYGTRLRpltLSTPKPLVDFCNKPILLHQVEALAAAG-VDHVILAVS-----YMSQMLEK 95
Cdd:COG1211    1 IIPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPpddieYFEELLAK 62
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
288-334 3.39e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 42.01  E-value: 3.39e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564365550 288 LVDPSARIGQNCSIGP------NVSLGPGVVVEDGVCIRRCTVL-RDAHIRSHS 334
Cdd:PRK05289  10 IVEPGAKIGENVEIGPfcvigpNVVIGDGTVIGSHVVIDGHTTIgKNNRIFPFA 63
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
280-384 1.61e-03

Acetyltransferase, isoleucine patch superfamily [General function prediction only];


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 38.31  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 280 GPGVV---GNVLVDPSARIGQNCSIGPNVSLGP--GVVVEDGVCI-RRCTVLRDAHIRSHSWLEscivgwrcrvgqWVRM 353
Cdd:COG0110   12 GDGVVigpGVRIYGGNITIGDNVYIGPGVTIDDpgGITIGDNVLIgPGVTILTGNHPIDDPATF------------PLRT 79

                         90       100       110
                 ....*....|....*....|....*....|.
gi 564365550 354 ENVTVlGEDVIVNdelylNGASVLPHKSIGE 384
Cdd:COG0110   80 GPVTI-GDDVWIG-----AGATILPGVTIGD 104
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 281-387 2.13e-03

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


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 38.50  E-value: 2.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 281 PGVVGNVLVDPSARIGQNCSIGPNVSLGPG---------VVVEDGV-----CI------RRCTVLRDAHIRSHSWLESCI 340
Cdd:cd04745    1 PVVDPSSFVHPTAVLIGDVIIGKNCYIGPHaslrgdfgrIVIRDGAnvqdnCVihgfpgQDTVLEENGHIGHGAILHGCT 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 564365550 341 VGWRCRVG-QWVRMENVTVlGEDVIVNDELYLNGASVLPHKSIGESVP 387
Cdd:cd04745   81 IGRNALVGmNAVVMDGAVI-GEESIVGAMAFVKAGTVIPPRSLIAGSP 127
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 281-365 2.45e-03

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 38.47  E-value: 2.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564365550 281 PGVVGNVLVDPSAR-IGqNCSIGPNVSLGPGVV---------------VEDGVCIR-----------RCTVlrdAHirsH 333
Cdd:COG0663   11 PQIHPSAFVAPTAVvIG-DVTIGEDVSVWPGAVlrgdvgpirigegsnIQDGVVLHvdpgypltigdDVTI---GH---G 83

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 564365550 334 SWLESCIVGWRCRVGqwvrMeNVTVL-----GEDVIV 365
Cdd:COG0663   84 AILHGCTIGDNVLIG----M-GAIVLdgaviGDGSIV 115
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 288-362 6.67e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 38.08  E-value: 6.67e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564365550 288 LVDPSARIGQNCSIGPNVSLGPGVVVEDGVCI-RRCTVLRDAHIRSHSWLescivGWRCRVGQWvrmenvTVLGED 362
Cdd:PRK12461   1 MIHPTAVIDPSAKLGSGVEIGPFAVIGANVEIgDGTWIGPHAVILGPTRI-----GKNNKIHQG------AVVGDE 65
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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