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Conserved domains on  [gi|2284970577|ref|NP_001397558|]
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mannose-1-phosphate guanyltransferase beta [Mus musculus]

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 ...
 1-233 1.47e-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: 476.70  E-value: 1.47e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   1 MKALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQEQRLGIRISMSHE 80
Cdd:cd06425     1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKKLGIKITFSIE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  81 EEPLGTAGPLALARDLLSETADPFFVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADTGRIHRFV 160
Cdd:cd06425    81 TEPLGTAGPLALARDLLGDDDEPFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDENTGRIERFV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2284970577 161 EKPQVFVSNKINAGMYILSPAVLQRIQLKPTSIEKEIFPVMAKEGQLYAMELQGFWMDIGQPKDFLTGMCLFL 233
Cdd:cd06425   161 EKPKVFVGNKINAGIYILNPSVLDRIPLRPTSIEKEIFPKMASEGQLYAYELPGFWMDIGQPKDFLKGMSLYL 233
LbetaH super family cl00160
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 255-334 7.83e-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: 117.25  E-value: 7.83e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 255 LVDPSARIGQNCSIGPNVSLGPGVVVEDGVCIRRCTVLRDAHIRSHSWLESCIVGWRCRVGQWVRMENVTVLGEDVIVND 334
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 ...
 1-233 1.47e-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: 476.70  E-value: 1.47e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   1 MKALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQEQRLGIRISMSHE 80
Cdd:cd06425     1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKKLGIKITFSIE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  81 EEPLGTAGPLALARDLLSETADPFFVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADTGRIHRFV 160
Cdd:cd06425    81 TEPLGTAGPLALARDLLGDDDEPFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDENTGRIERFV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2284970577 161 EKPQVFVSNKINAGMYILSPAVLQRIQLKPTSIEKEIFPVMAKEGQLYAMELQGFWMDIGQPKDFLTGMCLFL 233
Cdd:cd06425   161 EKPKVFVGNKINAGIYILNPSVLDRIPLRPTSIEKEIFPKMASEGQLYAYELPGFWMDIGQPKDFLKGMSLYL 233
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-234 2.76e-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: 2.76e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   2 KALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQEqRLGIRISMSHEE 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGS-RFGVRITYVDEG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  82 EPLGTAGPLALARDLLSEtaDPFFVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADtGRIHRFVE 161
Cdd:COG1208    80 EPLGTGGALKRALPLLGD--EPFLVLNGDILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGD-GRVTRFVE 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2284970577 162 KPQVFVSNKINAGMYILSPAVLQRIQLKPT-SIEkEIFPVMAKEGQLYAMELQGFWMDIGQPKDFLTGMCLFLQ 234
Cdd:COG1208   157 KPEEPPSNLINAGIYVLEPEIFDYIPEGEPfDLE-DLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLS 229
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-230 3.46e-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: 3.46e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   2 KALILVGGYGTRLRPLTLSTPKPLVDFCNK-PILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQEQRLGIRISMSHE 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  81 EEPLGTAGPLALARDLLSETADPFFVLNSDVICDFPFQAMVQFHRHHGQE--GSILVTKVEEPSKYGVVVCEaDTGRIHR 158
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSDVLVLGGDHIYRMDLEQAVKFHIEKAADatVTFGIVPVEPPTGYGVVEFD-DNGRVIR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 159 FVEKPQVFV-SNKINAGMYILSPAVLQRI--QLKP----TSIEKEIFPVMAKEGQL-YAMELQGF-WMDIGQPKDFLTGM 229
Cdd:pfam00483 160 FVEKPKLPKaSNYASMGIYIFNSGVLDFLakYLEElkrgEDEITDILPKALEDGKLaYAFIFKGYaWLDVGTWDSLWEAN 239


                  .
gi 2284970577 230 C 230
Cdd:pfam00483 240 L 240
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-315 2.38e-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: 2.38e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   1 MKALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAqEQRLGIRISMSHE 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGD-GSRGGVPIEYVVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  81 EEPLGTAGPLALARDLLSetaDPFFVLNSDVICDFP-FQAMVqfhrhHGQEGSILVTKVEEPSKYGVVvcEADTGRIHRF 159
Cdd:TIGR03992  80 EEQLGTADALGSAKEYVD---DEFLVLNGDVLLDSDlLERLI-----RAEAPAIAVVEVDDPSDYGVV--ETDGGRVTGI 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 160 VEKPQVFVSNKINAGMYILSPAV---LQRIQLKPTSiEKEIFPV---MAKEGQLYAMELQGFWMDIGQPKDFLTGMCLFL 233
Cdd:TIGR03992 150 VEKPENPPSNLINAGIYLFSPEIfelLEKTKLSPRG-EYELTDAlqlLIDEGKVKAVELDGFWLDVGRPWDLLDANEALL 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 234 QSLRQKHPERLYSGPGIVGNVLVDPSAR------------IGQNCSIGPN------VSLGPGVVVEDGVCIRRCTVLRDA 295
Cdd:TIGR03992 229 DNLEPRIEGTVEENVTIKGPVVIGEGAVirsgtyiegpvyIGKNCDIGPNayirpyTVIGNNVHIGNAVEIKNSIIMEGT 308

                         330       340
                  ....*....|....*....|
gi 2284970577 296 HIRSHSWLESCIVGWRCRVG 315
Cdd:TIGR03992 309 KIPHLSYVGDSVIGENCNFG 328
LbH_M1P_guanylylT_C cd05824
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 255-334 7.83e-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: 117.25  E-value: 7.83e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 255 LVDPSARIGQNCSIGPNVSLGPGVVVEDGVCIRRCTVLRDAHIRSHSWLESCIVGWRCRVGQWVRMENVTVLGEDVIVND 334
Cdd:cd05824     1 LIDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLENVTVLGDDVTIKD 80
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-330 2.15e-20

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 91.73  E-value: 2.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   3 ALILVGGYGTRLRPltlSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQEQrlgirISMSHEEE 82
Cdd:PRK14355    6 AIILAAGKGTRMKS---DLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDGD-----VSFALQEE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  83 PLGTAGPLALARDLLSETADPFFVLNSDV--ICDFPFQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADtGRIHRFV 160
Cdd:PRK14355   78 QLGTGHAVACAAPALDGFSGTVLILCGDVplLRAETLQGMLAAHRATGAAVTVLTARLENPFGYGRIVRDAD-GRVLRIV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 161 EK----PQVFVSNKINAGMYILSPAVLQRI--QLKPTSIEKE-----IFPVMAKEGQLY-------AMELQGF--WMDIG 220
Cdd:PRK14355  157 EEkdatPEERSIREVNSGIYCVEAAFLFDAigRLGNDNAQGEyyltdIVAMAAAEGLRClafpvadPDEIMGVndRAQLA 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 221 QPKDFLTGMC---LFLQSLRQKHPERLYSGPGIVgnvlVDPSARIGQNCSIGPNVSLGPGVVVEDGVCIRRCTVLRDAHI 297
Cdd:PRK14355  237 EAARVLRRRInreLMLAGVTLIDPETTYIDRGVV----IGRDTTIYPGVCISGDTRIGEGCTIEQGVVIKGCRIGDDVTV 312

                         330       340       350
                  ....*....|....*....|....*....|...
gi 2284970577 298 RSHSWLESCIVGWRCRVGQWVRMENVTVLGEDV 330
Cdd:PRK14355  313 KAGSVLEDSVVGDDVAIGPMAHLRPGTELSAHV 345
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 256-330 2.33e-11

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 63.88  E-value: 2.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 256 VDPSARIGQNCSIGPNVSLGPGVVVEDGVCIR-RCTVLRDAHIRSHSWLES-------CIVGWRCRV------------- 314
Cdd:COG1044   105 IDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGpGVVIGDGVVIGDDCVLHPnvtiyerCVIGDRVIIhsgavigadgfgf 184

                          90       100
                  ....*....|....*....|....
gi 2284970577 315 -----GQWVRME---NVtVLGEDV 330
Cdd:COG1044   185 apdedGGWVKIPqlgRV-VIGDDV 207
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 248-330 7.57e-11

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 62.46  E-value: 7.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 248 PGIVGNVLVDPSARIGQNCSIGPNVSLGPGVVVEDGVCI-------RRCTVLRDAHIRSH-SWLESCIVGWRCRV----- 314
Cdd:PRK00892  101 AGIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIgagavigDGVKIGADCRLHANvTIYHAVRIGNRVIIhsgav 180

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2284970577 315 ------------GQWVRME---NVtVLGEDV 330
Cdd:PRK00892  181 igsdgfgfandrGGWVKIPqlgRV-IIGDDV 210
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
259-287 6.50e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 39.63  E-value: 6.50e-05
                          10        20
                  ....*....|....*....|....*....
gi 2284970577 259 SARIGQNCSIGPNVSLGPGVVVEDGVCIR 287
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 ...
 1-233 1.47e-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: 476.70  E-value: 1.47e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   1 MKALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQEQRLGIRISMSHE 80
Cdd:cd06425     1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKKLGIKITFSIE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  81 EEPLGTAGPLALARDLLSETADPFFVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADTGRIHRFV 160
Cdd:cd06425    81 TEPLGTAGPLALARDLLGDDDEPFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDENTGRIERFV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2284970577 161 EKPQVFVSNKINAGMYILSPAVLQRIQLKPTSIEKEIFPVMAKEGQLYAMELQGFWMDIGQPKDFLTGMCLFL 233
Cdd:cd06425   161 EKPKVFVGNKINAGIYILNPSVLDRIPLRPTSIEKEIFPKMASEGQLYAYELPGFWMDIGQPKDFLKGMSLYL 233
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-234 2.76e-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: 2.76e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   2 KALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQEqRLGIRISMSHEE 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGS-RFGVRITYVDEG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  82 EPLGTAGPLALARDLLSEtaDPFFVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADtGRIHRFVE 161
Cdd:COG1208    80 EPLGTGGALKRALPLLGD--EPFLVLNGDILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGD-GRVTRFVE 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2284970577 162 KPQVFVSNKINAGMYILSPAVLQRIQLKPT-SIEkEIFPVMAKEGQLYAMELQGFWMDIGQPKDFLTGMCLFLQ 234
Cdd:COG1208   157 KPEEPPSNLINAGIYVLEPEIFDYIPEGEPfDLE-DLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLS 229
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-220 1.12e-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: 255.58  E-value: 1.12e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   3 ALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQEqRLGIRISMSHEEE 82
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGS-KFGVNIEYVVQEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  83 PLGTAGPLALARDLLSEtaDPFFVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEaDTGRIHRFVEK 162
Cdd:cd04181    80 PLGTAGAVRNAEDFLGD--DDFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEVEDPSRYGVVELD-DDGRVTRFVEK 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2284970577 163 PQVFVSNKINAGMYILSPAVLQRIQLKPTS---IEKEIFPVMAKEGQLYAMELQGFWMDIG 220
Cdd:cd04181   157 PTLPESNLANAGIYIFEPEILDYIPEILPRgedELTDAIPLLIEEGKVYGYPVDGYWLDIG 217
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-230 3.46e-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: 3.46e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   2 KALILVGGYGTRLRPLTLSTPKPLVDFCNK-PILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQEQRLGIRISMSHE 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  81 EEPLGTAGPLALARDLLSETADPFFVLNSDVICDFPFQAMVQFHRHHGQE--GSILVTKVEEPSKYGVVVCEaDTGRIHR 158
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSDVLVLGGDHIYRMDLEQAVKFHIEKAADatVTFGIVPVEPPTGYGVVEFD-DNGRVIR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 159 FVEKPQVFV-SNKINAGMYILSPAVLQRI--QLKP----TSIEKEIFPVMAKEGQL-YAMELQGF-WMDIGQPKDFLTGM 229
Cdd:pfam00483 160 FVEKPKLPKaSNYASMGIYIFNSGVLDFLakYLEElkrgEDEITDILPKALEDGKLaYAFIFKGYaWLDVGTWDSLWEAN 239


                  .
gi 2284970577 230 C 230
Cdd:pfam00483 240 L 240
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-315 2.38e-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: 2.38e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   1 MKALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAqEQRLGIRISMSHE 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGD-GSRGGVPIEYVVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  81 EEPLGTAGPLALARDLLSetaDPFFVLNSDVICDFP-FQAMVqfhrhHGQEGSILVTKVEEPSKYGVVvcEADTGRIHRF 159
Cdd:TIGR03992  80 EEQLGTADALGSAKEYVD---DEFLVLNGDVLLDSDlLERLI-----RAEAPAIAVVEVDDPSDYGVV--ETDGGRVTGI 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 160 VEKPQVFVSNKINAGMYILSPAV---LQRIQLKPTSiEKEIFPV---MAKEGQLYAMELQGFWMDIGQPKDFLTGMCLFL 233
Cdd:TIGR03992 150 VEKPENPPSNLINAGIYLFSPEIfelLEKTKLSPRG-EYELTDAlqlLIDEGKVKAVELDGFWLDVGRPWDLLDANEALL 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 234 QSLRQKHPERLYSGPGIVGNVLVDPSAR------------IGQNCSIGPN------VSLGPGVVVEDGVCIRRCTVLRDA 295
Cdd:TIGR03992 229 DNLEPRIEGTVEENVTIKGPVVIGEGAVirsgtyiegpvyIGKNCDIGPNayirpyTVIGNNVHIGNAVEIKNSIIMEGT 308

                         330       340
                  ....*....|....*....|
gi 2284970577 296 HIRSHSWLESCIVGWRCRVG 315
Cdd:TIGR03992 309 KIPHLSYVGDSVIGENCNFG 328
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 3-225 2.77e-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: 2.77e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   3 ALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMkAQEQRLGIRISMSHEEE 82
Cdd:cd06915     1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYF-GDGYRGGIRIYYVIEPE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  83 PLGTAGPLALARDLLSEtaDPFFVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADtGRIHRFVEK 162
Cdd:cd06915    80 PLGTGGAIKNALPKLPE--DQFLVLNGDTYFDVDLLALLAALRASGADATMALRRVPDASRYGNVTVDGD-GRVIAFVEK 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2284970577 163 PQVFVSNKINAGMYILSPAVLQRIQLKPTSIEKEIFPVMAKEGQLYAMELQGFWMDIGQPKDF 225
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 ...
 3-219 1.79e-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: 189.77  E-value: 1.79e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   3 ALILVGG--YGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAA-AGVDHVILAVSYMSQMLEKEMKAQEQRLGIRISMSH 79
Cdd:cd06428     1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKvPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  80 EEEPLGTAGPLALARD-LLSETADPFFVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKV--EEPSKYGVVVCEADTGRI 156
Cdd:cd06428    81 EYKPLGTAGGLYHFRDqILAGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEAsrEQASNYGCIVEDPSTGEV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 157 HRFVEKPQVFVSNKINAGMYILSPAVLQRIQL---------------------KPTSIEKEIFPVMAKEGQLYAMELQGF 215
Cdd:cd06428   161 LHYVEKPETFVSDLINCGVYLFSPEIFDTIKKafqsrqqeaqlgddnnregraEVIRLEQDVLTPLAGSGKLYVYKTDDF 240


                  ....
gi 2284970577 216 WMDI 219
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 ...
 2-227 3.14e-55

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: 180.46  E-value: 3.14e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   2 KALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMkaQEQRLGIRISMSHEE 81
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHL--GDSRFGLRITISDEP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  82 -EPLGTAGPLALARDLLSEtaDPFFVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKVEEPSK--YGVVVCEADtGRIHR 158
Cdd:cd06422    79 dELLETGGGIKKALPLLGD--EPFLVVNGDILWDGDLAPLLLLHAWRMDALLLLLPLVRNPGHngVGDFSLDAD-GRLRR 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2284970577 159 FVEKpqvFVSNKINAGMYILSPAVLQRIQLKPTSIeKEIFPVMAKEGQLYAMELQGFWMDIGQPKDFLT 227
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 ...
 3-225 3.48e-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: 172.31  E-value: 3.48e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   3 ALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKaQEQRLGIRISMSHEEE 82
Cdd:cd06426     1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFG-DGSKFGVNISYVREDK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  83 PLGTAGPLALARDLLSetaDPFFVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKVEEPSKYGVVvcEADTGRIHRFVEK 162
Cdd:cd06426    80 PLGTAGALSLLPEKPT---DPFLVMNGDILTNLNYEHLLDFHKENNADATVCVREYEVQVPYGVV--ETEGGRITSIEEK 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2284970577 163 P-QVFvsnKINAGMYILSPAVLQRIQLK-----PTSIEKEIfpvmAKEGQLYAMELQGFWMDIGQPKDF 225
Cdd:cd06426   155 PtHSF---LVNAGIYVLEPEVLDLIPKNeffdmPDLIEKLI----KEGKKVGVFPIHEYWLDIGRPEDY 216
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 1-233 4.48e-51

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: 4.48e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   1 MKALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLeKEMKAQEQRLGIRISMSHE 80
Cdd:cd04189     1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEI-KEALGDGSRFGVRITYILQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  81 EEPLGTAGPLALARDLLSEtaDPFFVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEAdtGRIHRFV 160
Cdd:cd04189    80 EEPLGLAHAVLAARDFLGD--EPFVVYLGDNLIQEGISPLVRDFLEEDADASILLAEVEDPRRFGVAVVDD--GRIVRLV 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2284970577 161 EKPQVFVSNKINAGMYILSPAVLQRI-QLKPTS-----IEKEIFPVMAKEGQLYAMELQGFWMDIGQPKDFLTGMCLFL 233
Cdd:cd04189   156 EKPKEPPSNLALVGVYAFTPAIFDAIsRLKPSWrgeleITDAIQWLIDRGRRVGYSIVTGWWKDTGTPEDLLEANRLLL 234
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 2-314 8.11e-49

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: 8.11e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   2 KALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQEQRLGIRISMSHEE 81
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  82 EPLGTAGPLALARDLLSEtaDPFFVLNSDVICDFpfqAMVQFHRHHGQEG---SILVTKVEEPSKYGVVVCEaDTGRIHR 158
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGD--DDFVVYLGDNLIQD---GISRFVKSFEEKDydaLILLTKVRDPTAFGVAVLE-DGKRILK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 159 FVEKPQVFVSNKINAGMYILSPAVLQRIQ-LKPT-----SIEKEIFPVMAKEGQLYAMELQGFWMDIGQPKDFLTGMCLF 232
Cdd:TIGR01208 155 LVEKPKEPPSNLAVVGLYMFRPLIFEAIKnIKPSwrgelEITDAIQWLIEKGYKVGGSKVTGWWKDTGKPEDLLDANRLI 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 233 LQS---------LRQKHPERLYSGPG--IVGNVLVDPsARIGQNCSI-----GPNVSLGPGVVVEDGVcIRRCTVLRDAH 296
Cdd:TIGR01208 235 LDEverevqgvdDESKIRGRVVVGEGakIVNSVIRGP-AVIGEDCIIensyiGPYTSIGEGVVIRDAE-VEHSIVLDESV 312

                         330
                  ....*....|....*....
gi 2284970577 297 IRS-HSWLESCIVGWRCRV 314
Cdd:TIGR01208 313 IEGvQARIVDSVIGKKVRI 331
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-273 1.90e-44

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 154.48  E-value: 1.90e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   1 MKALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVS-YMSQMLEKEMKAQEQrLGIRISMSH 79
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTpEDGPQFERLLGDGSQ-LGIKISYAV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  80 EEEPLGTAGPLALARDLLSEtaDPFFVLNSDVICDFP-FQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADtGRIHR 158
Cdd:COG1209    80 QPEPLGLAHAFIIAEDFIGG--DPVALVLGDNIFYGDgLSELLREAAARESGATIFGYKVEDPERYGVVEFDED-GRVVS 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 159 FVEKPQVFVSNKINAGMYILSPAVLQRIQ-LKP--------TSIEKEifpvMAKEGQLY-AMELQGF-WMDIGQPKDFL- 226
Cdd:COG1209   157 LEEKPKEPKSNLAVTGLYFYDNDVVEIAKnLKPsargeleiTDANQA----YLERGKLVvELLGRGFaWLDTGTHESLLe 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2284970577 227 TGMclFLQSLrQKHPERLYSGPGIV----GNVLVDPSARIGQ---NCSIGPNVS 273
Cdd:COG1209   233 ANR--FVLTI-EKRQGLKIACPEEIayrmGWIDAEQLAKLANsleKSGYGPYLL 283
LbH_M1P_guanylylT_C cd05824
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 255-334 7.83e-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: 117.25  E-value: 7.83e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 255 LVDPSARIGQNCSIGPNVSLGPGVVVEDGVCIRRCTVLRDAHIRSHSWLESCIVGWRCRVGQWVRMENVTVLGEDVIVND 334
Cdd:cd05824     1 LIDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLENVTVLGDDVTIKD 80
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 3-329 6.00e-32

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 123.26  E-value: 6.00e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   3 ALILVGGYGTRLRPLTLSTPKP---------LVDFcnkPI--LLHqvealaaAGVDHVILAVSYMSQMLEKEM-KAQEQR 70
Cdd:COG0448     4 AIILAGGRGSRLGPLTKDRAKPavpfggkyrIIDF---PLsnCVN-------SGIRRVGVLTQYKSHSLNDHIgSGKPWD 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  71 L-----GIRI-----SMSHEEEPLGTAGPLALARDLL-SETADPFFVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKV- 138
Cdd:COG0448    74 LdrkrgGVFIlppyqQREGEDWYQGTADAVYQNLDFIeRSDPDYVLILSGDHIYKMDYRQMLDFHIESGADITVACIEVp 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 139 -EEPSKYGVVVCEADtGRIHRFVEKPQVFVSNKINAGMYILSPAVLQRI--QLKPTSIE---KEIFPVMAKEGQLYAMEL 212
Cdd:COG0448   154 rEEASRFGVMEVDED-GRITEFEEKPKDPKSALASMGIYVFNKDVLIELleEDAPNSSHdfgKDIIPRLLDRGKVYAYEF 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 213 QGFWMDIGQPKDFL-TGMCLflqsLRQKHPERLY--SGPgIVGNVLVDPSARIGQN-----------CSIGPNVS---LG 275
Cdd:COG0448   233 DGYWRDVGTIDSYYeANMDL----LDPEPEFNLYdpEWP-IYTKQKDLPPAKFVRGgkvknslvsngCIISGTVEnsvLF 307

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2284970577 276 PGVVVEDGVCIRRCTVLRDAHIRSHSWLESCIVGWRCRVGqwvrmENVtVLGED 329
Cdd:COG0448   308 RGVRVESGAVVENSVIMPGVVIGEGAVIENAIIDKNVVIP-----PGV-VIGED 355
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 3-230 1.48e-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: 119.60  E-value: 1.48e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   3 ALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLeKE--MKAQEQRLGIRISMS-- 78
Cdd:cd02524     1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYKGHVI-KEyfLNYFLHNSDVTIDLGtn 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  79 ----HEEEPLG-------------TAGPLALARDLLsETADPFFVLNSDVICDFPFQAMVQFHRHHGqeGSILVTKVEEP 141
Cdd:cd02524    80 rielHNSDIEDwkvtlvdtglntmTGGRLKRVRRYL-GDDETFMLTYGDGVSDVNINALIEFHRSHG--KLATVTAVHPP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 142 SKYGVVVCEaDTGRIHRFVEKPQVfVSNKINAGMYILSPAVLQRIQLKPTSIEKEIFPVMAKEGQLYAMELQGFW--MDI 219
Cdd:cd02524   157 GRFGELDLD-DDGQVTSFTEKPQG-DGGWINGGFFVLEPEVFDYIDGDDTVFEREPLERLAKDGELMAYKHTGFWqcMDT 234

                         250
                  ....*....|.
gi 2284970577 220 GQPKDFLTGMC 230
Cdd:cd02524   235 LRDKQTLEELW 245
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 1-330 6.55e-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: 121.67  E-value: 6.55e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   1 MKALILVGGYGTRLRPltlSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQeqrlgiRISMSHE 80
Cdd:COG1207     3 LAVVILAAGKGTRMKS---KLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALADL------DVEFVLQ 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  81 EEPLGTAGPLALARDLLSETADPFFVLNSDVicdfPF------QAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADtG 154
Cdd:COG1207    74 EEQLGTGHAVQQALPALPGDDGTVLVLYGDV----PLiraetlKALLAAHRAAGAAATVLTAELDDPTGYGRIVRDED-G 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 155 RIHRFVE----KPQVFVSNKINAGMYILSPAVLQRI--QLKPTSIEKE-----IFPVMAKEG------------------ 205
Cdd:COG1207   149 RVLRIVEekdaTEEQRAIREINTGIYAFDAAALREAlpKLSNDNAQGEyyltdVIAIARADGlkvaavqpedpwevlgvn 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 206 ---QLYAME--LQG----FWMDIGqpkdfLTgmclflqsLRQkhPERLYsgpgivgnvlVDPSARIGQNCSIGPNV---- 272
Cdd:COG1207   229 drvQLAEAEriLQRriaeRLMRAG-----VT--------IID--PATTY----------IDGDVEIGRDVVIDPNVileg 283

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 273 --SLGPGVVVEDGVCIRRCTVLRDAHIRsHSWLESCIVGWRCRVGQWVRMENVTVLGEDV 330
Cdd:COG1207   284 ktVIGEGVVIGPNCTLKDSTIGDGVVIK-YSVIEDAVVGAGATVGPFARLRPGTVLGEGV 342
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-226 2.41e-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: 116.48  E-value: 2.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   1 MKALILVGGYGTRLRPLTLSTPK---PLVDfcnKPILLHQVEALAAAGVDHVILAVSYMSQMLEK------------EMK 65
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKemlPIVD---KPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDhfdrsyeleetlEKK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  66 AQEQRL--------GIRISMSHEEEPLGTAGPLALARDLLSEtaDPFFVLNSDVICD---FPFQAMVQFHRHHGqeGSIL 134
Cdd:cd02541    78 GKTDLLeevriisdLANIHYVRQKEPLGLGHAVLCAKPFIGD--EPFAVLLGDDLIDskePCLKQLIEAYEKTG--ASVI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 135 -VTKV--EEPSKYGVVVCEA---DTGRIHRFVEKPQVFV--SNKINAGMYILSPAVLQRIQLKPTSIEKEI-----FPVM 201
Cdd:cd02541   154 aVEEVppEDVSKYGIVKGEKidgDVFKVKGLVEKPKPEEapSNLAIVGRYVLTPDIFDILENTKPGKGGEIqltdaIAKL 233

                         250       260
                  ....*....|....*....|....*
gi 2284970577 202 AKEGQLYAMELQGFWMDIGQPKDFL 226
Cdd:cd02541   234 LEEEPVYAYVFEGKRYDCGNKLGYL 258
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-226 1.61e-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: 1.61e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   2 KALILVGGYGTRLRPLTLSTPK---PLVDfcnKPILLHQVEALAAAGVDHVILAVSY----------MSQMLEKEMKAQ- 67
Cdd:COG1210     5 KAVIPVAGLGTRFLPATKAIPKemlPIVD---KPLIQYVVEEAVAAGIEEIIFVTGRgkraiedhfdRSYELEATLEAKg 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  68 -EQRLGI--RISMSHE------EEPLGTAGPLALARDLLSEtaDPFFVLNSDVICD--FP-FQAMVQFHRHHGqeGSIL- 134
Cdd:COG1210    82 kEELLEEvrSISPLANihyvrqKEPLGLGHAVLCARPFVGD--EPFAVLLGDDLIDseKPcLKQMIEVYEETG--GSVIa 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 135 VTKV--EEPSKYGVVVCEADTGRIHR---FVEKPQV--FVSNKINAGMYILSPAV---LQR--------IQLkpT-SIEK 195
Cdd:COG1210   158 VQEVppEEVSKYGIVDGEEIEGGVYRvtgLVEKPAPeeAPSNLAIVGRYILTPEIfdiLEKtkpgaggeIQL--TdAIAA 235

                         250       260       270
                  ....*....|....*....|....*....|.
gi 2284970577 196 eifpvMAKEGQLYAMELQGFWMDIGQPKDFL 226
Cdd:COG1210   236 -----LAKEEPVYAYEFEGKRYDCGDKLGYL 261
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 3-225 1.81e-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: 1.81e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   3 ALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAqeqRLGIRISMSHEEE 82
Cdd:cd02523     1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKK---YPNIKFVYNPDYA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  83 PLGTAGPLALARDLLSEtadPFFVLNSDVICDfpfQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADTGRIHRFVEK 162
Cdd:cd02523    78 ETNNIYSLYLARDFLDE---DFLLLEGDVVFD---PSILERLLSSPADNAILVDKKTKEWEDEYVKDLDDAGVLLGIISK 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2284970577 163 PQvfVSNKINA---GMYILSPAVLQRI-----QLKPTSIEK----EIFPVMAKEGQLYAMELQ-GFWMDIGQPKDF 225
Cdd:cd02523   152 AK--NLEEIQGeyvGISKFSPEDADRLaealeELIEAGRVNlyyeDALQRLISEEGVKVKDISdGFWYEIDDLEDL 225
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-225 5.52e-27

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 106.86  E-value: 5.52e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   2 KALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEmkAQEQRLGIRISMSHEE 81
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEA--LARPGPDVTFVYNPDY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  82 EPLGTAGPLALARDLLSEtadPFFVLNSDVICDfP--FQAMVQfhrhHGQEGSILV-TKVEEPSKYGVVVCEADTGRIHR 158
Cdd:COG1213    79 DETNNIYSLWLAREALDE---DFLLLNGDVVFD-PaiLKRLLA----SDGDIVLLVdRKWEKPLDEEVKVRVDEDGRIVE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 159 FVEKPQvfvSNKINA---GMYILSPAVLQRI--QLKPTSIEK-------EIFPVMAKEG-QLYAMELQG-FWMDIGQPKD 224
Cdd:COG1213   151 IGKKLP---PEEADGeyiGIFKFSAEGAAALreALEALIDEGgpnlyyeDALQELIDEGgPVKAVDIGGlPWVEIDTPED 227


                  .
gi 2284970577 225 F 225
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 ...
 3-185 7.84e-21

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: 7.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   3 ALILVGGYGTRLRPltlSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKaqeqrlGIRISMSHEEE 82
Cdd:cd02540     1 AVILAAGKGTRMKS---DLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALA------NPNVEFVLQEE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  83 PLGTAGPLALARDLLSETADPFFVLNSDVicdfPF------QAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEaDTGRI 156
Cdd:cd02540    72 QLGTGHAVKQALPALKDFEGDVLVLYGDV----PLitpetlQRLLEAHREAGADVTVLTAELEDPTGYGRIIRD-GNGKV 146

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2284970577 157 HRFVE----KPQVFVSNKINAGMYILSPAVLQR 185
Cdd:cd02540   147 LRIVEekdaTEEEKAIREVNAGIYAFDAEFLFE 179
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-330 2.15e-20

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 91.73  E-value: 2.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   3 ALILVGGYGTRLRPltlSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQEQrlgirISMSHEEE 82
Cdd:PRK14355    6 AIILAAGKGTRMKS---DLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDGD-----VSFALQEE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  83 PLGTAGPLALARDLLSETADPFFVLNSDV--ICDFPFQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADtGRIHRFV 160
Cdd:PRK14355   78 QLGTGHAVACAAPALDGFSGTVLILCGDVplLRAETLQGMLAAHRATGAAVTVLTARLENPFGYGRIVRDAD-GRVLRIV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 161 EK----PQVFVSNKINAGMYILSPAVLQRI--QLKPTSIEKE-----IFPVMAKEGQLY-------AMELQGF--WMDIG 220
Cdd:PRK14355  157 EEkdatPEERSIREVNSGIYCVEAAFLFDAigRLGNDNAQGEyyltdIVAMAAAEGLRClafpvadPDEIMGVndRAQLA 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 221 QPKDFLTGMC---LFLQSLRQKHPERLYSGPGIVgnvlVDPSARIGQNCSIGPNVSLGPGVVVEDGVCIRRCTVLRDAHI 297
Cdd:PRK14355  237 EAARVLRRRInreLMLAGVTLIDPETTYIDRGVV----IGRDTTIYPGVCISGDTRIGEGCTIEQGVVIKGCRIGDDVTV 312

                         330       340       350
                  ....*....|....*....|....*....|...
gi 2284970577 298 RSHSWLESCIVGWRCRVGQWVRMENVTVLGEDV 330
Cdd:PRK14355  313 KAGSVLEDSVVGDDVAIGPMAHLRPGTELSAHV 345
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-226 1.19e-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: 1.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   1 MKALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVdHVILAVSYMSQM-LEKEMKAQEQRLGIRISMSH 79
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGI-REILIISTPEDLpLFKELLGDGSDLGIRITYAV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  80 EEEPLGTAGPLALARDLLSEtaDPF-FVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADtGRIHR 158
Cdd:cd02538    80 QPKPGGLAQAFIIGEEFIGD--DPVcLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDEN-GRVLS 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2284970577 159 FVEKPQVFVSNKINAGMYILSPAVLQRI-QLKPTSI-EKEIFPV---MAKEGQLYA--MELQGFWMDIGQPKDFL 226
Cdd:cd02538   157 IEEKPKKPKSNYAVTGLYFYDNDVFEIAkQLKPSARgELEITDVnneYLEKGKLSVelLGRGFAWLDTGTHESLL 231
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-353 7.17e-19

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 87.19  E-value: 7.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   3 ALILVGGYGTRLRPltlSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKemkaqeqRLGIRISMSHEEE 82
Cdd:PRK14354    5 AIILAAGKGTRMKS---KLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKE-------VLGDRSEFALQEE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  83 PLGTAGPLALARDLLSETADPFFVLNSDV--ICDFPFQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADtGRIHRFV 160
Cdd:PRK14354   75 QLGTGHAVMQAEEFLADKEGTTLVICGDTplITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNEN-GEVEKIV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 161 E----KPQVFVSNKINAGMYILSPAVLQRI--QLKPTSIEKE-----IFPVMAKEGQL---YAMElqgfwmdigqpkDFL 226
Cdd:PRK14354  154 EqkdaTEEEKQIKEINTGTYCFDNKALFEAlkKISNDNAQGEyyltdVIEILKNEGEKvgaYQTE------------DFE 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 227 TGM------CLFL--QSLRQ----KHPERlysgpgivGNVLVDPSarigqNCSIGPNVSLGPGVVVEDGVCIRRCTVL-R 293
Cdd:PRK14354  222 ESLgvndrvALAEaeKVMRRrineKHMVN--------GVTIIDPE-----STYIDADVEIGSDTVIEPGVVIKGNTVIgE 288

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 294 DAHIRSHSWLESCIVGWRCRVGQWVRMEnvTVLGEDVIVNDELYLNgasvlPHKSIGESV 353
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; ...
 1-183 9.64e-19

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


Pssm-ID: 133001 [Multi-domain]  Cd Length: 216  Bit Score: 83.46  E-value: 9.64e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   1 MKALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLE---KEMKAQEQRLGIRIS- 76
Cdd:cd02507     1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIehlLKSKWSSLSSKMIVDv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  77 -MSHEEEPLGTAgpLALaRDLLSETADPFFVLNSDVICDFPFQAMVQFHRHH--GQEGSILVTKVEEPS---------KY 144
Cdd:cd02507    81 iTSDLCESAGDA--LRL-RDIRGLIRSDFLLLSCDLVSNIPLSELLEERRKKdkNAIATLTVLLASPPVsteqskkteEE 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 145 GVVVCEADTGRIhRFVEK--------------------PQVFVSNK-INAGMYILSPAVL 183
Cdd:cd02507   158 DVIAVDSKTQRL-LLLHYeedldedleliirksllskhPNVTIRTDlLDCHIYICSPDVL 216
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 1-332 1.05e-18

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 86.46  E-value: 1.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   1 MKALILVGGYGTRLRPLTLSTPKPLVDFCNK-PILLHQVEALAAAGVDHVILAVSYMSQMLEKEmkaqeqrLGI------ 73
Cdd:PRK05293    4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCANSGIDTVGVLTQYQPLELNNH-------IGIgspwdl 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  74 -RIS---------MSHEEEP--LGTAGPLALARDLLsETADPFFV--LNSDVICDFPFQAMVQFHRHHGQEGSILVTKV- 138
Cdd:PRK05293   77 dRINggvtilppySESEGGKwyKGTAHAIYQNIDYI-DQYDPEYVliLSGDHIYKMDYDKMLDYHKEKEADVTIAVIEVp 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 139 -EEPSKYGVVVCEADtGRIHRFVEKPQVFVSNKINAGMYILSPAVLQRI----QLKPTSIE---KEIFPVMAKEG-QLYA 209
Cdd:PRK05293  156 wEEASRFGIMNTDEN-MRIVEFEEKPKNPKSNLASMGIYIFNWKRLKEYliedEKNPNSSHdfgKNVIPLYLEEGeKLYA 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 210 MELQGFWMDIGQpkdfltgmclfLQSLRQ-------KHPE--------RLYS----------GP-GIVGNVLVDPSARI- 262
Cdd:PRK05293  235 YPFKGYWKDVGT-----------IESLWEanmellrPENPlnlfdrnwRIYSvnpnlppqyiAEnAKVKNSLVVEGCVVy 303

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2284970577 263 G--QNCSIGPNVSLGPGVVVEDGVcirrctVLRDAHIRSHSWLESCIVGWRCRVGQWVRM----ENVTVLGEDVIV 332
Cdd:PRK05293  304 GtvEHSVLFQGVQVGEGSVVKDSV------IMPGAKIGENVVIERAIIGENAVIGDGVIIgggkEVITVIGENEVI 373
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-350 8.10e-17

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 81.13  E-value: 8.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   5 ILVGGYGTRLRPltlSTPKPLVDFCNKPIL---LHQVEALAaagVDHVILAVSYMSQMLEKEMKA--------QEQRLG- 72
Cdd:PRK14360    6 ILAAGKGTRMKS---SLPKVLHPLGGKSLVervLDSCEELK---PDRRLVIVGHQAEEVEQSLAHlpglefveQQPQLGt 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  73 ---IRISMSHEEEPLGtagplalarDLLsetadpffVLNSDVicdfPF------QAMVQFHRHHGQEGSILVTKVEEPSK 143
Cdd:PRK14360   80 ghaVQQLLPVLKGFEG---------DLL--------VLNGDV----PLlrpetlEALLNTHRSSNADVTLLTARLPNPKG 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 144 YGVVVCEADtGRIHRFVEK----PQVFVSNKINAGMYILSPAVLQRI--QLKPTSIEKEIF---------PVMAKEGQLY 208
Cdd:PRK14360  139 YGRVFCDGN-NLVEQIVEDrdctPAQRQNNRINAGIYCFNWPALAEVlpKLSSNNDQKEYYltdtvslldPVMAVEVEDY 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 209 aMELQGfwmdIGQPKDFLTGMCLFLQSLRQKH---------P------ERLYSGPgivgNVLVDPSARIGQNCSIGPNVS 273
Cdd:PRK14360  218 -QEING----INDRKQLAQCEEILQNRIKEKWmlagvtfidPasctisETVELGP----DVIIEPQTHLRGNTVIGSGCR 288

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 274 LGPGVVVEDGVCIRRCTVL----RDAHIRSHSWL-------ESCIVGWRCRVGQWVRMENvTVLGEDVIVNDELYLNGAS 342
Cdd:PRK14360  289 IGPGSLIENSQIGENVTVLysvvSDSQIGDGVKIgpyahlrPEAQIGSNCRIGNFVEIKK-SQLGEGSKVNHLSYIGDAT 367


                  ....*...
gi 2284970577 343 VLPHKSIG 350
Cdd:PRK14360  368 LGEQVNIG 375
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 1-330 9.02e-17

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 81.18  E-value: 9.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   1 MKALILVGGYGTRLRPltlSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKaqeqrlGIRISMSHE 80
Cdd:PRK14358    8 LDVVILAAGQGTRMKS---ALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQ------GSGVAFARQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  81 EEPLGTAGPLALARDLLSETADPFFVLNSDVICDFP--FQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADtGRIHR 158
Cdd:PRK14358   79 EQQLGTGDAFLSGASALTEGDADILVLYGDTPLLRPdtLRALVADHRAQGSAMTILTGELPDATGYGRIVRGAD-GAVER 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 159 FVEKPQVFVSNK----INAGMYIL---SPAVLQRIQLKptsiekeifpvmAKEGQLYAMELQGFWMDIG---------QP 222
Cdd:PRK14358  158 IVEQKDATDAEKaigeFNSGVYVFdarAPELARRIGND------------NKAGEYYLTDLLGLYRAGGaqvrafklsDP 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 223 KDFL-----TGMCLFLQSLRQkhpeRLYSGPGIVGNVLVDPSA-RIGQNCSIGPNVSLGPGVV------VEDGVCIRRCT 290
Cdd:PRK14358  226 DEVLgandrAGLAQLEATLRR----RINEAHMKAGVTLQDPGTiLIEDTVTLGRDVTIEPGVLlrgqtrVADGVTIGAYS 301

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 2284970577 291 VLRD------AHIRSHSWLESCIVGWRCRVGQWVRMENVTVLGEDV 330
Cdd:PRK14358  302 VVTDsvlhegAVIKPHSVLEGAEVGAGSDVGPFARLRPGTVLGEGV 347
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 255-334 1.79e-16

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


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 73.43  E-value: 1.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 255 LVDPSARIGQNCSIGPNVsLGPGVVVEDGVCIRRCTVLRDAHIRSHSWLESCIVGWRCRVGQWVRMENVTVLGEDVIVND 334
Cdd:cd03356     1 LIGESTVIGENAIIKNSV-IGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVNLCIIGDDVVVED 79
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-332 8.55e-16

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 77.98  E-value: 8.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   3 ALILVGGYGTRLRPltlSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMkaqeQRLGIRISMSHEEE 82
Cdd:PRK14353    8 AIILAAGEGTRMKS---SLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVAAAA----AKIAPDAEIFVQKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  83 PLGTAGPLALARDLLSETADPFFVLNSDV--ICDFPFQAMVQfHRHHGQEGSILVTKVEEPSKYGVVVceADTGRIHRFV 160
Cdd:PRK14353   81 RLGTAHAVLAAREALAGGYGDVLVLYGDTplITAETLARLRE-RLADGADVVVLGFRAADPTGYGRLI--VKGGRLVAIV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 161 E-KPQVFVSNKI---NAGMYILSPAVLQRI--QLKPTSIEKE-----IFPVMAKEGQLYAMelqgfwmdIGQPKDFLTGM 229
Cdd:PRK14353  158 EeKDASDEERAItlcNSGVMAADGADALALldRVGNDNAKGEyyltdIVAIARAEGLRVAV--------VEAPEDEVRGI 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 230 ----------CLFLQSLRQkhpERLYSGpgiVGnvLVDP-----SA--RIGQNCSIGPNVSLGPGVVVEDGvcirrctvl 292
Cdd:PRK14353  230 nsraelaeaeAVWQARRRR---AAMLAG---VT--LIAPetvffSYdtVIGRDVVIEPNVVFGPGVTVASG--------- 292

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 2284970577 293 rdAHIRSHSWLESCIVGWRCRVGQWVRMENVTVLGEDVIV 332
Cdd:PRK14353  293 --AVIHAFSHLEGAHVGEGAEVGPYARLRPGAELGEGAKV 330
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-332 1.05e-15

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 77.84  E-value: 1.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   3 ALILVGGYGTRLRPltlSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQEQRLGIrismshEEE 82
Cdd:PRK14356    8 ALILAAGKGTRMHS---DKPKVLQTLLGEPMLRFVYRALRPLFGDNVWTVVGHRADMVRAAFPDEDARFVL------QEQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  83 PLGTAGPLALARDLLSET-ADPFFVLNSD-------VICDFPFQAMvqfhrhhGQEGSILVTKVEEPSKYGVVVCEadTG 154
Cdd:PRK14356   79 QLGTGHALQCAWPSLTAAgLDRVLVVNGDtplvttdTIDDFLKEAA-------GADLAFMTLTLPDPGAYGRVVRR--NG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 155 RIHRFVE----KPQVF--VSNKINAGMYILSPAVLQRIQLKPTSIEK-------EIFPVMAKEGQ----LYAMELQGFwM 217
Cdd:PRK14356  150 HVAAIVEakdyDEALHgpETGEVNAGIYYLRLDAVESLLPRLTNANKsgeyyitDLVGLAVAEGMnvlgVNCGEDPNL-L 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 218 DIGQPKDFLTGMCLFLQSLRQKH---------PERLYSGPGIVgnvlVDPSARIGQNCSIGPNVSLGPGVVVEDGVCIRR 288
Cdd:PRK14356  229 GVNTPAELVRSEELLRARIVEKHlesgvlihaPESVRIGPRAT----IEPGAEIYGPCEIYGASRIARGAVIHSHCWLRD 304

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 2284970577 289 CTVLRDAHIRSHSWLESCIVGWRCRVGQWVRMENVTVLGEDVIV 332
Cdd:PRK14356  305 AVVSSGATIHSFSHLEGAEVGDGCSVGPYARLRPGAVLEEGARV 348
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 1-143 1.36e-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: 71.92  E-value: 1.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   1 MKALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVS-----YMSQMLEKEMKAQEQRLGIRI 75
Cdd:cd04198     1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPeeeqaEISTYLRSFPLNLKQKLDEVT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2284970577  76 SMSheEEPLGTAGPLalaRDLLSETADPFFVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKVEEPSK 143
Cdd:cd04198    81 IVL--DEDMGTADSL---RHIRKKIKKDFLVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVSSE 143
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 3-334 3.51e-14

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 72.94  E-value: 3.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   3 ALILVGGYGTRLRPLTLSTPKP---------LVDFC--NkpillhqveaLAAAGVDHVILAVSYMSQMLEKEMK------ 65
Cdd:PRK00844    8 AIVLAGGEGKRLMPLTADRAKPavpfggsyrLIDFVlsN----------LVNSGYLRIYVLTQYKSHSLDRHISqtwrls 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  66 -----------AQeQRLGIRISmsheeepLGTAGP----LALARDllsETADPFFVLNSDVICDFPFQAMVQFHRHHGQE 130
Cdd:PRK00844   78 gllgnyitpvpAQ-QRLGKRWY-------LGSADAiyqsLNLIED---EDPDYVVVFGADHVYRMDPRQMVDFHIESGAG 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 131 GSI--LVTKVEEPSKYGVVVCEADtGRIHRFVEKPQ-----------VFVSnkinAGMYILSPAVL----QRIQLKPTSI 193
Cdd:PRK00844  147 VTVaaIRVPREEASAFGVIEVDPD-GRIRGFLEKPAdppglpddpdeALAS----MGNYVFTTDALvdalRRDAADEDSS 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 194 E---KEIFPVMAKEGQLYAM------------ELQGFWMDIGQPKDFL-TGMclflqSLRQKHPE-RLY--SGPgIVGNV 254
Cdd:PRK00844  222 HdmgGDIIPRLVERGRAYVYdfstnevpgateRDRGYWRDVGTIDAYYdAHM-----DLLSVHPVfNLYnrEWP-IYTSS 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 255 LVDPSARI---GQNCSIGPNVSLGPGVVVEDGVcIRRCTVLRDAHIRSHSWLESCIVGWRCRVGQWVRMENVtVLGEDVI 331
Cdd:PRK00844  296 PNLPPAKFvdgGGRVGSAQDSLVSAGSIISGAT-VRNSVLSPNVVVESGAEVEDSVLMDGVRIGRGAVVRRA-ILDKNVV 373


                  ...
gi 2284970577 332 VND 334
Cdd:PRK00844  374 VPP 376
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-164 1.79e-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: 65.71  E-value: 1.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   3 ALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQEQRLG------IRIS 76
Cdd:cd04197     3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKSKWSKPksslmiVIII 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  77 MSHEEEPLGTAgplalARDLLSE--TADPFFVLNSDVICDFPFQAMVQFH--RHHGQEGSILVTKVEEPSKYG------- 145
Cdd:cd04197    83 MSEDCRSLGDA-----LRDLDAKglIRGDFILVSGDVVSNIDLKEILEEHkeRRKKDKNAIMTMVLKEASPPHrtrrtge 157

                         170       180
                  ....*....|....*....|.
gi 2284970577 146 --VVVCEADTGRIHRFVEKPQ 164
Cdd:cd04197   158 efVIAVDPKTSRLLHYEELPG 178
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-221 2.38e-12

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 66.84  E-value: 2.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   1 MKALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVIL-------AV------SY-MSQMLEKEMK- 65
Cdd:PRK10122    4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLvthasknAVenhfdtSYeLESLLEQRVKr 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  66 ---AQEQRL---GIRISMSHEEEPLGTAGPLALARDLLSEtaDPFFVLNSDVICD--------FPFQAMVQFHRHHGQEG 131
Cdd:PRK10122   84 qllAEVQSIcppGVTIMNVRQGQPLGLGHSILCARPAIGD--NPFVVVLPDVVIDdasadplrYNLAAMIARFNETGRSQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 132 SILVTKVEEPSKYGVV------VCEADTGRIHRFVEK---PQVFVSNKINAGMYILS-----------PAVLQRIQLKPT 191
Cdd:PRK10122  162 VLAKRMPGDLSEYSVIqtkeplDREGKVSRIVEFIEKpdqPQTLDSDLMAVGRYVLSadiwpelertePGAWGRIQLTDA 241

                         250       260       270
                  ....*....|....*....|....*....|
gi 2284970577 192 SIEkeifpvMAKEGQLYAMELQGFWMDIGQ 221
Cdd:PRK10122  242 IAE------LAKKQSVDAMLMTGDSYDCGK 265
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 256-330 2.33e-11

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 63.88  E-value: 2.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 256 VDPSARIGQNCSIGPNVSLGPGVVVEDGVCIR-RCTVLRDAHIRSHSWLES-------CIVGWRCRV------------- 314
Cdd:COG1044   105 IDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGpGVVIGDGVVIGDDCVLHPnvtiyerCVIGDRVIIhsgavigadgfgf 184

                          90       100
                  ....*....|....*....|....
gi 2284970577 315 -----GQWVRME---NVtVLGEDV 330
Cdd:COG1044   185 apdedGGWVKIPqlgRV-VIGDDV 207
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-330 2.67e-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: 2.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   1 MKALILVGGYGTRLRPltlSTPKPLVDFCNKPILLHQVEaLAAAGVDHVILAVSYMSQMLEKEMKAQeqrlgirISMSHE 80
Cdd:PRK14357    1 MRALVLAAGKGTRMKS---KIPKVLHKISGKPMINWVID-TAKKVAQKVGVVLGHEAELVKKLLPEW-------VKIFLQ 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  81 EEPLGTAGPLALARDLLSEtADPFFVLNSDV--ICDFPFQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADTGRIHR 158
Cdd:PRK14357   70 EEQLGTAHAVMCARDFIEP-GDDLLILYGDVplISENTLKRLIEEHNRKGADVTILVADLEDPTGYGRIIRDGGKYRIVE 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 159 FVEKPQVFVSNK-INAGMYILSPAVLQRIQlkptsieKEIFPVMAKeGQLYAMELQGFWMDIGQPK----DFLTGMCLFL 233
Cdd:PRK14357  149 DKDAPEEEKKIKeINTGIYVFSGDFLLEVL-------PKIKNENAK-GEYYLTDAVNFAEKVRVVKtedlLEITGVNTRI 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 234 Q------SLRQKHPERLY-SGPGIV--GNVLVDPSARIGQN------------CSIGPNVSLGPGVVVEDGVCIRRCTVL 292
Cdd:PRK14357  221 QlawlekQLRMRILEELMeNGVTILdpNTTYIHYDVEIGMDtiiypmtfiegkTRIGEDCEIGPMTRIVDCEIGNNVKII 300

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 2284970577 293 RdahirshSWLESCIVGWRCRVGQWVRMENVTVLGEDV 330
Cdd:PRK14357  301 R-------SECEKSVIEDDVSVGPFSRLREGTVLKKSV 331
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-220 4.35e-11

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 62.77  E-value: 4.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   2 KALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQEQRLGIRISMSHEE 81
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  82 EPLGTAGPLALARDLLSETaDPFFVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEaDTGRIHRFVE 161
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGD-DCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFD-QNGTAISLEE 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2284970577 162 KPQVFVSNKINAGMYILSPAVLQRIQ-LKPTS---IE-KEIFPVMAKEGQL-YAMELQGF-WMDIG 220
Cdd:PRK15480  163 KPLQPKSNYAVTGLYFYDNDVVEMAKnLKPSArgeLEiTDINRIYMEQGRLsVAMMGRGYaWLDTG 228
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 248-330 7.57e-11

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 62.46  E-value: 7.57e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 248 PGIVGNVLVDPSARIGQNCSIGPNVSLGPGVVVEDGVCI-------RRCTVLRDAHIRSH-SWLESCIVGWRCRV----- 314
Cdd:PRK00892  101 AGIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIgagavigDGVKIGADCRLHANvTIYHAVRIGNRVIIhsgav 180

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2284970577 315 ------------GQWVRME---NVtVLGEDV 330
Cdd:PRK00892  181 igsdgfgfandrGGWVKIPqlgRV-IIGDDV 210
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 253-330 1.23e-10

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: 60.13  E-value: 1.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 253 NVLVDPSARIGQNCSIGPNV------SLGPGVVVEDGVCIRRCTVLRDAHIRSHSWLESCIVGWRCRVGQWVRMENVTVL 326
Cdd:cd03353     9 TTYIDGDVEIGVDVVIDPGVilegktVIGEDCVIGPNCVIKDSTIGDGVVIKASSVIEGAVIGNGATVGPFAHLRPGTVL 88


                  ....
gi 2284970577 327 GEDV 330
Cdd:cd03353    89 GEGV 92
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 3-219 2.60e-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: 2.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   3 ALILVGGYGTRLRPLTLSTPKPLV---------DFC--NkpillhqveaLAAAGVDHVILAVSYMSQMLE------KEMK 65
Cdd:cd02508     1 AIILAGGEGTRLSPLTKKRAKPAVpfggryrliDFPlsN----------MVNSGIRNVGVLTQYKSRSLNdhlgsgKEWD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  66 AQEQRLGIRI---SMSHEEEPL-GTAGplALARDL---LSETADPFFVLNSDVICDFPFQAMVQFHRHHGqegsilvtkv 138
Cdd:cd02508    71 LDRKNGGLFIlppQQRKGGDWYrGTAD--AIYQNLdyiERSDPEYVLILSGDHIYNMDYREMLDFHIESG---------- 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 139 eepskygvvvceADtgrihrfvekpqVFVSNKINAGMYILSPAVLqrIQL-----KPTSIE--KEIFPVMAKEGQLYAME 211
Cdd:cd02508   139 ------------AD------------ITVVYKASMGIYIFSKDLL--IELleedaADGSHDfgKDIIPAMLKKLKIYAYE 192


                  ....*...
gi 2284970577 212 LQGFWMDI 219
Cdd:cd02508   193 FNGYWADI 200
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 1-220 4.89e-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: 4.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   1 MKALILVGGYGTRLRPL-TLSTPKPLVDFCNKPILLHQ-VE-ALAAAGVDHVILAVS--YMSQMLEkemKAQEQRLGIRI 75
Cdd:cd02509     1 IYPVILAGGSGTRLWPLsRESYPKQFLKLFGDKSLLQQtLDrLKGLVPPDRILVVTNeeYRFLVRE---QLPEGLPEENI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  76 SMsheeEPLG--TAGPLALARDLLSETA--DPFFVLNSD-VICDFP-FQAMVQFHRHHGQEGSIlVT---KVEEPS-KYG 145
Cdd:cd02509    78 IL----EPEGrnTAPAIALAALYLAKRDpdAVLLVLPSDhLIEDVEaFLKAVKKAVEAAEEGYL-VTfgiKPTRPEtGYG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 146 VVVCEADTG----RIHRFVEKP-----QVFVSNK---INAGMYILSPAVLQRI--QLKPT------------------SI 193
Cdd:cd02509   153 YIEAGEKLGggvyRVKRFVEKPdletaKEYLESGnylWNSGIFLFRAKTFLEElkKHAPDiyealekalaaagtddflRL 232

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2284970577 194 EKEIFP----------VMAKEGQLYAMELQGFWMDIG 220
Cdd:cd02509   233 LEEAFAkipsisidyaVMEKTKKVAVVPADFGWSDLG 269
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 259-329 1.06e-09

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: 57.42  E-value: 1.06e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2284970577 259 SARIGQNCSIGPNVSLGPGVVVEDGVCIR-RCTVLRDAHIRSHSWLES-CIVGWRCRVGQWVRMENVTVLGED 329
Cdd:cd03352     1 SAKIGENVSIGPNAVIGEGVVIGDGVVIGpGVVIGDGVVIGDDCVIHPnVTIYEGCIIGDRVIIHSGAVIGSD 73
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 3-157 4.01e-09

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: 54.89  E-value: 4.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   3 ALILVGGYGTRLRpltlsTPKPLVDFCNKPILLHQVEALAAAGvDHVILAVSYmsqmleKEMKAQEQRLGIRISmsheEE 82
Cdd:pfam12804   1 AVILAGGRSSRMG-----GDKALLPLGGKPLLERVLERLRPAG-DEVVVVAND------EEVLAALAGLGVPVV----PD 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  83 PLGTAGPL-----ALARdllSETADPFFVLNsdviCDFPF--QAMVQFHRHHGqegsilvtkveEPSKYGVVVCEADTGR 155
Cdd:pfam12804  65 PDPGQGPLagllaALRA---APGADAVLVLA----CDMPFltPELLRRLLAAA-----------EESGADIVVPVYDGGR 126


                  ..
gi 2284970577 156 IH 157
Cdd:pfam12804 127 GH 128
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 4-176 4.85e-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: 4.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   4 LILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSymsqmleKEMKAQEQrLGIRISMSH---- 79
Cdd:cd04183     2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFICR-------DEHNTKFH-LDESLKLLApnat 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  80 ----EEEPLGTAGPLALARDLLsETADPFFVLNSDVICDFPFQAMVQFHRHHGQEGSILVTKVEEPsKYGVVVCEADtGR 155
Cdd:cd04183    74 vvelDGETLGAACTVLLAADLI-DNDDPLLIFNCDQIVESDLLAFLAAFRERDLDGGVLTFFSSHP-RWSYVKLDEN-GR 150

                         170       180
                  ....*....|....*....|.
gi 2284970577 156 IHRFVEKpqVFVSNKINAGMY 176
Cdd:cd04183   151 VIETAEK--EPISDLATAGLY 169
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 1-329 1.02e-08

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 56.43  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   1 MK---ALILVGGYGTRLRPLTLSTPKPLVDFCNK------PI------------LLHQ---------------------- 37
Cdd:PRK02862    1 MKrvlAIILGGGAGTRLYPLTKLRAKPAVPLAGKyrlidiPIsncinsginkiyVLTQfnsaslnrhisqtynfdgfsgg 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  38 -VEALAAagvdhvilavsymSQMLEKEMKAQEQRLGIRISMSHEEEPlgtagplalardllseTADPFFVLNSDVICDFP 116
Cdd:PRK02862   81 fVEVLAA-------------QQTPENPSWFQGTADAVRKYLWHFQEW----------------DVDEYLILSGDQLYRMD 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 117 FQAMVQFHRHHGQEGSILVTKVEE--PSKYGVVVCEaDTGRIHRFVEKPQ------------VFVSNKINA--------- 173
Cdd:PRK02862  132 YRLFVQHHRETGADITLAVLPVDEkdASGFGLMKTD-DDGRITEFSEKPKgdelkamavdtsRLGLSPEEAkgkpylasm 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 174 GMYILSPAVLQRI---QLKPTSIEKEIFPVMAKEGQLYAMELQGFWMDIGQPKDF------LTgmclflqslRQKHPE-R 243
Cdd:PRK02862  211 GIYVFSRDVLFDLlnkNPEYTDFGKEIIPEAIRDYKVQSYLFDGYWEDIGTIEAFyeanlaLT---------QQPNPPfS 281

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 244 LYsgpgivgnvlvDPSARIG-----------QNCSIgpnvslgPGVVVEDGVCIRRCTVlrdahirshswlESCIVGWRC 312
Cdd:PRK02862  282 FY-----------DEKAPIYtrarylppsklLDATI-------TESIIAEGCIIKNCSI------------HHSVLGIRS 331

                         410
                  ....*....|....*..
gi 2284970577 313 RVGQWVRMENVTVLGED 329
Cdd:PRK02862  332 RIESGCTIEDTLVMGAD 348
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-197 1.29e-07

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 52.60  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   2 KALILVGGYGTRLRPLTLSTPKPLVDFCNKPILLHQVEALAAAGVDHVILaVSYMSQ---------------MLEKEMKA 66
Cdd:PRK13389   10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVL-VTHSSKnsienhfdtsfeleaMLEKRVKR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  67 Q----EQRL---GIRISMSHEEEPLGTAGPLALARDLLSEtaDPFFVLNSDVICDF--------PFQAMVQFHRHHGQEg 131
Cdd:PRK13389   89 QlldeVQSIcppHVTIMQVRQGLAKGLGHAVLCAHPVVGD--EPVAVILPDVILDEyesdlsqdNLAEMIRRFDETGHS- 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2284970577 132 SILVTKVEEPSKYGVVVCE------ADTGRIHRFVEKPQVFV--SNKINAGMYILSPAVLQRIQLKPTSIEKEI 197
Cdd:PRK13389  166 QIMVEPVADVTAYGVVDCKgvelapGESVPMVGVVEKPKADVapSNLAIVGRYVLSADIWPLLAKTPPGAGDEI 239
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-308 2.70e-07

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 51.91  E-value: 2.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   4 LILVGGYGTRLRPltlSTPKPLVDFCNKPILLHQV-EALAAAGVDHVILavSYMSQMLEKEMkaQEQRLGIRI-SMSHEE 81
Cdd:PRK14359    6 IILAAGKGTRMKS---SLPKVLHTICGKPMLFYILkEAFAISDDVHVVL--HHQKERIKEAV--LEYFPGVIFhTQDLEN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  82 EPlGTAGplALARDLLSetADPFFVLNSDVicdfPF---QAMVQFHRHHGQEgSILVTKVEEPSKYGVVVCEadTGRIHR 158
Cdd:PRK14359   79 YP-GTGG--ALMGIEPK--HERVLILNGDM----PLvekDELEKLLENDADI-VMSVFHLADPKGYGRVVIE--NGQVKK 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 159 FVE----KPQVFVSNKINAGMYILSPAVLQRI--QLKPTSIEKE----------------IFPVMAKEGQLYAM------ 210
Cdd:PRK14359  147 IVEqkdaNEEELKIKSVNAGVYLFDRKLLEEYlpLLKNQNAQKEyyltdiialaiekgetIKAVFVDEENFMGVnskfel 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 211 ---------ELQGFWMDIGqpkdflTGMCLflqslrqkhPERLYsgpgivgnvlvdpsarigqncsIGPNVSLGPGVVVE 281
Cdd:PRK14359  227 akaeeimqeRIKKNAMKQG------VIMRL---------PETIY----------------------IESGVEFEGECELE 269

                         330       340
                  ....*....|....*....|....*..
gi 2284970577 282 DGVCIRRCTVLRDAHIRSHSWLESCIV 308
Cdd:PRK14359  270 EGVRILGKSKIENSHIKAHSVIEESII 296
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 8-54 7.05e-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: 7.05e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2284970577   8 GGYGTRLRpltlSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVS 54
Cdd:COG2266     3 GGKGTRLG----GGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVS 45
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 262-316 8.40e-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: 46.03  E-value: 8.40e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2284970577 262 IGQNCSIGPNVSLG-----PGVVVEDGVCIRRCTVLRDAHIRSHSWLE-SCIVGWRCRVGQ 316
Cdd:cd05787    19 IGRNCKIGKNVVIDnsyiwDDVTIEDGCTIHHSIVADGAVIGKGCTIPpGSLISFGVVIGD 79
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-184 8.83e-07

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 50.32  E-value: 8.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   3 ALILVGGYGTRLRPltlSTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQEQRLGIRIsmshEEE 82
Cdd:PRK14352    7 VIVLAAGAGTRMRS---DTPKVLHTLAGRSMLGHVLHAAAGLAPQHLVVVVGHDRERVAPAVAELAPEVDIAV----QDE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  83 PLGT--AGPLALArDLLSETADPFFVLNSDVicdfPF------QAMVQFHRHHGQEGSILVTKVEEPSKYGVVVCEADtG 154
Cdd:PRK14352   80 QPGTghAVQCALE-ALPADFDGTVVVTAGDV----PLldgetlADLVATHTAEGNAVTVLTTTLDDPTGYGRILRDQD-G 153

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2284970577 155 RIHRFVEK----PQVFVSNKINAGMYILSPAVLQ 184
Cdd:PRK14352  154 EVTAIVEQkdatPSQRAIREVNSGVYAFDAAVLR 187
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 3-220 1.42e-06

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 49.84  E-value: 1.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   3 ALILVGGYGTRLRPLTLSTPKPLV---------DFcnkpillhqveALAAA---GVDHVILAVSYMSQMLEKEMkaQE-- 68
Cdd:PRK00725   18 ALILAGGRGSRLKELTDKRAKPAVyfggkfriiDF-----------ALSNCinsGIRRIGVLTQYKAHSLIRHI--QRgw 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  69 ----QRLG--IRI---SMSHEEEP--LGTAGPLALARDLLsETADPFFV--LNSDVICDFPFQAMVQFHRHHGQE---GS 132
Cdd:PRK00725   85 sffrEELGefVDLlpaQQRVDEENwyRGTADAVYQNLDII-RRYDPKYVviLAGDHIYKMDYSRMLADHVESGADctvAC 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 133 ILVTkVEEPSKYGVVvCEADTGRIHRFVEKPQ-----------VFVSnkinAGMYILSPAVLQRiQLK-----PTS---I 193
Cdd:PRK00725  164 LEVP-REEASAFGVM-AVDENDRITAFVEKPAnppampgdpdkSLAS----MGIYVFNADYLYE-LLEedaedPNSshdF 236

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2284970577 194 EKEIFPVMAKEGQLYA-----------MELQGFWMDIG 220
Cdd:PRK00725  237 GKDIIPKIVEEGKVYAhpfsdscvrsdPEEEPYWRDVG 274
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-117 1.54e-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: 47.88  E-value: 1.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   1 MKALILVGGYGTRLRpltlsTPKPLVDFCNKPILLHQVEALAAAgVDHVILAVSYmsqmlekemKAQEQRLGIRIsmsHE 80
Cdd:COG0746     5 ITGVILAGGRSRRMG-----QDKALLPLGGRPLLERVLERLRPQ-VDEVVIVANR---------PERYAALGVPV---VP 66

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2284970577  81 EEPLGtAGPLA--LArdLLSETADPFFVLnsdVICDFPF 117
Cdd:COG0746    67 DDPPG-AGPLAgiLA--ALEAAPAEWVLV---LACDMPF 99
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 1-157 1.57e-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: 47.96  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   1 MKALILVGGYGTRlrpltLSTPKPLVDFCNKPILLHQVEALAAAgVDHVILAVsymsqmleKEMKAQEQRLGIRISmshe 80
Cdd:cd02503     1 ITGVILAGGKSRR-----MGGDKALLELGGKPLLEHVLERLKPL-VDEVVISA--------NRDQERYALLGVPVI---- 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577  81 EEPLGTAGPLA-LARDLLSETADPFFVLNsdviCDFPF--QAMVQFhrhhgqegsiLVTKVEEPskYGVVVCEaDTGRIH 157
Cdd:cd02503    63 PDEPPGKGPLAgILAALRAAPADWVLVLA----CDMPFlpPELLER----------LLAAAEEG--ADAVVPK-SGGRLQ 125
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-128 5.30e-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: 46.40  E-value: 5.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577   3 ALILVGGYGTRLRpltlsTPKPLVDFCNKPILLHQVEALAAAGVDHVILAVSYMSQMLEKEMKAQEQRLgirISMSHEEE 82
Cdd:cd04182     3 AIILAAGRSSRMG-----GNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVV---VINPDWEE 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2284970577  83 PLGTAgpLALARDLLSETADPFFVLNsdviCDFPF------QAMVQFHRHHG 128
Cdd:cd04182    75 GMSSS--LAAGLEALPADADAVLILL----ADQPLvtaetlRALIDAFREDG 120
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 3-54 1.98e-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: 45.21  E-value: 1.98e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2284970577   3 ALILVGGYGTRLRpltLSTPKPLVDFCNKPILLHQVEALAAAG-VDHVILAVS 54
Cdd:cd02516     3 AIILAAGSGSRMG---ADIPKQFLELGGKPVLEHTLEAFLAHPaIDEIVVVVP 52
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 255-297 2.23e-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: 2.23e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2284970577 255 LVDPSARIGQNCSIGP------NVSLGPGVVVEDGVCIRRCTVL-RDAHI 297
Cdd:COG1043     9 IVDPGAKLGENVEIGPfcvigpDVEIGDGTVIGSHVVIEGPTTIgKNNRI 58
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 255-286 2.84e-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: 2.84e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2284970577 255 LVDPSARIGQNCSIGPNVSLGPGVVVEDGVCI 286
Cdd:cd03351     7 IVDPGAKIGENVEIGPFCVIGPNVEIGDGTVI 38
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 262-309 3.21e-05

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


Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 41.79  E-value: 3.21e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2284970577 262 IGQNCSIGPNVSLG-----PGVVVEDGVCIRRCTVLRDAHIRSHSWLESCIVG 309
Cdd:cd04652    19 IGANCKIGKRVKITncvimDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLVG 71
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 250-309 4.12e-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: 42.49  E-value: 4.12e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2284970577 250 IVG-NVLVDPSARIGQNCSIGPNVSLGPGVVVEDGVCIRRCTVL-RDAHIRSHSWLESCIVG 309
Cdd:cd03358     6 IIGtNVFIENDVKIGDNVKIQSNVSIYEGVTIEDDVFIGPNVVFtNDLYPRSKIYRKWELKG 67
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
3-54 4.51e-05

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 43.97  E-value: 4.51e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2284970577   3 ALILVGGYGTRLRPltlSTPKPLVDFCNKPILLHQVEALAAAG-VDHVILAVS 54
Cdd:PRK00155    6 AIIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVP 55
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
259-287 6.50e-05

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 39.63  E-value: 6.50e-05
                          10        20
                  ....*....|....*....|....*....
gi 2284970577 259 SARIGQNCSIGPNVSLGPGVVVEDGVCIR 287
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIG 29
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 246-315 9.30e-05

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


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 42.19  E-value: 9.30e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 246 SGPGIVGNVLVDPSARIGQNCSIGPNVSLGPGVVVEDGVCIRRCTVLRDAHIRSHSWLESCIVGWRCRVG 315
Cdd:cd05636    28 SGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSIIMDGTKVPHLNYVGDSVLGENVNLG 97
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 254-351 1.16e-04

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


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 42.47  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 254 VLVDPSARIGQNCSIG------PNVSLGPGVVVEDGVCI-RRCTVLRDAHIRSHswlesCIVGWrcrvgqwvrmeNVTVL 326
Cdd:cd03360    85 TLIHPSAVVSPSAVIGegcvimAGAVINPDARIGDNVIInTGAVIGHDCVIGDF-----VHIAP-----------GVVLS 148

                          90       100
                  ....*....|....*....|....*.
gi 2284970577 327 GeDVIVNDELYLN-GASVLPHKSIGE 351
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 ...
 255-333 1.48e-04

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: 39.87  E-value: 1.48e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2284970577 255 LVDPSARIGQNCSIGPNVsLGPGVVVEDGVCIRRCTVLRDAHIRSHSWLESCIVGWRCRVGQWVRMENVTVlGEDVIVN 333
Cdd:cd04652     1 LVGENTQVGEKTSIKRSV-IGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLV-GSGYRVE 77
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 4-62 1.56e-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: 42.42  E-value: 1.56e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2284970577   4 LILVGGYGTRLRpltLSTPKPLVDFCNKPILLHQVEALAAAG-VDHVILAVS-----YMSQMLEK 62
Cdd:COG1211     1 IIPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPpddieYFEELLAK 62
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
255-301 3.43e-04

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 41.62  E-value: 3.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2284970577 255 LVDPSARIGQNCSIGP------NVSLGPGVVVEDGVCIRRCTVL-RDAHIRSHS 301
Cdd:PRK05289   10 IVEPGAKIGENVEIGPfcvigpNVVIGDGTVIGSHVVIDGHTTIgKNNRIFPFA 63
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 239-330 3.64e-04

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: 41.24  E-value: 3.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 239 KHPERLYSGPGIVG--------NVLVDPSARIGQNCSIGPNVSLGPGVVVEDGVCI-RRCTVlrdahirsHSwleSCIVG 309
Cdd:cd03352     3 KIGENVSIGPNAVIgegvvigdGVVIGPGVVIGDGVVIGDDCVIHPNVTIYEGCIIgDRVII--------HS---GAVIG 71

                          90       100
                  ....*....|....*....|....*...
gi 2284970577 310 -----WRCRVGQWVRMENV--TVLGEDV 330
Cdd:cd03352    72 sdgfgFAPDGGGWVKIPQLggVIIGDDV 99
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 248-332 1.29e-03

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 39.24  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 248 PGIVGNVLVDPSAR-IGqNCSIGPNVSLGPGVV---------------VEDGVCIR-----------RCTVlrdAHirsH 300
Cdd:COG0663    11 PQIHPSAFVAPTAVvIG-DVTIGEDVSVWPGAVlrgdvgpirigegsnIQDGVVLHvdpgypltigdDVTI---GH---G 83

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2284970577 301 SWLESCIVGWRCRVGqwvrMeNVTVL-----GEDVIV 332
Cdd:COG0663    84 AILHGCTIGDNVLIG----M-GAIVLdgaviGDGSIV 115
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 248-354 2.25e-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: 38.12  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 248 PGIVGNVLVDPSARIGQNCSIGPNVSLGPG---------VVVEDGV-----CI------RRCTVLRDAHIRSHSWLESCI 307
Cdd:cd04745     1 PVVDPSSFVHPTAVLIGDVIIGKNCYIGPHaslrgdfgrIVIRDGAnvqdnCVihgfpgQDTVLEENGHIGHGAILHGCT 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2284970577 308 VGWRCRVG-QWVRMENVTVlGEDVIVNDELYLNGASVLPHKSIGESVP 354
Cdd:cd04745    81 IGRNALVGmNAVVMDGAVI-GEESIVGAMAFVKAGTVIPPRSLIAGSP 127
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
260-351 2.82e-03

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 37.54  E-value: 2.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2284970577 260 ARIGQNCSIGPNVSLGPG-VVVEDGVCI-RRCTVLRDAHIRshswLES-CIVGWRCRVG-----------QWVRMENVTV 325
Cdd:COG0110     9 ARIGDGVVIGPGVRIYGGnITIGDNVYIgPGVTIDDPGGIT----IGDnVLIGPGVTILtgnhpiddpatFPLRTGPVTI 84

                          90       100
                  ....*....|....*....|....*.
gi 2284970577 326 lGEDVIVNdelylNGASVLPHKSIGE 351
Cdd:COG0110    85 -GDDVWIG-----AGATILPGVTIGD 104
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 255-329 6.72e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 37.69  E-value: 6.72e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2284970577 255 LVDPSARIGQNCSIGPNVSLGPGVVVEDGVCI-RRCTVLRDAHIRSHSWLescivGWRCRVGQWvrmenvTVLGED 329
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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