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Conserved domains on  [gi|1907070242|ref|XP_036009312|]
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mannose-1-phosphate guanyltransferase alpha isoform X2 [Mus musculus]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 4-261 2.72e-171

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: 479.44  E-value: 2.72e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   4 AVILIGGPQKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVPGMQEILLIGFYqPDEALTQFLEAAQQEFNLPVRYL 83
Cdd:cd06428     1 AVILVGGPQKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVPDLKEVLLIGFY-PESVFSDFISDAQQEFNVPIRYL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  84 QEFAPLGTGGGLYHFRDQILAGAPEAFFVLNADVCSDFPLSAMLEAHRRQRHPFLLLGTTANRTQSLNYGCIVENPQTHE 163
Cdd:cd06428    80 QEYKPLGTAGGLYHFRDQILAGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEASREQASNYGCIVEDPSTGE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 164 VLHYVEKPSTFISDIINCGIYLFSPEALKPLRDVFQRNQQDGQLEESPGSWPGAGTIRLEQDVFSALAGQGQIYVHLTDG 243
Cdd:cd06428   160 VLHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNREGRAEVIRLEQDVLTPLAGSGKLYVYKTDD 239

                         250
                  ....*....|....*...
gi 1907070242 244 IWSQIKSAGSALYASRLY 261
Cdd:cd06428   240 FWSQIKTAGSAIYANRLY 257
LbetaH super family cl00160
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 289-355 2.62e-23

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


The actual alignment was detected with superfamily member cd05824:

Pssm-ID: 469633 [Multi-domain]  Cd Length: 80  Bit Score: 92.99  E-value: 2.62e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907070242 289 IHPTAKVAPSAVLGPNVSIGKGVTIGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVGRWARVEG 355
Cdd:cd05824     2 IDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLEN 68
 
Name Accession Description Interval E-value
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 4-261 2.72e-171

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: 479.44  E-value: 2.72e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   4 AVILIGGPQKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVPGMQEILLIGFYqPDEALTQFLEAAQQEFNLPVRYL 83
Cdd:cd06428     1 AVILVGGPQKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVPDLKEVLLIGFY-PESVFSDFISDAQQEFNVPIRYL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  84 QEFAPLGTGGGLYHFRDQILAGAPEAFFVLNADVCSDFPLSAMLEAHRRQRHPFLLLGTTANRTQSLNYGCIVENPQTHE 163
Cdd:cd06428    80 QEYKPLGTAGGLYHFRDQILAGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEASREQASNYGCIVEDPSTGE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 164 VLHYVEKPSTFISDIINCGIYLFSPEALKPLRDVFQRNQQDGQLEESPGSWPGAGTIRLEQDVFSALAGQGQIYVHLTDG 243
Cdd:cd06428   160 VLHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNREGRAEVIRLEQDVLTPLAGSGKLYVYKTDD 239

                         250
                  ....*....|....*...
gi 1907070242 244 IWSQIKSAGSALYASRLY 261
Cdd:cd06428   240 FWSQIKTAGSAIYANRLY 257
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 3-245 6.03e-47

NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 161.09  E-value: 6.03e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   3 KAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIGFYQPdEALTQFLeAAQQEFNLPVRY 82
Cdd:COG1208     1 KAVILAGG--LGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAA-GITEIVINVGYLA-EQIEEYF-GDGSRFGVRITY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  83 LQEFAPLGTGGGLYHFRDQIlagAPEAFFVLNADVCSDFPLSAMLEAHRRQRHPFLLLgTTANRTQSlNYGCIVENPQtH 162
Cdd:COG1208    76 VDEGEPLGTGGALKRALPLL---GDEPFLVLNGDILTDLDLAALLAFHREKGADATLA-LVPVPDPS-RYGVVELDGD-G 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 163 EVLHYVEKPSTFISDIINCGIYLFSPEALKplrdvfqrnqqdgqleespgSWPGAGTIRLEqDVFSALAGQGQIYVHLTD 242
Cdd:COG1208   150 RVTRFVEKPEEPPSNLINAGIYVLEPEIFD--------------------YIPEGEPFDLE-DLLPRLIAEGRVYGYVHD 208


                  ...
gi 1907070242 243 GIW 245
Cdd:COG1208   209 GYW 211
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 2-348 5.24e-34

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: 130.79  E-value: 5.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   2 LKAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIGFYQpDEALTQFLEaAQQEFNLPVR 81
Cdd:TIGR03992   1 MKAVILAAG--KGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDA-GIDDFVFVVGYG-KEKVREYFG-DGSRGGVPIE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  82 YLQEFAPLGTGGGLYHFRDQIlagaPEAFFVLNADVCSDFP-LSAMLEAHRrqrhPFLLLGTTANRTQslnYGCI-VENp 159
Cdd:TIGR03992  76 YVVQEEQLGTADALGSAKEYV----DDEFLVLNGDVLLDSDlLERLIRAEA----PAIAVVEVDDPSD---YGVVeTDG- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 160 qtHEVLHYVEKPSTFISDIINCGIYLFSPEALKPLRDVfqrnqqdgqlEESPgswpgAGTIRLeQDVFSALAGQGQIYVH 239
Cdd:TIGR03992 144 --GRVTGIVEKPENPPSNLINAGIYLFSPEIFELLEKT----------KLSP-----RGEYEL-TDALQLLIDEGKVKAV 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 240 LTDGIWSQIKSAGSALYASRLYL------------------GRYQIthpERLARHTPGGpRIRGNVYIHPTAKVAPSAVL 301
Cdd:TIGR03992 206 ELDGFWLDVGRPWDLLDANEALLdnlepriegtveenvtikGPVVI---GEGAVIRSGT-YIEGPVYIGKNCDIGPNAYI 281

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1907070242 302 GPNVSIGKGVTIGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVG 348
Cdd:TIGR03992 282 RPYTVIGNNVHIGNAVEIKNSIIMEGTKIPHLSYVGDSVIGENCNFG 328
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 3-191 3.51e-30

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 116.58  E-value: 3.51e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   3 KAVILIGGpqKGTRFRPLSFEVPKPLFPVAG-VPMIQHHIEACAQVpGMQEILLI-GFYQPDEALTQFLEAAQqeFNLPV 80
Cdd:pfam00483   1 KAIILAGG--SGTRLWPLTRTLAKPLVPVGGkYPLIDYPLSRLANA-GIREIIVIlTQEHRFMLNELLGDGSK--FGVQI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  81 RYLQEFAPLGTGGGLYHFRDQILAGAPEaFFVLNADVCSDFPLSAMLEAHR-RQRHPFLLLGTTANRTQSlNYGCIVENP 159
Cdd:pfam00483  76 TYALQPEGKGTAPAVALAADFLGDEKSD-VLVLGGDHIYRMDLEQAVKFHIeKAADATVTFGIVPVEPPT-GYGVVEFDD 153

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1907070242 160 QThEVLHYVEKPSTF-ISDIINCGIYLFSPEAL 191
Cdd:pfam00483 154 NG-RVIRFVEKPKLPkASNYASMGIYIFNSGVL 185
LbH_M1P_guanylylT_C cd05824
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 289-355 2.62e-23

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


Pssm-ID: 100062 [Multi-domain]  Cd Length: 80  Bit Score: 92.99  E-value: 2.62e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907070242 289 IHPTAKVAPSAVLGPNVSIGKGVTIGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVGRWARVEG 355
Cdd:cd05824     2 IDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLEN 68
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 2-348 1.73e-13

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 71.70  E-value: 1.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   2 LKAVILIGGpqKGTRFRPlsfEVPKPLFPVAGVPMIQHHIEAcAQVPGMQEILLIGFYQPDEALTQFLEAAQQEFNlpvr 81
Cdd:PRK14355    4 LAAIILAAG--KGTRMKS---DLVKVMHPLAGRPMVSWPVAA-AREAGAGRIVLVVGHQAEKVREHFAGDGDVSFA---- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  82 yLQEfAPLGTGGGLYHFRDQiLAGAPEAFFVLnadvCSDFP------LSAMLEAHRRQRHPFLLLgtTANRTQSLNYGCI 155
Cdd:PRK14355   74 -LQE-EQLGTGHAVACAAPA-LDGFSGTVLIL----CGDVPllraetLQGMLAAHRATGAAVTVL--TARLENPFGYGRI 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 156 VENpQTHEVLHYVEK----PSTFISDIINCGIYLFSPEALkplrdvfqrnqqdgqleespgswpgagtirleqdvFSALA 231
Cdd:PRK14355  145 VRD-ADGRVLRIVEEkdatPEERSIREVNSGIYCVEAAFL-----------------------------------FDAIG 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 232 G------QGQIYvhLTDgIWSQIKSAGSALYA-----SRLYLG---RYQITHPERLARHtpggpRIRGN----------- 286
Cdd:PRK14355  189 RlgndnaQGEYY--LTD-IVAMAAAEGLRCLAfpvadPDEIMGvndRAQLAEAARVLRR-----RINRElmlagvtlidp 260

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907070242 287 --VYIHPTAKVAPSAVLGPNVSIGKGVTIGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVG 348
Cdd:PRK14355  261 etTYIDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVIKGCRIGDDVTVKAGSVLEDSVVG 324
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 272-353 3.58e-10

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 60.92  E-value: 3.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 272 RLARHTPGGPRIRGNVYIHPTAKVAPSAVLGPNVSIGKGVTIGEGVRLRESIVLHGatlqehtcvlHSIVGWGSTVGR-- 349
Cdd:PRK00892   86 RLAQLFDPPATPSPAAGIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGA----------GAVIGDGVKIGAdc 155


                  ....*.
gi 1907070242 350 --WARV 353
Cdd:PRK00892  156 rlHANV 161
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 289-353 8.42e-10

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 59.65  E-value: 8.42e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907070242 289 IHPTAKVAPSAVLGPNVSIGKGVTIGEGVRLRESIVLHGatlqehtcvlHSIVGWGSTVGR----WARV 353
Cdd:COG1044    99 IHPSAVIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGP----------GVVIGDGVVIGDdcvlHPNV 157
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
286-315 1.65e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.78  E-value: 1.65e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1907070242 286 NVYIHPTAKVAPSAVLGPNVSIGKGVTIGE 315
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
Name Accession Description Interval E-value
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 4-261 2.72e-171

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: 479.44  E-value: 2.72e-171
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   4 AVILIGGPQKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVPGMQEILLIGFYqPDEALTQFLEAAQQEFNLPVRYL 83
Cdd:cd06428     1 AVILVGGPQKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVPDLKEVLLIGFY-PESVFSDFISDAQQEFNVPIRYL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  84 QEFAPLGTGGGLYHFRDQILAGAPEAFFVLNADVCSDFPLSAMLEAHRRQRHPFLLLGTTANRTQSLNYGCIVENPQTHE 163
Cdd:cd06428    80 QEYKPLGTAGGLYHFRDQILAGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEASREQASNYGCIVEDPSTGE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 164 VLHYVEKPSTFISDIINCGIYLFSPEALKPLRDVFQRNQQDGQLEESPGSWPGAGTIRLEQDVFSALAGQGQIYVHLTDG 243
Cdd:cd06428   160 VLHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNREGRAEVIRLEQDVLTPLAGSGKLYVYKTDD 239

                         250
                  ....*....|....*...
gi 1907070242 244 IWSQIKSAGSALYASRLY 261
Cdd:cd06428   240 FWSQIKTAGSAIYANRLY 257
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 4-248 6.37e-55

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: 181.24  E-value: 6.37e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   4 AVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIGFYQPDEALTQFLEAAQqeFNLPVRYL 83
Cdd:cd04181     1 AVILAAG--KGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARA-GIDEIILVVGYLGEQIEEYFGDGSK--FGVNIEYV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  84 QEFAPLGTGGGLYHFRDQILagaPEAFFVLNADVCSDFPLSAMLEAHRRQRHPFLLLGTTANRTQSlnYGCIVENPQtHE 163
Cdd:cd04181    76 VQEEPLGTAGAVRNAEDFLG---DDDFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEVEDPSR--YGVVELDDD-GR 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 164 VLHYVEKPSTFISDIINCGIYLFSPEALKPLRDVFQRnqqdGQLEespgswpgagtirlEQDVFSALAGQGQIYVHLTDG 243
Cdd:cd04181   150 VTRFVEKPTLPESNLANAGIYIFEPEILDYIPEILPR----GEDE--------------LTDAIPLLIEEGKVYGYPVDG 211


                  ....*
gi 1907070242 244 IWSQI 248
Cdd:cd04181   212 YWLDI 216
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 2-262 8.29e-55

N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain and a C-terminal Lefthanded-beta-Helix fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes, such as cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133047 [Multi-domain]  Cd Length: 233  Bit Score: 181.25  E-value: 8.29e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   2 LKAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIGFYQPDEaLTQFLEAAQQEFNLPVR 81
Cdd:cd06425     1 MKALILVGG--YGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKA-GVKEIILAVNYRPED-MVPFLKEYEKKLGIKIT 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  82 YLQEFAPLGTGGGLYHFRDqILAGAPEAFFVLNADVCSDFPLSAMLEAHRRQRHPFLLLGTTAnrTQSLNYGCIVENPQT 161
Cdd:cd06425    77 FSIETEPLGTAGPLALARD-LLGDDDEPFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKV--EDPSKYGVVVHDENT 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 162 HEVLHYVEKPSTFISDIINCGIYLFSPEALKplrdvfqrnqqdgQLEESPGSwpgagtirLEQDVFSALAGQGQIYVHLT 241
Cdd:cd06425   154 GRIERFVEKPKVFVGNKINAGIYILNPSVLD-------------RIPLRPTS--------IEKEIFPKMASEGQLYAYEL 212

                         250       260
                  ....*....|....*....|.
gi 1907070242 242 DGIWSQIKSAGSALYASRLYL 262
Cdd:cd06425   213 PGFWMDIGQPKDFLKGMSLYL 233
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 3-245 6.03e-47

NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440821 [Multi-domain]  Cd Length: 238  Bit Score: 161.09  E-value: 6.03e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   3 KAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIGFYQPdEALTQFLeAAQQEFNLPVRY 82
Cdd:COG1208     1 KAVILAGG--LGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAA-GITEIVINVGYLA-EQIEEYF-GDGSRFGVRITY 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  83 LQEFAPLGTGGGLYHFRDQIlagAPEAFFVLNADVCSDFPLSAMLEAHRRQRHPFLLLgTTANRTQSlNYGCIVENPQtH 162
Cdd:COG1208    76 VDEGEPLGTGGALKRALPLL---GDEPFLVLNGDILTDLDLAALLAFHREKGADATLA-LVPVPDPS-RYGVVELDGD-G 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 163 EVLHYVEKPSTFISDIINCGIYLFSPEALKplrdvfqrnqqdgqleespgSWPGAGTIRLEqDVFSALAGQGQIYVHLTD 242
Cdd:COG1208   150 RVTRFVEKPEEPPSNLINAGIYVLEPEIFD--------------------YIPEGEPFDLE-DLLPRLIAEGRVYGYVHD 208


                  ...
gi 1907070242 243 GIW 245
Cdd:COG1208   209 GYW 211
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 2-348 5.24e-34

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: 130.79  E-value: 5.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   2 LKAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIGFYQpDEALTQFLEaAQQEFNLPVR 81
Cdd:TIGR03992   1 MKAVILAAG--KGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDA-GIDDFVFVVGYG-KEKVREYFG-DGSRGGVPIE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  82 YLQEFAPLGTGGGLYHFRDQIlagaPEAFFVLNADVCSDFP-LSAMLEAHRrqrhPFLLLGTTANRTQslnYGCI-VENp 159
Cdd:TIGR03992  76 YVVQEEQLGTADALGSAKEYV----DDEFLVLNGDVLLDSDlLERLIRAEA----PAIAVVEVDDPSD---YGVVeTDG- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 160 qtHEVLHYVEKPSTFISDIINCGIYLFSPEALKPLRDVfqrnqqdgqlEESPgswpgAGTIRLeQDVFSALAGQGQIYVH 239
Cdd:TIGR03992 144 --GRVTGIVEKPENPPSNLINAGIYLFSPEIFELLEKT----------KLSP-----RGEYEL-TDALQLLIDEGKVKAV 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 240 LTDGIWSQIKSAGSALYASRLYL------------------GRYQIthpERLARHTPGGpRIRGNVYIHPTAKVAPSAVL 301
Cdd:TIGR03992 206 ELDGFWLDVGRPWDLLDANEALLdnlepriegtveenvtikGPVVI---GEGAVIRSGT-YIEGPVYIGKNCDIGPNAYI 281

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1907070242 302 GPNVSIGKGVTIGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVG 348
Cdd:TIGR03992 282 RPYTVIGNNVHIGNAVEIKNSIIMEGTKIPHLSYVGDSVIGENCNFG 328
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 3-191 3.51e-30

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 116.58  E-value: 3.51e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   3 KAVILIGGpqKGTRFRPLSFEVPKPLFPVAG-VPMIQHHIEACAQVpGMQEILLI-GFYQPDEALTQFLEAAQqeFNLPV 80
Cdd:pfam00483   1 KAIILAGG--SGTRLWPLTRTLAKPLVPVGGkYPLIDYPLSRLANA-GIREIIVIlTQEHRFMLNELLGDGSK--FGVQI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  81 RYLQEFAPLGTGGGLYHFRDQILAGAPEaFFVLNADVCSDFPLSAMLEAHR-RQRHPFLLLGTTANRTQSlNYGCIVENP 159
Cdd:pfam00483  76 TYALQPEGKGTAPAVALAADFLGDEKSD-VLVLGGDHIYRMDLEQAVKFHIeKAADATVTFGIVPVEPPT-GYGVVEFDD 153

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1907070242 160 QThEVLHYVEKPSTF-ISDIINCGIYLFSPEAL 191
Cdd:pfam00483 154 NG-RVIRFVEKPKLPkASNYASMGIYIFNSGVL 185
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 4-243 9.70e-28

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: 109.56  E-value: 9.70e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   4 AVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQvPGMQEILL-IGFyqpdeaLTQFLEAAQQE---FNLP 79
Cdd:cd06915     1 AVILAGG--LGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLAR-QGISRIVLsVGY------LAEQIEEYFGDgyrGGIR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  80 VRYLQEFAPLGTGGGLYHFRDQILAgapEAFFVLNADVCSDFPLSAMLEAHRRQRHPFLLLGtTANRTQSlNYGCIVENp 159
Cdd:cd06915    72 IYYVIEPEPLGTGGAIKNALPKLPE---DQFLVLNGDTYFDVDLLALLAALRASGADATMAL-RRVPDAS-RYGNVTVD- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 160 QTHEVLHYVEKPSTFISDIINCGIYLFSPEALKplrdvfqrnqqdgQLEESPGSwpgagtirLEQDVFSALAGQGQIYVH 239
Cdd:cd06915   146 GDGRVIAFVEKGPGAAPGLINGGVYLLRKEILA-------------EIPADAFS--------LEADVLPALVKRGRLYGF 204


                  ....
gi 1907070242 240 LTDG 243
Cdd:cd06915   205 EVDG 208
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 3-214 1.89e-25

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


Pssm-ID: 133044 [Multi-domain]  Cd Length: 221  Bit Score: 103.03  E-value: 1.89e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   3 KAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIGFYQPDeALTQFLEAaqQEFNLPVRY 82
Cdd:cd06422     1 KAMILAAG--LGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAA-GIRRIVVNTHHLAD-QIEAHLGD--SRFGLRITI 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  83 LQE-FAPLGTGGGLYHFRDqILAGAPeaFFVLNADVCSDFPLSAMLEAHRRQRHPFLLLGTTANRTQSLNYGCIVENPQT 161
Cdd:cd06422    75 SDEpDELLETGGGIKKALP-LLGDEP--FLVVNGDILWDGDLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFSLDADG 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907070242 162 HevLHYveKPSTFISDIINCGIYLFSPEALK-------PLRDVFQRNQQDGQL--EESPGSW 214
Cdd:cd06422   152 R--LRR--GGGGAVAPFTFTGIQILSPELFAgippgkfSLNPLWDRAIAAGRLfgLVYDGLW 209
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 3-360 4.04e-24

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: 102.48  E-value: 4.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   3 KAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEI-LLIGFYQPDEALTQFLEAaqQEFNLPVR 81
Cdd:TIGR01208   1 KALILAAG--KGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEA-GITDIgIVVGPVTGEEIKEIVGEG--ERFGAKIT 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  82 YLQEFAPLGTGGGLYHFRDQIlagAPEAFFVLNADVCSDFPLSAMLEaHRRQRHP--FLLLGTTANRTQslnYGCIVENP 159
Cdd:TIGR01208  76 YIVQGEPLGLAHAVYTARDFL---GDDDFVVYLGDNLIQDGISRFVK-SFEEKDYdaLILLTKVRDPTA---FGVAVLED 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 160 QtHEVLHYVEKPSTFISDIINCGIYLFSPEALKPLRDVfqrnqqdgqleesPGSWPGAGTIrleQDVFSALAGQGQ-IYV 238
Cdd:TIGR01208 149 G-KRILKLVEKPKEPPSNLAVVGLYMFRPLIFEAIKNI-------------KPSWRGELEI---TDAIQWLIEKGYkVGG 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 239 HLTDGIWSQIKSAGSALYASRLYLgryqithpERLARHTPG---GPRIRGNVYIHPTAKVAPSAVLGP----------NV 305
Cdd:TIGR01208 212 SKVTGWWKDTGKPEDLLDANRLIL--------DEVEREVQGvddESKIRGRVVVGEGAKIVNSVIRGPavigedciieNS 283

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 306 SIGKGVTIGEGVRLRESIVLHGATLQEhtcvlHSIVGWG-----STVGRWARVEGTPNDP 360
Cdd:TIGR01208 284 YIGPYTSIGEGVVIRDAEVEHSIVLDE-----SVIEGVQarivdSVIGKKVRIKGNRRRP 338
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 4-192 1.28e-23

NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133048 [Multi-domain]  Cd Length: 220  Bit Score: 97.97  E-value: 1.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   4 AVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIGFYQPDEALTQFLEAaqQEFNLPVRYL 83
Cdd:cd06426     1 VVIMAGG--KGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQ-GFRNFYISVNYLAEMIEDYFGDG--SKFGVNISYV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  84 QEFAPLGTGGGLYHFRDQIlagaPEAFFVLNADVCSDFPLSAMLEAHRRQRHpfllLGTTANRTQSLN--YGCIVENpqT 161
Cdd:cd06426    76 REDKPLGTAGALSLLPEKP----TDPFLVMNGDILTNLNYEHLLDFHKENNA----DATVCVREYEVQvpYGVVETE--G 145

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1907070242 162 HEVLHYVEKPStfISDIINCGIYLFSPEALK 192
Cdd:cd06426   146 GRITSIEEKPT--HSFLVNAGIYVLEPEVLD 174
LbH_M1P_guanylylT_C cd05824
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 289-355 2.62e-23

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


Pssm-ID: 100062 [Multi-domain]  Cd Length: 80  Bit Score: 92.99  E-value: 2.62e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907070242 289 IHPTAKVAPSAVLGPNVSIGKGVTIGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVGRWARVEG 355
Cdd:cd05824     2 IDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLEN 68
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 3-262 7.62e-22

G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose.


Pssm-ID: 133032 [Multi-domain]  Cd Length: 236  Bit Score: 93.40  E-value: 7.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   3 KAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIGFYQPDEALTQFLEAAQqeFNLPVRY 82
Cdd:cd04189     2 KGLILAGG--KGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREA-GIEDIGIVVGPTGEEIKEALGDGSR--FGVRITY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  83 LQEFAPLGTGGGLYHFRDQIlagAPEAFFVLNADVCSDFPLSAMLEAHRRQRH-PFLLLGTTANRTQslnYGCIVenPQT 161
Cdd:cd04189    77 ILQEEPLGLAHAVLAARDFL---GDEPFVVYLGDNLIQEGISPLVRDFLEEDAdASILLAEVEDPRR---FGVAV--VDD 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 162 HEVLHYVEKPSTFISDIINCGIYLFSPE------ALKPlrdvfqrnqqdgqleespgSWPGagtiRLE-QDVFSALAGQG 234
Cdd:cd04189   149 GRIVRLVEKPKEPPSNLALVGVYAFTPAifdaisRLKP-------------------SWRG----ELEiTDAIQWLIDRG 205

                         250       260
                  ....*....|....*....|....*....
gi 1907070242 235 -QIYVHLTDGIWSQIKSAGSALYASRLYL 262
Cdd:cd04189   206 rRVGYSIVTGWWKDTGTPEDLLEANRLLL 234
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 2-352 7.31e-20

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: 91.24  E-value: 7.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   2 LKAVILIGGpqKGTRFRplSfEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIGFYQPDEaltqfLEAAQQEFNlpVR 81
Cdd:COG1207     3 LAVVILAAG--KGTRMK--S-KLPKVLHPLAGKPMLEHVLDAARAL-GPDRIVVVVGHGAEQ-----VRAALADLD--VE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  82 Y-LQEfAPLGTGGGLYHFRDQiLAGAPEAFFVLNADVcsdfPL------SAMLEAHRRQRHPFLLLgtTANRTQSLNYGC 154
Cdd:COG1207    70 FvLQE-EQLGTGHAVQQALPA-LPGDDGTVLVLYGDV----PLiraetlKALLAAHRAAGAAATVL--TAELDDPTGYGR 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 155 IVENpQTHEVLHYVE-KpstfisDI---------INCGIYLFSPEALkplrdvfqrnqqdgqleespgswpgagtirleq 224
Cdd:COG1207   142 IVRD-EDGRVLRIVEeK------DAteeqraireINTGIYAFDAAAL--------------------------------- 181

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 225 dvFSALAG------QGQIYvhLTDgIWSQIKSAG---SALYASRLY--LG---RYQITHPERLARHtpggpRIR------ 284
Cdd:COG1207   182 --REALPKlsndnaQGEYY--LTD-VIAIARADGlkvAAVQPEDPWevLGvndRVQLAEAERILQR-----RIAerlmra 251

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 285 G-------NVYIHPTAKVAPSAVLGPNV------SIGKGVTIGEGVRLRESIVLHGATLQeHTCVLHSIVGWGSTVGRWA 351
Cdd:COG1207   252 GvtiidpaTTYIDGDVEIGRDVVIDPNVilegktVIGEGVVIGPNCTLKDSTIGDGVVIK-YSVIEDAVVGAGATVGPFA 330


                  .
gi 1907070242 352 R 352
Cdd:COG1207   331 R 331
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 2-191 1.11e-16

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


Pssm-ID: 133001 [Multi-domain]  Cd Length: 216  Bit Score: 78.45  E-value: 1.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   2 LKAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLigFYQPDEAltQFLEAAQQEFNLPVR 81
Cdd:cd02507     1 FQAVVLADG--FGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKA-GVEEVFV--VCCEHSQ--AIIEHLLKSKWSSLS 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  82 YLQEF--------APLGTGGGLYHFRDQIlagaPEAFFVLNADVCSDFPLSAMLEAhRRQRHP------FLLLGTTANRT 147
Cdd:cd02507    74 SKMIVdvitsdlcESAGDALRLRDIRGLI----RSDFLLLSCDLVSNIPLSELLEE-RRKKDKnaiatlTVLLASPPVST 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907070242 148 QSL----NYGCIVENPQTHE--VLHY---VEKPSTFI---------------SDIINCGIYLFSPEAL 191
Cdd:cd02507   149 EQSkkteEEDVIAVDSKTQRllLLHYeedLDEDLELIirksllskhpnvtirTDLLDCHIYICSPDVL 216
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
3-243 1.27e-16

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 78.74  E-value: 1.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   3 KAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIGFYQPDEaltqfLEAAQQEFNLPVRY 82
Cdd:COG1213     1 KAVILAAG--RGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAA-GIKDIVVVTGYKAEL-----IEEALARPGPDVTF 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  83 LQ--EFAPLGTGGGLYHFRDQIlagaPEAFFVLNAD-VCSDFPLSAMLEAhrrqRHPFLLLGTTANRTQSlnygcivenp 159
Cdd:COG1213    73 VYnpDYDETNNIYSLWLAREAL----DEDFLLLNGDvVFDPAILKRLLAS----DGDIVLLVDRKWEKPL---------- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 160 qtHEVLHYVEKPSTFISDI--------INC---GIYLFSPEALKPLRDVFQRNQQDGQLEESpgswpgagtirLEqDVFS 228
Cdd:COG1213   135 --DEEVKVRVDEDGRIVEIgkklppeeADGeyiGIFKFSAEGAAALREALEALIDEGGPNLY-----------YE-DALQ 200

                         250
                  ....*....|....*.
gi 1907070242 229 ALAGQG-QIYVHLTDG 243
Cdd:COG1213   201 ELIDEGgPVKAVDIGG 216
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 2-132 1.48e-14

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


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 72.31  E-value: 1.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   2 LKAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIgfyqPDEALTQFLEAAQQEF--NLP 79
Cdd:cd04198     1 FQAVILAGG--GGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKA-GFEDVIVV----VPEEEQAEISTYLRSFplNLK 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907070242  80 VRYLQEFAPL----GTGGGLYHFRDQIlagaPEAFFVLNADVCSDFPLSAMLEAHRR 132
Cdd:cd04198    74 QKLDEVTIVLdedmGTADSLRHIRKKI----KKDFLVLSCDLITDLPLIELVDLHRS 126
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 4-194 1.65e-14

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: 72.55  E-value: 1.65e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   4 AVILIGGpqKGTRFRplsFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIGFYQpDEALTQFLEAAQQEFnlpvrYL 83
Cdd:cd02540     1 AVILAAG--KGTRMK---SDLPKVLHPLAGKPMLEHVLDAARAL-GPDRIVVVVGHG-AEQVKKALANPNVEF-----VL 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  84 QEfAPLGTGGGLYHFRDQiLAGAPEAFFVLNADVcsdfPL------SAMLEAHRRQRHPFLLLgtTANRTQSLNYGCIVE 157
Cdd:cd02540    69 QE-EQLGTGHAVKQALPA-LKDFEGDVLVLYGDV----PLitpetlQRLLEAHREAGADVTVL--TAELEDPTGYGRIIR 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1907070242 158 NpQTHEVLHYVE----KPSTFISDIINCGIYLFSPEALKPL 194
Cdd:cd02540   141 D-GNGKVLRIVEekdaTEEEKAIREVNAGIYAFDAEFLFEA 180
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 4-248 1.71e-14

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


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 72.26  E-value: 1.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   4 AVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIGFYQPDealtQFLEAAQQEFNLPVRYL 83
Cdd:cd02523     1 AIILAAG--RGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEA-GIDDIVIVTGYKKE----QIEELLKKYPNIKFVYN 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  84 QEFAPLGTGGGLYHFRDQIlagaPEAFFVLNADVCSDfplSAMLEAHRRQRHPFLLLGTTANRTQSLNYGCIVENPQthe 163
Cdd:cd02523    74 PDYAETNNIYSLYLARDFL----DEDFLLLEGDVVFD---PSILERLLSSPADNAILVDKKTKEWEDEYVKDLDDAG--- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 164 VLHYVEKPSTFISDI--INCGIYLFSPEALKPLRDVFQRNQQDGQLEEspgSWPgagtirleqDVFSALAGQGQIYVH-L 240
Cdd:cd02523   144 VLLGIISKAKNLEEIqgEYVGISKFSPEDADRLAEALEELIEAGRVNL---YYE---------DALQRLISEEGVKVKdI 211


                  ....*...
gi 1907070242 241 TDGIWSQI 248
Cdd:cd02523   212 SDGFWYEI 219
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 2-348 1.73e-13

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 71.70  E-value: 1.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   2 LKAVILIGGpqKGTRFRPlsfEVPKPLFPVAGVPMIQHHIEAcAQVPGMQEILLIGFYQPDEALTQFLEAAQQEFNlpvr 81
Cdd:PRK14355    4 LAAIILAAG--KGTRMKS---DLVKVMHPLAGRPMVSWPVAA-AREAGAGRIVLVVGHQAEKVREHFAGDGDVSFA---- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  82 yLQEfAPLGTGGGLYHFRDQiLAGAPEAFFVLnadvCSDFP------LSAMLEAHRRQRHPFLLLgtTANRTQSLNYGCI 155
Cdd:PRK14355   74 -LQE-EQLGTGHAVACAAPA-LDGFSGTVLIL----CGDVPllraetLQGMLAAHRATGAAVTVL--TARLENPFGYGRI 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 156 VENpQTHEVLHYVEK----PSTFISDIINCGIYLFSPEALkplrdvfqrnqqdgqleespgswpgagtirleqdvFSALA 231
Cdd:PRK14355  145 VRD-ADGRVLRIVEEkdatPEERSIREVNSGIYCVEAAFL-----------------------------------FDAIG 188

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 232 G------QGQIYvhLTDgIWSQIKSAGSALYA-----SRLYLG---RYQITHPERLARHtpggpRIRGN----------- 286
Cdd:PRK14355  189 RlgndnaQGEYY--LTD-IVAMAAAEGLRCLAfpvadPDEIMGvndRAQLAEAARVLRR-----RINRElmlagvtlidp 260

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907070242 287 --VYIHPTAKVAPSAVLGPNVSIGKGVTIGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVG 348
Cdd:PRK14355  261 etTYIDRGVVIGRDTTIYPGVCISGDTRIGEGCTIEQGVVIKGCRIGDDVTVKAGSVLEDSVVG 324
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 2-351 4.29e-13

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 70.63  E-value: 4.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   2 LKAVILIGGpqKGTRFRPlsfEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLI---GFYQPDEALTQFLEAAQQEfnl 78
Cdd:PRK14354    3 RYAIILAAG--KGTRMKS---KLPKVLHKVCGKPMVEHVVDSVKKA-GIDKIVTVvghGAEEVKEVLGDRSEFALQE--- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  79 pvrylqefAPLGTGGGLYHFRDqILAGAPEAFFVlnadVCSDFPL------SAMLEAHRRQR-HPFLLLGTTANRTqslN 151
Cdd:PRK14354   74 --------EQLGTGHAVMQAEE-FLADKEGTTLV----ICGDTPLitaetlKNLIDFHEEHKaAATILTAIAENPT---G 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 152 YGCIVENPQThEVLHYVEKP--STFISDI--INCGIYLFSPEAL-KPLRDVFQRNQQdgqleespgswpgagtirleqdv 226
Cdd:PRK14354  138 YGRIIRNENG-EVEKIVEQKdaTEEEKQIkeINTGTYCFDNKALfEALKKISNDNAQ----------------------- 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 227 fsalagqGQIYvhLTDGIwSQIKSAGS--ALYASRLY---LG---RYQITHPERLARHtpggpRI------RG------- 285
Cdd:PRK14354  194 -------GEYY--LTDVI-EILKNEGEkvGAYQTEDFeesLGvndRVALAEAEKVMRR-----RInekhmvNGvtiidpe 258

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907070242 286 NVYIHPTAKVAPSAVLGPNV------SIGKGVTIGEGVRLRESIVLHGATLQeHTCVLHSIVGWGSTVGRWA 351
Cdd:PRK14354  259 STYIDADVEIGSDTVIEPGVvikgntVIGEDCVIGPGSRIVDSTIGDGVTIT-NSVIEESKVGDNVTVGPFA 329
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
3-207 6.01e-13

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 68.96  E-value: 6.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   3 KAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIgfyqpdeaLT-QFLEAAQQ------E 75
Cdd:COG1209     2 KGIILAGG--SGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLA-GIREILII--------STpEDGPQFERllgdgsQ 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  76 FNLPVRY-LQEfAPLGTGgglyhfrDQILAGAPeafFVLNADVC---SD--F---PLSAMLEAHRRQRHpflllGTTAnr 146
Cdd:COG1209    71 LGIKISYaVQP-EPLGLA-------HAFIIAED---FIGGDPVAlvlGDniFygdGLSELLREAAARES-----GATI-- 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 147 tqslnYGCIVENPQ---------THEVLHYVEKPSTFISDIINCGIYLFSP------EALKP-------LRDVFQRNQQD 204
Cdd:COG1209   133 -----FGYKVEDPErygvvefdeDGRVVSLEEKPKEPKSNLAVTGLYFYDNdvveiaKNLKPsargeleITDANQAYLER 207


                  ...
gi 1907070242 205 GQL 207
Cdd:COG1209   208 GKL 210
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 2-353 5.42e-12

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 67.31  E-value: 5.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   2 LKAVILIGGpqKGTRFRPlsfEVPKPLFPVAGVPMIQHHIEAcAQVPGMQEILLIGFYQPDEaltqfLEAAQQEFNlpVR 81
Cdd:PRK14358    8 LDVVILAAG--QGTRMKS---ALPKVLHPVAGRPMVAWAVKA-ARDLGARKIVVVTGHGAEQ-----VEAALQGSG--VA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  82 YLQEFAPLGTGgglyhfrDQILAGApEAFFVLNADVC---SDFP------LSAMLEAHRRQRHPFLLLgtTANRTQSLNY 152
Cdd:PRK14358   75 FARQEQQLGTG-------DAFLSGA-SALTEGDADILvlyGDTPllrpdtLRALVADHRAQGSAMTIL--TGELPDATGY 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 153 GCIVENPQTHEVLHYVEKPSTFISDII---NCGIYLFSPEALKPLRDVFQRNQqdgqleespgswpgAGTIRLEQ--DVF 227
Cdd:PRK14358  145 GRIVRGADGAVERIVEQKDATDAEKAIgefNSGVYVFDARAPELARRIGNDNK--------------AGEYYLTDllGLY 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 228 SALAGQGQIYvHLTDgiwsqiksAGSALYAS-RLYLGRYQITHPERLAR-HTPGGPRIR--GNVYIHPTAK------VAP 297
Cdd:PRK14358  211 RAGGAQVRAF-KLSD--------PDEVLGANdRAGLAQLEATLRRRINEaHMKAGVTLQdpGTILIEDTVTlgrdvtIEP 281

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907070242 298 SAVLGPNVSIGKGVTIGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVGRWARV 353
Cdd:PRK14358  282 GVLLRGQTRVADGVTIGAYSVVTDSVLHEGAVIKPHSVLEGAEVGAGSDVGPFARL 337
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 288-355 5.34e-11

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: 58.41  E-value: 5.34e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907070242 288 YIHPTAKVAPSAVLGPNVsIGKGVTIGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVGRWARVEG 355
Cdd:cd03356     1 LIGESTVIGENAIIKNSV-IGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVN 67
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 3-243 2.39e-10

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: 60.62  E-value: 2.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   3 KAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIG---------FYQPDEALTQFLEAAQ 73
Cdd:cd02541     2 KAVIPAAG--LGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAA-GIEDIIIVTgrgkraiedHFDRSYELEETLEKKG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  74 QEFNL----------PVRYLQEFAPLGTGgglyhfrDQILAGAP----EAFFVLNADV---CSDFPLSAMLEAHRRQRHP 136
Cdd:cd02541    79 KTDLLeevriisdlaNIHYVRQKEPLGLG-------HAVLCAKPfigdEPFAVLLGDDlidSKEPCLKQLIEAYEKTGAS 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 137 FLLLGTTANRTQSlNYGCIV---ENPQTHEVLHYVEKPStfISD------IIncGIYLFSPEALKPLrdvfqRNQQdgql 207
Cdd:cd02541   152 VIAVEEVPPEDVS-KYGIVKgekIDGDVFKVKGLVEKPK--PEEapsnlaIV--GRYVLTPDIFDIL-----ENTK---- 217

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1907070242 208 eespgswPGA-GTIRLeQDVFSALAGQGQIYVHLTDG 243
Cdd:cd02541   218 -------PGKgGEIQL-TDAIAKLLEEEPVYAYVFEG 246
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 272-353 3.58e-10

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 60.92  E-value: 3.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 272 RLARHTPGGPRIRGNVYIHPTAKVAPSAVLGPNVSIGKGVTIGEGVRLRESIVLHGatlqehtcvlHSIVGWGSTVGR-- 349
Cdd:PRK00892   86 RLAQLFDPPATPSPAAGIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGA----------GAVIGDGVKIGAdc 155


                  ....*.
gi 1907070242 350 --WARV 353
Cdd:PRK00892  156 rlHANV 161
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 289-353 8.42e-10

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 59.65  E-value: 8.42e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907070242 289 IHPTAKVAPSAVLGPNVSIGKGVTIGEGVRLRESIVLHGatlqehtcvlHSIVGWGSTVGR----WARV 353
Cdd:COG1044    99 IHPSAVIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGP----------GVVIGDGVVIGDdcvlHPNV 157
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 288-348 2.44e-09

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 58.49  E-value: 2.44e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907070242 288 YIHPTAKVAPSAVLGPNVSIGKGVTIGEGVRL-------------RESIVLHGATLQEHT-----CVLHSivgwGSTVG 348
Cdd:COG1044   104 VIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIgpgvvigdgvvigDDCVLHPNVTIYERCvigdrVIIHS----GAVIG 178
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 2-191 4.29e-09

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


Pssm-ID: 133040 [Multi-domain]  Cd Length: 217  Bit Score: 56.46  E-value: 4.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   2 LKAVILigGPQKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQvPGMQEILLigFYQPD-EALTQFLEAAQQEfNLPV 80
Cdd:cd04197     1 LQAVVL--ADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLAL-NGVEEVFV--FCCSHsDQIKEYIEKSKWS-KPKS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  81 RYLQEFAPLGT-----GGGLyhfRD----QILAGapeAFFVLNADVCSDFPLSAMLEAHRRQR---------------HP 136
Cdd:cd04197    75 SLMIVIIIMSEdcrslGDAL---RDldakGLIRG---DFILVSGDVVSNIDLKEILEEHKERRkkdknaimtmvlkeaSP 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907070242 137 FLLlgtTANRTQSLNygcIVENPQTHEVLHYVEKP----STFIS----------------DIINCGIYLFSPEAL 191
Cdd:cd04197   149 PHR---TRRTGEEFV---IAVDPKTSRLLHYEELPgskyRSITDlpsellgsnseveirhDLLDCHIDICSPDVL 217
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 4-361 9.96e-09

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 56.62  E-value: 9.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   4 AVILIGGpqKGTRFRPLSFEVPKPLFPVAG------VP---MIQHhieacaqvpGMQEILLIGFYQP---DEALTQ---- 67
Cdd:COG0448     4 AIILAGG--RGSRLGPLTKDRAKPAVPFGGkyriidFPlsnCVNS---------GIRRVGVLTQYKShslNDHIGSgkpw 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  68 -------FLE--AAQQEFNLPVRYLqefaplGTGGGLYHFRDQILAGAPEAFFVLNAD-VCS-DFplSAMLEAHRRQRHP 136
Cdd:COG0448    73 dldrkrgGVFilPPYQQREGEDWYQ------GTADAVYQNLDFIERSDPDYVLILSGDhIYKmDY--RQMLDFHIESGAD 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 137 FLLLGTTANRTQSLNYGCIVENPQtHEVLHYVEKPSTFISDIINCGIYLFSPEAlkpLRDVFQRNQQDGQLEespgswpg 216
Cdd:COG0448   145 ITVACIEVPREEASRFGVMEVDED-GRITEFEEKPKDPKSALASMGIYVFNKDV---LIELLEEDAPNSSHD-------- 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 217 agtirLEQDVFSALAGQGQIYVHLTDGIWSQIKSAGSalYasrlylgrYQ----ITHPE-RLARHTPGGPrIRGNVYIHP 291
Cdd:COG0448   213 -----FGKDIIPRLLDRGKVYAYEFDGYWRDVGTIDS--Y--------YEanmdLLDPEpEFNLYDPEWP-IYTKQKDLP 276

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 292 TAKVAPSA--------------------VLGPNVSIGKGVTIgegvrlRESIVLHGATLQEHTCVLHSIVGWGSTVGRWA 351
Cdd:COG0448   277 PAKFVRGGkvknslvsngciisgtvensVLFRGVRVESGAVV------ENSVIMPGVVIGEGAVIENAIIDKNVVIPPGV 350

                         410
                  ....*....|
gi 1907070242 352 RVEGTPNDPN 361
Cdd:COG0448   351 VIGEDPEEDR 360
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
289-329 1.73e-08

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 55.10  E-value: 1.73e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1907070242 289 IHPTAKVAPSAVLGPNVSIG------KGVTIGEGVRLRESIVLHGAT 329
Cdd:PRK05289    5 IHPTAIVEPGAKIGENVEIGpfcvigPNVVIGDGTVIGSHVVIDGHT 51
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 289-329 2.44e-08

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: 54.75  E-value: 2.44e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1907070242 289 IHPTAKVAPSAVLGPNVSIG------KGVTIGEGVRLRESIVLHGAT 329
Cdd:cd03351     2 IHPTAIVDPGAKIGENVEIGpfcvigPNVEIGDGTVIGSHVVIDGPT 48
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 280-348 2.46e-08

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 53.95  E-value: 2.46e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907070242 280 GPRIRGNVYIHPTAKVAPSAVLGPNVSIGKGVTIGEGVRLREsivlhGATLQEHT-----CVLHSivgwGSTVG 348
Cdd:cd03352     7 NVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIHP-----NVTIYEGCiigdrVIIHS----GAVIG 71
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 289-329 2.60e-08

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: 54.64  E-value: 2.60e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1907070242 289 IHPTAKVAPSAVLGPNVSIG------KGVTIGEGVRLRESIVLHGAT 329
Cdd:COG1043     4 IHPTAIVDPGAKLGENVEIGpfcvigPDVEIGDGTVIGSHVVIEGPT 50
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 286-353 4.06e-08

N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix (LbH) acetyltransferase domain: GlmU is also known as UDP-N-acetylglucosamine pyrophosphorylase. It is a bifunctional bacterial enzyme that catalyzes two consecutive steps in the formation of UDP-N-acetylglucosamine (UDP-GlcNAc), an important precursor in bacterial cell wall formation. The two enzymatic activities, uridyltransferase and acetyltransferase, are carried out by two independent domains. The C-terminal LbH domain possesses the acetyltransferase activity. It catalyzes the CoA-dependent acetylation of GlcN-1-phosphate to GlcNAc-1-phosphate. The LbH domain contains 10 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X. The acetyltransferase active site is located at the interface between two subunits of the active LbH trimer.


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 53.19  E-value: 4.06e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907070242 286 NVYIHPTAKVAPSAVLGPNV------SIGKGVTIGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVGRWARV 353
Cdd:cd03353     9 TTYIDGDVEIGVDVVIDPGVilegktVIGEDCVIGPNCVIKDSTIGDGVVIKASSVIEGAVIGNGATVGPFAHL 82
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 289-412 4.43e-08

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


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 51.99  E-value: 4.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 289 IHPTAKVAPSAVLGPNVSIGKGVTIGEGVRLR---ESIVLH-GATLQEhTCVLHS------IVGWGSTVGRWARVEGTPN 358
Cdd:cd04745     3 VDPSSFVHPTAVLIGDVIIGKNCYIGPHASLRgdfGRIVIRdGANVQD-NCVIHGfpgqdtVLEENGHIGHGAILHGCTI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 359 DPNpndprARMDSESLFKDGKLLPAITILGC------RVRIPAEVLILNSIVLPHKELSR 412
Cdd:cd04745    82 GRN-----ALVGMNAVVMDGAVIGEESIVGAmafvkaGTVIPPRSLIAGSPAKVIRELSD 136
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 4-245 9.32e-08

G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; Alpha-D-Glucose-1-phosphate Cytidylyltransferase catalyzes the production of CDP-D-Glucose from alpha-D-Glucose-1-phosphate and MgCTP as substrate. CDP-D-Glucose is the precursor for synthesizing four of the five naturally occurring 3,6-dideoxy sugars-abequose (3,6-dideoxy-D-Xylo-hexose), ascarylose (3,6-dideoxy-L-arabino-hexose), paratose (3,6-dideoxy-D-ribohexose), and tyvelose (3,6-dideoxy-D-arabino-hexose. Deoxysugars are ubiquitous in nature where they function in a variety of biological processes, including cell adhesion, immune response, determination of ABO blood groups, fertilization, antibiotic function, and microbial pathogenicity.


Pssm-ID: 133015 [Multi-domain]  Cd Length: 253  Bit Score: 52.96  E-value: 9.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   4 AVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQE-ILLIGF-----------YQP---------D 62
Cdd:cd02524     1 VVILAGG--LGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHY-GHNDfILCLGYkghvikeyflnYFLhnsdvtidlG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  63 EALTQFLEAAQQEFNLpvrylqEFAPLG----TGGGLYHFRDQIlaGAPEAFFVLNADVCSDFPLSAMLEAHRRQRhpfl 138
Cdd:cd02524    78 TNRIELHNSDIEDWKV------TLVDTGlntmTGGRLKRVRRYL--GDDETFMLTYGDGVSDVNINALIEFHRSHG---- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 139 LLGTTANRTQSLNYGCIVENPQtHEVLHYVEKPSTFISdIINCGIYLFSPEALKPLrdvfqrnqqdgqleespgswPGAG 218
Cdd:cd02524   146 KLATVTAVHPPGRFGELDLDDD-GQVTSFTEKPQGDGG-WINGGFFVLEPEVFDYI--------------------DGDD 203

                         250       260
                  ....*....|....*....|....*..
gi 1907070242 219 TIrLEQDVFSALAGQGQIYVHLTDGIW 245
Cdd:cd02524   204 TV-FEREPLERLAKDGELMAYKHTGFW 229
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
3-245 9.76e-08

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 53.11  E-value: 9.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   3 KAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIG---------FYQPDEALTQFLEAA- 72
Cdd:COG1210     5 KAVIPVAG--LGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAA-GIEEIIFVTgrgkraiedHFDRSYELEATLEAKg 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  73 -QQEFNLpVRYLQEFA---------PLGTGgglyhfrDQILAGAP----EAFFVLNAD--VCSDFP-LSAMLEAHRRQRH 135
Cdd:COG1210    82 kEELLEE-VRSISPLAnihyvrqkePLGLG-------HAVLCARPfvgdEPFAVLLGDdlIDSEKPcLKQMIEVYEETGG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 136 PFLLLGTTAnRTQSLNYGCIV---ENPQTHEVLHYVEKPS--TFISDIINCGIYLFSPEalkplrdVFQRnqqdgqLEES 210
Cdd:COG1210   154 SVIAVQEVP-PEEVSKYGIVDgeeIEGGVYRVTGLVEKPApeEAPSNLAIVGRYILTPE-------IFDI------LEKT 219

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1907070242 211 PgswPGA-GTIRLeQDVFSALAGQGQIYVHLTDGIW 245
Cdd:COG1210   220 K---PGAgGEIQL-TDAIAALAKEEPVYAYEFEGKR 251
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 4-117 3.57e-07

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


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 49.50  E-value: 3.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   4 AVILIGGpqKGTRFRplsfeVPKPLFPVAGVPMIQHHIEACAQVPGmqEILLIGfyqPDEALTQFLEAaqqefnLPVRYL 83
Cdd:pfam12804   1 AVILAGG--RSSRMG-----GDKALLPLGGKPLLERVLERLRPAGD--EVVVVA---NDEEVLAALAG------LGVPVV 62

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1907070242  84 -QEFAPLGTGGGLYHFRDQilAGAPEAFFVLNADV 117
Cdd:pfam12804  63 pDPDPGQGPLAGLLAALRA--APGADAVLVLACDM 95
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 287-348 4.79e-07

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


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 49.79  E-value: 4.79e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907070242 287 VYIHPTAKVAPSAVLGPNVSIGKGVTIGEGVRL-RESIVLHGATLqEHTCVL--HSIVGWGSTVG 348
Cdd:cd03360    85 TLIHPSAVVSPSAVIGEGCVIMAGAVINPDARIgDNVIINTGAVI-GHDCVIgdFVHIAPGVVLS 148
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-169 5.59e-07

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 51.40  E-value: 5.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   4 AVILIGGpqKGTRFRPlsfEVPKPLFPVAGVPMIQHHIEACAQVPGMQEILLIGFYQPDealtqfLEAAQQEFNLPVR-Y 82
Cdd:PRK14353    8 AIILAAG--EGTRMKS---SLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEA------VAAAAAKIAPDAEiF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  83 LQEfAPLGTGGGLYHFRDQILAGAPEAfFVLNADV--CSDFPLSAMLEaHRRQRHPFLLLGT-TANRTQslnYGCIVEnp 159
Cdd:PRK14353   77 VQK-ERLGTAHAVLAAREALAGGYGDV-LVLYGDTplITAETLARLRE-RLADGADVVVLGFrAADPTG---YGRLIV-- 148

                         170
                  ....*....|
gi 1907070242 160 QTHEVLHYVE 169
Cdd:PRK14353  149 KGGRLVAIVE 158
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-352 7.24e-07

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 51.26  E-value: 7.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   4 AVILIGGpqKGTRFRPlsfEVPKPLFPVAGVPMIQHHIEACAQVPGMQEILLIGFyQPDEALTQFLEaaqqefnLPVRYL 83
Cdd:PRK14356    8 ALILAAG--KGTRMHS---DKPKVLQTLLGEPMLRFVYRALRPLFGDNVWTVVGH-RADMVRAAFPD-------EDARFV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  84 QEFAPLGTGGGLYHFRDQILAGAPEAFFVLNAD--VCSDFPLSAMLEAHRRQRHPFLllgtTANRTQSLNYG-------- 153
Cdd:PRK14356   75 LQEQQLGTGHALQCAWPSLTAAGLDRVLVVNGDtpLVTTDTIDDFLKEAAGADLAFM----TLTLPDPGAYGrvvrrngh 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 154 --CIVENPQTHEVLHYVEkpstfiSDIINCGIYLFSPEALKPLRDVFQRNQQDGQ--LEESPGSWPGAGtirleQDVFSA 229
Cdd:PRK14356  151 vaAIVEAKDYDEALHGPE------TGEVNAGIYYLRLDAVESLLPRLTNANKSGEyyITDLVGLAVAEG-----MNVLGV 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 230 LAGQGQIYVhltdGIWSQIK-SAGSALYASRLYLGRYQithpERLARHTPGGPRIRGNVYIHPTAKV-APSAVLGPNvSI 307
Cdd:PRK14356  220 NCGEDPNLL----GVNTPAElVRSEELLRARIVEKHLE----SGVLIHAPESVRIGPRATIEPGAEIyGPCEIYGAS-RI 290

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1907070242 308 GKGVTIGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVGRWAR 352
Cdd:PRK14356  291 ARGAVIHSHCWLRDAVVSSGATIHSFSHLEGAEVGDGCSVGPYAR 335
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 3-219 8.21e-07

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


Pssm-ID: 133019 [Multi-domain]  Cd Length: 240  Bit Score: 49.88  E-value: 8.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   3 KAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLIGfyQPdEALTQFLEAaqqefnlpvry 82
Cdd:cd02538     2 KGIILAGG--SGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLA-GIREILIIS--TP-EDLPLFKEL----------- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  83 lqefapLGTG---GGLYHFRDQILA-GAPEAF-----FVLNADVC--------SDFPLSAMLEAHRRQRHPFLLLGTTAN 145
Cdd:cd02538    65 ------LGDGsdlGIRITYAVQPKPgGLAQAFiigeeFIGDDPVClilgdnifYGQGLSPILQRAAAQKEGATVFGYEVN 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 146 RTQslNYGcIVENPQTHEVLHYVEKPSTFISDIINCGIYLFSPEA------LKP-------LRDV----FQRNQQDGQLE 208
Cdd:cd02538   139 DPE--RYG-VVEFDENGRVLSIEEKPKKPKSNYAVTGLYFYDNDVfeiakqLKPsargeleITDVnneyLEKGKLSVELL 215

                         250
                  ....*....|.
gi 1907070242 209 ESPGSWPGAGT 219
Cdd:cd02538   216 GRGFAWLDTGT 226
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 2-215 3.41e-06

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


Pssm-ID: 133003 [Multi-domain]  Cd Length: 274  Bit Score: 48.34  E-value: 3.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   2 LKAVILIGGpqKGTRFRPLSFE-VPKPLFPVAGV-PMIQHHIEACAQVPGMQEILLIGfyqpDEALtQFLEAAQ-QEFNL 78
Cdd:cd02509     1 IYPVILAGG--SGTRLWPLSREsYPKQFLKLFGDkSLLQQTLDRLKGLVPPDRILVVT----NEEY-RFLVREQlPEGLP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  79 PVRYLQEFAPLGTGG----GLYHFRDQilagAPEA-FFVLNAD-VCSDFP-----LSAMLEAHRRQRhpFLLLGTTANRT 147
Cdd:cd02509    74 EENIILEPEGRNTAPaialAALYLAKR----DPDAvLLVLPSDhLIEDVEaflkaVKKAVEAAEEGY--LVTFGIKPTRP 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 148 QSlNYGCI----VENPQTHEVLHYVEKPST-----FISD---IINCGIYLFS------------PEALKPLRDVFQRNQQ 203
Cdd:cd02509   148 ET-GYGYIeageKLGGGVYRVKRFVEKPDLetakeYLESgnyLWNSGIFLFRaktfleelkkhaPDIYEALEKALAAAGT 226

                         250
                  ....*....|..
gi 1907070242 204 DGQLEESPGSWP 215
Cdd:cd02509   227 DDFLRLLEEAFA 238
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 289-349 3.87e-06

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 46.94  E-value: 3.87e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907070242 289 IHPTAKVAPSAVLGPNVSIGKGVTIGEGVRLR---ESIVL-HGATLQEHtCVLHSIVGWGSTVGR 349
Cdd:COG0663    13 IHPSAFVAPTAVVIGDVTIGEDVSVWPGAVLRgdvGPIRIgEGSNIQDG-VVLHVDPGYPLTIGD 76
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 5-187 5.26e-06

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


Pssm-ID: 133026 [Multi-domain]  Cd Length: 231  Bit Score: 47.25  E-value: 5.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   5 VILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAQVPGMQEILLIGfyqpDEALTQFLEAAQQEFNLPVRYLQ 84
Cdd:cd04183     2 IIPMAG--LGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFICR----DEHNTKFHLDESLKLLAPNATVV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  85 EFAPLgTGGGL---YHFRDQILAGAPeaFFVLNADVCSDFPLSAMLEAHRrqrhpflllgttanrtQSLNYGCIVENPQT 161
Cdd:cd04183    76 ELDGE-TLGAActvLLAADLIDNDDP--LLIFNCDQIVESDLLAFLAAFR----------------ERDLDGGVLTFFSS 136

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1907070242 162 HEVLHYVEKPS------TF----ISDIINCGIYLFS 187
Cdd:cd04183   137 HPRWSYVKLDEngrvieTAekepISDLATAGLYYFK 172
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 278-348 5.61e-06

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


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 46.04  E-value: 5.61e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907070242 278 PGGPRIRGNVYIHPTAKVAPSAVLGPNVSIGKGVTIGEGVRLRESIVLH-GATLQEHTCVLHSIVGWGSTVG 348
Cdd:cd05636     9 EEGVTIKGPVWIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGdGCVVGNSVEVKNSIIMDGTKVP 80
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 283-348 6.41e-06

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


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 46.04  E-value: 6.41e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907070242 283 IRGNVYIHPTAKVAPSAVLGPNVSIGKGVTIGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVG 348
Cdd:cd05636    32 IEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSIIMDGTKVPHLNYVGDSVLGENVNLG 97
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 295-349 1.28e-05

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


Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 42.95  E-value: 1.28e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 295 VAPSAVLGPNVSI-----GKGVTIGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVGR 349
Cdd:cd04652     2 VGENTQVGEKTSIkrsviGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGE 61
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 289-350 2.54e-05

Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 43.94  E-value: 2.54e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907070242 289 IHPTAKVAPSAVLGPNVSIGKGVTIGEGVRLR---ESIVL-HGATLQEHtCVLHSIVGWGSTVGRW 350
Cdd:cd04645     2 IDPSAFIAPNATVIGDVTLGEGSSVWFGAVLRgdvNPIRIgERTNIQDG-SVLHVDPGYPTIIGDN 66
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 289-350 4.05e-05

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 45.01  E-value: 4.05e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907070242 289 IHPTAKVAPSAVL------GPNVSIGKGVTIGEGVRLRESIVLHGATLQEHTCVLHSivgwGSTVGRW 350
Cdd:PRK12461    2 IHPTAVIDPSAKLgsgveiGPFAVIGANVEIGDGTWIGPHAVILGPTRIGKNNKIHQ----GAVVGDE 65
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 281-354 6.42e-05

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 43.09  E-value: 6.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 281 PRIRGNVYIHPTAK------------VAPSAVL---------GPNVSI----------GKGVTIGEGVrlresIVLHGAT 329
Cdd:COG0663    11 PQIHPSAFVAPTAVvigdvtigedvsVWPGAVLrgdvgpiriGEGSNIqdgvvlhvdpGYPLTIGDDV-----TIGHGAI 85

                          90       100
                  ....*....|....*....|....*..
gi 1907070242 330 LqeHTCVL--HSIVGWGSTVGRWARVE 354
Cdd:COG0663    86 L--HGCTIgdNVLIGMGAIVLDGAVIG 110
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 2-56 7.10e-05

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 45.02  E-value: 7.10e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907070242   2 LKAVILIGGpqKGTRfrpLSFEVPKPLFPVAGVPMIQHHIEACAQVpGMQEILLI 56
Cdd:PRK09451    6 MSVVILAAG--KGTR---MYSDLPKVLHTLAGKPMVQHVIDAANEL-GAQHVHLV 54
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
2-243 9.84e-05

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 44.11  E-value: 9.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   2 LKAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIEACAqVPGMQEILLIGFYQPDEALTQFLEAAQQEFNLPVR 81
Cdd:PRK10122    4 LKAVIPVAG--LGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIV-AAGIKEIVLVTHASKNAVENHFDTSYELESLLEQR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  82 Y-------LQEFAPLGTG---------GGLYHfrdQILAGAP----EAFFVLNADVCSD--------FPLSAML----EA 129
Cdd:PRK10122   81 VkrqllaeVQSICPPGVTimnvrqgqpLGLGH---SILCARPaigdNPFVVVLPDVVIDdasadplrYNLAAMIarfnET 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 130 HRRQ----RHPFLLLGTTANRTQSlnygcIVENP-QTHEVLHYVEK---PSTFISDIINCGIYLFSPealkplrDVFQrn 201
Cdd:PRK10122  158 GRSQvlakRMPGDLSEYSVIQTKE-----PLDREgKVSRIVEFIEKpdqPQTLDSDLMAVGRYVLSA-------DIWP-- 223

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1907070242 202 qqdgQLEES-PGSWpgaGTIRLeQDVFSALAGQGQIYVHLTDG 243
Cdd:PRK10122  224 ----ELERTePGAW---GRIQL-TDAIAELAKKQSVDAMLMTG 258
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 3-238 9.99e-05

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 43.89  E-value: 9.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   3 KAVILIGGpqKGTRFRPLSFEVPKPLFPVAGVPMIQHHIeACAQVPGMQEILLIGFYQPDEALTQFLEAAQQeFNLPVRY 82
Cdd:PRK15480    5 KGIILAGG--SGTRLYPVTMAVSKQLLPIYDKPMIYYPL-STLMLAGIRDILIISTPQDTPRFQQLLGDGSQ-WGLNLQY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  83 LQEFAPLGTGGGLYHFRDQIlaGAPEAFFVLNADVCSDFPLSAMLEAHRRQRHPFLLLGTTANRTQslNYGcIVENPQTH 162
Cdd:PRK15480   81 KVQPSPDGLAQAFIIGEEFI--GGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPE--RYG-VVEFDQNG 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907070242 163 EVLHYVEKPSTFISDIINCGIYLFSPEALKPLRDVfqRNQQDGQLEESpgswpGAGTIRLEQDVFS-ALAGQGQIYV 238
Cdd:PRK15480  156 TAISLEEKPLQPKSNYAVTGLYFYDNDVVEMAKNL--KPSARGELEIT-----DINRIYMEQGRLSvAMMGRGYAWL 225
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-191 1.15e-04

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 44.15  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   1 MLKAVILIGGpqKGTRFRPlsfEVPKPLFPVAGVPMIQHHIEACAQVPGMQEILLIGfYQPDEALTQFLEAAQQEFnlpv 80
Cdd:PRK14360    1 MLAVAILAAG--KGTRMKS---SLPKVLHPLGGKSLVERVLDSCEELKPDRRLVIVG-HQAEEVEQSLAHLPGLEF---- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  81 rYLQEfAPLGTGgglyHFRDQILA---GAPEAFFVLNADVcsdfPL------SAMLEAHRRQRHPFLLLgtTANRTQSLN 151
Cdd:PRK14360   71 -VEQQ-PQLGTG----HAVQQLLPvlkGFEGDLLVLNGDV----PLlrpetlEALLNTHRSSNADVTLL--TARLPNPKG 138

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1907070242 152 YGCIVENPQTHeVLHYVEK----PSTFISDIINCGIYLFSPEAL 191
Cdd:PRK14360  139 YGRVFCDGNNL-VEQIVEDrdctPAQRQNNRINAGIYCFNWPAL 181
PRK13627 PRK13627
carnitine operon protein CaiE; Provisional
 289-338 1.60e-04

carnitine operon protein CaiE; Provisional


Pssm-ID: 184189 [Multi-domain]  Cd Length: 196  Bit Score: 42.49  E-value: 1.60e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907070242 289 IHPTAKVAPSAVLGPNVSIGKGVTIGEGVRLRES----IVLHGATLQEhTCVLH 338
Cdd:PRK13627   13 VHPTAFVHPSAVLIGDVIVGAGVYIGPLASLRGDygrlIVQAGANLQD-GCIMH 65
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 300-349 1.67e-04

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


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 39.87  E-value: 1.67e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907070242 300 VLGPNVSIGK-----------GVTIGEGVRLRESIVLHGATLQEHtCVL--HSIVGWGSTVGR 349
Cdd:cd05787    18 VIGRNCKIGKnvvidnsyiwdDVTIEDGCTIHHSIVADGAVIGKG-CTIppGSLISFGVVIGD 79
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 4-55 3.30e-04

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


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 41.74  E-value: 3.30e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907070242   4 AVILIGGpqKGTRFrplSFEVPKPLFPVAGVPMIQHHIEACAQVPGMQEILL 55
Cdd:cd02516     3 AIILAAG--SGSRM---GADIPKQFLELGGKPVLEHTLEAFLAHPAIDEIVV 49
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 304-354 3.44e-04

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


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 39.10  E-value: 3.44e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1907070242 304 NVSIGKGVTIGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVGRWARVE 354
Cdd:cd05787    16 NSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIP 66
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 282-354 4.84e-04

Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), Ferripyochelin Binding Protein (FBP), E. coli paaY protein, and similar proteins. CAs are zinc-containing enzymes that catalyze the reversible hydration of carbon dioxide in a two-step mechanism, involving the nucleophilic attack of a zinc-bound hydroxide ion on carbon dioxide, followed by the regeneration of the active site by ionization of the zinc-bound water molecule and removal of a proton from the active site. They are ubiquitous enzymes involved in fundamental processes like photosynthesis, respiration, pH homeostasis and ion transport. There are three evolutionary distinct groups - alpha, beta and gamma carbonic anhydrases - which show no significant sequence identity or structural similarity. Gamma CAs are trimeric enzymes with left-handed parallel beta helix (LbH) structural domain.


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 40.47  E-value: 4.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 282 RIRGNVYIHPTAKVAPSAVLGPNVS-------------------------------------IGKGVTIGEGVrlresiV 324
Cdd:cd04645     1 EIDPSAFIAPNATVIGDVTLGEGSSvwfgavlrgdvnpirigertniqdgsvlhvdpgyptiIGDNVTVGHGA------V 74

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907070242 325 LHGATLQEHTCV-LHSIVGWGSTVGRWARVE 354
Cdd:cd04645    75 LHGCTIGDNCLIgMGAIILDGAVIGKGSIVA 105
LbH_gamma_CA cd00710
Gamma carbonic anhydrases (CA): Carbonic anhydrases are zinc-containing enzymes that catalyze ...
 281-347 4.99e-04

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


Pssm-ID: 100039 [Multi-domain]  Cd Length: 167  Bit Score: 40.69  E-value: 4.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 281 PRIRGNVYIHPTAKVAPSAVLGPNVSIGKGV----------TIGEGVRLRESIVLHG-----ATLQEHTCVLH------- 338
Cdd:cd00710     3 PVIDPSAYVHPTAVVIGDVIIGDNVFVGPGAsiradegtpiIIGANVNIQDGVVIHAlegysVWIGKNVSIAHgaivhgp 82

                          90
                  ....*....|....*
gi 1907070242 339 ------SIVGWGSTV 347
Cdd:cd00710    83 ayigdnCFIGFRSVV 97
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-230 5.15e-04

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


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 41.98  E-value: 5.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242   1 MLKAVILIGGpqKGTRFRPLSFEV-PKPLFPVAG-VPMIQHHIEACAQVPGMQEILLIgfyqpdealT----QFLEAAQ- 73
Cdd:COG0836     2 MIYPVILAGG--SGTRLWPLSRESyPKQFLPLLGeKSLLQQTVERLAGLVPPENILVV---------TneehRFLVAEQl 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242  74 QEFNlPVRYLQEfaPLGtggglyhfRD----------QILAGAPEA-FFVLNAD-VCSD---FpLSAMLEAHR--RQRHp 136
Cdd:COG0836    71 PELG-PANILLE--PVG--------RNtapaialaalLIAKRDPDAvLLVLPADhLIEDeeaF-REAVRAAVEaaEAGK- 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 137 FLLLGTTANR--TqslNYGCI-----VENPQTHEVLHYVEKPS-----TFISD---IINCGIYLFSPEAlkpLRDVFQRN 201
Cdd:COG0836   138 LVTFGIKPTRpeT---GYGYIeageaLGGAGAYKVKRFVEKPDletaeEYLASgnyLWNSGMFVFRAST---ILEELERH 211

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1907070242 202 QQD--GQLEESPGSWPGAGTIRLEQDVFSAL 230
Cdd:COG0836   212 APEiyAALEAAVAAAGTDLEVRLDAEAFAAL 242
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 282-348 6.75e-04

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 38.00  E-value: 6.75e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907070242 282 RIRGNVYIHPTAKVAPSAVLGPNVSIGKGVTIG---EGVRLRESIVLHGATLQEHTCVL-------HSIVGWGSTVG 348
Cdd:cd00208     2 FIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGaatGPNEKNPTIIGDNVEIGANAVIHggvkigdNAVIGAGAVVT 78
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 2-57 8.55e-04

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


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 40.18  E-value: 8.55e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907070242   2 LKAVILIGGpqKGTRFRplsfeVPKPLFPVAGVPMIQHHIEACAQVPGmqEILLIG 57
Cdd:COG0746     5 ITGVILAGG--RSRRMG-----QDKALLPLGGRPLLERVLERLRPQVD--EVVIVA 51
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 287-355 1.38e-03

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 37.23  E-value: 1.38e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907070242 287 VYIHPTAKVAPSAVLGPNVSIGKGVTIGEGVRLResivlhgaTLQEHTCVLHSIVGWGSTVGRWARVEG 355
Cdd:cd00208     1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIG--------AATGPNEKNPTIIGDNVEIGANAVIHG 61
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
286-315 1.65e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.78  E-value: 1.65e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1907070242 286 NVYIHPTAKVAPSAVLGPNVSIGKGVTIGE 315
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 298-353 1.97e-03

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 39.31  E-value: 1.97e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 298 SAVLGPNVSIGKGVTIGEGVRLRESIVLHGatlqehtcvlHSIVGWGSTVGR----WARV 353
Cdd:cd03352     1 SAKIGENVSIGPNAVIGEGVVIGDGVVIGP----------GVVIGDGVVIGDdcviHPNV 50
PRK13368 PRK13368
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 26-55 3.07e-03

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 184007  Cd Length: 238  Bit Score: 38.79  E-value: 3.07e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1907070242  26 KPLFPVAGVPMIQHHIEACAQVPGMQEILL 55
Cdd:PRK13368   19 KPLLDILGKPMIQHVYERAAQAAGVEEVYV 48
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 288-359 3.42e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 39.47  E-value: 3.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907070242 288 YIHPTAKVAPS------AVLGpNVS---IGKGVTIGEGVRLRESIVLHGATLQEHTCVLHSIVGWGSTVGRWARVEGTPN 358
Cdd:PRK05293  284 YIAENAKVKNSlvvegcVVYG-TVEhsvLFQGVQVGEGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVIIGGGKE 362


                  .
gi 1907070242 359 D 359
Cdd:PRK05293  363 V 363
LbH_unknown cd05635
Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group ...
 282-343 3.87e-03

Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group are uncharacterized bacterial proteins containing a LbH domain with multiple turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100059 [Multi-domain]  Cd Length: 101  Bit Score: 36.49  E-value: 3.87e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907070242 282 RIRGNVYIHPTAKVAPSAVLGPNVSIGKGVTIGEGVrlrESIVLHGATLQEHTCVL-HSIVG-W 343
Cdd:cd05635    25 VIEGPVYIGPGSRVKMGARIYGNTTIGPTCKIGGEV---EDSIIEGYSNKQHDGFLgHSYLGsW 85
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
280-308 5.80e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 34.23  E-value: 5.80e-03
                          10        20
                  ....*....|....*....|....*....
gi 1907070242 280 GPRIRGNVYIHPTAKVAPSAVLGPNVSIG 308
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIG 29
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 5-81 9.07e-03

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


Pssm-ID: 440824  Cd Length: 224  Bit Score: 37.42  E-value: 9.07e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907070242   5 VILIGGpqKGTRFRPlsfEVPKPLFPVAGVPMIQHHIEACAQVPGMQEILLIGfyqPDEALTQFLEAAQQ-EFNLPVR 81
Cdd:COG1211     1 IIPAAG--SGSRMGA---GIPKQFLPLGGKPVLEHTLEAFLAHPRIDEIVVVV---PPDDIEYFEELLAKyGIDKPVR 70
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 288-328 9.81e-03

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 37.81  E-value: 9.81e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907070242 288 YIHPTAKVAPSAVLGPNVSIGKG------------------------------VTIGEGVRLRESIVLH-GA 328
Cdd:PRK00892  108 VIDPSAKIGEGVSIGPNAVIGAGvvigdgvvigagavigdgvkigadcrlhanVTIYHAVRIGNRVIIHsGA 179
 
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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