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Conserved domains on  [gi|1063706262|ref|NP_001325272|]
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Glucose-1-phosphate adenylyltransferase family protein [Arabidopsis thaliana]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-234 1.28e-161

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: 451.66  E-value: 1.28e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   1 MKALILVGGFGTRLRPLTLSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEVMLNFLKDFETKLEIKITCSQE 80
Cdd:cd06425     1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKKLGIKITFSIE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  81 TEPLGTAGPLALARDkLLDGSGEPFFVLNSDVISEYPLKEMLEFHKSHGGEASIMVTKVDEPSKYGVVVMEESTGRVEKF 160
Cdd:cd06425    81 TEPLGTAGPLALARD-LLGDDDEPFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDENTGRIERF 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063706262 161 VEKPKLYVGNKINAGIYLLNPSVLDKIELRPTSIEKETFPKIAAAQGLYAMVLPGFWMDIGQPRDYITGLRLYL 234
Cdd:cd06425   160 VEKPKVFVGNKINAGIYILNPSVLDRIPLRPTSIEKEIFPKMASEGQLYAYELPGFWMDIGQPKDFLKGMSLYL 233
LbetaH super family cl00160
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 256-335 1.03e-29

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: 109.16  E-value: 1.03e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 256 LVDETATIGEGCLIGPDVAIGPGCIVESGVRLSRCTVMRGVRIKKHACISSSIIGWHSTVGQWARIENMTILGEDVHVSD 335
Cdd:cd05824     1 LIDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLENVTVLGDDVTIKD 80
 
Name Accession Description Interval E-value
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-234 1.28e-161

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: 451.66  E-value: 1.28e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   1 MKALILVGGFGTRLRPLTLSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEVMLNFLKDFETKLEIKITCSQE 80
Cdd:cd06425     1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKKLGIKITFSIE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  81 TEPLGTAGPLALARDkLLDGSGEPFFVLNSDVISEYPLKEMLEFHKSHGGEASIMVTKVDEPSKYGVVVMEESTGRVEKF 160
Cdd:cd06425    81 TEPLGTAGPLALARD-LLGDDDEPFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDENTGRIERF 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063706262 161 VEKPKLYVGNKINAGIYLLNPSVLDKIELRPTSIEKETFPKIAAAQGLYAMVLPGFWMDIGQPRDYITGLRLYL 234
Cdd:cd06425   160 VEKPKVFVGNKINAGIYILNPSVLDRIPLRPTSIEKEIFPKMASEGQLYAYELPGFWMDIGQPKDFLKGMSLYL 233
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-245 2.06e-87

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: 263.55  E-value: 2.06e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   2 KALILVGGFGTRLRPLTLSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEVMLNFLKDFEtKLEIKITCSQET 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGS-RFGVRITYVDEG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  82 EPLGTAGPLALARDKLLDgsgEPFFVLNSDVISEYPLKEMLEFHKSHGGEASIMVTKVDEPSKYGVVVMEEStGRVEKFV 161
Cdd:COG1208    80 EPLGTGGALKRALPLLGD---EPFLVLNGDILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGD-GRVTRFV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 162 EKPKLYVGNKINAGIYLLNPSVLDKIELRPT-SIEkETFPKIAAAQGLYAMVLPGFWMDIGQPRDYITGLRLYLDslrKK 240
Cdd:COG1208   156 EKPEEPPSNLINAGIYVLEPEIFDYIPEGEPfDLE-DLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLS---GK 231


                  ....*
gi 1063706262 241 SPAKL 245
Cdd:COG1208   232 APVVI 236
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-234 6.99e-76

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: 234.07  E-value: 6.99e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   2 KALILVGGFGTRLRPLTLSFPKPLVDFANK-PMILHQIEALKAVGVDEVVLAINYQPEVMLNFLKDFETKLEIKITCSQE 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  81 TEPLGTAGPLALARDKLLDGSGePFFVLNSDVISEYPLKEMLEFHKSHGGE--ASIMVTKVDEPSKYGVVVMEEsTGRVE 158
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKS-DVLVLGGDHIYRMDLEQAVKFHIEKAADatVTFGIVPVEPPTGYGVVEFDD-NGRVI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 159 KFVEKPKLYV-GNKINAGIYLLNPSVLDKI-----EL--RPTSIEKETFPKIAAAQGLYAMVLPGF-WMDIGQPRDYITG 229
Cdd:pfam00483 159 RFVEKPKLPKaSNYASMGIYIFNSGVLDFLakyleELkrGEDEITDILPKALEDGKLAYAFIFKGYaWLDVGTWDSLWEA 238


                  ....*
gi 1063706262 230 LRLYL 234
Cdd:pfam00483 239 NLFLL 243
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-310 3.82e-65

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: 211.30  E-value: 3.82e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   1 MKALILVGGFGTRLRPLTLSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEVMLNFLKDfETKLEIKITCSQE 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGD-GSRGGVPIEYVVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  81 TEPLGTAGPLALARDKLLDgsgePFFVLNSDVISEYP-LKEMLEfhkshGGEASIMVTKVDEPSKYGVVVMEEstGRVEK 159
Cdd:TIGR03992  80 EEQLGTADALGSAKEYVDD----EFLVLNGDVLLDSDlLERLIR-----AEAPAIAVVEVDDPSDYGVVETDG--GRVTG 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 160 FVEKPKLYVGNKINAGIYLLNPSVLDKIELRPTSIEKE-----TFPKIAAAQGLYAMVLPGFWMDIGQPRDYITGLRLYL 234
Cdd:TIGR03992 149 IVEKPENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEyeltdALQLLIDEGKVKAVELDGFWLDVGRPWDLLDANEALL 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 235 DSLRKKSPAKLTSGPHIVGNVLVDETAT------------IGEGCLIGPD------VAIGPGCIVESGVRLSRCTVMRGV 296
Cdd:TIGR03992 229 DNLEPRIEGTVEENVTIKGPVVIGEGAVirsgtyiegpvyIGKNCDIGPNayirpyTVIGNNVHIGNAVEIKNSIIMEGT 308

                         330
                  ....*....|....
gi 1063706262 297 RIKKHACISSSIIG 310
Cdd:TIGR03992 309 KIPHLSYVGDSVIG 322
LbH_M1P_guanylylT_C cd05824
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 256-335 1.03e-29

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: 109.16  E-value: 1.03e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 256 LVDETATIGEGCLIGPDVAIGPGCIVESGVRLSRCTVMRGVRIKKHACISSSIIGWHSTVGQWARIENMTILGEDVHVSD 335
Cdd:cd05824     1 LIDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLENVTVLGDDVTIKD 80
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-337 2.97e-26

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 108.77  E-value: 2.97e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   3 ALILVGGFGTRLRPltlSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEvmlnflkDFETKLEIKITCSQETE 82
Cdd:PRK14354    5 AIILAAGKGTRMKS---KLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAE-------EVKEVLGDRSEFALQEE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  83 PLGTAGPLALARDKLLDGSGEpFFVLNSDV--ISEYPLKEMLEFHKSHGGEASIMVTKVDEPSKYGVVVMEEStGRVEKF 160
Cdd:PRK14354   75 QLGTGHAVMQAEEFLADKEGT-TLVICGDTplITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNEN-GEVEKI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 161 VE-----KPKLYVgNKINAGIYLLNPSVLdkielrptsieKETFPKI--AAAQGLY-----------------AMVLPGF 216
Cdd:PRK14354  153 VEqkdatEEEKQI-KEINTGTYCFDNKAL-----------FEALKKIsnDNAQGEYyltdvieilknegekvgAYQTEDF 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 217 wmdigqprDYITGL--RLYL----DSLRKKSPAKltsgpHIVGNV-LVD-ETATIGEGCLIGPDVAIGPG---------- 278
Cdd:PRK14354  221 --------EESLGVndRVALaeaeKVMRRRINEK-----HMVNGVtIIDpESTYIDADVEIGSDTVIEPGvvikgntvig 287

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063706262 279 --CIVESGVRLSRCTVMRGVRIkKHACISSSIIGWHSTVGQWARIENMTILGEDVHVSD--EI 337
Cdd:PRK14354  288 edCVIGPGSRIVDSTIGDGVTI-TNSVIEESKVGDNVTVGPFAHLRPGSVIGEEVKIGNfvEI 349
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 254-340 3.75e-07

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 51.17  E-value: 3.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 254 NVLVDETATIGEGCLIGPDVAIGPGCIVESGVRL-------SRCTVMRGVRIKKHaCI--SSSIIG-------WHSTvGQ 317
Cdd:COG1044   114 GVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIgddcvlhPNVTIYERCVIGDR-VIihSGAVIGadgfgfaPDED-GG 191

                          90       100
                  ....*....|....*....|....*
gi 1063706262 318 WARIENM--TILGEDVhvsdEIYSN 340
Cdd:COG1044   192 WVKIPQLgrVVIGDDV----EIGAN 212
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 260-330 2.53e-06

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


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 48.03  E-value: 2.53e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063706262 260 TATIGEGCLIGPDVAIGPGCIVESGVRLSrctvmRGVRIKKHACISSsiigwHSTVGQWARIENMTILGED 330
Cdd:TIGR01852   4 TAIIEPGAEIGENVEIGPFCIVGPGVKIG-----DGVELKSHVVILG-----HTTIGEGTRIFPGAVIGGV 64
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
256-304 1.59e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 45.86  E-value: 1.59e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063706262 256 LVDETATIGEG------CLIGPDVAIGPGCIVESGVRLSRCTVM-RGVRIKKHACI 304
Cdd:PRK05289   10 IVEPGAKIGENveigpfCVIGPNVVIGDGTVIGSHVVIDGHTTIgKNNRIFPFASI 65
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
261-287 2.23e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.01  E-value: 2.23e-03
                          10        20
                  ....*....|....*....|....*..
gi 1063706262 261 ATIGEGCLIGPDVAIGPGCIVESGVRL 287
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVII 28
 
Name Accession Description Interval E-value
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-234 1.28e-161

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: 451.66  E-value: 1.28e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   1 MKALILVGGFGTRLRPLTLSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEVMLNFLKDFETKLEIKITCSQE 80
Cdd:cd06425     1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKKLGIKITFSIE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  81 TEPLGTAGPLALARDkLLDGSGEPFFVLNSDVISEYPLKEMLEFHKSHGGEASIMVTKVDEPSKYGVVVMEESTGRVEKF 160
Cdd:cd06425    81 TEPLGTAGPLALARD-LLGDDDEPFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDENTGRIERF 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063706262 161 VEKPKLYVGNKINAGIYLLNPSVLDKIELRPTSIEKETFPKIAAAQGLYAMVLPGFWMDIGQPRDYITGLRLYL 234
Cdd:cd06425   160 VEKPKVFVGNKINAGIYILNPSVLDRIPLRPTSIEKEIFPKMASEGQLYAYELPGFWMDIGQPKDFLKGMSLYL 233
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-245 2.06e-87

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: 263.55  E-value: 2.06e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   2 KALILVGGFGTRLRPLTLSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEVMLNFLKDFEtKLEIKITCSQET 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGS-RFGVRITYVDEG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  82 EPLGTAGPLALARDKLLDgsgEPFFVLNSDVISEYPLKEMLEFHKSHGGEASIMVTKVDEPSKYGVVVMEEStGRVEKFV 161
Cdd:COG1208    80 EPLGTGGALKRALPLLGD---EPFLVLNGDILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGD-GRVTRFV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 162 EKPKLYVGNKINAGIYLLNPSVLDKIELRPT-SIEkETFPKIAAAQGLYAMVLPGFWMDIGQPRDYITGLRLYLDslrKK 240
Cdd:COG1208   156 EKPEEPPSNLINAGIYVLEPEIFDYIPEGEPfDLE-DLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLS---GK 231


                  ....*
gi 1063706262 241 SPAKL 245
Cdd:COG1208   232 APVVI 236
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-221 8.35e-82

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: 248.26  E-value: 8.35e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   3 ALILVGGFGTRLRPLTLSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEVMLNFLKDfETKLEIKITCSQETE 82
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGD-GSKFGVNIEYVVQEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  83 PLGTAGPLALARDKLLDgsgEPFFVLNSDVISEYPLKEMLEFHKSHGGEASIMVTKVDEPSKYGVVVMEEStGRVEKFVE 162
Cdd:cd04181    80 PLGTAGAVRNAEDFLGD---DDFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDD-GRVTRFVE 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063706262 163 KPKLYVGNKINAGIYLLNPSVLD---KIELRPTSIEKETFPKIAAAQGLYAMVLPGFWMDIG 221
Cdd:cd04181   156 KPTLPESNLANAGIYIFEPEILDyipEILPRGEDELTDAIPLLIEEGKVYGYPVDGYWLDIG 217
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-234 6.99e-76

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: 234.07  E-value: 6.99e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   2 KALILVGGFGTRLRPLTLSFPKPLVDFANK-PMILHQIEALKAVGVDEVVLAINYQPEVMLNFLKDFETKLEIKITCSQE 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  81 TEPLGTAGPLALARDKLLDGSGePFFVLNSDVISEYPLKEMLEFHKSHGGE--ASIMVTKVDEPSKYGVVVMEEsTGRVE 158
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKS-DVLVLGGDHIYRMDLEQAVKFHIEKAADatVTFGIVPVEPPTGYGVVEFDD-NGRVI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 159 KFVEKPKLYV-GNKINAGIYLLNPSVLDKI-----EL--RPTSIEKETFPKIAAAQGLYAMVLPGF-WMDIGQPRDYITG 229
Cdd:pfam00483 159 RFVEKPKLPKaSNYASMGIYIFNSGVLDFLakyleELkrGEDEITDILPKALEDGKLAYAFIFKGYaWLDVGTWDSLWEA 238


                  ....*
gi 1063706262 230 LRLYL 234
Cdd:pfam00483 239 NLFLL 243
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-310 3.82e-65

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: 211.30  E-value: 3.82e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   1 MKALILVGGFGTRLRPLTLSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEVMLNFLKDfETKLEIKITCSQE 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGD-GSRGGVPIEYVVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  81 TEPLGTAGPLALARDKLLDgsgePFFVLNSDVISEYP-LKEMLEfhkshGGEASIMVTKVDEPSKYGVVVMEEstGRVEK 159
Cdd:TIGR03992  80 EEQLGTADALGSAKEYVDD----EFLVLNGDVLLDSDlLERLIR-----AEAPAIAVVEVDDPSDYGVVETDG--GRVTG 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 160 FVEKPKLYVGNKINAGIYLLNPSVLDKIELRPTSIEKE-----TFPKIAAAQGLYAMVLPGFWMDIGQPRDYITGLRLYL 234
Cdd:TIGR03992 149 IVEKPENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEyeltdALQLLIDEGKVKAVELDGFWLDVGRPWDLLDANEALL 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 235 DSLRKKSPAKLTSGPHIVGNVLVDETAT------------IGEGCLIGPD------VAIGPGCIVESGVRLSRCTVMRGV 296
Cdd:TIGR03992 229 DNLEPRIEGTVEENVTIKGPVVIGEGAVirsgtyiegpvyIGKNCDIGPNayirpyTVIGNNVHIGNAVEIKNSIIMEGT 308

                         330
                  ....*....|....
gi 1063706262 297 RIKKHACISSSIIG 310
Cdd:TIGR03992 309 KIPHLSYVGDSVIG 322
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 3-233 8.59e-62

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: 198.63  E-value: 8.59e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   3 ALILVGG--FGTRLRPLTLSFPKPLVDFANKPMILHQIEALKAV-GVDEVVLAINYQPEVMLNFLKDFETKLEIKITCSQ 79
Cdd:cd06428     1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVpDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  80 ETEPLGTAGPLALARDKLLDGSGEPFFVLNSDVISEYPLKEMLEFHKSHGGEASIMVTKV--DEPSKYGVVVMEESTGRV 157
Cdd:cd06428    81 EYKPLGTAGGLYHFRDQILAGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEAsrEQASNYGCIVEDPSTGEV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 158 EKFVEKPKLYVGNKINAGIYLLNPSVLDKIEL---------------------RPTSIEKETFPKIAAAQGLYAMVLPGF 216
Cdd:cd06428   161 LHYVEKPETFVSDLINCGVYLFSPEIFDTIKKafqsrqqeaqlgddnnregraEVIRLEQDVLTPLAGSGKLYVYKTDDF 240

                         250
                  ....*....|....*..
gi 1063706262 217 WMDIGQPRDYITGLRLY 233
Cdd:cd06428   241 WSQIKTAGSAIYANRLY 257
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 3-226 2.48e-54

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: 178.13  E-value: 2.48e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   3 ALILVGGFGTRLRPLTLSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEVMLNFLKDfETKLEIKITCSQETE 82
Cdd:cd06915     1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGD-GYRGGIRIYYVIEPE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  83 PLGTAGPLALARDKLLDgsgEPFFVLNSDVISEYPLKEMLEFHKSHGGEASIMVTKVDEPSKYGVVVMEEStGRVEKFVE 162
Cdd:cd06915    80 PLGTGGAIKNALPKLPE---DQFLVLNGDTYFDVDLLALLAALRASGADATMALRRVPDASRYGNVTVDGD-GRVIAFVE 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063706262 163 KPKLYVGNKINAGIYLLNPSVLDKIELRPTSIEKETFPKIAAAQGLYAMVLPGFWMDIGQPRDY 226
Cdd:cd06915   156 KGPGAAPGLINGGVYLLRKEILAEIPADAFSLEADVLPALVKRGRLYGFEVDGYFIDIGIPEDY 219
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 3-226 6.85e-53

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


Pssm-ID: 133048 [Multi-domain]  Cd Length: 220  Bit Score: 174.24  E-value: 6.85e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   3 ALILVGGFGTRLRPLTLSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEVMLNFLKDfETKLEIKITCSQETE 82
Cdd:cd06426     1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGD-GSKFGVNISYVREDK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  83 PLGTAGPLALARDKLldgsGEPFFVLNSDVISEYPLKEMLEFHKSHGGEASIMVTKVDEPSKYGVVVMEEstGRVEKFVE 162
Cdd:cd06426    80 PLGTAGALSLLPEKP----TDPFLVMNGDILTNLNYEHLLDFHKENNADATVCVREYEVQVPYGVVETEG--GRITSIEE 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063706262 163 KPKLYVgnKINAGIYLLNPSVLDKIELR-----PTSIEKETfpkiaaAQGLYAMVLP--GFWMDIGQPRDY 226
Cdd:cd06426   154 KPTHSF--LVNAGIYVLEPEVLDLIPKNeffdmPDLIEKLI------KEGKKVGVFPihEYWLDIGRPEDY 216
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 1-236 7.59e-50

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


Pssm-ID: 133032 [Multi-domain]  Cd Length: 236  Bit Score: 166.98  E-value: 7.59e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   1 MKALILVGGFGTRLRPLTLSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEVMLNFLKDfETKLEIKITCSQE 80
Cdd:cd04189     1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGD-GSRFGVRITYILQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  81 TEPLGTAGPLALARDKLldgSGEPFFVLNSDVISEYPLKEMLEFHKSHGGEASIMVTKVDEPSKYGVVVMEEstGRVEKF 160
Cdd:cd04189    80 EEPLGLAHAVLAARDFL---GDEPFVVYLGDNLIQEGISPLVRDFLEEDADASILLAEVEDPRRFGVAVVDD--GRIVRL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 161 VEKPKLYVGNKINAGIYLLNPSVLDKI-ELRPTS---IEketfpkIA-AAQGLY-------AMVLPGFWMDIGQPRDYIT 228
Cdd:cd04189   155 VEKPKEPPSNLALVGVYAFTPAIFDAIsRLKPSWrgeLE------ITdAIQWLIdrgrrvgYSIVTGWWKDTGTPEDLLE 228


                  ....*...
gi 1063706262 229 GLRLYLDS 236
Cdd:cd04189   229 ANRLLLDK 236
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-226 8.08e-48

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: 161.20  E-value: 8.08e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   2 KALILVGGFGTRLRPLTLSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEVMLNFLKDFETKLEIKItcSQE- 80
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGDSRFGLRITI--SDEp 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  81 TEPLGTAGPLALARDKLldgSGEPFFVLNSDVISEYPLKEMLEFHKSHGGEASIMVTKVDEPSK--YGVVVMEEsTGRVE 158
Cdd:cd06422    79 DELLETGGGIKKALPLL---GDEPFLVVNGDILWDGDLAPLLLLHAWRMDALLLLLPLVRNPGHngVGDFSLDA-DGRLR 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063706262 159 KFVEKpklYVGNKINAGIYLLNPSVLDKIELRPTSIeKETFPKIAAAQGLYAMVLPGFWMDIGQPRDY 226
Cdd:cd06422   155 RGGGG---AVAPFTFTGIQILSPELFAGIPPGKFSL-NPLWDRAIAAGRLFGLVYDGLWFDVGTPERL 218
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 2-338 6.99e-45

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: 157.56  E-value: 6.99e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   2 KALILVGGFGTRLRPLTLSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQ-PEVMLNFLKDFEtKLEIKITCSQE 80
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVtGEEIKEIVGEGE-RFGAKITYIVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  81 TEPLGTAGPLALARDKLLDgsgEPFFVLNSDVISEYPLKEMLE-FHKSHgGEASIMVTKVDEPSKYGVVVMEEStGRVEK 159
Cdd:TIGR01208  80 GEPLGLAHAVYTARDFLGD---DDFVVYLGDNLIQDGISRFVKsFEEKD-YDALILLTKVRDPTAFGVAVLEDG-KRILK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 160 FVEKPKLYVGNKINAGIYLLNPSVLDKIELRPTSIEKEtFPKIAAAQGL----YAMV---LPGFWMDIGQPRDYITGLRL 232
Cdd:TIGR01208 155 LVEKPKEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGE-LEITDAIQWLiekgYKVGgskVTGWWKDTGKPEDLLDANRL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 233 YLDSLrKKSPAKLTSGPHIVGNVLVDETATIGEGCLIGPdVAIGPGCIVESGVRLSRCTVMRGVRIKKHACISSSIIGWH 312
Cdd:TIGR01208 234 ILDEV-EREVQGVDDESKIRGRVVVGEGAKIVNSVIRGP-AVIGEDCIIENSYIGPYTSIGEGVVIRDAEVEHSIVLDES 311

                         330       340
                  ....*....|....*....|....*...
gi 1063706262 313 STVGQWARIENmTILGEDVHV--SDEIY 338
Cdd:TIGR01208 312 VIEGVQARIVD-SVIGKKVRIkgNRRRP 338
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-191 1.22e-36

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 134.06  E-value: 1.22e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   1 MKALILVGGFGTRLRPLTLSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAI--NYQPEVMlNFLKDFEtKLEIKITCS 78
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIIStpEDGPQFE-RLLGDGS-QLGIKISYA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  79 QETEPLGTAGPLALARDKLldgSGEPFF-VLNSDVISEYPLKEMLEFHKSHGGEASIMVTKVDEPSKYGVVVMEEStGRV 157
Cdd:COG1209    79 VQPEPLGLAHAFIIAEDFI---GGDPVAlVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDED-GRV 154

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1063706262 158 EKFVEKPKLYVGNKINAGIYLLNPSVLDKIE-LRP 191
Cdd:COG1209   155 VSLEEKPKEPKSNLAVTGLYFYDNDVVEIAKnLKP 189
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 3-243 1.89e-33

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: 124.61  E-value: 1.89e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   3 ALILVGGFGTRLRPLTLSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEVMLNFLKDFET------------K 70
Cdd:cd02524     1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYKGHVIKEYFLNYFLhnsdvtidlgtnR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  71 LEI--------KITCSQETEPLGTAGPLALARDKLldGSGEPFFVLNSDVISEYPLKEMLEFHKSHGGEAsiMVTKVDEP 142
Cdd:cd02524    81 IELhnsdiedwKVTLVDTGLNTMTGGRLKRVRRYL--GDDETFMLTYGDGVSDVNINALIEFHRSHGKLA--TVTAVHPP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 143 SKYGVVVMEEStGRVEKFVEKPKLyVGNKINAGIYLLNPSVLDKIELRPTSIEKETFPKIAAAQGLYAMVLPGFW--MDi 220
Cdd:cd02524   157 GRFGELDLDDD-GQVTSFTEKPQG-DGGWINGGFFVLEPEVFDYIDGDDTVFEREPLERLAKDGELMAYKHTGFWqcMD- 233

                         250       260
                  ....*....|....*....|...
gi 1063706262 221 gQPRDYitglrLYLDSLRKKSPA 243
Cdd:cd02524   234 -TLRDK-----QTLEELWNSGKA 250
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 1-333 4.22e-31

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 122.44  E-value: 4.22e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   1 MKALILVGGFGTRLRPltlSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEVMLNFLKDFEtkleikITCSQE 80
Cdd:COG1207     3 LAVVILAAGKGTRMKS---KLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALADLD------VEFVLQ 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  81 TEPLGTAGPLALARDkLLDGSGEPFFVLNSDV--ISEYPLKEMLEFHKSHGGEASIMVTKVDEPSKYGVVVMEEsTGRVE 158
Cdd:COG1207    74 EEQLGTGHAVQQALP-ALPGDDGTVLVLYGDVplIRAETLKALLAAHRAAGAAATVLTAELDDPTGYGRIVRDE-DGRVL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 159 KFVE---------KPKlyvgnKINAGIYLLNPSVLDKI--ELRPTSIEKE-----TFpKIAAAQGLYAMVLpgfwmdigQ 222
Cdd:COG1207   152 RIVEekdateeqrAIR-----EINTGIYAFDAAALREAlpKLSNDNAQGEyyltdVI-AIARADGLKVAAV--------Q 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 223 PRDY--ITGL--RLYL----DSLRKKSPAKL-TSGPHIV--GNVLVDETATIGEGCLIGP------DVAIGPGCIVESGV 285
Cdd:COG1207   218 PEDPweVLGVndRVQLaeaeRILQRRIAERLmRAGVTIIdpATTYIDGDVEIGRDVVIDPnvilegKTVIGEGVVIGPNC 297

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1063706262 286 RLSRCTVMRGVRIkKHACISSSIIGWHSTVGQWARIENMTILGEDVHV 333
Cdd:COG1207   298 TLKDSTIGDGVVI-KYSVIEDAVVGAGATVGPFARLRPGTVLGEGVKI 344
LbH_M1P_guanylylT_C cd05824
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 256-335 1.03e-29

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: 109.16  E-value: 1.03e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 256 LVDETATIGEGCLIGPDVAIGPGCIVESGVRLSRCTVMRGVRIKKHACISSSIIGWHSTVGQWARIENMTILGEDVHVSD 335
Cdd:cd05824     1 LIDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLENVTVLGDDVTIKD 80
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 3-226 3.96e-28

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


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 109.63  E-value: 3.96e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   3 ALILVGGFGTRLRPLTLSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEVMLNFLKDFetkLEIKITCSQETE 82
Cdd:cd02523     1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKY---PNIKFVYNPDYA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  83 PLGTAGPLALARDKLldgsGEPFFVLNSDVISEyplKEMLEFHKSHGGEASIMVTKVDEPSKYGVVVMEESTGRVEKFVE 162
Cdd:cd02523    78 ETNNIYSLYLARDFL----DEDFLLLEGDVVFD---PSILERLLSSPADNAILVDKKTKEWEDEYVKDLDDAGVLLGIIS 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063706262 163 KPKlyVGNKINA---GIYLLNPSVLDKI-----ELRPTSIEKETFP----KIAAAQGLYAMVLP-GFWMDIGQPRDY 226
Cdd:cd02523   151 KAK--NLEEIQGeyvGISKFSPEDADRLaealeELIEAGRVNLYYEdalqRLISEEGVKVKDISdGFWYEIDDLEDL 225
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-233 2.88e-27

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 107.63  E-value: 2.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   2 KALILVGGFGTRLRPLTLSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEVmlnfLKDFETKLEIKITC---- 77
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAEL----IEEALARPGPDVTFvynp 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  78 -SQETeplGTAGPLALARDKLldgsGEPFFVLNSDVI-SEYPLKEMLEfhkshgGEASIMV---TKVDEPSKYGVVVMEE 152
Cdd:COG1213    77 dYDET---NNIYSLWLAREAL----DEDFLLLNGDVVfDPAILKRLLA------SDGDIVLlvdRKWEKPLDEEVKVRVD 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 153 STGRVEKFVEKPKLYVGNKINAGIYLLNPSVLDKIELRPTSIEKETFPKI--------AAAQGLYAMVLP---GFWMDIG 221
Cdd:COG1213   144 EDGRIVEIGKKLPPEEADGEYIGIFKFSAEGAAALREALEALIDEGGPNLyyedalqeLIDEGGPVKAVDiggLPWVEID 223

                         250
                  ....*....|..
gi 1063706262 222 QPRDYITGLRLY 233
Cdd:COG1213   224 TPEDLERAEELF 235
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-337 2.97e-26

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 108.77  E-value: 2.97e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   3 ALILVGGFGTRLRPltlSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEvmlnflkDFETKLEIKITCSQETE 82
Cdd:PRK14354    5 AIILAAGKGTRMKS---KLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAE-------EVKEVLGDRSEFALQEE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  83 PLGTAGPLALARDKLLDGSGEpFFVLNSDV--ISEYPLKEMLEFHKSHGGEASIMVTKVDEPSKYGVVVMEEStGRVEKF 160
Cdd:PRK14354   75 QLGTGHAVMQAEEFLADKEGT-TLVICGDTplITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNEN-GEVEKI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 161 VE-----KPKLYVgNKINAGIYLLNPSVLdkielrptsieKETFPKI--AAAQGLY-----------------AMVLPGF 216
Cdd:PRK14354  153 VEqkdatEEEKQI-KEINTGTYCFDNKAL-----------FEALKKIsnDNAQGEYyltdvieilknegekvgAYQTEDF 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 217 wmdigqprDYITGL--RLYL----DSLRKKSPAKltsgpHIVGNV-LVD-ETATIGEGCLIGPDVAIGPG---------- 278
Cdd:PRK14354  221 --------EESLGVndRVALaeaeKVMRRRINEK-----HMVNGVtIIDpESTYIDADVEIGSDTVIEPGvvikgntvig 287

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063706262 279 --CIVESGVRLSRCTVMRGVRIkKHACISSSIIGWHSTVGQWARIENMTILGEDVHVSD--EI 337
Cdd:PRK14354  288 edCVIGPGSRIVDSTIGDGVTI-TNSVIEESKVGDNVTVGPFAHLRPGSVIGEEVKIGNfvEI 349
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-333 6.64e-26

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 107.91  E-value: 6.64e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   3 ALILVGGFGTRLRPltlSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEVMLNFLKDfetklEIKITCSQETE 82
Cdd:PRK14355    6 AIILAAGKGTRMKS---DLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAG-----DGDVSFALQEE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  83 PLGTAGPLALARDKLLDGSGEpFFVLNSDV--ISEYPLKEMLEFHKSHGGEASIMVTKVDEPSKYGVVVmEESTGRVEKF 160
Cdd:PRK14355   78 QLGTGHAVACAAPALDGFSGT-VLILCGDVplLRAETLQGMLAAHRATGAAVTVLTARLENPFGYGRIV-RDADGRVLRI 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 161 VEK----PKLYVGNKINAGIYLLNPSVL-DKI-ELRPTSIEKETF----PKIAAAQGLYAMVLPgfwmdIGQPRDyITGL 230
Cdd:PRK14355  156 VEEkdatPEERSIREVNSGIYCVEAAFLfDAIgRLGNDNAQGEYYltdiVAMAAAEGLRCLAFP-----VADPDE-IMGV 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 231 --RLYLDSLRKKSPAKLTSGPHIVGNVLVD-ETATIGEGCLIGPD------------VAIGPGCIVESGVRLSRCTVMRG 295
Cdd:PRK14355  230 ndRAQLAEAARVLRRRINRELMLAGVTLIDpETTYIDRGVVIGRDttiypgvcisgdTRIGEGCTIEQGVVIKGCRIGDD 309

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1063706262 296 VRIKKHACISSSIIGWHSTVGQWARIENMTILGEDVHV 333
Cdd:PRK14355  310 VTVKAGSVLEDSVVGDDVAIGPMAHLRPGTELSAHVKI 347
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-227 8.63e-26

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: 104.15  E-value: 8.63e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   1 MKALILVGGFGTRLRPLTLSFPK---PLVDfanKPMILHQIEALKAVGVDEVVL-------AI------NYQPEVMLNF- 63
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKemlPIVD---KPVIQYIVEEAVAAGIEDIIIvtgrgkrAIedhfdrSYELEETLEKk 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  64 ----LKDFETKLEIKITCS--QETEPLGTAGPLALARDKLLDgsgEPFFVLNSDVI--SEYP-LKEMLEFHKSHGGeASI 134
Cdd:cd02541    78 gktdLLEEVRIISDLANIHyvRQKEPLGLGHAVLCAKPFIGD---EPFAVLLGDDLidSKEPcLKQLIEAYEKTGA-SVI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 135 MVTKVDEP--SKYGVVVMEESTG---RVEKFVEKPKLYVG--NKINAGIYLLNPSVLDKIELRPTSIEKE-----TFPKI 202
Cdd:cd02541   154 AVEEVPPEdvSKYGIVKGEKIDGdvfKVKGLVEKPKPEEApsNLAIVGRYVLTPDIFDILENTKPGKGGEiqltdAIAKL 233

                         250       260
                  ....*....|....*....|....*
gi 1063706262 203 AAAQGLYAMVLPGFWMDIGQPRDYI 227
Cdd:cd02541   234 LEEEPVYAYVFEGKRYDCGNKLGYL 258
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 3-345 3.20e-25

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 104.77  E-value: 3.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   3 ALILVGGFGTRLRPLTLSFPKP---------LVDFA--NkpmilhqiealkAV--GVDEVVLAINYQPEVMLNFLK---- 65
Cdd:COG0448     4 AIILAGGRGSRLGPLTKDRAKPavpfggkyrIIDFPlsN------------CVnsGIRRVGVLTQYKSHSLNDHIGsgkp 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  66 -DFETK---LEIKITCSQETEP---LGTAgplalarD------KLLDGSGEPFF-VLNSDVISEYPLKEMLEFHKSHGGE 131
Cdd:COG0448    72 wDLDRKrggVFILPPYQQREGEdwyQGTA-------DavyqnlDFIERSDPDYVlILSGDHIYKMDYRQMLDFHIESGAD 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 132 ASIMVTKVD--EPSKYGVVVMEEsTGRVEKFVEKPKLYVGNKINAGIYLLNPSVLDKI--ELRPTSIE---KETFPKIAA 204
Cdd:COG0448   145 ITVACIEVPreEASRFGVMEVDE-DGRITEFEEKPKDPKSALASMGIYVFNKDVLIELleEDAPNSSHdfgKDIIPRLLD 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 205 AQGLYAMVLPGFWMDIGQPRDY----------ITGLRLYLDS--LRKKS----PAKLTSGPHIVgNVLvdetatIGEGCL 268
Cdd:COG0448   224 RGKVYAYEFDGYWRDVGTIDSYyeanmdlldpEPEFNLYDPEwpIYTKQkdlpPAKFVRGGKVK-NSL------VSNGCI 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 269 IGPDVA---IGPGCIVESGVRLSRCTVMRGVRIKKHACISSSIIGWHSTVGqwariENMTILGEDVHVSDEIYSNGGVVL 345
Cdd:COG0448   297 ISGTVEnsvLFRGVRVESGAVVENSVIMPGVVIGEGAVIENAIIDKNVVIP-----PGVVIGEDPEEDRKRFTVSSGIVV 371
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 3-186 5.85e-24

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: 98.36  E-value: 5.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   3 ALILVGGFGTRLRPltlSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEVMLNFLKDFetkleiKITCSQETE 82
Cdd:cd02540     1 AVILAAGKGTRMKS---DLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALANP------NVEFVLQEE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  83 PLGTAGPLALARDKLLDGSGEpFFVLNSDV--ISEYPLKEMLEFHKSHGGEASIMVTKVDEPSKYGVVVMEEStGRVEKF 160
Cdd:cd02540    72 QLGTGHAVKQALPALKDFEGD-VLVLYGDVplITPETLQRLLEAHREAGADVTVLTAELEDPTGYGRIIRDGN-GKVLRI 149

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1063706262 161 VE---------KPKLyvgnkINAGIYLLNPSVLDK 186
Cdd:cd02540   150 VEekdateeekAIRE-----VNAGIYAFDAEFLFE 179
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 1-184 2.09e-22

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: 93.86  E-value: 2.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   1 MKALILVGGFGTRLRPLTLSFPKPLVDFANKPMILHQIEALKAVGVDEV-VLAINYQPEVMLNFLKDFETKLEIKIT--- 76
Cdd:cd02507     1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVfVVCCEHSQAIIEHLLKSKWSSLSSKMIvdv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  77 -CSQETEPLGTAgplalarDKLLDGSGE---PFFVLNSDVISEYPLKEMLE----FHKSHggEASIMVTKVDEPS----- 143
Cdd:cd02507    81 iTSDLCESAGDA-------LRLRDIRGLirsDFLLLSCDLVSNIPLSELLEerrkKDKNA--IATLTVLLASPPVsteqs 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063706262 144 ----KYGVVVMEESTGR---------VEKFVEK----------PKLYVGNK-INAGIYLLNPSVL 184
Cdd:cd02507   152 kkteEEDVIAVDSKTQRllllhyeedLDEDLELiirksllskhPNVTIRTDlLDCHIYICSPDVL 216
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 256-335 8.56e-20

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: 82.67  E-value: 8.56e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 256 LVDETATIGEGCLIGPDVaIGPGCIVESGVRLSRCTVMRGVRIKKHACISSSIIGWHSTVGQWARIENMTILGEDVHVSD 335
Cdd:cd03356     1 LIGESTVIGENAIIKNSV-IGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVNLCIIGDDVVVED 79
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-227 9.00e-20

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 88.17  E-value: 9.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   2 KALILVGGFGTRLRPLTLSFPK---PLVDfanKPMILHQIEALKAVGVDEVVL-------AI----NYQPEvmlnflkdF 67
Cdd:COG1210     5 KAVIPVAGLGTRFLPATKAIPKemlPIVD---KPLIQYVVEEAVAAGIEEIIFvtgrgkrAIedhfDRSYE--------L 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  68 ETKLEIK---------------ITCS---QEtEPLGTAGPLALARDKLLDgsgEPFFVLNSDVI--SEYP-LKEMLEFHK 126
Cdd:COG1210    74 EATLEAKgkeelleevrsisplANIHyvrQK-EPLGLGHAVLCARPFVGD---EPFAVLLGDDLidSEKPcLKQMIEVYE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 127 SHGGeASIMVTKV--DEPSKYGVVVMEESTG---RVEKFVEKPKlyVG----NKINAGIYLLNPSVLDKIElrptsiekE 197
Cdd:COG1210   150 ETGG-SVIAVQEVppEEVSKYGIVDGEEIEGgvyRVTGLVEKPA--PEeapsNLAIVGRYILTPEIFDILE--------K 218

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1063706262 198 TFP-------------KIAAAQGLYAMVLPGFWMDIGQPRDYI 227
Cdd:COG1210   219 TKPgaggeiqltdaiaALAKEEPVYAYEFEGKRYDCGDKLGYL 261
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-193 1.81e-19

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


Pssm-ID: 133019 [Multi-domain]  Cd Length: 240  Bit Score: 86.09  E-value: 1.81e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   1 MKALILVGGFGTRLRPLTLSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINyqPEVMLNFLK------DFETKLEIK 74
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIIST--PEDLPLFKEllgdgsDLGIRITYA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  75 ItcsQEtEPLGTAGPLALARDKLldgSGEPFFVLNSDVISE-YPLKEMLEFHKSHGGEASIMVTKVDEPSKYGVVVMEES 153
Cdd:cd02538    79 V---QP-KPGGLAQAFIIGEEFI---GDDPVCLILGDNIFYgQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDEN 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1063706262 154 tGRVEKFVEKPKLYVGNKINAGIYLLNPSVLDKIE-LRPTS 193
Cdd:cd02538   152 -GRVLSIEEKPKKPKSNYAVTGLYFYDNDVFEIAKqLKPSA 191
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-333 1.34e-18

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 86.70  E-value: 1.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   3 ALILVGGFGTRLRPltlSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEVMLNFLKDFETKLEIkitcsQEtE 82
Cdd:PRK14356    8 ALILAAGKGTRMHS---DKPKVLQTLLGEPMLRFVYRALRPLFGDNVWTVVGHRADMVRAAFPDEDARFVL-----QE-Q 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  83 PLGTAGPLALARDKLLDGSGEPFFVLNSD--VISEYPLKEMLEfhKSHGGEASIMVTKVDEPSKYGVVVMEEstGRVEKF 160
Cdd:PRK14356   79 QLGTGHALQCAWPSLTAAGLDRVLVVNGDtpLVTTDTIDDFLK--EAAGADLAFMTLTLPDPGAYGRVVRRN--GHVAAI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 161 VE----KPKLY--VGNKINAGIYLLNPSVLDKIELRPTSIEKE------TFPKIAAAQGLYAMVL-----PGFwMDIGQP 223
Cdd:PRK14356  155 VEakdyDEALHgpETGEVNAGIYYLRLDAVESLLPRLTNANKSgeyyitDLVGLAVAEGMNVLGVncgedPNL-LGVNTP 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 224 RDYITGLRLyldsLRKKSPAK-LTSGPHI--VGNVLVDETATIGEGCLI-GP-----DVAIGPGCIVESGVRLSRCTVMR 294
Cdd:PRK14356  234 AELVRSEEL----LRARIVEKhLESGVLIhaPESVRIGPRATIEPGAEIyGPceiygASRIARGAVIHSHCWLRDAVVSS 309

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1063706262 295 GVRIKKHACISSSIIGWHSTVGQWARIENMTILGEDVHV 333
Cdd:PRK14356  310 GATIHSFSHLEGAEVGDGCSVGPYARLRPGAVLEEGARV 348
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 1-144 3.87e-17

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: 79.24  E-value: 3.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   1 MKALILVGGFGTRLRPLTLSFPKPLVDFANKPMILHQIEALKAVGVDE--VVLAINYQPEVML---NFLKDFETKLEIKI 75
Cdd:cd04198     1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDviVVVPEEEQAEISTylrSFPLNLKQKLDEVT 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063706262  76 TCSQetEPLGTAGPLALARDKLLdgsgEPFFVLNSDVISEYPLKEMLEFHKSHGGEASIMVTKVDEPSK 144
Cdd:cd04198    81 IVLD--EDMGTADSLRHIRKKIK----KDFLVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVSSE 143
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-333 5.75e-17

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 81.73  E-value: 5.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   1 MKALILVGGFGTRLRPltlSFPKPLVDFANKPMILHQIEALKAVGvDEVVLAINYQPEVMLNFLKDfetklEIKITcsQE 80
Cdd:PRK14357    1 MRALVLAAGKGTRMKS---KIPKVLHKISGKPMINWVIDTAKKVA-QKVGVVLGHEAELVKKLLPE-----WVKIF--LQ 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  81 TEPLGTAGPLALARDKLldGSGEPFFVLNSDV--ISEYPLKEMLEFHKSHGGEASIMVTKVDEPSKYGVVVMEESTGR-V 157
Cdd:PRK14357   70 EEQLGTAHAVMCARDFI--EPGDDLLILYGDVplISENTLKRLIEEHNRKGADVTILVADLEDPTGYGRIIRDGGKYRiV 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 158 EKFVEKPKLYVGNKINAGIYLLNPSVLdkielrptsieKETFPKIAA--AQGLYAMV-LPGFWMDIGQPR----DYITGL 230
Cdd:PRK14357  148 EDKDAPEEEKKIKEINTGIYVFSGDFL-----------LEVLPKIKNenAKGEYYLTdAVNFAEKVRVVKtedlLEITGV 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 231 --RLYL----DSLRKKSPAKLT-SGPHIV--GNVLVDETATIGEGCLIGP------DVAIGPGCIVESGVRLSRCTVMRG 295
Cdd:PRK14357  217 ntRIQLawleKQLRMRILEELMeNGVTILdpNTTYIHYDVEIGMDTIIYPmtfiegKTRIGEDCEIGPMTRIVDCEIGNN 296

                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1063706262 296 VRIKKHACiSSSIIGWHSTVGQWARIENMTILGEDVHV 333
Cdd:PRK14357  297 VKIIRSEC-EKSVIEDDVSVGPFSRLREGTVLKKSVKI 333
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 1-354 1.00e-16

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 80.68  E-value: 1.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   1 MKALILVGGFGTRLRPLTLSFPKPLVDFANKPMIlhqIE-ALKAV---GVDEVVLAINYQPEVMLNFLK-----DFE--- 68
Cdd:PRK05293    4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGKYRI---IDfTLSNCansGIDTVGVLTQYQPLELNNHIGigspwDLDrin 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  69 ---TKLEIKITCSQETEPLGTAGPLALARDKLLDGSGEPFFVLNSDVISEYPLKEMLEFHKSHGGEASIMVTKV--DEPS 143
Cdd:PRK05293   81 ggvTILPPYSESEGGKWYKGTAHAIYQNIDYIDQYDPEYVLILSGDHIYKMDYDKMLDYHKEKEADVTIAVIEVpwEEAS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 144 KYGVVVMEEsTGRVEKFVEKPKLYVGNKINAGIYLLNPSVLDKI----ELRPTSIE---KETFPKIAAAQG-LYAMVLPG 215
Cdd:PRK05293  161 RFGIMNTDE-NMRIVEFEEKPKNPKSNLASMGIYIFNWKRLKEYliedEKNPNSSHdfgKNVIPLYLEEGEkLYAYPFKG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 216 FWMDIGQPRDY----------ITGLRLYLDSLR------KKSPAKLTSGPHIVgNVLVDEtatigegcligpdvaigpGC 279
Cdd:PRK05293  240 YWKDVGTIESLweanmellrpENPLNLFDRNWRiysvnpNLPPQYIAENAKVK-NSLVVE------------------GC 300

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 280 IVESGVRLSrcTVMRGVRIKKHACISSSIIGWHSTVGQWARIENmTILGEDVHVSDEIYSNGG-----VVLPHKEIKSNI 354
Cdd:PRK05293  301 VVYGTVEHS--VLFQGVQVGEGSVVKDSVIMPGAKIGENVVIER-AIIGENAVIGDGVIIGGGkevitVIGENEVIGVGT 377
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 1-335 3.33e-16

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 79.64  E-value: 3.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   1 MKALILVGGFGTRLRPltlSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEvmlnflkDFETKLEIK-ITCSQ 79
Cdd:PRK14358    8 LDVVILAAGQGTRMKS---ALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAE-------QVEAALQGSgVAFAR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  80 ETEPLGTAGPLALARDKLLDGSGEpFFVLNSD--VISEYPLKEMLEFHKSHGGEASIMVTKVDEPSKYGVVVMEEStGRV 157
Cdd:PRK14358   78 QEQQLGTGDAFLSGASALTEGDAD-ILVLYGDtpLLRPDTLRALVADHRAQGSAMTILTGELPDATGYGRIVRGAD-GAV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 158 EKFVEK----PKLYVGNKINAGIYLLNpsvldkielrptsiekETFPKIA-------AAQGLYAMVLPGFWMDIG-QPR- 224
Cdd:PRK14358  156 ERIVEQkdatDAEKAIGEFNSGVYVFD----------------ARAPELArrigndnKAGEYYLTDLLGLYRAGGaQVRa 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 225 ------DYITGL--RLYLDSL-----RKKSPAKLTSGPHIV--GNVLVDETATIGEgcligpDVAIGPGCIVESGVRLSR 289
Cdd:PRK14358  220 fklsdpDEVLGAndRAGLAQLeatlrRRINEAHMKAGVTLQdpGTILIEDTVTLGR------DVTIEPGVLLRGQTRVAD 293

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1063706262 290 CTVM------------RGVRIKKHACISSSIIGWHSTVGQWARIENMTILGEDVHVSD 335
Cdd:PRK14358  294 GVTIgaysvvtdsvlhEGAVIKPHSVLEGAEVGAGSDVGPFARLRPGTVLGEGVHIGN 351
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-184 2.80e-15

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: 73.80  E-value: 2.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   3 ALILVGGFGTRLRPLTLSFPKPLVDFANKPMILHQIEALKAVGVDEV-VLAINYQPEVMlNFLKDFE------TKLEIKI 75
Cdd:cd04197     3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVfVFCCSHSDQIK-EYIEKSKwskpksSLMIVII 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  76 TCSQETEPLGTAgplalARDklLDGSG---EPFFVLNSDVISEYPLKEMLEFH----KSHGGEASIMVTK---VDEPSKY 145
Cdd:cd04197    82 IMSEDCRSLGDA-----LRD--LDAKGlirGDFILVSGDVVSNIDLKEILEEHkerrKKDKNAIMTMVLKeasPPHRTRR 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063706262 146 G----VVVMEESTGRV-----------EKFVEKPKLYVG---------NKINAGIYLLNPSVL 184
Cdd:cd04197   155 TgeefVIAVDPKTSRLlhyeelpgskyRSITDLPSELLGsnseveirhDLLDCHIDICSPDVL 217
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-333 3.31e-15

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 76.44  E-value: 3.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   3 ALILVGGFGTRLRPltlSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEVMLNFLKDFETKLEIkitCSQEtE 82
Cdd:PRK14353    8 AIILAAGEGTRMKS---SLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVAAAAAKIAPDAEI---FVQK-E 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  83 PLGTAGPLALARDKLLDGSGEpFFVLNSDV--ISEYPLKEMLEfHKSHGGEASIMVTKVDEPSKYGVVVMEEstGRVEKF 160
Cdd:PRK14353   81 RLGTAHAVLAAREALAGGYGD-VLVLYGDTplITAETLARLRE-RLADGADVVVLGFRAADPTGYGRLIVKG--GRLVAI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 161 VE---------KPKLyvgnkINAGIYLLNP----SVLDKI-------ELRPTSIeketfPKIAAAQGLYAMVlpgfwmdI 220
Cdd:PRK14353  157 VEekdasdeerAITL-----CNSGVMAADGadalALLDRVgndnakgEYYLTDI-----VAIARAEGLRVAV-------V 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 221 GQPRDYITGL--RLYL---DSL--RKKSPAKLTSGphiVGnvLVD-ET------ATIGEGCLIGPDVAIGPGCIVESGVR 286
Cdd:PRK14353  220 EAPEDEVRGInsRAELaeaEAVwqARRRRAAMLAG---VT--LIApETvffsydTVIGRDVVIEPNVVFGPGVTVASGAV 294

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063706262 287 ------LSRCTVMRGVrikkhacisssiigwhsTVGQWARIENMTILGEDVHV 333
Cdd:PRK14353  295 ihafshLEGAHVGEGA-----------------EVGPYARLRPGAELGEGAKV 330
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-321 7.85e-15

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 75.35  E-value: 7.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   5 ILVGGFGTRLRPltlSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEVMLNFLKDfETKLEIKItcsqETEPL 84
Cdd:PRK14360    6 ILAAGKGTRMKS---SLPKVLHPLGGKSLVERVLDSCEELKPDRRLVIVGHQAEEVEQSLAH-LPGLEFVE----QQPQL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  85 GTAGPLALARDKLLDGSGEpFFVLNSDV--ISEYPLKEMLEFHKSHGGEASIMVTKVDEPSKYGVVVMEEStGRVEKFVE 162
Cdd:PRK14360   78 GTGHAVQQLLPVLKGFEGD-LLVLNGDVplLRPETLEALLNTHRSSNADVTLLTARLPNPKGYGRVFCDGN-NLVEQIVE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 163 K----PKLYVGNKINAGIYLLNPSVLDKIelrptsieketFPKIAA--AQGLY------AMVLPGFWMDIGQPrDYITGL 230
Cdd:PRK14360  156 DrdctPAQRQNNRINAGIYCFNWPALAEV-----------LPKLSSnnDQKEYyltdtvSLLDPVMAVEVEDY-QEINGI 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 231 --RLYL--------DSLRKKspakltsgpHIVGNV-LVD-ETATIGEGCLIGPDVAI------------------GPGCI 280
Cdd:PRK14360  224 ndRKQLaqceeilqNRIKEK---------WMLAGVtFIDpASCTISETVELGPDVIIepqthlrgntvigsgcriGPGSL 294

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1063706262 281 VESGVRLSRCTVMrgvrikkHACISSSIIGWHSTVGQWARI 321
Cdd:PRK14360  295 IENSQIGENVTVL-------YSVVSDSQIGDGVKIGPYAHL 328
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-333 2.04e-14

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 73.87  E-value: 2.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   4 LILVGGFGTRLRPltlSFPKPLVDFANKPMILHQIEALKAVGvDEVVLAINYQPEVMLNFLKDFETKLEIKItcsQETEP 83
Cdd:PRK14359    6 IILAAGKGTRMKS---SLPKVLHTICGKPMLFYILKEAFAIS-DDVHVVLHHQKERIKEAVLEYFPGVIFHT---QDLEN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  84 L-GTAGPLalardKLLDGSGEPFFVLNSDViseyPL--KEMLEFHKSHGGEASIMVTKVDEPSKYGVVVMEEstGRVEKF 160
Cdd:PRK14359   79 YpGTGGAL-----MGIEPKHERVLILNGDM----PLveKDELEKLLENDADIVMSVFHLADPKGYGRVVIEN--GQVKKI 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 161 VE-----KPKLYVgNKINAGIYLLNPSVLDKI--ELRPTSIEKETF----PKIAAAQGLY---AMVLPGFWMDIGQPRDY 226
Cdd:PRK14359  148 VEqkdanEEELKI-KSVNAGVYLFDRKLLEEYlpLLKNQNAQKEYYltdiIALAIEKGETikaVFVDEENFMGVNSKFEL 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 227 ITGLRLYLDSLRKKSpakLTSGphivgnVLVDETATIgegcLIGPDVAIGPGCIVESGVRLSRCTVMRGVRIKKHACISS 306
Cdd:PRK14359  227 AKAEEIMQERIKKNA---MKQG------VIMRLPETI----YIESGVEFEGECELEEGVRILGKSKIENSHIKAHSVIEE 293

                         330       340
                  ....*....|....*....|....*..
gi 1063706262 307 SIIGwHSTVGQWARIENMTILgEDVHV 333
Cdd:PRK14359  294 SIIE-NSDVGPLAHIRPKSEI-KNTHI 318
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-227 6.68e-13

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 68.55  E-value: 6.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   2 KALILVGGFGTRLRPLTLSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEVMLNFLKDFETKLEIKITCSQET 81
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  82 EPLGTAGPLALARDKLldGSGEPFFVLNSDVISEYPLKEMLEFHKSHGGEASIMVTKVDEPSKYGVVVMEEStGRVEKFV 161
Cdd:PRK15480   85 SPDGLAQAFIIGEEFI--GGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQN-GTAISLE 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063706262 162 EKPKLYVGNKINAGIYLLNPSVLDKIE-LRPTS---IEKETFPKIAAAQGLYAMVLPG---FWMDIGQPRDYI 227
Cdd:PRK15480  162 EKPLQPKSNYAVTGLYFYDNDVVEMAKnLKPSArgeLEITDINRIYMEQGRLSVAMMGrgyAWLDTGTHQSLI 234
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 254-333 7.37e-13

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: 66.29  E-value: 7.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 254 NVLVDETATIGEGCLIGP------DVAIGPGCIVESGVRLSRCTVMRGVRIKKHACISSSIIGWHSTVGQWARIENMTIL 327
Cdd:cd03353     9 TTYIDGDVEIGVDVVIDPgvilegKTVIGEDCVIGPNCVIKDSTIGDGVVIKASSVIEGAVIGNGATVGPFAHLRPGTVL 88


                  ....*.
gi 1063706262 328 GEDVHV 333
Cdd:cd03353    89 GEGVHI 94
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 243-340 1.12e-10

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 60.50  E-value: 1.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 243 AKLTSGPHIVGNVLVDETATIGEGCLIGPDVAIGPGCIVESGVRL-SRCTVMRGVRIKKHaCI--SSSIIG-----WHST 314
Cdd:cd03352     2 AKIGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIhPNVTIYEGCIIGDR-VIihSGAVIGsdgfgFAPD 80

                          90       100
                  ....*....|....*....|....*...
gi 1063706262 315 VGQWARIENM--TILGEDVhvsdEIYSN 340
Cdd:cd03352    81 GGGWVKIPQLggVIIGDDV----EIGAN 104
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-231 1.13e-10

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 61.83  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   1 MKALILVGGFGTRLRPLTLSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAIN-------------YQPEVMLNFLKDF 67
Cdd:PRK10122    4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHasknavenhfdtsYELESLLEQRVKR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  68 ETKLEIKITCS--------QETEPLGTAGPLALARDKLLDgsgEPFFVLNSDVISE--------YPLKEML-EFHKShgG 130
Cdd:PRK10122   84 QLLAEVQSICPpgvtimnvRQGQPLGLGHSILCARPAIGD---NPFVVVLPDVVIDdasadplrYNLAAMIaRFNET--G 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 131 EASIMVTKV-DEPSKYGVVVMEE------STGRVEKFVEK---PKLYVGNKINAGIYLLNPSVLDKIE-LRPTSIEK--- 196
Cdd:PRK10122  159 RSQVLAKRMpGDLSEYSVIQTKEpldregKVSRIVEFIEKpdqPQTLDSDLMAVGRYVLSADIWPELErTEPGAWGRiql 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1063706262 197 -ETFPKIAAAQGLYAMVLPGFWMDIGQPRDYIT-----GLR 231
Cdd:PRK10122  239 tDAIAELAKKQSVDAMLMTGDSYDCGKKMGYMQafvkyGLR 279
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 1-184 2.13e-10

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


Pssm-ID: 133003 [Multi-domain]  Cd Length: 274  Bit Score: 60.67  E-value: 2.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   1 MKALILVGGFGTRLRPL-TLSFPKPLVD-FANKPMILHQIE-ALKAVGVDEVVLAINYQPEvmlnflkdFETKLEIKITC 77
Cdd:cd02509     1 IYPVILAGGSGTRLWPLsRESYPKQFLKlFGDKSLLQQTLDrLKGLVPPDRILVVTNEEYR--------FLVREQLPEGL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  78 SQET---EPLG--TAGPLALARDKLLD-GSGEPFFVLNSD-VISEYP-----LKEMLEFHKshggEASImVT---KVDEP 142
Cdd:cd02509    73 PEENiilEPEGrnTAPAIALAALYLAKrDPDAVLLVLPSDhLIEDVEaflkaVKKAVEAAE----EGYL-VTfgiKPTRP 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1063706262 143 S-KYGVVVMEESTG----RVEKFVEKPKL-----YV--GNKI-NAGIYLLNPSVL 184
Cdd:cd02509   148 EtGYGYIEAGEKLGggvyRVKRFVEKPDLetakeYLesGNYLwNSGIFLFRAKTF 202
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 4-177 2.78e-10

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: 59.57  E-value: 2.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   4 LILVGGFGTRLRPLTLSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINyqpevmlnflKDFETKLEIKITCSQ---- 79
Cdd:cd04183     2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFICR----------DEHNTKFHLDESLKLlapn 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  80 ------ETEPLGTAGPLALARDKLldGSGEPFFVLNSDVISEYPLKEMLEFHKSHGGEASIMVTKVDEPsKYGVVVMEES 153
Cdd:cd04183    72 atvvelDGETLGAACTVLLAADLI--DNDDPLLIFNCDQIVESDLLAFLAAFRERDLDGGVLTFFSSHP-RWSYVKLDEN 148

                         170       180
                  ....*....|....*....|....
gi 1063706262 154 tGRVEKFVEKPKlyVGNKINAGIY 177
Cdd:cd04183   149 -GRVIETAEKEP--ISDLATAGLY 169
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 256-323 3.05e-10

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: 56.05  E-value: 3.05e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063706262 256 LVDETATIGEGCLIGPDVaIGPGCIVESGVRLSRCTVMRGVRIKKHACISSSIIGWHSTVGQWARIEN 323
Cdd:cd04652     1 LVGENTQVGEKTSIKRSV-IGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKD 67
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-330 1.85e-09

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 58.80  E-value: 1.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   3 ALILVGGFGTRLRPLTlsfPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEVMLNFLKDFETKLEIKItcsQEtE 82
Cdd:PRK14352    7 VIVLAAGAGTRMRSDT---PKVLHTLAGRSMLGHVLHAAAGLAPQHLVVVVGHDRERVAPAVAELAPEVDIAV---QD-E 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  83 PLGTAGPLALARDKLLDGSGEPFFVLNSDV--ISEYPLKEMLEFHKSHGGEASIMVTKVDEPSKYGVVVmEESTGRVEKF 160
Cdd:PRK14352   80 QPGTGHAVQCALEALPADFDGTVVVTAGDVplLDGETLADLVATHTAEGNAVTVLTTTLDDPTGYGRIL-RDQDGEVTAI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 161 VEK----PKLYVGNKINAGIYLLNPSVLDKIELRPTSieketfpkiAAAQG-LYAMVLPGFWMDIGQP------RDY--I 227
Cdd:PRK14352  159 VEQkdatPSQRAIREVNSGVYAFDAAVLRSALARLSS---------DNAQGeLYLTDVLAIAREAGHRvgahhaDDSaeV 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 228 TGL--RLYLDSLRKKSPAKLTSGPHIVGNVLVDETAT-IGEGCLIGPDVAIGPGC-------IVESGV-----RLSRCTV 292
Cdd:PRK14352  230 AGVndRVQLAALGAELNRRIVEAWMRAGVTIVDPATTwIDVDVTIGRDVVIHPGTqllgrttIGEDAVvgpdtTLTDVTV 309

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1063706262 293 MRGVR-IKKHAciSSSIIGWHSTVGQWARIENMTILGED 330
Cdd:PRK14352  310 GEGASvVRTHG--SESEIGAGATVGPFTYLRPGTVLGEE 346
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-333 3.13e-09

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 58.11  E-value: 3.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   1 MKALILVGGFGTRLRPltlSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEVMLNFLKDfetkleIKITCSQE 80
Cdd:PRK09451    6 MSVVILAAGKGTRMYS---DLPKVLHTLAGKPMVQHVIDAANELGAQHVHLVYGHGGDLLKQTLAD------EPLNWVLQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  81 TEPLGTAGPLALArdklldgsgEPFFVLNSDVISEY---PL--KEMLE---FHKSHGGEASIMVtKVDEPSKYGVVVMEe 152
Cdd:PRK09451   77 AEQLGTGHAMQQA---------APFFADDEDILMLYgdvPLisVETLQrlrDAKPQGGIGLLTV-KLDNPTGYGRITRE- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 153 sTGRVEKFVEK----PKLYVGNKINAGIYLLNPSVLDKIELRPTSieketfpkiAAAQGLYAMV-------LPGFWMDIG 221
Cdd:PRK09451  146 -NGKVVGIVEQkdatDEQRQIQEINTGILVANGADLKRWLAKLTN---------NNAQGEYYITdiialahQEGREIVAV 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 222 QPRDYI--TGL--RLYLDSLRK-----------------KSPAK------LTSGPHIV--GNVLVDETATIGEGcligpd 272
Cdd:PRK09451  216 HPQRLSevEGVnnRLQLARLERvyqaeqaeklllagvmlRDPARfdlrgtLTHGRDVEidTNVIIEGNVTLGNR------ 289

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063706262 273 VAIGPGCIvesgvrLSRCTVMRGVRIKKHACISSSIIGWHSTVGQWARIENMTILGEDVHV 333
Cdd:PRK09451  290 VKIGAGCV------LKNCVIGDDCEISPYSVVEDANLGAACTIGPFARLRPGAELAEGAHV 344
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 3-346 4.87e-09

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 57.53  E-value: 4.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   3 ALILVGGFGTRLRPLTLSFPKP---------LVDFANKPMI---LHQIealkavgvdeVVLaINYQPE----------VM 60
Cdd:PRK00844    8 AIVLAGGEGKRLMPLTADRAKPavpfggsyrLIDFVLSNLVnsgYLRI----------YVL-TQYKSHsldrhisqtwRL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  61 LNFLKDFetkleikITC---SQETEP---LGTAgplalarDKLL-------DGSGEPFFVLNSDVISEYPLKEMLEFHKS 127
Cdd:PRK00844   77 SGLLGNY-------ITPvpaQQRLGKrwyLGSA-------DAIYqslnlieDEDPDYVVVFGADHVYRMDPRQMVDFHIE 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 128 HGGEASI--MVTKVDEPSKYGVVVMEEStGRVEKFVEKPKLYVG-----NKINA--GIYLLNPSVLDKiELR-----PTS 193
Cdd:PRK00844  143 SGAGVTVaaIRVPREEASAFGVIEVDPD-GRIRGFLEKPADPPGlpddpDEALAsmGNYVFTTDALVD-ALRrdaadEDS 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 194 IE---KETFPKIAAAQGLYAM-----VLPG-------FWMDIG---------------QPRdyitgLRLYLD------SL 237
Cdd:PRK00844  221 SHdmgGDIIPRLVERGRAYVYdfstnEVPGaterdrgYWRDVGtidayydahmdllsvHPV-----FNLYNRewpiytSS 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 238 RKKSPAKLTSGPHIVGNVlvdETATIGEGCLI-GPDVA---IGPGCIVESGVRLSRCTVMRGVRIKKHACISSSIIGWHS 313
Cdd:PRK00844  296 PNLPPAKFVDGGGRVGSA---QDSLVSAGSIIsGATVRnsvLSPNVVVESGAEVEDSVLMDGVRIGRGAVVRRAILDKNV 372

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 1063706262 314 TVGQWARIenmtilGEDV-------HVSDEiysnGGVVLP 346
Cdd:PRK00844  373 VVPPGATI------GVDLeedrrrfTVSEG----GIVVVP 402
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 3-138 6.08e-08

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


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 51.43  E-value: 6.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   3 ALILVGGFGTRLRpltlsFPKPLVDFANKPMILHQIEALKAVGvDEVVLAINYQPevmlnfLKDFETKLEIKITcsqeTE 82
Cdd:pfam12804   1 AVILAGGRSSRMG-----GDKALLPLGGKPLLERVLERLRPAG-DEVVVVANDEE------VLAALAGLGVPVV----PD 64

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063706262  83 PLGTAGPL-----ALARDKlldgSGEPFFVLNSDV--ISEYPLKEMLEFHKSHGGEASIMVTK 138
Cdd:pfam12804  65 PDPGQGPLagllaALRAAP----GADAVLVLACDMpfLTPELLRRLLAAAEESGADIVVPVYD 123
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 8-149 1.44e-07

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


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 51.04  E-value: 1.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   8 GGFGTRLRPLTlsfpKPLVDFANKPMILHQIEALKAVGVDEVVLAI-NYQPEVmLNFLKdfETKLEIkItcsqETEPLGT 86
Cdd:COG2266     3 GGKGTRLGGGE----KPLLEICGKPMIDRVIDALEESCIDKIYVAVsPNTPKT-REYLK--ERGVEV-I----ETPGEGY 70

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063706262  87 AGPLALArdklLDGSGEPFFVLNSDV--ISEYPLKEMLEFHKSHGGEASIMVTKVDEPSKYGVVV 149
Cdd:COG2266    71 VEDLNEA----LESISGPVLVVPADLplLTPEIIDDIIDAYLESGKPSLTVVVPAALKRELGVSP 131
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 173-340 2.01e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 52.06  E-value: 2.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 173 NAGIYLLNPSVLDKIELRPTSIEKETfPKIA---AAQGLYAMVLPGFWMDIgQPRDYItglrlyldslrkKSPAKLTSGP 249
Cdd:PRK00892   54 KAGAVIVSPDDAEFVPAGNALLVVKN-PYLAfarLAQLFDPPATPSPAAGI-HPSAVI------------DPSAKIGEGV 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 250 HIVGNVLVDETATIGEGCLIGPDVAIGPGCIVESGVRL-SRCTVMRGVRIKKHaCI--SSSIIG-----WHSTVGQWARI 321
Cdd:PRK00892  120 SIGPNAVIGAGVVIGDGVVIGAGAVIGDGVKIGADCRLhANVTIYHAVRIGNR-VIihSGAVIGsdgfgFANDRGGWVKI 198

                         170       180
                  ....*....|....*....|.
gi 1063706262 322 ENM--TILGEDVhvsdEIYSN 340
Cdd:PRK00892  199 PQLgrVIIGDDV----EIGAN 215
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-191 2.58e-07

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 51.45  E-value: 2.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   2 KALILVGGFGTRLRPLTLSFPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEVMLNflkDFETKLEI-----KIT 76
Cdd:PRK13389   10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIEN---HFDTSFELeamleKRV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  77 CSQETEPLGTAGP----LALARDKLLDGSG------------EPFFVLNSDVI-SEYP-------LKEMLE-FHKShgGE 131
Cdd:PRK13389   87 KRQLLDEVQSICPphvtIMQVRQGLAKGLGhavlcahpvvgdEPVAVILPDVIlDEYEsdlsqdnLAEMIRrFDET--GH 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063706262 132 ASIMVTKVDEPSKYGVVVME-------ESTGRVeKFVEKPKLYVG--NKINAGIYLLNPSVLDKIELRP 191
Cdd:PRK13389  165 SQIMVEPVADVTAYGVVDCKgvelapgESVPMV-GVVEKPKADVApsNLAIVGRYVLSADIWPLLAKTP 232
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 254-340 3.75e-07

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 51.17  E-value: 3.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 254 NVLVDETATIGEGCLIGPDVAIGPGCIVESGVRL-------SRCTVMRGVRIKKHaCI--SSSIIG-------WHSTvGQ 317
Cdd:COG1044   114 GVSIGPFAVIGAGVVIGDGVVIGPGVVIGDGVVIgddcvlhPNVTIYERCVIGDR-VIihSGAVIGadgfgfaPDED-GG 191

                          90       100
                  ....*....|....*....|....*
gi 1063706262 318 WARIENM--TILGEDVhvsdEIYSN 340
Cdd:COG1044   192 WVKIPQLgrVVIGDDV----EIGAN 212
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 260-353 4.78e-07

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 49.71  E-value: 4.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 260 TATIGEGCLIGPDVAIGPGCIVESGVRL-SRCTVMRGVRIKKHACISS-SIIGWHSTVGQWARIENMTILGED------- 330
Cdd:cd03352     1 SAKIGENVSIGPNAVIGEGVVIGDGVVIgPGVVIGDGVVIGDDCVIHPnVTIYEGCIIGDRVIIHSGAVIGSDgfgfapd 80

                          90       100
                  ....*....|....*....|....*.
gi 1063706262 331 --VHVsdEIYSNGGVVL-PHKEIKSN 353
Cdd:cd03352    81 ggGWV--KIPQLGGVIIgDDVEIGAN 104
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-54 1.63e-06

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


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 47.88  E-value: 1.63e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1063706262   1 MKALILVGGFGTRLRpltlsFPKPLVDFANKPMILHQIEALKAVgVDEVVLAIN 54
Cdd:COG0746     5 ITGVILAGGRSRRMG-----QDKALLPLGGRPLLERVLERLRPQ-VDEVVIVAN 52
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 118-346 1.66e-06

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 49.50  E-value: 1.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 118 LKEMLEFHKSHGGEASIMVTKVDEPSKYGVVVME-ESTGRVEKFVEKPKlyvGNKINA---------------------- 174
Cdd:PRK02862  132 YRLFVQHHRETGADITLAVLPVDEKDASGFGLMKtDDDGRITEFSEKPK---GDELKAmavdtsrlglspeeakgkpyla 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 175 --GIYLLNPSVLDKI-ELRPTSIE--KETFPKIAAAQGLYAMVLPGFWMDIGQPRD-YITGLRLYLDSL----------- 237
Cdd:PRK02862  209 smGIYVFSRDVLFDLlNKNPEYTDfgKEIIPEAIRDYKVQSYLFDGYWEDIGTIEAfYEANLALTQQPNppfsfydekap 288

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 238 -----RKKSPAKltsgphivgnvLVDETAT---IGEGCLIGPDV----AIGPGCIVESGVRLSRCTVMRGVRIKKHACIS 305
Cdd:PRK02862  289 iytraRYLPPSK-----------LLDATITesiIAEGCIIKNCSihhsVLGIRSRIESGCTIEDTLVMGADFYESSEERE 357

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063706262 306 SSI--------IGWHSTV-----GQWARI-ENMTILGEDvHV-----SDEIYS--NGGVVLP 346
Cdd:PRK02862  358 ELRkegkpplgIGEGTTIkraiiDKNARIgNNVRIVNKD-NVeeadrEDQGFYirDGIVVVV 418
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 1-63 1.90e-06

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


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 47.57  E-value: 1.90e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063706262   1 MKALILVGGFGTRLrpltlSFPKPLVDFANKPMILHQIEALKAVgVDEVVLAINYQPEVMLNF 63
Cdd:cd02503     1 ITGVILAGGKSRRM-----GGDKALLELGGKPLLEHVLERLKPL-VDEVVISANRDQERYALL 57
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 257-345 2.24e-06

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 48.86  E-value: 2.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 257 VDETATIGEGCLIGPDVAIGPGCIVESGVRLSrctvmRGVRIKKHAcisssIIGWHSTVGQWARIENMTILGEDVHVSDE 336
Cdd:COG1044    99 IHPSAVIDPSAKIGEGVSIGPFAVIGAGVVIG-----DGVVIGPGV-----VIGDGVVIGDDCVLHPNVTIYERCVIGDR 168

                          90
                  ....*....|.
gi 1063706262 337 --IYSngGVVL 345
Cdd:COG1044   169 viIHS--GAVI 177
lipid_A_lpxA TIGR01852
acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase; This model describes ...
 260-330 2.53e-06

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


Pssm-ID: 188173 [Multi-domain]  Cd Length: 254  Bit Score: 48.03  E-value: 2.53e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063706262 260 TATIGEGCLIGPDVAIGPGCIVESGVRLSrctvmRGVRIKKHACISSsiigwHSTVGQWARIENMTILGED 330
Cdd:TIGR01852   4 TAIIEPGAEIGENVEIGPFCIVGPGVKIG-----DGVELKSHVVILG-----HTTIGEGTRIFPGAVIGGV 64
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-58 3.06e-06

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 47.08  E-value: 3.06e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063706262   3 ALILVGGFGTRLRPltlsfPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPE 58
Cdd:COG2068     6 AIILAAGASSRMGR-----PKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAE 56
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-130 6.73e-06

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


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 46.01  E-value: 6.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   3 ALILVGGFGTRLRPltlsfPKPLVDFANKPMILHQIEALKAVGVDEVVLAINYQPEVMLNFLKDFETKLeikITCSQETE 82
Cdd:cd04182     3 AIILAAGRSSRMGG-----NKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVV---VINPDWEE 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1063706262  83 PLGTAgpLALARDKLLDGSgEPFFVLNSDV--ISEYPLKEMLEFHKSHGG 130
Cdd:cd04182    75 GMSSS--LAAGLEALPADA-DAVLILLADQplVTAETLRALIDAFREDGA 121
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 243-333 7.00e-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: 45.66  E-value: 7.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 243 AKLTSGPHIVGNVLVDETATIGEGCLIGPDVAIGPGCIVESGVRLSRCTVMRGVRIKKHACISSSIIGWHSTVGQWARIE 322
Cdd:cd05636    24 AIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSIIMDGTKVPHLNYVGDSVLGENVNLGAGTITA 103

                          90
                  ....*....|.
gi 1063706262 323 NMTILGEDVHV 333
Cdd:cd05636   104 NLRFDDKPVKV 114
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 256-304 7.51e-06

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: 46.94  E-value: 7.51e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063706262 256 LVDETATIGEG------CLIGPDVAIGPGCIVESGVRLSRCTVM-RGVRIKKHACI 304
Cdd:COG1043     9 IVDPGAKLGENveigpfCVIGPDVEIGDGTVIGSHVVIEGPTTIgKNNRIFPFASI 64
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
256-304 1.59e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 45.86  E-value: 1.59e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063706262 256 LVDETATIGEG------CLIGPDVAIGPGCIVESGVRLSRCTVM-RGVRIKKHACI 304
Cdd:PRK05289   10 IVEPGAKIGENveigpfCVIGPNVVIGDGTVIGSHVVIDGHTTIgKNNRIFPFASI 65
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 256-304 1.82e-05

UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this family catalyze the transfer of (R)-3-hydroxymyristic acid from its acyl carrier protein thioester to UDP-GlcNAc. It is the first enzyme in the lipid A biosynthetic pathway and is also referred to as LpxA. Lipid A is essential for the growth of Escherichia coli and related bacteria. It is also essential for maintaining the integrity of the outer membrane. UDP-GlcNAc acyltransferase is a homotrimer of left-handed parallel beta helix (LbH) subunits. Each subunit contains an N-terminal LbH region with 9 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal alpha-helical region.


Pssm-ID: 100042 [Multi-domain]  Cd Length: 254  Bit Score: 45.50  E-value: 1.82e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063706262 256 LVDETATIGEG------CLIGPDVAIGPGCIVESGVRLSRCTVM-RGVRIKKHACI 304
Cdd:cd03351     7 IVDPGAKIGENveigpfCVIGPNVEIGDGTVIGSHVVIDGPTTIgKNNRIFPFASI 62
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 3-73 2.05e-05

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


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 45.21  E-value: 2.05e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063706262   3 ALILVGGFGTRLRpltLSFPKPLVDFANKPMILHQIEALKAVG-VDEVVLAIN--YQPEVMLNFLKDFETKLEI 73
Cdd:cd02516     3 AIILAAGSGSRMG---ADIPKQFLELGGKPVLEHTLEAFLAHPaIDEIVVVVPpdDIDLAKELAKYGLSKVVKI 73
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
254-330 2.25e-05

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 45.47  E-value: 2.25e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1063706262 254 NVLVDETATIGEGCLIGPDVAIGPGCIVESGVRLSrctvmRGVRIKKHACISSsiigwHSTVGQWARIENMTILGED 330
Cdd:PRK05289    2 MAKIHPTAIVEPGAKIGENVEIGPFCVIGPNVVIG-----DGTVIGSHVVIDG-----HTTIGKNNRIFPFASIGED 68
KdsB COG1212
CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; ...
 21-52 4.21e-05

CMP-2-keto-3-deoxyoctulosonic acid synthetase [Cell wall/membrane/envelope biogenesis]; CMP-2-keto-3-deoxyoctulosonic acid synthetase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440825  Cd Length: 242  Bit Score: 44.28  E-value: 4.21e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1063706262  21 FP-KPLVDFANKPMILHQIE-ALKAVGVDEVVLA 52
Cdd:COG1212    16 LPgKPLADIAGKPMIQRVYErALASKGADRVVVA 49
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 257-330 7.24e-05

Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane/envelope biogenesis]; Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440665 [Multi-domain]  Cd Length: 258  Bit Score: 43.85  E-value: 7.24e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063706262 257 VDETATIGEGCLIGPDVAIGPGCIVESGVRLSrctvmRGVRIKKHACISSsiigwHSTVGQWARIENMTILGED 330
Cdd:COG1043     4 IHPTAIVDPGAKLGENVEIGPFCVIGPDVEIG-----DGTVIGSHVVIEG-----PTTIGKNNRIFPFASIGEE 67
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 1-58 7.37e-05

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 43.25  E-value: 7.37e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063706262   1 MKALILVGGFGTRlrpltlsF---PKPLVDFANKPMILHQIEALKAVgVDEVVLAINYQPE 58
Cdd:PRK00317    4 ITGVILAGGRSRR-------MggvDKGLQELNGKPLIQHVIERLAPQ-VDEIVINANRNLA 56
PRK05450 PRK05450
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 21-52 9.82e-05

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 235473  Cd Length: 245  Bit Score: 43.18  E-value: 9.82e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1063706262  21 FP-KPLVDFANKPMILHQIEALKAVGVDEVVLA 52
Cdd:PRK05450   16 LPgKPLADIGGKPMIVRVYERASKAGADRVVVA 48
CMP-KDO-Synthetase cd02517
CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the ...
 21-52 1.07e-04

CMP-KDO synthetase catalyzes the activation of KDO which is an essential component of the lipopolysaccharide; CMP-KDO Synthetase: 3-Deoxy-D-manno-octulosonate cytidylyltransferase (CMP-KDO synthetase) catalyzes the conversion of CTP and 3-deoxy-D-manno-octulosonate into CMP-3-deoxy-D-manno-octulosonate (CMP-KDO) and pyrophosphate. KDO is an essential component of the lipopolysaccharide found in the outer surface of gram-negative eubacteria. It is also a constituent of the capsular polysaccharides of some gram-negative eubacteria. Its presence in the cell wall polysaccharides of green algae and plant were also discovered. However, they have not been found in yeast and animals. The absence of the enzyme in mammalian cells makes it an attractive target molecule for drug design.


Pssm-ID: 133010  Cd Length: 239  Bit Score: 43.23  E-value: 1.07e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1063706262  21 FP-KPLVDFANKPMILHQIE-ALKAVGVDEVVLA 52
Cdd:cd02517    15 LPgKPLADIAGKPMIQHVYErAKKAKGLDEVVVA 48
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 263-345 1.24e-04

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


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 40.91  E-value: 1.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 263 IGEGCLIGPDVA----IGPGCIVESGVRLSRCTVMRGVRIKKHACISSSIIGWHSTVGqwariENMTILGEDVHVSDEIY 338
Cdd:cd04651    15 VSEGCIISGGTVensvLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIIDKNVVIP-----DGVVIGGDPEEDRARFY 89


                  ....*...
gi 1063706262 339 -SNGGVVL 345
Cdd:cd04651    90 vTEDGIVV 97
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 257-333 1.39e-04

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


Pssm-ID: 100050 [Multi-domain]  Cd Length: 197  Bit Score: 42.47  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 257 VDETATIGEGCLIGPDVAIGPGCIVESGVRL-SRCTVMRGVRIKKHACISSS-------IIGWHSTVGQWARIENMTILG 328
Cdd:cd03360    93 VSPSAVIGEGCVIMAGAVINPDARIGDNVIInTGAVIGHDCVIGDFVHIAPGvvlsggvTIGEGAFIGAGATIIQGVTIG 172


                  ....*
gi 1063706262 329 EDVHV 333
Cdd:cd03360   173 AGAII 177
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 263-335 1.74e-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: 39.48  E-value: 1.74e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063706262 263 IGEGCLIGPDVaIGPGCIVESGVRLSRCTVMRGVRIKKHACISSSIIGWHSTVGQWARIENMTILGEDVHVSD 335
Cdd:cd05787     8 IGEGTTIKNSV-IGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIPPGSLISFGVVIGD 79
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 257-330 2.33e-04

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: 42.03  E-value: 2.33e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063706262 257 VDETATIGEGCLIGPDVAIGPGCIVESGVRLSrctvmRGVRIKKHACISSsiigwHSTVGQWARIENMTILGED 330
Cdd:cd03351     2 IHPTAIVDPGAKIGENVEIGPFCVIGPNVEIG-----DGTVIGSHVVIDG-----PTTIGKNNRIFPFASIGEA 65
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 4-54 3.44e-04

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


Pssm-ID: 440824  Cd Length: 224  Bit Score: 41.27  E-value: 3.44e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1063706262   4 LILVGGFGTRLRpltLSFPKPLVDFANKPMILHQIEALKAVG-VDEVVLAIN 54
Cdd:COG1211     1 IIPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVP 49
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
3-54 3.64e-04

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 41.27  E-value: 3.64e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1063706262   3 ALILVGGFGTRLRPltlSFPKPLVDFANKPMILHQIEALKAVG-VDEVVLAIN 54
Cdd:PRK00155    6 AIIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVP 55
PRK13368 PRK13368
3-deoxy-manno-octulosonate cytidylyltransferase; Provisional
 21-52 4.70e-04

3-deoxy-manno-octulosonate cytidylyltransferase; Provisional


Pssm-ID: 184007  Cd Length: 238  Bit Score: 41.10  E-value: 4.70e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1063706262  21 FP-KPLVDFANKPMILHQIE-ALKAVGVDEVVLA 52
Cdd:PRK13368   16 LPgKPLLDILGKPMIQHVYErAAQAAGVEEVYVA 49
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 261-355 5.79e-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: 39.70  E-value: 5.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 261 ATIGEGCLIGPDVAIGPGCIVESgvrlsrCTVMRGVrikkhacisssIIGWHSTVGQWARIENMTILGEdvhvsdeiysn 340
Cdd:cd04645    55 VDPGYPTIIGDNVTVGHGAVLHG------CTIGDNC-----------LIGMGAIILDGAVIGKGSIVAA----------- 106

                          90
                  ....*....|....*
gi 1063706262 341 GGVVLPHKEIKSNIL 355
Cdd:cd04645   107 GSLVPPGKVIPPGSL 121
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
250-315 9.62e-04

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 39.08  E-value: 9.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 250 HIVGNVLVDETA--TIGEGCLIGPDVAIGPG----------------CIVESGVRL-SRCTVMRGVRIKKHAcisssIIG 310
Cdd:COG0110    35 YIGPGVTIDDPGgiTIGDNVLIGPGVTILTGnhpiddpatfplrtgpVTIGDDVWIgAGATILPGVTIGDGA-----VVG 109


                  ....*
gi 1063706262 311 WHSTV 315
Cdd:COG0110   110 AGSVV 114
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 250-333 1.34e-03

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: 39.11  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 250 HIVGNVLVDETATIGEGCLIGPDVAIGPGCIVESGVRLsR--CTVMRGVRIKKHACISSSIIGWHSTVGQWARIENmTIL 327
Cdd:cd05636    13 TIKGPVWIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYI-RgyTVLGDGCVVGNSVEVKNSIIMDGTKVPHLNYVGD-SVL 90


                  ....*.
gi 1063706262 328 GEDVHV 333
Cdd:cd05636    91 GENVNL 96
PRK14489 PRK14489
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ...
 3-58 1.53e-03

putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; Provisional


Pssm-ID: 237727 [Multi-domain]  Cd Length: 366  Bit Score: 40.12  E-value: 1.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1063706262   3 ALILVGGFGTRLRpltlSFPKPLVDFANKPMILHQIEALKAVgVDEVVLAINYQPE 58
Cdd:PRK14489    8 GVILAGGLSRRMN----GRDKALILLGGKPLIERVVDRLRPQ-FARIHLNINRDPA 58
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 256-330 1.66e-03

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 39.62  E-value: 1.66e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063706262 256 LVDETATIGEGCLIGPDVAIGPGCIVESGVrlsrcTVMRGVRIKKHAcissSIIGWhSTVGQWARIENMTILGED 330
Cdd:PRK12461    1 MIHPTAVIDPSAKLGSGVEIGPFAVIGANV-----EIGDGTWIGPHA----VILGP-TRIGKNNKIHQGAVVGDE 65
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
261-287 2.23e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.01  E-value: 2.23e-03
                          10        20
                  ....*....|....*....|....*..
gi 1063706262 261 ATIGEGCLIGPDVAIGPGCIVESGVRL 287
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVII 28
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 3-298 2.92e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 39.44  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262   3 ALILVGGFGTRLRPLTLSFPKPLVDFANKPMIlhqIE-AL-KAV--GVDEVVLAINYQPEVML-------NFLK-DFETK 70
Cdd:PRK00725   18 ALILAGGRGSRLKELTDKRAKPAVYFGGKFRI---IDfALsNCInsGIRRIGVLTQYKAHSLIrhiqrgwSFFReELGEF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262  71 LEIkITCSQETEP----LGTAGplALARDKLLDGSGEPFFV--LNSDVISEYPLKEMLEFHKSHGGEASI--MVTKVDEP 142
Cdd:PRK00725   95 VDL-LPAQQRVDEenwyRGTAD--AVYQNLDIIRRYDPKYVviLAGDHIYKMDYSRMLADHVESGADCTVacLEVPREEA 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 143 SKYGVVVMEEStGRVEKFVEKPKL---YVGNKINA----GIYLLNPSVLDKIELR----PTS---IEKETFPKIAAAQGL 208
Cdd:PRK00725  172 SAFGVMAVDEN-DRITAFVEKPANppaMPGDPDKSlasmGIYVFNADYLYELLEEdaedPNSshdFGKDIIPKIVEEGKV 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063706262 209 YA-----------MVLPGFWMDIGQPRDY------ITG----LRLYlDS---LRKKS----PAK---------------L 245
Cdd:PRK00725  251 YAhpfsdscvrsdPEEEPYWRDVGTLDAYwqanldLASvtpeLDLY-DRnwpIWTYQeqlpPAKfvfdrsgrrgmainsL 329

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063706262 246 TSGPHIVG-----------NVLVDETATIgEGCLIGPDVAIGPGCivesgvRLSRCTVMRGVRI 298
Cdd:PRK00725  330 VSGGCIISgavvrrsvlfsRVRVNSFSNV-EDSVLLPDVNVGRSC------RLRRCVIDRGCVI 386
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 262-317 6.42e-03

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


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 35.25  E-value: 6.42e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063706262 262 TIGEGCLIGPDVAIG-----PGCIVESGVRLSRCTVMRGVRIKKHACIS-SSIIGWHSTVGQ 317
Cdd:cd05787    18 VIGRNCKIGKNVVIDnsyiwDDVTIEDGCTIHHSIVADGAVIGKGCTIPpGSLISFGVVIGD 79
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 263-304 7.83e-03

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


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 35.94  E-value: 7.83e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1063706262 263 IGEGCLIGPDVAIGPGCIVESGVRL-SRCTVMRGVRIKKHACI 304
Cdd:cd03358     1 IGDNCIIGTNVFIENDVKIGDNVKIqSNVSIYEGVTIEDDVFI 43
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 268-345 8.45e-03

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


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 34.86  E-value: 8.45e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063706262 268 LIGPDVAIGPGCIVESGVRLSRCTVMRGVRIKKhacissSIIGWHSTVGQWARIeNMTILGEDVHVSDEIYSNGGVVL 345
Cdd:cd05787     1 VIGRGTSIGEGTTIKNSVIGRNCKIGKNVVIDN------SYIWDDVTIEDGCTI-HHSIVADGAVIGKGCTIPPGSLI 71
 
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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