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Conserved domains on  [gi|2158414772|ref|XP_002633494|]
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Protein CBR-TAG-335 [Caenorhabditis briggsae]

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 ...
 1-231 2.42e-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: 450.89  E-value: 2.42e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   1 MKALILVGGYGTRLRPLTLTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSYRAEQLEAEMTVHADRLGVKLIFSLE 80
Cdd:cd06425     1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKKLGIKITFSIE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  81 EEPLGTAGPLALARKHL-EDDDPFFVLNSDVICDFPFKQMVEFHKQHGKEGTIAVTKVEEPSKYGVVVFKED-GKIDDFV 158
Cdd:cd06425    81 TEPLGTAGPLALARDLLgDDDEPFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDENtGRIERFV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2158414772 159 EKPQEYVGNKINAGLYIFNSAILDRIPLKPTSIEKEIFPQMATSGNLYAYVLPGFWMDVGQPKDFLKGMSLFL 231
Cdd:cd06425   161 EKPKVFVGNKINAGIYILNPSVLDRIPLRPTSIEKEIFPKMASEGQLYAYELPGFWMDIGQPKDFLKGMSLYL 233
LbetaH super family cl00160
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 259-338 7.64e-30

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: 109.55  E-value: 7.64e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 259 LVDPSATVGENCVIGPDVVIGPRVQIEGGVRIQHSTILSDSTVGNYSWVSGSIIGRECHIGSWVRMENVCVLGDDVVVKD 338
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 ...
 1-231 2.42e-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: 450.89  E-value: 2.42e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   1 MKALILVGGYGTRLRPLTLTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSYRAEQLEAEMTVHADRLGVKLIFSLE 80
Cdd:cd06425     1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKKLGIKITFSIE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  81 EEPLGTAGPLALARKHL-EDDDPFFVLNSDVICDFPFKQMVEFHKQHGKEGTIAVTKVEEPSKYGVVVFKED-GKIDDFV 158
Cdd:cd06425    81 TEPLGTAGPLALARDLLgDDDEPFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDENtGRIERFV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2158414772 159 EKPQEYVGNKINAGLYIFNSAILDRIPLKPTSIEKEIFPQMATSGNLYAYVLPGFWMDVGQPKDFLKGMSLFL 231
Cdd:cd06425   161 EKPKVFVGNKINAGIYILNPSVLDRIPLRPTSIEKEIFPKMASEGQLYAYELPGFWMDIGQPKDFLKGMSLYL 233
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-232 3.87e-92

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: 275.49  E-value: 3.87e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   2 KALILVGGYGTRLRPLTLTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSYRAEQLEAEMTvHADRLGVKLIFSLEE 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFG-DGSRFGVRITYVDEG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  82 EPLGTAGPLALARKHLeDDDPFFVLNSDVICDFPFKQMVEFHKQHGKEGTIAVTKVEEPSKYGVVVFKEDGKIDDFVEKP 161
Cdd:COG1208    80 EPLGTGGALKRALPLL-GDEPFLVLNGDILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRVTRFVEKP 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2158414772 162 QEYVGNKINAGLYIFNSAILDRIPLKPT-SIEkEIFPQMATSGNLYAYVLPGFWMDVGQPKDFLKGMSLFLN 232
Cdd:COG1208   159 EEPPSNLINAGIYVLEPEIFDYIPEGEPfDLE-DLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLS 229
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-319 6.59e-72

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: 229.02  E-value: 6.59e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   1 MKALILVGGYGTRLRPLTLTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSYRAEQLEaEMTVHADRLGVKLIFSLE 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVR-EYFGDGSRGGVPIEYVVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  81 EEPLGTAGPLALARKHLedDDPFFVLNSDVICDFP-FKQMVEfhkqhGKEGTIAVTKVEEPSKYGVVVfKEDGKIDDFVE 159
Cdd:TIGR03992  80 EEQLGTADALGSAKEYV--DDEFLVLNGDVLLDSDlLERLIR-----AEAPAIAVVEVDDPSDYGVVE-TDGGRVTGIVE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 160 KPQEYVGNKINAGLYIFNSAI---LDRIPLKPTSiEKEI---FPQMATSGNLYAYVLPGFWMDVGQPKDFLKGMSLFLNH 233
Cdd:TIGR03992 152 KPENPPSNLINAGIYLFSPEIfelLEKTKLSPRG-EYELtdaLQLLIDEGKVKAVELDGFWLDVGRPWDLLDANEALLDN 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 234 VQTTRTGALATGSNIHGT------ATIRGSVLVDPSATVGENCVIGPD------VVIGPRVQIEGGVRIQHSTILSDSTV 301
Cdd:TIGR03992 231 LEPRIEGTVEENVTIKGPvvigegAVIRSGTYIEGPVYIGKNCDIGPNayirpyTVIGNNVHIGNAVEIKNSIIMEGTKI 310

                         330
                  ....*....|....*...
gi 2158414772 302 GNYSWVSGSIIGRECHIG 319
Cdd:TIGR03992 311 PHLSYVGDSVIGENCNFG 328
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-227 2.35e-71

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: 222.51  E-value: 2.35e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   2 KALILVGGYGTRLRPLTLTQPKPLVEFANK-PMMLHQMEALAAVGVDTVVLAVSYRAEQLEAEMTVHADRLGVKLIFSLE 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  81 EEPLGTAGPLALARKHLEDDD-PFFVLNSDVICDFPFKQMVEFHKQHG--KEGTIAVTKVEEPSKYGVVVFKEDGKIDDF 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKsDVLVLGGDHIYRMDLEQAVKFHIEKAadATVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2158414772 158 VEKPQEYV-GNKINAGLYIFNSAILDRI-----PLKPTSIE-KEIFPQMATSGNL-YAYVLPGF-WMDVGQPKDFLKGM 227
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDFLakyleELKRGEDEiTDILPKALEDGKLaYAFIFKGYaWLDVGTWDSLWEAN 239
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 1-340 3.73e-30

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 118.82  E-value: 3.73e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   1 MKALILVGGYGTRLRPLTLTQPKPLVEFANKPMMLH-QMEALAAVGVDTVVLAVSYRAEQLEAEMTVHA----DRL--GV 73
Cdd:PRK05293    4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGKYRIIDfTLSNCANSGIDTVGVLTQYQPLELNNHIGIGSpwdlDRIngGV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  74 KLI--FSLEEEP---LGTAGPLALARKHLEDDDPFFV--LNSDVICDFPFKQMVEFHKQHGKEGTIAVTKV--EEPSKYG 144
Cdd:PRK05293   84 TILppYSESEGGkwyKGTAHAIYQNIDYIDQYDPEYVliLSGDHIYKMDYDKMLDYHKEKEADVTIAVIEVpwEEASRFG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 145 VVVFKEDGKIDDFVEKPQEYVGNKINAGLYIFNSAILDRI----PLKPTSIE---KEIFPQMATSG-NLYAYVLPGFWMD 216
Cdd:PRK05293  164 IMNTDENMRIVEFEEKPKNPKSNLASMGIYIFNWKRLKEYliedEKNPNSSHdfgKNVIPLYLEEGeKLYAYPFKGYWKD 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 217 VGQPK-------DFLKGMSLF-----------LNHVQTTRTgaLATGSNIHgtatirgsvlvdpSATVGENCVIGPDV-- 276
Cdd:PRK05293  244 VGTIEslweanmELLRPENPLnlfdrnwriysVNPNLPPQY--IAENAKVK-------------NSLVVEGCVVYGTVeh 308

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2158414772 277 -VIGPRVQIEGGVRIQHSTILSDSTVGNYSWVSGSIIGRECHIGSWVRM----ENVCVLGDDVVVKDEV 340
Cdd:PRK05293  309 sVLFQGVQVGEGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVIIgggkEVITVIGENEVIGVGT 377
LbH_M1P_guanylylT_C cd05824
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 259-338 7.64e-30

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: 109.55  E-value: 7.64e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 259 LVDPSATVGENCVIGPDVVIGPRVQIEGGVRIQHSTILSDSTVGNYSWVSGSIIGRECHIGSWVRMENVCVLGDDVVVKD 338
Cdd:cd05824     1 LIDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLENVTVLGDDVTIKD 80
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 233-334 2.95e-12

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 66.70  E-value: 2.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 233 HVQTTRTGAlatgSNIHGTATIRGSVLVDPSATVGENCVIGPDVVIGPRVQIEGGVRI-QHSTILSDSTVG-NYSWVSGS 310
Cdd:PRK00892   92 DPPATPSPA----AGIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIgDGVKIGADCRLHaNVTIYHAV 167

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2158414772 311 IIGRECHI-----------------GSWVRME---NVcVLGDDV 334
Cdd:PRK00892  168 RIGNRVIIhsgavigsdgfgfandrGGWVKIPqlgRV-IIGDDV 210
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 248-334 1.11e-11

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 65.04  E-value: 1.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 248 IHGTATIRGSVLVDPSATVGENCVIGPDVVIGPRVQIEGGVriqhsTILSDSTVGNYSWV-------SGSIIGRECHI-- 318
Cdd:COG1044    99 IHPSAVIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGV-----VIGDGVVIGDDCVLhpnvtiyERCVIGDRVIIhs 173

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2158414772 319 ----------------GSWVRME---NVcVLGDDV 334
Cdd:COG1044   174 gavigadgfgfapdedGGWVKIPqlgRV-VIGDDV 207
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 258-338 1.17e-03

sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff.


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 39.78  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 258 VLVDPSATVGENCVIGPDVVIGPRVQIEGGVRIqhstilsdstvGNYSWV-SGSIIGRECHIGSWvrmenvCVLG-DDVV 335
Cdd:TIGR03570 124 VIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVI-----------GEGVFIgAGATIIQGVTIGAG------AIVGaGAVV 186


                  ...
gi 2158414772 336 VKD 338
Cdd:TIGR03570 187 TKD 189
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
263-292 2.06e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.39  E-value: 2.06e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2158414772 263 SATVGENCVIGPDVVIGPRVQIEGGVRIQH 292
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
 
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 ...
 1-231 2.42e-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: 450.89  E-value: 2.42e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   1 MKALILVGGYGTRLRPLTLTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSYRAEQLEAEMTVHADRLGVKLIFSLE 80
Cdd:cd06425     1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKKLGIKITFSIE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  81 EEPLGTAGPLALARKHL-EDDDPFFVLNSDVICDFPFKQMVEFHKQHGKEGTIAVTKVEEPSKYGVVVFKED-GKIDDFV 158
Cdd:cd06425    81 TEPLGTAGPLALARDLLgDDDEPFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVVVHDENtGRIERFV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2158414772 159 EKPQEYVGNKINAGLYIFNSAILDRIPLKPTSIEKEIFPQMATSGNLYAYVLPGFWMDVGQPKDFLKGMSLFL 231
Cdd:cd06425   161 EKPKVFVGNKINAGIYILNPSVLDRIPLRPTSIEKEIFPKMASEGQLYAYELPGFWMDIGQPKDFLKGMSLYL 233
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-232 3.87e-92

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: 275.49  E-value: 3.87e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   2 KALILVGGYGTRLRPLTLTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSYRAEQLEAEMTvHADRLGVKLIFSLEE 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFG-DGSRFGVRITYVDEG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  82 EPLGTAGPLALARKHLeDDDPFFVLNSDVICDFPFKQMVEFHKQHGKEGTIAVTKVEEPSKYGVVVFKEDGKIDDFVEKP 161
Cdd:COG1208    80 EPLGTGGALKRALPLL-GDEPFLVLNGDILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRVTRFVEKP 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2158414772 162 QEYVGNKINAGLYIFNSAILDRIPLKPT-SIEkEIFPQMATSGNLYAYVLPGFWMDVGQPKDFLKGMSLFLN 232
Cdd:COG1208   159 EEPPSNLINAGIYVLEPEIFDYIPEGEPfDLE-DLLPRLIAEGRVYGYVHDGYWLDIGTPEDLLEANALLLS 229
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-218 5.93e-86

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: 259.05  E-value: 5.93e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   3 ALILVGGYGTRLRPLTLTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSYRAEQLEAEMTvHADRLGVKLIFSLEEE 82
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFG-DGSKFGVNIEYVVQEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  83 PLGTAGPLALARKHLeDDDPFFVLNSDVICDFPFKQMVEFHKQHGKEGTIAVTKVEEPSKYGVVVFKEDGKIDDFVEKPQ 162
Cdd:cd04181    80 PLGTAGAVRNAEDFL-GDDDFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKPT 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2158414772 163 EYVGNKINAGLYIFNSAILDRIPLKPTS---IEKEIFPQMATSGNLYAYVLPGFWMDVG 218
Cdd:cd04181   159 LPESNLANAGIYIFEPEILDYIPEILPRgedELTDAIPLLIEEGKVYGYPVDGYWLDIG 217
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-319 6.59e-72

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: 229.02  E-value: 6.59e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   1 MKALILVGGYGTRLRPLTLTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSYRAEQLEaEMTVHADRLGVKLIFSLE 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVR-EYFGDGSRGGVPIEYVVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  81 EEPLGTAGPLALARKHLedDDPFFVLNSDVICDFP-FKQMVEfhkqhGKEGTIAVTKVEEPSKYGVVVfKEDGKIDDFVE 159
Cdd:TIGR03992  80 EEQLGTADALGSAKEYV--DDEFLVLNGDVLLDSDlLERLIR-----AEAPAIAVVEVDDPSDYGVVE-TDGGRVTGIVE 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 160 KPQEYVGNKINAGLYIFNSAI---LDRIPLKPTSiEKEI---FPQMATSGNLYAYVLPGFWMDVGQPKDFLKGMSLFLNH 233
Cdd:TIGR03992 152 KPENPPSNLINAGIYLFSPEIfelLEKTKLSPRG-EYELtdaLQLLIDEGKVKAVELDGFWLDVGRPWDLLDANEALLDN 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 234 VQTTRTGALATGSNIHGT------ATIRGSVLVDPSATVGENCVIGPD------VVIGPRVQIEGGVRIQHSTILSDSTV 301
Cdd:TIGR03992 231 LEPRIEGTVEENVTIKGPvvigegAVIRSGTYIEGPVYIGKNCDIGPNayirpyTVIGNNVHIGNAVEIKNSIIMEGTKI 310

                         330
                  ....*....|....*...
gi 2158414772 302 GNYSWVSGSIIGRECHIG 319
Cdd:TIGR03992 311 PHLSYVGDSVIGENCNFG 328
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-227 2.35e-71

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: 222.51  E-value: 2.35e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   2 KALILVGGYGTRLRPLTLTQPKPLVEFANK-PMMLHQMEALAAVGVDTVVLAVSYRAEQLEAEMTVHADRLGVKLIFSLE 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  81 EEPLGTAGPLALARKHLEDDD-PFFVLNSDVICDFPFKQMVEFHKQHG--KEGTIAVTKVEEPSKYGVVVFKEDGKIDDF 157
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKsDVLVLGGDHIYRMDLEQAVKFHIEKAadATVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2158414772 158 VEKPQEYV-GNKINAGLYIFNSAILDRI-----PLKPTSIE-KEIFPQMATSGNL-YAYVLPGF-WMDVGQPKDFLKGM 227
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDFLakyleELKRGEDEiTDILPKALEDGKLaYAFIFKGYaWLDVGTWDSLWEAN 239
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 3-223 6.06e-65

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: 205.48  E-value: 6.06e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   3 ALILVGGYGTRLRPLTLTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSYRAEQLEAEMtVHADRLGVKLIFSLEEE 82
Cdd:cd06915     1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYF-GDGYRGGIRIYYVIEPE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  83 PLGTAGPLALARKHLEdDDPFFVLNSDVICDFPFKQMVEFHKQHGKEGTIAVTKVEEPSKYGVVVFKEDGKIDDFVEKPQ 162
Cdd:cd06915    80 PLGTGGAIKNALPKLP-EDQFLVLNGDTYFDVDLLALLAALRASGADATMALRRVPDASRYGNVTVDGDGRVIAFVEKGP 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2158414772 163 EYVGNKINAGLYIFNSAILDRIPLKPTSIEKEIFPQMATSGNLYAYVLPGFWMDVGQPKDF 223
Cdd:cd06915   159 GAAPGLINGGVYLLRKEILAEIPADAFSLEADVLPALVKRGRLYGFEVDGYFIDIGIPEDY 219
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-224 2.63e-55

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


Pssm-ID: 133044 [Multi-domain]  Cd Length: 221  Bit Score: 180.46  E-value: 2.63e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   2 KALILVGGYGTRLRPLTLTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSYRAEQLEAemTVHADRLGVKLIFSLEE 81
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEA--HLGDSRFGLRITISDEP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  82 -EPLGTAGPLALARKHLeDDDPFFVLNSDVICDFPFKQMVEFHKQHGKEGTIAVTKVEEPSKYGVVVF--KEDGKIDDfv 158
Cdd:cd06422    79 dELLETGGGIKKALPLL-GDEPFLVVNGDILWDGDLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFslDADGRLRR-- 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2158414772 159 eKPQEYVGNKINAGLYIFNSAILDRIPLKPTSIeKEIFPQMATSGNLYAYVLPGFWMDVGQPKDFL 224
Cdd:cd06422   156 -GGGGAVAPFTFTGIQILSPELFAGIPPGKFSL-NPLWDRAIAAGRLFGLVYDGLWFDVGTPERLL 219
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 1-231 2.46e-54

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: 178.53  E-value: 2.46e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   1 MKALILVGGYGTRLRPLTLTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSYRAEQLEaEMTVHADRLGVKLIFSLE 80
Cdd:cd04189     1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIK-EALGDGSRFGVRITYILQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  81 EEPLGTAGPLALARKHLeDDDPFFVLNSDVICDFPFKQMVEFHKQHGKEGTIAVTKVEEPSKYGVVVFkEDGKIDDFVEK 160
Cdd:cd04189    80 EEPLGLAHAVLAARDFL-GDEPFVVYLGDNLIQEGISPLVRDFLEEDADASILLAEVEDPRRFGVAVV-DDGRIVRLVEK 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2158414772 161 PQEYVGNKINAGLYIFNSAILDRIP-LKPTS-----IEKEIFPQMATSGNLYAYVLPGFWMDVGQPKDFLKGMSLFL 231
Cdd:cd04189   158 PKEPPSNLALVGVYAFTPAIFDAISrLKPSWrgeleITDAIQWLIDRGRRVGYSIVTGWWKDTGTPEDLLEANRLLL 234
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 3-225 8.15e-54

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: 176.93  E-value: 8.15e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   3 ALILVGGYGTRLRPLTLTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSYRAEQLEAemtvH---ADRLGVKLIFSL 79
Cdd:cd06426     1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIED----YfgdGSKFGVNISYVR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  80 EEEPLGTAGPLALARKHLedDDPFFVLNSDVICDFPFKQMVEFHKQHGKEGTIAVTKVEEPSKYGVVVfKEDGKIDDFVE 159
Cdd:cd06426    77 EDKPLGTAGALSLLPEKP--TDPFLVMNGDILTNLNYEHLLDFHKENNADATVCVREYEVQVPYGVVE-TEGGRITSIEE 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2158414772 160 KPQEYVgnKINAGLYIFNSAILDRIPLK-----PTSIEKEIfpqmATSGNLYAYVLPGFWMDVGQPKDFLK 225
Cdd:cd06426   154 KPTHSF--LVNAGIYVLEPEVLDLIPKNeffdmPDLIEKLI----KEGKKVGVFPIHEYWLDIGRPEDYEK 218
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 2-318 1.11e-53

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: 180.68  E-value: 1.11e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   2 KALILVGGYGTRLRPLTLTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSYRAEQLEAEMTVHADRLGVKLIFSLEE 81
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  82 EPLGTAGPLALARKHLEDDDpFFVLNSDVICDFPFKQMVEFHKQHGKEGTIAVTKVEEPSKYGVVVFKEDGKIDDFVEKP 161
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDD-FVVYLGDNLIQDGISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 162 QEYVGNKINAGLYIFNSAILDRIP-LKPTSI-EKEI---FPQMATSG-NLYAYVLPGFWMDVGQPKDFLKGMSLFLNHVQ 235
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKnIKPSWRgELEItdaIQWLIEKGyKVGGSKVTGWWKDTGKPEDLLDANRLILDEVE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 236 TTRTGaLATGSNIHG------TATIRGSVLVDPsATVGENCVIGpDVVIGPRVQIEGGVRI-----QHSTILSDST-VGN 303
Cdd:TIGR01208 240 REVQG-VDDESKIRGrvvvgeGAKIVNSVIRGP-AVIGEDCIIE-NSYIGPYTSIGEGVVIrdaevEHSIVLDESViEGV 316

                         330
                  ....*....|....*
gi 2158414772 304 YSWVSGSIIGRECHI 318
Cdd:TIGR01208 317 QARIVDSVIGKKVRI 331
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 3-214 6.44e-52

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: 173.21  E-value: 6.44e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   3 ALILVGG--YGTRLRPLTLTQPKPLVEFANKPMMLHQMEALAAV-GVDTVVLAVSYRAEQLEAEMTVHADRLGVKLIFSL 79
Cdd:cd06428     1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVpDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  80 EEEPLGTAGPLALARKHLEDDDP--FFVLNSDVICDFPFKQMVEFHKQHGKEGTIAVTKV--EEPSKYGVVVFKED-GKI 154
Cdd:cd06428    81 EYKPLGTAGGLYHFRDQILAGNPsaFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEAsrEQASNYGCIVEDPStGEV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 155 DDFVEKPQEYVGNKINAGLYIFNSAILDRI---------------------PLKPTSIEKEIFPQMATSGNLYAYVLPGF 213
Cdd:cd06428   161 LHYVEKPETFVSDLINCGVYLFSPEIFDTIkkafqsrqqeaqlgddnnregRAEVIRLEQDVLTPLAGSGKLYVYKTDDF 240


                  .
gi 2158414772 214 W 214
Cdd:cd06428   241 W 241
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-224 1.42e-43

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 152.55  E-value: 1.42e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   1 MKALILVGGYGTRLRPLTLTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVS-YRAEQLEAEMTVHAdRLGVKLIFSL 79
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTpEDGPQFERLLGDGS-QLGIKISYAV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  80 EEEPLGTAGPLALARKHLeDDDPFFVLNSDVICDFP-FKQMVEFHKQHGKEGTIAVTKVEEPSKYGVVVFKEDGKIDDFV 158
Cdd:COG1209    80 QPEPLGLAHAFIIAEDFI-GGDPVALVLGDNIFYGDgLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLE 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2158414772 159 EKPQEYVGNKINAGLYIFNSAILDRIP-LKP--------TSIEKEifpqMATSGNLYAYVLP-GF-WMDVGQPKDFL 224
Cdd:COG1209   159 EKPKEPKSNLAVTGLYFYDNDVVEIAKnLKPsargeleiTDANQA----YLERGKLVVELLGrGFaWLDTGTHESLL 231
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 3-227 1.11e-40

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: 143.48  E-value: 1.11e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   3 ALILVGGYGTRLRPLTLTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSYRAEQL-------------------EAE 63
Cdd:cd02524     1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYKGHVIkeyflnyflhnsdvtidlgTNR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  64 MTVHADRLG---VKLIFSLEEEPlgTAGPLALARKHLEDDDPFFVLNSDVICDFPFKQMVEFHKQHGKEGTiaVTKVEEP 140
Cdd:cd02524    81 IELHNSDIEdwkVTLVDTGLNTM--TGGRLKRVRRYLGDDETFMLTYGDGVSDVNINALIEFHRSHGKLAT--VTAVHPP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 141 SKYGVVVFKEDGKIDDFVEKPQEyVGNKINAGLYIFNSAILDRIPLKPTSIEKEIFPQMATSGNLYAYVLPGFW--MDVG 218
Cdd:cd02524   157 GRFGELDLDDDGQVTSFTEKPQG-DGGWINGGFFVLEPEVFDYIDGDDTVFEREPLERLAKDGELMAYKHTGFWqcMDTL 235


                  ....*....
gi 2158414772 219 QPKDFLKGM 227
Cdd:cd02524   236 RDKQTLEEL 244
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 3-333 1.00e-34

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 130.97  E-value: 1.00e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   3 ALILVGGYGTRLRPLTLTQPKPLVEFANK------PM--MLHQmealaavGVDTVVLAVSYRAeqleAEMTVH------- 67
Cdd:COG0448     4 AIILAGGRGSRLGPLTKDRAKPAVPFGGKyriidfPLsnCVNS-------GIRRVGVLTQYKS----HSLNDHigsgkpw 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  68 -ADRL--GVKLI--FSLEEEP---LGTAGPLALARKHLEDDDP--FFVLNSDVICDFPFKQMVEFHKQHGKEGTIAVTKV 137
Cdd:COG0448    73 dLDRKrgGVFILppYQQREGEdwyQGTADAVYQNLDFIERSDPdyVLILSGDHIYKMDYRQMLDFHIESGADITVACIEV 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 138 --EEPSKYGVVVFKEDGKIDDFVEKPQEYVGNKINAGLYIFNSAILDRIpLK---PTSIE---KEIFPQMATSGNLYAYV 209
Cdd:COG0448   153 prEEASRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFNKDVLIEL-LEedaPNSSHdfgKDIIPRLLDRGKVYAYE 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 210 LPGFWMDVGQPKDFLKG-MSLFLNHVQT----------TRTGALAtGSNIHGTATIRGSVlvdpsatVGENCVIGPDV-- 276
Cdd:COG0448   232 FDGYWRDVGTIDSYYEAnMDLLDPEPEFnlydpewpiyTKQKDLP-PAKFVRGGKVKNSL-------VSNGCIISGTVen 303

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2158414772 277 -VIGPRVQIEGGVRIQHSTILSDSTVGNYSWVSGSIIGRECHIGswvrmENVcVLGDD 333
Cdd:COG0448   304 sVLFRGVRVESGAVVENSVIMPGVVIGEGAVIENAIIDKNVVIP-----PGV-VIGED 355
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 1-334 1.20e-33

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: 129.38  E-value: 1.20e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   1 MKALILVGGYGTRLRPltlTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSYRAEQLEAEMTvhadrlGVKLIFSLE 80
Cdd:COG1207     3 LAVVILAAGKGTRMKS---KLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALA------DLDVEFVLQ 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  81 EEPLGTAGPLALARKHLEDDD-PFFVLNSDVicdfPF------KQMVEFHKQHGKEGTIAVTKVEEPSKYGVVVFKEDGK 153
Cdd:COG1207    74 EEQLGTGHAVQQALPALPGDDgTVLVLYGDV----PLiraetlKALLAAHRAAGAAATVLTAELDDPTGYGRIVRDEDGR 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 154 IDDFVE----KPQEYVGNKINAGLYIFNSAILDR-IP-LKPTSIEKE-----IFPQMATSGnlyayvlpgfwMDVG--QP 220
Cdd:COG1207   150 VLRIVEekdaTEEQRAIREINTGIYAFDAAALREaLPkLSNDNAQGEyyltdVIAIARADG-----------LKVAavQP 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 221 KDFlkgmSLFL---NHVQttrtgaLATGSNIHGTATIR-----GSVLVDPSAT-VGENCVIGPDVVIGPRVQIEG----- 286
Cdd:COG1207   219 EDP----WEVLgvnDRVQ------LAEAERILQRRIAErlmraGVTIIDPATTyIDGDVEIGRDVVIDPNVILEGktvig 288

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2158414772 287 -GVRIQHSTILSDSTVGN-----YSWVSGSIIGRECHIGSWVRMENVCVLGDDV 334
Cdd:COG1207   289 eGVVIGPNCTLKDSTIGDgvvikYSVIEDAVVGAGATVGPFARLRPGTVLGEGV 342
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-230 1.02e-30

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 116.88  E-value: 1.02e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   2 KALILVGGYGTRLRPLTLTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSYRAEQLEAEmtVHADRLGVKLIFSLEE 81
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEA--LARPGPDVTFVYNPDY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  82 EPLGTAGPLALARKHLEDDdpFFVLNSDVICDfpfKQMVEFHKQHGKEGTIAV-TKVEEPSKYGV-VVFKEDGKIDDFVE 159
Cdd:COG1213    79 DETNNIYSLWLAREALDED--FLLLNGDVVFD---PAILKRLLASDGDIVLLVdRKWEKPLDEEVkVRVDEDGRIVEIGK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 160 KPQEYVGNKINAGLYIFNSAILDRIPLKPTSIEKEIFPQM----------ATSGNLYA-YVLPGFWMDVGQPKDFLKGMS 228
Cdd:COG1213   154 KLPPEEADGEYIGIFKFSAEGAAALREALEALIDEGGPNLyyedalqeliDEGGPVKAvDIGGLPWVEIDTPEDLERAEE 233


                  ..
gi 2158414772 229 LF 230
Cdd:COG1213   234 LF 235
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 1-340 3.73e-30

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 118.82  E-value: 3.73e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   1 MKALILVGGYGTRLRPLTLTQPKPLVEFANKPMMLH-QMEALAAVGVDTVVLAVSYRAEQLEAEMTVHA----DRL--GV 73
Cdd:PRK05293    4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGKYRIIDfTLSNCANSGIDTVGVLTQYQPLELNNHIGIGSpwdlDRIngGV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  74 KLI--FSLEEEP---LGTAGPLALARKHLEDDDPFFV--LNSDVICDFPFKQMVEFHKQHGKEGTIAVTKV--EEPSKYG 144
Cdd:PRK05293   84 TILppYSESEGGkwyKGTAHAIYQNIDYIDQYDPEYVliLSGDHIYKMDYDKMLDYHKEKEADVTIAVIEVpwEEASRFG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 145 VVVFKEDGKIDDFVEKPQEYVGNKINAGLYIFNSAILDRI----PLKPTSIE---KEIFPQMATSG-NLYAYVLPGFWMD 216
Cdd:PRK05293  164 IMNTDENMRIVEFEEKPKNPKSNLASMGIYIFNWKRLKEYliedEKNPNSSHdfgKNVIPLYLEEGeKLYAYPFKGYWKD 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 217 VGQPK-------DFLKGMSLF-----------LNHVQTTRTgaLATGSNIHgtatirgsvlvdpSATVGENCVIGPDV-- 276
Cdd:PRK05293  244 VGTIEslweanmELLRPENPLnlfdrnwriysVNPNLPPQY--IAENAKVK-------------NSLVVEGCVVYGTVeh 308

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2158414772 277 -VIGPRVQIEGGVRIQHSTILSDSTVGNYSWVSGSIIGRECHIGSWVRM----ENVCVLGDDVVVKDEV 340
Cdd:PRK05293  309 sVLFQGVQVGEGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVIIgggkEVITVIGENEVIGVGT 377
LbH_M1P_guanylylT_C cd05824
Mannose-1-phosphate guanylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 259-338 7.64e-30

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: 109.55  E-value: 7.64e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 259 LVDPSATVGENCVIGPDVVIGPRVQIEGGVRIQHSTILSDSTVGNYSWVSGSIIGRECHIGSWVRMENVCVLGDDVVVKD 338
Cdd:cd05824     1 LIDPSAKIGKTAKIGPNVVIGPNVTIGDGVRLQRCVILSNSTVRDHSWVKSSIVGWNSTVGRWTRLENVTVLGDDVTIKD 80
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-225 1.29e-28

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: 111.86  E-value: 1.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   1 MKALILVGGYGTRLRPLTLTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSY----------RAEQLEAEMT----- 65
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRgkraiedhfdRSYELEETLEkkgkt 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  66 -----VHADRLGVKLIFSLEEEPLGTAGPLALARKHLeDDDPFFVLNSDVICD---FPFKQMVEFHKQHGKeGTIAVTKV 137
Cdd:cd02541    81 dlleeVRIISDLANIHYVRQKEPLGLGHAVLCAKPFI-GDEPFAVLLGDDLIDskePCLKQLIEAYEKTGA-SVIAVEEV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 138 --EEPSKYGVVVFKEDG----KIDDFVEKP--QEYVGNKINAGLYIFNSAILDRIPLKPTSIEKEI-----FPQMATSGN 204
Cdd:cd02541   159 ppEDVSKYGIVKGEKIDgdvfKVKGLVEKPkpEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIqltdaIAKLLEEEP 238

                         250       260
                  ....*....|....*....|.
gi 2158414772 205 LYAYVLPGFWMDVGQPKDFLK 225
Cdd:cd02541   239 VYAYVFEGKRYDCGNKLGYLK 259
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-336 2.77e-28

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 114.54  E-value: 2.77e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   3 ALILVGGYGTRLRPltlTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSYRAEQLEAemtvhadRLGVKLIFSLEEE 82
Cdd:PRK14354    5 AIILAAGKGTRMKS---KLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKE-------VLGDRSEFALQEE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  83 PLGTAGPLALARKHLEDDDPFfVLnsdVIC-DFP------FKQMVEFHKQHGKEGTIAVTKVEEPSKYGVVVFKEDGKID 155
Cdd:PRK14354   75 QLGTGHAVMQAEEFLADKEGT-TL---VICgDTPlitaetLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNENGEVE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 156 DFVE----KPQEYVGNKINAGLYIFNSAILDRIpLK-------------PTSIekEIFPQMAtsGNLYAYVLPGFwmdvg 218
Cdd:PRK14354  151 KIVEqkdaTEEEKQIKEINTGTYCFDNKALFEA-LKkisndnaqgeyylTDVI--EILKNEG--EKVGAYQTEDF----- 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 219 qpkdflkGMSLFLNhvqtTRTgALATG-----SNIHGTATIRGSVLVDPSATvgencVIGPDVVIGPRVQIEGGVRIQ-H 292
Cdd:PRK14354  221 -------EESLGVN----DRV-ALAEAekvmrRRINEKHMVNGVTIIDPEST-----YIDADVEIGSDTVIEPGVVIKgN 283

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 2158414772 293 STILSDSTVGNYSWVSGSIIGRECHIGSWVRMENvcVLGDDVVV 336
Cdd:PRK14354  284 TVIGEDCVIGPGSRIVDSTIGDGVTITNSVIEES--KVGDNVTV 325
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 3-223 4.35e-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: 4.35e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   3 ALILVGGYGTRLRPLTLTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSYRAEQLEAEMtvhADRLGVKLIFSLEEE 82
Cdd:cd02523     1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELL---KKYPNIKFVYNPDYA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  83 PLGTAGPLALARKHLEDDdpFFVLNSDVICDfpfKQMVEFHKQHGKEGTIAVTKV--EEPSKYGVV-----VFKEDGKID 155
Cdd:cd02523    78 ETNNIYSLYLARDFLDED--FLLLEGDVVFD---PSILERLLSSPADNAILVDKKtkEWEDEYVKDlddagVLLGIISKA 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2158414772 156 DFVEKPQ-EYVgnkinaGLYIFNSAILDRIPLKPTSIEKEIFPQM---------ATSGNLYAYVLP-GFWMDVGQPKDF 223
Cdd:cd02523   153 KNLEEIQgEYV------GISKFSPEDADRLAEALEELIEAGRVNLyyedalqrlISEEGVKVKDISdGFWYEIDDLEDL 225
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-353 9.18e-26

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 107.52  E-value: 9.18e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   3 ALILVGGYGTRLRPltlTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSYRAEQLEAEMTVHADrlgvkLIFSLEEE 82
Cdd:PRK14355    6 AIILAAGKGTRMKS---DLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDGD-----VSFALQEE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  83 PLGTAGPLALARKHLeddDPF----FVLNSDV--ICDFPFKQMVEFHKQHGKEGTIAVTKVEEPSKYGVVVFKEDGKIDD 156
Cdd:PRK14355   78 QLGTGHAVACAAPAL---DGFsgtvLILCGDVplLRAETLQGMLAAHRATGAAVTVLTARLENPFGYGRIVRDADGRVLR 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 157 FVEK----PQEYVGNKINAGLYIFNSAIL-DRIP-LKPTSIEKEIF----PQMATSGNLYAYVLPgfwmdVGQPKDFLkG 226
Cdd:PRK14355  155 IVEEkdatPEERSIREVNSGIYCVEAAFLfDAIGrLGNDNAQGEYYltdiVAMAAAEGLRCLAFP-----VADPDEIM-G 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 227 MSlflNHVQTTRTGALATGsNIHGTATIRGSVLVDPSAT-VGENCVIGPDVVIGPRVQIEGGVRiqhstilsdstvgnys 305
Cdd:PRK14355  229 VN---DRAQLAEAARVLRR-RINRELMLAGVTLIDPETTyIDRGVVIGRDTTIYPGVCISGDTR---------------- 288

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 2158414772 306 wvsgsiIGRECHIGSWVRMENvCVLGDDVVVKDEVYLNEASVLPHKVI 353
Cdd:PRK14355  289 ------IGEGCTIEQGVVIKG-CRIGDDVTVKAGSVLEDSVVGDDVAI 329
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 3-183 1.26e-25

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: 102.98  E-value: 1.26e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   3 ALILVGGYGTRLRPltlTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSYRAEQLEAEMTvhadrlGVKLIFSLEEE 82
Cdd:cd02540     1 AVILAAGKGTRMKS---DLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALA------NPNVEFVLQEE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  83 PLGTAGPLALARKHLED-DDPFFVLNSDV--ICDFPFKQMVEFHKQHGKEGTIAVTKVEEPSKYGVVVFKEDGKIDDFVE 159
Cdd:cd02540    72 QLGTGHAVKQALPALKDfEGDVLVLYGDVplITPETLQRLLEAHREAGADVTVLTAELEDPTGYGRIIRDGNGKVLRIVE 151

                         170       180
                  ....*....|....*....|....*...
gi 2158414772 160 ----KPQEYVGNKINAGLYIFNSAILDR 183
Cdd:cd02540   152 ekdaTEEEKAIREVNAGIYAFDAEFLFE 179
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-225 6.12e-24

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 99.72  E-value: 6.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   2 KALILVGGYGTRLRPLTLTQPK---PLVefaNKPMMlhQM---EALAAvGVDTVVLAVSY----------RAEQLEAEM- 64
Cdd:COG1210     5 KAVIPVAGLGTRFLPATKAIPKemlPIV---DKPLI--QYvveEAVAA-GIEEIIFVTGRgkraiedhfdRSYELEATLe 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  65 ---------TVHADRLGVKLIFSLEEEPLGTAGPLALARKHLeDDDPFFVLNSDVICDFP---FKQMVEFHKQHGKeGTI 132
Cdd:COG1210    79 akgkeelleEVRSISPLANIHYVRQKEPLGLGHAVLCARPFV-GDEPFAVLLGDDLIDSEkpcLKQMIEVYEETGG-SVI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 133 AVTKV--EEPSKYGVVVFKEDG----KIDDFVEKPQ--EYVGNKINAGLYIFNSAILDRipLKPTSIEK--EIfpQ---- 198
Cdd:COG1210   157 AVQEVppEEVSKYGIVDGEEIEggvyRVTGLVEKPApeEAPSNLAIVGRYILTPEIFDI--LEKTKPGAggEI--Qltda 232

                         250       260       270
                  ....*....|....*....|....*....|
gi 2158414772 199 ---MATSGNLYAYVLPGFWMDVGQPKDFLK 225
Cdd:COG1210   233 iaaLAKEEPVYAYEFEGKRYDCGDKLGYLK 262
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-225 5.29e-23

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: 96.10  E-value: 5.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   1 MKALILVGGYGTRLRPLTLTQPKPLVEFANKPMMLHQMEALAAVGVdTVVLAVSYRaEQLEA--EMTVHADRLGVKLIFS 78
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGI-REILIISTP-EDLPLfkELLGDGSDLGIRITYA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  79 LEEEPLGTAGPLALARKHLEDDDPFFVLNSDVICDFPFKQMVEFHKQHGKEGTIAVTKVEEPSKYGVVVFKEDGKIDDFV 158
Cdd:cd02538    79 VQPKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIE 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2158414772 159 EKPQEYVGNKINAGLYIFNSAILDRIP-LKPTSI-EKEIfpqmaTS--------GNLYAYVLP--GFWMDVGQPKDFLK 225
Cdd:cd02538   159 EKPKKPKSNYAVTGLYFYDNDVFEIAKqLKPSARgELEI-----TDvnneylekGKLSVELLGrgFAWLDTGTHESLLE 232
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 259-338 1.03e-22

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: 90.38  E-value: 1.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 259 LVDPSATVGENCVIGPdVVIGPRVQIEGGVRIQHSTILSDSTVGNYSWVSGSIIGRECHIGSWVRMENVCVLGDDVVVKD 338
Cdd:cd03356     1 LIGESTVIGENAIIKN-SVIGDNVRIGDGVTITNSILMDNVTIGANSVIVDSIIGDNAVIGENVRVVNLCIIGDDVVVED 79
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-347 1.50e-21

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 95.38  E-value: 1.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   5 ILVGGYGTRLRPltlTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSYRAEQLEAEMTVHADrlgvkLIFSLEEEPL 84
Cdd:PRK14360    6 ILAAGKGTRMKS---SLPKVLHPLGGKSLVERVLDSCEELKPDRRLVIVGHQAEEVEQSLAHLPG-----LEFVEQQPQL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  85 GTAGPLALARKHLED-DDPFFVLNSDVicdfPF------KQMVEFHKQHGKEGTIAVTKVEEPSKYGVVVFKEDGKIDDF 157
Cdd:PRK14360   78 GTGHAVQQLLPVLKGfEGDLLVLNGDV----PLlrpetlEALLNTHRSSNADVTLLTARLPNPKGYGRVFCDGNNLVEQI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 158 VEK----PQEYVGNKINAGLYIFN----SAILDRipLKPTSIEKEIFPQMATSgnlyaYVLPGFWMDVGQPkDFLKGMSl 229
Cdd:PRK14360  154 VEDrdctPAQRQNNRINAGIYCFNwpalAEVLPK--LSSNNDQKEYYLTDTVS-----LLDPVMAVEVEDY-QEINGIN- 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 230 flNHVQttrtgaLATGSNIHGTaTIR------GSVLVDP-SATVGENCVIGPDVVIGPRVQIEG---------------- 286
Cdd:PRK14360  225 --DRKQ------LAQCEEILQN-RIKekwmlaGVTFIDPaSCTISETVELGPDVIIEPQTHLRGntvigsgcrigpgsli 295

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2158414772 287 -------GVRIQHSTIlSDSTVGNYSWVS-------GSIIGRECHIGSWVRMENVCvLGDDVVVKDEVYLNEASV 347
Cdd:PRK14360  296 ensqigeNVTVLYSVV-SDSQIGDGVKIGpyahlrpEAQIGSNCRIGNFVEIKKSQ-LGEGSKVNHLSYIGDATL 368
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-350 4.65e-20

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 90.94  E-value: 4.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   3 ALILVGGYGTRLRPltlTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSYRAEQLEAEMTVHADRlgvkliFSLEEE 82
Cdd:PRK14356    8 ALILAAGKGTRMHS---DKPKVLQTLLGEPMLRFVYRALRPLFGDNVWTVVGHRADMVRAAFPDEDAR------FVLQEQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  83 PLGTAGPLALARKHLED-----------DDPffVLNSDVICDFpfkqmveFHKQHGKEGTIAVTKVEEPSKYGVVVfKED 151
Cdd:PRK14356   79 QLGTGHALQCAWPSLTAagldrvlvvngDTP--LVTTDTIDDF-------LKEAAGADLAFMTLTLPDPGAYGRVV-RRN 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 152 GKIDDFVE----KPQEY--VGNKINAGLYIFN----SAILDRIPLKPTSIEKEI--FPQMATSGNL-----YAYVLPGFw 214
Cdd:PRK14356  149 GHVAAIVEakdyDEALHgpETGEVNAGIYYLRldavESLLPRLTNANKSGEYYItdLVGLAVAEGMnvlgvNCGEDPNL- 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 215 MDVGQPKDFLKGMSLflnhvQTTRT--GALATGSNIHGTATIRgsvlvdpsatvgencvIGPDVVIGPRVQIEGG----- 287
Cdd:PRK14356  228 LGVNTPAELVRSEEL-----LRARIveKHLESGVLIHAPESVR----------------IGPRATIEPGAEIYGPceiyg 286

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2158414772 288 -------------VRIQHSTILSDSTVGNYSWVSGSIIGRECHIGSWVRMENVCVLGDDVVVKDEVYLNEASVLPH 350
Cdd:PRK14356  287 asriargavihshCWLRDAVVSSGATIHSFSHLEGAEVGDGCSVGPYARLRPGAVLEEGARVGNFVEMKKAVLGKG 362
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 1-182 8.66e-19

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


Pssm-ID: 133001 [Multi-domain]  Cd Length: 216  Bit Score: 83.84  E-value: 8.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   1 MKALILVGGYGTRLRPLTLTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSYRAEQLEA---EMTVHADRLGVKL-- 75
Cdd:cd02507     1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEhllKSKWSSLSSKMIVdv 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  76 IFSLEEEPLGTAGPLALARKHLEDDdpFFVLNSDVICDFPFKQMVEFHKQHGKeGTIA-VTKVEEPSKYGVVVFKEDGKI 154
Cdd:cd02507    81 ITSDLCESAGDALRLRDIRGLIRSD--FLLLSCDLVSNIPLSELLEERRKKDK-NAIAtLTVLLASPPVSTEQSKKTEEE 157

                         170       180
                  ....*....|....*....|....*...
gi 2158414772 155 DDFVekpqeyVGNKINAGLYIFNSAILD 182
Cdd:cd02507   158 DVIA------VDSKTQRLLLLHYEEDLD 179
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 1-334 1.67e-17

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 83.49  E-value: 1.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   1 MKALILVGGYGTRLRPltlTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSYRAEQLEAEMTvhadrlGVKLIFSLE 80
Cdd:PRK14358    8 LDVVILAAGQGTRMKS---ALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQ------GSGVAFARQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  81 EEPLGTAGPLALARKHL-EDDDPFFVLNSDVICDFP--FKQMVEFHKQHGKEGTIAVTKVEEPSKYGVVVFKEDGKIDDF 157
Cdd:PRK14358   79 EQQLGTGDAFLSGASALtEGDADILVLYGDTPLLRPdtLRALVADHRAQGSAMTILTGELPDATGYGRIVRGADGAVERI 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 158 VEK----PQEYVGNKINAGLYIFNSaildRIPLKPTSIEKEifpqmATSGNLYAYVLPGFWMDVG-QPKDF--------- 223
Cdd:PRK14358  159 VEQkdatDAEKAIGEFNSGVYVFDA----RAPELARRIGND-----NKAGEYYLTDLLGLYRAGGaQVRAFklsdpdevl 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 224 -------LKGMSLFLNhvQTTRTGALATGSNIHGTATIrgsvLVDPSATVGENCVIGPDVVIGPRVQIEGGVRIQHSTIL 296
Cdd:PRK14358  230 gandragLAQLEATLR--RRINEAHMKAGVTLQDPGTI----LIEDTVTLGRDVTIEPGVLLRGQTRVADGVTIGAYSVV 303

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 2158414772 297 SDSTVGN------YSWVSGSIIGRECHIGSWVRMENVCVLGDDV 334
Cdd:PRK14358  304 TDSVLHEgavikpHSVLEGAEVGAGSDVGPFARLRPGTVLGEGV 347
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-352 2.38e-17

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 82.89  E-value: 2.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   1 MKALILVGGYGTRLRPltlTQPKPLVEFANKPMMLHQMEALAAVGvDTVVLAVSYRAEQLEAEMTVHADrlgvklIFsLE 80
Cdd:PRK14357    1 MRALVLAAGKGTRMKS---KIPKVLHKISGKPMINWVIDTAKKVA-QKVGVVLGHEAELVKKLLPEWVK------IF-LQ 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  81 EEPLGTAGPLALARKHLEDDDPFFVLNSDV--ICDFPFKQMVEFHKQHGKEGTIAVTKVEEPSKYGVVVfKEDGKIDDFV 158
Cdd:PRK14357   70 EEQLGTAHAVMCARDFIEPGDDLLILYGDVplISENTLKRLIEEHNRKGADVTILVADLEDPTGYGRII-RDGGKYRIVE 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 159 EK---PQEYVGNKINAGLYIFnsaildriplkptsiekeifpqmatSGNLYAYVLPGFWMDVGQPKDFLKGMSLFLNHVQ 235
Cdd:PRK14357  149 DKdapEEEKKIKEINTGIYVF-------------------------SGDFLLEVLPKIKNENAKGEYYLTDAVNFAEKVR 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 236 TTRTGAL--ATGSN---------------IHGTATIRGSVLVDPSAT-VGENCVIGPDVVIGPRVQIEGGVRIQHstils 297
Cdd:PRK14357  204 VVKTEDLleITGVNtriqlawlekqlrmrILEELMENGVTILDPNTTyIHYDVEIGMDTIIYPMTFIEGKTRIGE----- 278

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2158414772 298 DSTVGNYSWVSGSIIGRECHIgswVRME-NVCVLGDDVVVKDEVYLNEASVLPHKV 352
Cdd:PRK14357  279 DCEIGPMTRIVDCEIGNNVKI---IRSEcEKSVIEDDVSVGPFSRLREGTVLKKSV 331
glgC PRK00844
glucose-1-phosphate adenylyltransferase; Provisional
 3-338 2.51e-17

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234846 [Multi-domain]  Cd Length: 407  Bit Score: 82.57  E-value: 2.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   3 ALILVGGYGTRLRPLTLTQPKP---------LVEFA--NkpmmlhqmeaLAAVGVDTVVLAVSYRAEQLEAEMT------ 65
Cdd:PRK00844    8 AIVLAGGEGKRLMPLTADRAKPavpfggsyrLIDFVlsN----------LVNSGYLRIYVLTQYKSHSLDRHISqtwrls 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  66 ---------VHAD-RLGvKLIFsleeepLGTAGPLALARKHLEDDDP--FFVLNSDVICDFPFKQMVEFHKQHGKEGTIA 133
Cdd:PRK00844   78 gllgnyitpVPAQqRLG-KRWY------LGSADAIYQSLNLIEDEDPdyVVVFGADHVYRMDPRQMVDFHIESGAGVTVA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 134 VTKV--EEPSKYGVVVFKEDGKIDDFVEKPQEYVG-----NKINA--GLYIFNS----AILDRIPLKPTSIE---KEIFP 197
Cdd:PRK00844  151 AIRVprEEASAFGVIEVDPDGRIRGFLEKPADPPGlpddpDEALAsmGNYVFTTdalvDALRRDAADEDSSHdmgGDIIP 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 198 QMATSGNLYAY-----VLPG-------FWMDVG---------------QPKdflkgMSLFlnhvqtTRTGALATGSNIHG 250
Cdd:PRK00844  231 RLVERGRAYVYdfstnEVPGaterdrgYWRDVGtidayydahmdllsvHPV-----FNLY------NREWPIYTSSPNLP 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 251 TATIRGSvlvDPSATVGENCVIGPDVVIgprvqieGGVRIQHSTILSDSTVGNYSWVSGSIIGRECHIGSWVRMENvCVL 330
Cdd:PRK00844  300 PAKFVDG---GGRVGSAQDSLVSAGSII-------SGATVRNSVLSPNVVVESGAEVEDSVLMDGVRIGRGAVVRR-AIL 368


                  ....*...
gi 2158414772 331 GDDVVVKD 338
Cdd:PRK00844  369 DKNVVVPP 376
glgC PRK02862
glucose-1-phosphate adenylyltransferase; Provisional
 1-326 1.10e-16

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179486 [Multi-domain]  Cd Length: 429  Bit Score: 80.70  E-value: 1.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   1 MK---ALILVGGYGTRLRPLTLTQPKPLVEFANK------PMM------LHQMEALaavgvdTVVLAVS--------YR- 56
Cdd:PRK02862    1 MKrvlAIILGGGAGTRLYPLTKLRAKPAVPLAGKyrlidiPISncinsgINKIYVL------TQFNSASlnrhisqtYNf 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  57 -------AEQLEAEMTVhadrlgvklifsleEEP---LGTAGPLalaRK---HLEDDDP--FFVLNSDVICDFPFKQMVE 121
Cdd:PRK02862   75 dgfsggfVEVLAAQQTP--------------ENPswfQGTADAV---RKylwHFQEWDVdeYLILSGDQLYRMDYRLFVQ 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 122 FHKQHGKEGTIAVTKVEE--PSKYGVVVFKEDGKIDDFVEKPQeyvGNKINA------------------------GLYI 175
Cdd:PRK02862  138 HHRETGADITLAVLPVDEkdASGFGLMKTDDDGRITEFSEKPK---GDELKAmavdtsrlglspeeakgkpylasmGIYV 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 176 FNSAILDRIpLK--PTSIE--KEIFPQMATSGNLYAYVLPGFWMDVGQPKDFLKGmSLFLNHVQT-------------TR 238
Cdd:PRK02862  215 FSRDVLFDL-LNknPEYTDfgKEIIPEAIRDYKVQSYLFDGYWEDIGTIEAFYEA-NLALTQQPNppfsfydekapiyTR 292

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 239 TGALATgSNIHGtATIRGSVlvdpsatVGENCVIGPDV----VIGPRVQIEGGVRIQHSTIL-SDS-------------- 299
Cdd:PRK02862  293 ARYLPP-SKLLD-ATITESI-------IAEGCIIKNCSihhsVLGIRSRIESGCTIEDTLVMgADFyesseereelrkeg 363

                         410       420       430
                  ....*....|....*....|....*....|.
gi 2158414772 300 ----TVGNYSWVSGSIIGRECHIGSWVRMEN 326
Cdd:PRK02862  364 kpplGIGEGTTIKRAIIDKNARIGNNVRIVN 394
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-190 3.06e-16

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 78.18  E-value: 3.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   2 KALILVGGYGTRLRPLTLTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSYRAEQLEAEMTVHADRLGVKLIFSLEE 81
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  82 EPLGTAGPLALARKHLEDDDPFFVLNSDVICDFPFKQMVEFHKQHGKEGTIAVTKVEEPSKYGVVVFKEDGKIDDFVEKP 161
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164

                         170       180       190
                  ....*....|....*....|....*....|
gi 2158414772 162 QEYVGNKINAGLYIFNSAILDRIP-LKPTS 190
Cdd:PRK15480  165 LQPKSNYAVTGLYFYDNDVVEMAKnLKPSA 194
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-333 1.58e-15

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 77.67  E-value: 1.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   3 ALILVGGYGTRLRPLTltqPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSYRAEQLEAemtvHADRLGVKLIFSLEEE 82
Cdd:PRK14352    7 VIVLAAGAGTRMRSDT---PKVLHTLAGRSMLGHVLHAAAGLAPQHLVVVVGHDRERVAP----AVAELAPEVDIAVQDE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  83 PLGTAGPLALARKHLED--DDPFFVLNSDVicdfPF------KQMVEFHKQHGKEGTIAVTKVEEPSKYGVVVFKEDGKI 154
Cdd:PRK14352   80 QPGTGHAVQCALEALPAdfDGTVVVTAGDV----PLldgetlADLVATHTAEGNAVTVLTTTLDDPTGYGRILRDQDGEV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 155 DDFVEK----PQEYVGNKINAGLYIFNSAILdRIPLKPTSIEKeifpqmaTSGNLY----------------AYVLPGFW 214
Cdd:PRK14352  156 TAIVEQkdatPSQRAIREVNSGVYAFDAAVL-RSALARLSSDN-------AQGELYltdvlaiareaghrvgAHHADDSA 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 215 MdvgqpkdfLKGMSlflNHVQttrtgaLATGSNIHGTATIR-----GSVLVDPSAT-VGENCVIGPDVVIGPRVQIEGGV 288
Cdd:PRK14352  228 E--------VAGVN---DRVQ------LAALGAELNRRIVEawmraGVTIVDPATTwIDVDVTIGRDVVIHPGTQLLGRT 290

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2158414772 289 RIQHS------TILSDSTVGNYSWV-----SGSIIGRECHIGSWVRMENVCVLGDD 333
Cdd:PRK14352  291 TIGEDavvgpdTTLTDVTVGEGASVvrthgSESEIGAGATVGPFTYLRPGTVLGEE 346
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-347 5.44e-15

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 75.67  E-value: 5.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   3 ALILVGGYGTRLR-PLtltqPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSYRAEQLEAEmtvhADRLGVKLIFSLEE 81
Cdd:PRK14353    8 AIILAAGEGTRMKsSL----PKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVAAA----AAKIAPDAEIFVQK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  82 EPLGTAGPLALARKHLED-DDPFFVLNSDV--ICDFPFKQMVEfHKQHGKEGTIAVTKVEEPSKYGVVVfKEDGKIDDFV 158
Cdd:PRK14353   80 ERLGTAHAVLAAREALAGgYGDVLVLYGDTplITAETLARLRE-RLADGADVVVLGFRAADPTGYGRLI-VKGGRLVAIV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 159 EK----PQEYvgnKI---NAGLYIFNSA----ILDRIplKPTSIEKEIF----PQMATSGNLYAYVlpgfwmdVGQPKDF 223
Cdd:PRK14353  158 EEkdasDEER---AItlcNSGVMAADGAdalaLLDRV--GNDNAKGEYYltdiVAIARAEGLRVAV-------VEAPEDE 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 224 LKGM----------SLFlnhvQT-TRTGALATGsnihgtATirgsvLVDPsATV--------GENCVIGPDVVIGPRVQI 284
Cdd:PRK14353  226 VRGInsraelaeaeAVW----QArRRRAAMLAG------VT-----LIAP-ETVffsydtviGRDVVIEPNVVFGPGVTV 289

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2158414772 285 EGGVRIqHS-------TILSDSTVGNYSWVS-GSIIGRECHIGSWVRMENVcVLGDDVVVKDEVYLNEASV 347
Cdd:PRK14353  290 ASGAVI-HAfshlegaHVGEGAEVGPYARLRpGAELGEGAKVGNFVEVKNA-KLGEGAKVNHLTYIGDATI 358
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 2-236 7.33e-15

glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase homotetramer This model describes a tightly conserved but broadly distributed subfamily (here designated as short form) of known and putative bacterial glucose-1-phosphate thymidylyltransferases. It is well characterized in several species as the first of four enzymes involved in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 130274 [Multi-domain]  Cd Length: 286  Bit Score: 73.97  E-value: 7.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   2 KALILVGGYGTRLRPLTLTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSYRAEQLEAEMTVHADRLGVKLIFSLEE 81
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  82 EPLGTAGPLALARKHLEDDDPFFVLNSDVICDFPFKQMVEF--HKQHGkeGTIAVTKVEEPSKYGVVVFKEDGKIDDFVE 159
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRaaARTEG--ATVFAYQVSDPERYGVVEFDSNGRAISIEE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 160 KPQEYVGNKINAGLYIFNSAILD---------RIPLKPTSIEKEIFPQmatsGNLYAYVLP-GF-WMDVGQpKDFLKGMS 228
Cdd:TIGR01207 159 KPAQPKSNYAVTGLYFYDNRVVEiarqlkpsaRGELEITDLNRVYLEE----GRLSVELLGrGYaWLDTGT-HDSLLEAS 233


                  ....*...
gi 2158414772 229 LFLNHVQT 236
Cdd:TIGR01207 234 NFIQTIEK 241
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 1-126 3.35e-14

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


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 70.77  E-value: 3.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   1 MKALILVGGYGTRLRPLTLTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSyRAEQLEAEMTVHADRLGVKLIFSLE 80
Cdd:cd04198     1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVP-EEEQAEISTYLRSFPLNLKQKLDEV 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2158414772  81 ----EEPLGTAGPLALARKHLEDDdpFFVLNSDVICDFPFKQMVEFHKQH 126
Cdd:cd04198    80 tivlDEDMGTADSLRHIRKKIKKD--FLVLSCDLITDLPLIELVDLHRSH 127
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 4-206 5.07e-14

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: 70.75  E-value: 5.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   4 LILVGGYGTRLRPLTLTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVsyRAEQLEAEMTVHADRLGVKL--IFSLEE 81
Cdd:cd04183     2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFIC--RDEHNTKFHLDESLKLLAPNatVVELDG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  82 EPLGTAGPLALARKHLEDDDPFFVLNSDVICDFPFKQMVEFHKQHGKEGTIAVTKVEEPsKYGVVVFKEDGKIDDFVEKp 161
Cdd:cd04183    80 ETLGAACTVLLAADLIDNDDPLLIFNCDQIVESDLLAFLAAFRERDLDGGVLTFFSSHP-RWSYVKLDENGRVIETAEK- 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2158414772 162 qEYVGNKINAGLYIFNSAILDRiplkpTSIEKEIFPQMATSGNLY 206
Cdd:cd04183   158 -EPISDLATAGLYYFKSGSLFV-----EAAKKMIRKDDSVNGEFY 196
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
 3-318 3.09e-13

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 70.25  E-value: 3.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   3 ALILVGGYGTRLRPLTLTQPKPLVEFANK------PM--MLHQmealaavGVDTVVLAVSYRAEQL-----------EAE 63
Cdd:PRK00725   18 ALILAGGRGSRLKELTDKRAKPAVYFGGKfriidfALsnCINS-------GIRRIGVLTQYKAHSLirhiqrgwsffREE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  64 MTVHADRLGVKLIFSLEEEPLGTAGP----LALARKHleddDPFFV--LNSDVICDFPFKQMVEFHKQHGKEGTIAVTKV 137
Cdd:PRK00725   91 LGEFVDLLPAQQRVDEENWYRGTADAvyqnLDIIRRY----DPKYVviLAGDHIYKMDYSRMLADHVESGADCTVACLEV 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 138 --EEPSKYGVVVFKEDGKIDDFVEKPQE---YVGNKINA----GLYIFNSA----ILDRIPLKPTS---IEKEIFPQMAT 201
Cdd:PRK00725  167 prEEASAFGVMAVDENDRITAFVEKPANppaMPGDPDKSlasmGIYVFNADylyeLLEEDAEDPNSshdFGKDIIPKIVE 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 202 SGNLYAY-----------VLPGFWMDVGQPKDFLKG-MSLF-----LNHVQT-----TRTGALATGSNIHGTATIRGSVL 259
Cdd:PRK00725  247 EGKVYAHpfsdscvrsdpEEEPYWRDVGTLDAYWQAnLDLAsvtpeLDLYDRnwpiwTYQEQLPPAKFVFDRSGRRGMAI 326

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2158414772 260 vdpSATVGENCVI-GPDV---VIGPRVQIEGGVRIQHSTILSDSTVGNYSWVSGSIIGRECHI 318
Cdd:PRK00725  327 ---NSLVSGGCIIsGAVVrrsVLFSRVRVNSFSNVEDSVLLPDVNVGRSCRLRRCVIDRGCVI 386
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 233-334 2.95e-12

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 66.70  E-value: 2.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 233 HVQTTRTGAlatgSNIHGTATIRGSVLVDPSATVGENCVIGPDVVIGPRVQIEGGVRI-QHSTILSDSTVG-NYSWVSGS 310
Cdd:PRK00892   92 DPPATPSPA----AGIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVIGDGVVIGAGAVIgDGVKIGADCRLHaNVTIYHAV 167

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2158414772 311 IIGRECHI-----------------GSWVRME---NVcVLGDDV 334
Cdd:PRK00892  168 RIGNRVIIhsgavigsdgfgfandrGGWVKIPqlgRV-IIGDDV 210
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 3-138 3.09e-12

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: 63.75  E-value: 3.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   3 ALILVGGYGTRLRpltltQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAvsyRAEQLEAemtvHADRLGVKLIfsleEE 82
Cdd:pfam12804   1 AVILAGGRSSRMG-----GDKALLPLGGKPLLERVLERLRPAGDEVVVVA---NDEEVLA----ALAGLGVPVV----PD 64

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2158414772  83 PLGTAGPLA---LARKHLEDDDPFFVLNsdviCDFPF------KQMVEFHKQHGKEGTIAVTKVE 138
Cdd:pfam12804  65 PDPGQGPLAgllAALRAAPGADAVLVLA----CDMPFltpellRRLLAAAEESGADIVVPVYDGG 125
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-129 5.91e-12

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


Pssm-ID: 133040 [Multi-domain]  Cd Length: 217  Bit Score: 64.55  E-value: 5.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   3 ALILVGGYGTRLRPLTLTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSYRAEQLEA-------------EMTVHad 69
Cdd:cd04197     3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEyiekskwskpkssLMIVI-- 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2158414772  70 rlgvkLIFSLEEEPLGTAgpL-ALARKHLEDDDpFFVLNSDVICDFPFKQMVEFHKQHGKE 129
Cdd:cd04197    81 -----IIMSEDCRSLGDA--LrDLDAKGLIRGD-FILVSGDVVSNIDLKEILEEHKERRKK 133
LpxD COG1044
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase [Cell wall/membrane/envelope ...
 248-334 1.11e-11

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


Pssm-ID: 440666 [Multi-domain]  Cd Length: 335  Bit Score: 65.04  E-value: 1.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 248 IHGTATIRGSVLVDPSATVGENCVIGPDVVIGPRVQIEGGVriqhsTILSDSTVGNYSWV-------SGSIIGRECHI-- 318
Cdd:COG1044    99 IHPSAVIDPSAKIGEGVSIGPFAVIGAGVVIGDGVVIGPGV-----VIGDGVVIGDDCVLhpnvtiyERCVIGDRVIIhs 173

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2158414772 319 ----------------GSWVRME---NVcVLGDDV 334
Cdd:COG1044   174 gavigadgfgfapdedGGWVKIPqlgRV-VIGDDV 207
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 251-336 2.81e-11

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 62.05  E-value: 2.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 251 TATIRGSVLVDPSATVGENCVIGPDVVIGPRVQIEGGVRIQHSTILSDSTVGNYSWVSGSIIGRECHIGSWVRMENVCVL 330
Cdd:cd03353     9 TTYIDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIKDSTIGDGVVIKASSVIEGAVIGNGATVGPFAHLRPGTVL 88


                  ....*.
gi 2158414772 331 GDDVVV 336
Cdd:cd03353    89 GEGVHI 94
PLN02241 PLN02241
glucose-1-phosphate adenylyltransferase
 3-296 3.53e-11

glucose-1-phosphate adenylyltransferase


Pssm-ID: 215133 [Multi-domain]  Cd Length: 436  Bit Score: 64.11  E-value: 3.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   3 ALILVGGYGTRLRPLTLTQPKPLVEFA------------------NKPMMLHQMEA------LAA-----VGVDT----V 49
Cdd:PLN02241    6 AIILGGGAGTRLFPLTKRRAKPAVPIGgnyrlidipmsncinsgiNKIYVLTQFNSaslnrhLSRaynfgNGGNFgdgfV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  50 -VLAvsyrAEQleaemtvhadrlgvklifSLEEE--PLGTAGPLalaRKHL--------EDDDPFFVLNSDVICDFPFKQ 118
Cdd:PLN02241   86 eVLA----ATQ------------------TPGEKgwFQGTADAV---RQFLwlfedaknKNVEEVLILSGDHLYRMDYMD 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 119 MVEFHKQHGKEGTIAVTKVEE--PSKYGVVVFKEDGKIDDFVEKPQ------------------------EYVGNkinAG 172
Cdd:PLN02241  141 FVQKHRESGADITIACLPVDEsrASDFGLMKIDDTGRIIEFSEKPKgdelkamqvdttvlglspeeakekPYIAS---MG 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 173 LYIFNSAILDRIpLK---PTSIE--KEIFPQMATSG-NLYAYVLPGFWMDVGQPKDFLKG-MSLflnhvqTTRTGALA-- 243
Cdd:PLN02241  218 IYVFKKDVLLKL-LRwrfPTANDfgSEIIPGAIKEGyNVQAYLFDGYWEDIGTIKSFYEAnLAL------TKQPPKFSfy 290

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2158414772 244 -------TGSNIHGTATIRGSVLVDpsATVGENCVIG----PDVVIGPRVQIEGGVRIQHSTIL 296
Cdd:PLN02241  291 dpdapiyTSPRFLPPSKIEDCRITD--SIISHGCFLReckiEHSVVGLRSRIGEGVEIEDTVMM 352
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
 3-217 3.89e-11

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


Pssm-ID: 133002 [Multi-domain]  Cd Length: 200  Bit Score: 61.79  E-value: 3.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   3 ALILVGGYGTRLRPLTLTQPKPLVEFANK------PM--MLHQmealaavGVDTVVLAVSYRAEQLE------AEMTVHA 68
Cdd:cd02508     1 AIILAGGEGTRLSPLTKKRAKPAVPFGGRyrlidfPLsnMVNS-------GIRNVGVLTQYKSRSLNdhlgsgKEWDLDR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  69 DRLGVKLIF---SLEEEPL-GTAGPLALARKHLEDDDP--FFVLNSDVICDFPFKQMVEFHKQHGKEGTIAVtkveepsk 142
Cdd:cd02508    74 KNGGLFILPpqqRKGGDWYrGTADAIYQNLDYIERSDPeyVLILSGDHIYNMDYREMLDFHIESGADITVVY-------- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 143 ygvvvfkedgkiddfvekpqeyvgnKINAGLYIFNSAILdrIPL-----KPTSIE--KEIFPQMATSGNLYAYVLPGFWM 215
Cdd:cd02508   146 -------------------------KASMGIYIFSKDLL--IELleedaADGSHDfgKDIIPAMLKKLKIYAYEFNGYWA 198


                  ..
gi 2158414772 216 DV 217
Cdd:cd02508   199 DI 200
LbH_GlmU_C cd03353
N-acetyl-glucosamine-1-phosphate uridyltransferase (GlmU), C-terminal left-handed beta-helix ...
 248-347 8.29e-11

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


Pssm-ID: 100044 [Multi-domain]  Cd Length: 193  Bit Score: 60.51  E-value: 8.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 248 IHGTATIRGSVLVDPSATVGENCVIGPDVVIGPRVQIEG-----GVRIQHSTILSDSTVGNYSWV-------SGSIIGRE 315
Cdd:cd03353    12 IDGDVEIGVDVVIDPGVILEGKTVIGEDCVIGPNCVIKDstigdGVVIKASSVIEGAVIGNGATVgpfahlrPGTVLGEG 91

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2158414772 316 CHIGSWVRMENVcVLGDDVVVKDEVYLNEASV 347
Cdd:cd03353    92 VHIGNFVEIKKS-TIGEGSKANHLSYLGDAEI 122
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 263-333 1.58e-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: 60.11  E-value: 1.58e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2158414772 263 SATVGENCVIGPDVVIGPRVQIEGGVRIQ-HSTILSDSTVGNYSWV-SGSIIGRECHIGSWVRMENVCVLGDD 333
Cdd:cd03352     1 SAKIGENVSIGPNAVIGEGVVIGDGVVIGpGVVIGDGVVIGDDCVIhPNVTIYEGCIIGDRVIIHSGAVIGSD 73
glmU PRK09451
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-324 1.79e-10

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


Pssm-ID: 181867 [Multi-domain]  Cd Length: 456  Bit Score: 61.97  E-value: 1.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   1 MKALILVGGYGTRLRPltlTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSYRAEQLEAEMTvhadrlGVKLIFSLE 80
Cdd:PRK09451    6 MSVVILAAGKGTRMYS---DLPKVLHTLAGKPMVQHVIDAANELGAQHVHLVYGHGGDLLKQTLA------DEPLNWVLQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  81 EEPLGTAGPLALARKHLEDDDPFFVLNSDVicdfPF--KQMVEFHKQHGKEGTIAVTKV--EEPSKYGVVVfKEDGKIDD 156
Cdd:PRK09451   77 AEQLGTGHAMQQAAPFFADDEDILMLYGDV----PLisVETLQRLRDAKPQGGIGLLTVklDNPTGYGRIT-RENGKVVG 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 157 FVEK----PQEYVGNKINAGLYIFNSAILDR--IPLKPTSIEKE-----IFPQMATSGNLYAYVLPGFWMDVGQPKDFLK 225
Cdd:PRK09451  152 IVEQkdatDEQRQIQEINTGILVANGADLKRwlAKLTNNNAQGEyyitdIIALAHQEGREIVAVHPQRLSEVEGVNNRLQ 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 226 gMSLFLNHVQTTRTGALatgsnihgtaTIRGSVLVDPSA-------TVGENCVIGPDVVI------GPRVQIEGGVRIQH 292
Cdd:PRK09451  232 -LARLERVYQAEQAEKL----------LLAGVMLRDPARfdlrgtlTHGRDVEIDTNVIIegnvtlGNRVKIGAGCVLKN 300

                         330       340       350
                  ....*....|....*....|....*....|..
gi 2158414772 293 STILSDSTVGNYSWVSGSIIGRECHIGSWVRM 324
Cdd:PRK09451  301 CVIGDDCEISPYSVVEDANLGAACTIGPFARL 332
LbH_LpxD cd03352
UDP-3-O-acyl-glucosamine N-acyltransferase (LpxD): The enzyme catalyzes the transfer of ...
 248-336 3.51e-10

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


Pssm-ID: 100043 [Multi-domain]  Cd Length: 205  Bit Score: 58.96  E-value: 3.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 248 IHGTATIRGSVLVDPSATVGENCVIGPDVVIGPRVQIEGGVRI-QHSTILSDSTVGNYSWV-SGSIIGREC-----HIGS 320
Cdd:cd03352     4 IGENVSIGPNAVIGEGVVIGDGVVIGPGVVIGDGVVIGDDCVIhPNVTIYEGCIIGDRVIIhSGAVIGSDGfgfapDGGG 83

                          90
                  ....*....|....*....
gi 2158414772 321 WVRME---NVcVLGDDVVV 336
Cdd:cd03352    84 WVKIPqlgGV-IIGDDVEI 101
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 1-184 4.60e-10

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


Pssm-ID: 133003 [Multi-domain]  Cd Length: 274  Bit Score: 59.51  E-value: 4.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   1 MKALILVGGYGTRLRPL-TLTQPKPLVEFANKPMMLHQ-MEALAAVGVDTVVLAV---SYR---AEQLEAEMtvhadrLG 72
Cdd:cd02509     1 IYPVILAGGSGTRLWPLsRESYPKQFLKLFGDKSLLQQtLDRLKGLVPPDRILVVtneEYRflvREQLPEGL------PE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  73 VKLIFsleeEPLG--TAGPLALARKHLE---DDDPFFVLNSD-VICDFP-FKQMVEFHKQHGKEGTIaVT---KVEEPS- 141
Cdd:cd02509    75 ENIIL----EPEGrnTAPAIALAALYLAkrdPDAVLLVLPSDhLIEDVEaFLKAVKKAVEAAEEGYL-VTfgiKPTRPEt 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2158414772 142 KYGVVVFKEDG-----KIDDFVEKP-----QEYV--GNKI-NAGLYIFNSA-ILDRI 184
Cdd:cd02509   150 GYGYIEAGEKLgggvyRVKRFVEKPdletaKEYLesGNYLwNSGIFLFRAKtFLEEL 206
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-180 5.03e-10

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 59.90  E-value: 5.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   1 MKALILVGGYGTRLRPLTLTQPKPLVEFANKPMMLHQMEALAAVGVDTVVL-------AV------SYRAEQLeAEMTVH 67
Cdd:PRK10122    4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLvthasknAVenhfdtSYELESL-LEQRVK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  68 ADRL---------GVKLIFSLEEEPLGTAGPLALARKHLeDDDPFFVLNSDVICD--------FPFKQMVEFHKQHGKEG 130
Cdd:PRK10122   83 RQLLaevqsicppGVTIMNVRQGQPLGLGHSILCARPAI-GDNPFVVVLPDVVIDdasadplrYNLAAMIARFNETGRSQ 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 131 TIAVTKVEEPSKYGVVVFKE----DGKID---DFVEK---PQEYVGNKINAGLYIFNSAI 180
Cdd:PRK10122  162 VLAKRMPGDLSEYSVIQTKEpldrEGKVSrivEFIEKpdqPQTLDSDLMAVGRYVLSADI 221
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-326 6.21e-10

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 60.39  E-value: 6.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   4 LILVGGYGTRLRPLTltqPKPLVEFANKPMMLHQMEALAAVGVD-TVVLavSYRAEQLEAEMTVHADrlGVKLIFSLEEE 82
Cdd:PRK14359    6 IILAAGKGTRMKSSL---PKVLHTICGKPMLFYILKEAFAISDDvHVVL--HHQKERIKEAVLEYFP--GVIFHTQDLEN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  83 PLGTAGPL-ALARKHleddDPFFVLNSDVicdfPFKQMVEFHKQHGKEGTIA--VTKVEEPSKYGVVVFkEDGKIDDFVE 159
Cdd:PRK14359   79 YPGTGGALmGIEPKH----ERVLILNGDM----PLVEKDELEKLLENDADIVmsVFHLADPKGYGRVVI-ENGQVKKIVE 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 160 ----KPQEYVGNKINAGLYIFNSAILDR-IP-LKPTSIEKEIF----PQMATSGNLY---AYVLPGFWMDVGQPKDFLKG 226
Cdd:PRK14359  150 qkdaNEEELKIKSVNAGVYLFDRKLLEEyLPlLKNQNAQKEYYltdiIALAIEKGETikaVFVDEENFMGVNSKFELAKA 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 227 MSLFLNHVqttRTGALATGSNIHGTATIrgsvLVDPSAT-VGEnCVIGPDVVIGPRVQIEGGVRIQHSTI----LSDSTV 301
Cdd:PRK14359  230 EEIMQERI---KKNAMKQGVIMRLPETI----YIESGVEfEGE-CELEEGVRILGKSKIENSHIKAHSVIeesiIENSDV 301

                         330       340
                  ....*....|....*....|....*.
gi 2158414772 302 GNYSWVS-GSIIgRECHIGSWVRMEN 326
Cdd:PRK14359  302 GPLAHIRpKSEI-KNTHIGNFVETKN 326
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 259-338 1.91e-09

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: 53.74  E-value: 1.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 259 LVDPSATVGENCVIGpDVVIGPRVQIEGGVRIQHSTILSDSTVGNYSWVSGSIIGRECHIGSWVRMENVCVLGDDVVVKD 338
Cdd:cd05787     1 VIGRGTSIGEGTTIK-NSVIGRNCKIGKNVVIDNSYIWDDVTIEDGCTIHHSIVADGAVIGKGCTIPPGSLISFGVVIGD 79
LbH_AT_putative cd03360
Putative Acyltransferase (AT), Left-handed parallel beta-Helix (LbH) domain; This group is ...
 248-336 2.26e-09

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: 56.34  E-value: 2.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 248 IHGTATirgsvlVDPSATVGENCVIGPDVVIGPRVQIEGGVRIQHSTILS-DSTVGNYSWVS-------GSIIGRECHIG 319
Cdd:cd03360    87 IHPSAV------VSPSAVIGEGCVIMAGAVINPDARIGDNVIINTGAVIGhDCVIGDFVHIApgvvlsgGVTIGEGAFIG 160

                          90       100
                  ....*....|....*....|..
gi 2158414772 320 SwvrmeNVCVL-----GDDVVV 336
Cdd:cd03360   161 A-----GATIIqgvtiGAGAII 177
LpxA COG1043
Acyl-[acyl carrier protein]--UDP-N-acetylglucosamine O-acyltransferase [Cell wall/membrane ...
 246-320 2.57e-09

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: 57.34  E-value: 2.57e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2158414772 246 SNIHGTAtirgsvLVDPSATVGENCVIGPDVVIGPRVQIEGGVRI-QHSTILSDSTvgnyswvsgsiIGRECHIGS 320
Cdd:COG1043     2 AMIHPTA------IVDPGAKLGENVEIGPFCVIGPDVEIGDGTVIgSHVVIEGPTT-----------IGKNNRIFP 60
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 8-154 9.88e-09

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: 54.51  E-value: 9.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   8 GGYGTRLRPLTltqpKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSYRAEQLEAemtvHADRLGVKLIFsleeeplgTA 87
Cdd:COG2266     3 GGKGTRLGGGE----KPLLEICGKPMIDRVIDALEESCIDKIYVAVSPNTPKTRE----YLKERGVEVIE--------TP 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  88 GP-----LALARKHLedDDPFFVLNSDVicdfPF------KQMVEFHKQHGKEGTIAVTKVEEPSKYGV---VVFKEDGK 153
Cdd:COG2266    67 GEgyvedLNEALESI--SGPVLVVPADL----PLltpeiiDDIIDAYLESGKPSLTVVVPAALKRELGVspdTTFEIDGE 140


                  .
gi 2158414772 154 I 154
Cdd:COG2266   141 L 141
PRK05289 PRK05289
acyl-ACP--UDP-N-acetylglucosamine O-acyltransferase;
246-320 1.93e-08

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


Pssm-ID: 235390 [Multi-domain]  Cd Length: 262  Bit Score: 54.72  E-value: 1.93e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2158414772 246 SNIHGTAtirgsvLVDPSATVGENCVIGPDVVIGPRVQIEGGVRI-QHSTILSDSTvgnyswvsgsiIGRECHIGS 320
Cdd:PRK05289    3 AKIHPTA------IVEPGAKIGENVEIGPFCVIGPNVVIGDGTVIgSHVVIDGHTT-----------IGKNNRIFP 61
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 264-336 2.09e-08

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 50.71  E-value: 2.09e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2158414772 264 ATVGENCVIGPDVVIGPRVQIEGGVRIQHSTILSDSTVGNYSwvSGSIIGRECHIGSWVRMENVCVLGDDVVV 336
Cdd:cd00208     1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAATGPNEK--NPTIIGDNVEIGANAVIHGGVKIGDNAVI 71
LbH_Dynactin_5 cd03359
Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that ...
 248-349 2.60e-08

Dynactin 5 (or subunit p25); Dynactin is a major component of the activator complex that stimulates dynein-mediated vesicle transport. Dynactin is a heterocomplex of at least eight subunits, including a 150,000-MW protein called Glued, the actin-capping protein Arp1, and dynamatin. In vitro binding experiments show that dynactin enhances dynein-dependent motility, possibly through interaction with microtubules and vesicles. Subunit p25 is part of the pointed-end subcomplex in dynactin that also includes p26, p27, and Arp11. This subcomplex interacts with membranous cargoes. p25 and p27 contain imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), indicating a left-handed parallel beta helix (LbH) structural domain. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100049 [Multi-domain]  Cd Length: 161  Bit Score: 52.60  E-value: 2.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 248 IHGTATIRGSVLvdpSATVGENCVIGPDVVIGPRVQIEGGVrIQHSTIlsdsTVGNYSWV-SGSIIgRECHIGSWVRMEN 326
Cdd:cd03359    30 IQSDVIIRGDLA---TVSIGRYCILSEGCVIRPPFKKFSKG-VAFFPL----HIGDYVFIgENCVV-NAAQIGSYVHIGK 100

                          90       100
                  ....*....|....*....|...
gi 2158414772 327 VCVLGDDVVVKDEVYLNEASVLP 349
Cdd:cd03359   101 NCVIGRRCIIKDCVKILDGTVVP 123
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 241-337 6.49e-08

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: 51.43  E-value: 6.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 241 ALATGSNIHGTATIRGSVLVDPSATVGENCVIGPDVVIGPRVQIEGGVRIQHSTILSDSTVGNYSWVSGSIIGRECHIGS 320
Cdd:cd05636    19 WIGEGAIVRSGAYIEGPVIIGKGCEIGPNAYIRGYTVLGDGCVVGNSVEVKNSIIMDGTKVPHLNYVGDSVLGENVNLGA 98

                          90
                  ....*....|....*..
gi 2158414772 321 WVRMENVCVLGDDVVVK 337
Cdd:cd05636    99 GTITANLRFDDKPVKVR 115
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 1-139 1.07e-07

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: 51.42  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   1 MKALILVGGYGTRLrpltlTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAvsyRAEQLEAEmtvhadRLGVKLIfsle 80
Cdd:cd02503     1 ITGVILAGGKSRRM-----GGDKALLELGGKPLLEHVLERLKPLVDEVVISA---NRDQERYA------LLGVPVI---- 62

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2158414772  81 EEPLGTAGPLA---LARKHLEDDDpFFVLNsdviCDFPF--KQMVEFHKQHGKEGT-IAVTKVEE 139
Cdd:cd02503    63 PDEPPGKGPLAgilAALRAAPADW-VLVLA----CDMPFlpPELLERLLAAAEEGAdAVVPKSGG 122
lpxD PRK00892
UDP-3-O-[3-hydroxymyristoyl] glucosamine N-acyltransferase; Provisional
 249-353 1.87e-07

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


Pssm-ID: 234858 [Multi-domain]  Cd Length: 343  Bit Score: 52.06  E-value: 1.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 249 HGTATIRGSVLVDPSATVGENCVIGPDVVIGPRVQIEGGVRIqhstilsdstvGNyswvsGSIIGRECHIGSWVRMENVC 328
Cdd:PRK00892   92 DPPATPSPAAGIHPSAVIDPSAKIGEGVSIGPNAVIGAGVVI-----------GD-----GVVIGAGAVIGDGVKIGADC 155

                          90       100
                  ....*....|....*....|....*.
gi 2158414772 329 VLGDDVVVKDEVYL-NEASVLPHKVI 353
Cdd:PRK00892  156 RLHANVTIYHAVRIgNRVIIHSGAVI 181
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-116 2.82e-07

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: 50.19  E-value: 2.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   1 MKALILVGGYGTRLRpltltQPKPLVEFANKPMMLHQMEALAAVgVDTVVLaVSYRAEQLEAemtvhadrLGVKLIfsle 80
Cdd:COG0746     5 ITGVILAGGRSRRMG-----QDKALLPLGGRPLLERVLERLRPQ-VDEVVI-VANRPERYAA--------LGVPVV---- 65

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2158414772  81 EEPLGTAGPLA---LARKHLEDDDpFFVlnsdVICDFPF 116
Cdd:COG0746    66 PDDPPGAGPLAgilAALEAAPAEW-VLV----LACDMPF 99
LbH_paaY_like cd04745
paaY-like: This group is composed by uncharacterized proteins with similarity to the protein ...
 246-362 6.20e-07

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


Pssm-ID: 100058 [Multi-domain]  Cd Length: 155  Bit Score: 48.52  E-value: 6.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 246 SNIHGTATIRGSVlvdpsaTVGENCVIGPDVVI---GPRVQIEGGVRIQ-----HSTILSDSTVGNYSWVS------GSI 311
Cdd:cd04745     7 SFVHPTAVLIGDV------IIGKNCYIGPHASLrgdFGRIVIRDGANVQdncviHGFPGQDTVLEENGHIGhgailhGCT 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2158414772 312 IGRECHIG-SWVRMENVcVLGDDVVVKDEVYLNEASVLPHKVIAVNVPSKDI 362
Cdd:cd04745    81 IGRNALVGmNAVVMDGA-VIGEESIVGAMAFVKAGTVIPPRSLIAGSPAKVI 131
LbH_UDP-GlcNAc_AT cd03351
UDP-N-acetylglucosamine O-acyltransferase (UDP-GlcNAc acyltransferase): Proteins in this ...
 247-316 9.99e-07

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: 49.35  E-value: 9.99e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2158414772 247 NIHGTAtirgsvLVDPSATVGEN------CVIGPDVVIGPRVQIEGGVRIQ-HSTILSDSTVGnyswvSGSIIGREC 316
Cdd:cd03351     1 MIHPTA------IVDPGAKIGENveigpfCVIGPNVEIGDGTVIGSHVVIDgPTTIGKNNRIF-----PFASIGEAP 66
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-109 3.66e-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: 46.78  E-value: 3.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   3 ALILVGGYGTRLRpltltQPKPLVEFANKPMMLHQMEALAAVGVDTVVLAVSYRAEQLEAEMtvhaDRLGVKLIFSLE-E 81
Cdd:cd04182     3 AIILAAGRSSRMG-----GNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAAL----AGLPVVVVINPDwE 73

                          90       100
                  ....*....|....*....|....*....
gi 2158414772  82 EPLGTAgpLALARKHLEDD-DPFFVLNSD 109
Cdd:cd04182    74 EGMSSS--LAAGLEALPADaDAVLILLAD 100
LbH_G1P_AT_C cd04651
Glucose-1-phosphate adenylyltransferase, C-terminal Left-handed parallel beta helix (LbH) ...
 266-335 8.56e-06

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


Pssm-ID: 100056 [Multi-domain]  Cd Length: 104  Bit Score: 43.99  E-value: 8.56e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2158414772 266 VGENCVI-GPDV---VIGPRVQIEGGVRIQHSTILSDSTVGNYSWVSGSIIGRECHIGswvrmENVCVLGDDVV 335
Cdd:cd04651    15 VSEGCIIsGGTVensVLFRGVRVGSGSVVEDSVIMPNVGIGRNAVIRRAIIDKNVVIP-----DGVVIGGDPEE 83
PRK12461 PRK12461
UDP-N-acetylglucosamine acyltransferase; Provisional
 247-356 1.39e-05

UDP-N-acetylglucosamine acyltransferase; Provisional


Pssm-ID: 183539 [Multi-domain]  Cd Length: 255  Bit Score: 46.17  E-value: 1.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 247 NIHGTATIrgsvlvDPSATVGENCVIGPDVVIGPRVQIEGGVRI-QHSTILSDSTVGNYSWV------------------ 307
Cdd:PRK12461    1 MIHPTAVI------DPSAKLGSGVEIGPFAVIGANVEIGDGTWIgPHAVILGPTRIGKNNKIhqgavvgdepqdftykge 74

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2158414772 308 -SGSIIGRECHIGSWV------RMENVCVLGDDVVVKDEVYLNEASVLPHKVIAVN 356
Cdd:PRK12461   75 eSRLEIGDRNVIREGVtihrgtKGGGVTRIGNDNLLMAYSHVAHDCQIGNNVILVN 130
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 259-336 3.34e-05

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


Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 41.79  E-value: 3.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 259 LVDPSATVGE-----NCVIGPDVVIGPRVqieggvRIQHSTILSDSTVGNYSWVSGSIIGRECHIGSWVRMENvCVLGDD 333
Cdd:cd04652     1 LVGENTQVGEktsikRSVIGANCKIGKRV------KITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKD-CLVGSG 73


                  ...
gi 2158414772 334 VVV 336
Cdd:cd04652    74 YRV 76
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 299-353 3.91e-05

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


Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 41.41  E-value: 3.91e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2158414772 299 STVGNYSWVSGSIIGRECHIGSWVRMENvCVLGDDVVVKDEVYLnEASVLPHKVI 353
Cdd:cd04652     6 TQVGEKTSIKRSVIGANCKIGKRVKITN-CVIMDNVTIEDGCTL-ENCIIGNGAV 58
LbH_WxcM_N_like cd03358
WcxM-like, Left-handed parallel beta-Helix (LbH) N-terminal domain: This group is composed of ...
 266-307 6.96e-05

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


Pssm-ID: 100048 [Multi-domain]  Cd Length: 119  Bit Score: 41.72  E-value: 6.96e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2158414772 266 VGENCVIGPDVVIGPRVQIEGGVRIQ-HSTILSDSTVGNYSWV 307
Cdd:cd03358     1 IGDNCIIGTNVFIENDVKIGDNVKIQsNVSIYEGVTIEDDVFI 43
PaaY COG0663
Carbonic anhydrase or acetyltransferase, isoleucine patch superfamily [General function ...
 248-336 8.06e-05

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


Pssm-ID: 440427 [Multi-domain]  Cd Length: 170  Bit Score: 42.71  E-value: 8.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 248 IHGTATIRGSVLVDPSATVGENCVIGPDV---VIGPRVQIEGGVRI----QHSTIL-SDSTVGNYSWVSGSIIGRECHIG 319
Cdd:COG0663    19 VAPTAVVIGDVTIGEDVSVWPGAVLRGDVgpiRIGEGSNIQDGVVLhvdpGYPLTIgDDVTIGHGAILHGCTIGDNVLIG 98

                          90
                  ....*....|....*..
gi 2158414772 320 SWVRMENVCVLGDDVVV 336
Cdd:COG0663    99 MGAIVLDGAVIGDGSIV 115
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
 1-116 1.42e-04

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 42.48  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   1 MKALILVGGYGTRLRpltlTQPKPLVEFANKPMMLHQMEALAAVgVDTVVLAVSYRAEQLEAemtvhadrLGVKLIfsLE 80
Cdd:PRK00317    4 ITGVILAGGRSRRMG----GVDKGLQELNGKPLIQHVIERLAPQ-VDEIVINANRNLARYAA--------FGLPVI--PD 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 2158414772  81 EEPlGTAGPLA-----LARKHLEDddpFFVlnsdVICDFPF 116
Cdd:PRK00317   69 SLA-DFPGPLAgilagLKQARTEW---VLV----VPCDTPF 101
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 252-335 2.41e-04

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 39.15  E-value: 2.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 252 ATIRGSVLVDPSATVGENCVIGPDVVIGPRVQIEGGvriQHSTILSDSTVGNYSWVSG-SIIGRECHIGswvrmENVCVL 330
Cdd:cd00208     1 VFIGEGVKIHPKAVIRGPVVIGDNVNIGPGAVIGAA---TGPNEKNPTIIGDNVEIGAnAVIHGGVKIG-----DNAVIG 72


                  ....*
gi 2158414772 331 GDDVV 335
Cdd:cd00208    73 AGAVV 77
LbH_gamma_CA_like cd04645
Gamma carbonic anhydrase-like: This family is composed of gamma carbonic anhydrase (CA), ...
 248-322 2.61e-04

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


Pssm-ID: 100051 [Multi-domain]  Cd Length: 153  Bit Score: 40.86  E-value: 2.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 248 IHGTATIRGSVLVDPSATVGENCVIGPDV---VIGPR----------------VQIEGGVRIQHSTILSDSTVGNYSWV- 307
Cdd:cd04645     8 IAPNATVIGDVTLGEGSSVWFGAVLRGDVnpiRIGERtniqdgsvlhvdpgypTIIGDNVTVGHGAVLHGCTIGDNCLIg 87

                          90
                  ....*....|....*
gi 2158414772 308 SGSIIGRECHIGSWV 322
Cdd:cd04645    88 MGAIILDGAVIGKGS 102
LbetaH cd00208
Left-handed parallel beta-Helix (LbetaH or LbH) domain: The alignment contains 5 turns, each ...
 245-307 5.24e-04

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


Pssm-ID: 100038 [Multi-domain]  Cd Length: 78  Bit Score: 38.38  E-value: 5.24e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2158414772 245 GSNIHGTATIRGSVLVDPSATVGENCVIG--------PDVVIGPRVQIEGGVRI-QHSTILSDSTVGNYSWV 307
Cdd:cd00208     6 GVKIHPKAVIRGPVVIGDNVNIGPGAVIGaatgpnekNPTIIGDNVEIGANAVIhGGVKIGDNAVIGAGAVV 77
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 3-54 8.56e-04

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


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 40.20  E-value: 8.56e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2158414772   3 ALILVGGYGTRLRpltLTQPKPLVEFANKPMMLHQMEALAAVG-VDTVVLAVS 54
Cdd:cd02516     3 AIILAAGSGSRMG---ADIPKQFLELGGKPVLEHTLEAFLAHPaIDEIVVVVP 52
NeuD_NnaD TIGR03570
sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins ...
 258-338 1.17e-03

sugar O-acyltransferase, sialic acid O-acetyltransferase NeuD family; This family of proteins includes the characterized NeuD sialic acid O-acetyltransferase enzymes from E. coli and Streptococcus agalactiae (group B strep). These two are quite closely related to one another, so extension of this annotation to other members of the family in unsupported without additional independent evidence. The neuD gene is often observed in close proximity to the neuABC genes for the biosynthesis of CMP-N-acetylneuraminic acid (CMP-sialic acid), and NeuD sequences from these organisms were used to construct the seed for this model. Nevertheless, there are numerous instances of sequences identified by this model which are observed in a different genomic context (although almost universally in exopolysaccharide biosynthesis-related loci), as well as in genomes for which the biosynthesis of sialic acid (SA) is undemonstrated. Even in the cases where the association with SA biosynthesis is strong, it is unclear in the literature whether the biological substrate is SA iteself, CMP-SA, or a polymer containing SA. Similarly, it is unclear to what extent the enzyme has a preference for acetylation at the 7, 8 or 9 positions. In the absence of evidence of association with SA, members of this family may be involved with the acetylation of differring sugar substrates, or possibly the delivery of alternative acyl groups. The closest related sequences to this family (and those used to root the phylogenetic tree constructed to create this model) are believed to be succinyltransferases involved in lysine biosynthesis. These proteins contain repeats of the bacterial transferase hexapeptide (pfam00132), although often these do not register above the trusted cutoff.


Pssm-ID: 274656 [Multi-domain]  Cd Length: 201  Bit Score: 39.78  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 258 VLVDPSATVGENCVIGPDVVIGPRVQIEGGVRIqhstilsdstvGNYSWV-SGSIIGRECHIGSWvrmenvCVLG-DDVV 335
Cdd:TIGR03570 124 VIINTGAIVEHDCVIGDFVHIAPGVTLSGGVVI-----------GEGVFIgAGATIIQGVTIGAG------AIVGaGAVV 186


                  ...
gi 2158414772 336 VKD 338
Cdd:TIGR03570 187 TKD 189
LbH_MAT_like cd04647
Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, ...
 265-336 1.74e-03

Maltose O-acyltransferase (MAT)-like: This family is composed of maltose O-acetyltransferase, galactoside O-acetyltransferase (GAT), xenobiotic acyltransferase (XAT) and similar proteins. MAT and GAT catalyze the CoA-dependent acetylation of the 6-hydroxyl group of their respective sugar substrates. MAT acetylates maltose and glucose exclusively while GAT specifically acetylates galactopyranosides. XAT catalyzes the CoA-dependent acetylation of a variety of hydroxyl-bearing acceptors such as chloramphenicol and streptogramin, among others. XATs are implicated in inactivating xenobiotics leading to xenobiotic resistance in patients. Members of this family contain a a left-handed parallel beta-helix (LbH) domain with at least 5 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). They are trimeric in their active form.


Pssm-ID: 100053 [Multi-domain]  Cd Length: 109  Bit Score: 37.44  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 265 TVGENCVIGPD--------VVIGPRVQIEGGVRIQ-HSTILSDSTVGNYSWVSGS--IIGRECHIGSwvrmeNVCVL--- 330
Cdd:cd04647     3 SIGDNVYIGPGcvisagggITIGDNVLIGPNVTIYdHNHDIDDPERPIEQGVTSApiVIGDDVWIGA-----NVVILpgv 77


                  ....*...
gi 2158414772 331 --GDDVVV 336
Cdd:cd04647    78 tiGDGAVV 85
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
263-292 2.06e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 35.39  E-value: 2.06e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2158414772 263 SATVGENCVIGPDVVIGPRVQIEGGVRIQH 292
Cdd:pfam00132   1 GTVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
CysE COG1045
Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is ...
 244-362 2.56e-03

Serine acetyltransferase [Amino acid transport and metabolism]; Serine acetyltransferase is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 440667 [Multi-domain]  Cd Length: 174  Bit Score: 38.14  E-value: 2.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 244 TGSNIHGTATIRGSVLVDPSATVgencVIGPDVVIGPRVQIEGGVriqhstilsdsTVGNYSWVSGS---IIGRECHIGS 320
Cdd:COG1045    64 TGIDIHPGATIGRGFFIDHGTGV----VIGETAVIGDNVTIYQGV-----------TLGGTGKEKGKrhpTIGDNVVIGA 128

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2158414772 321 wvrmeNVCVLGDD------------VVVKDevylneasVLPHKViAVNVPSKDI 362
Cdd:COG1045   129 -----GAKILGPItigdnakigansVVLKD--------VPPGST-VVGVPARIV 168
LbH_unknown cd05635
Uncharacterized proteins, Left-handed parallel beta-Helix (LbH) domain: Members in this group ...
 256-311 3.04e-03

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


Pssm-ID: 100059 [Multi-domain]  Cd Length: 101  Bit Score: 36.87  E-value: 3.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2158414772 256 GSVLVDPSATVGENCVIGPDVVIGPrvqieGGVRIQHSTILSDSTVGNYSWVSGSI 311
Cdd:cd05635    10 GPIYIGKDAVIEPFAVIEGPVYIGP-----GSRVKMGARIYGNTTIGPTCKIGGEV 60
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
269-353 3.23e-03

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 37.54  E-value: 3.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 269 NCVIGPDVVIGPRVQIEGG-VRI-QHSTILSDSTVGNYSWVsgsIIGRECHIGSWVRM----------ENVCVLGDDVVV 336
Cdd:COG0110     8 GARIGDGVVIGPGVRIYGGnITIgDNVYIGPGVTIDDPGGI---TIGDNVLIGPGVTIltgnhpiddpATFPLRTGPVTI 84

                          90
                  ....*....|....*...
gi 2158414772 337 KDEVYL-NEASVLPHKVI 353
Cdd:COG0110    85 GDDVWIgAGATILPGVTI 102
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-195 4.13e-03

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 38.73  E-value: 4.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772   2 KALILVGGYGTRLRPLTLTQPKPLVEFANKPMMLHQMEALAAVGVDTVVLaVSYRAE-----------QLEAEMTVHADR 70
Cdd:PRK13389   10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVL-VTHSSKnsienhfdtsfELEAMLEKRVKR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772  71 LGVKLIFSLEEEPL-------GTA---GPLALARKHLEDDDPFFVLNSDVICDF--------PFKQMVEFHKQHGKEgTI 132
Cdd:PRK13389   89 QLLDEVQSICPPHVtimqvrqGLAkglGHAVLCAHPVVGDEPVAVILPDVILDEyesdlsqdNLAEMIRRFDETGHS-QI 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2158414772 133 AVTKVEEPSKYGVVVFK-------EDGKIDDFVEKPQ--EYVGNKINAGLYIFNSAILDRIPLKPTSIEKEI 195
Cdd:PRK13389  168 MVEPVADVTAYGVVDCKgvelapgESVPMVGVVEKPKadVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEI 239
WbbJ COG0110
Acetyltransferase, isoleucine patch superfamily [General function prediction only];
252-362 4.47e-03

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


Pssm-ID: 439880 [Multi-domain]  Cd Length: 140  Bit Score: 37.16  E-value: 4.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2158414772 252 ATIRGSVLVDPSATV-GENCVIGPDVVIGPRVQIE--GGVRI-------QHSTILSDS----------------TVGNYS 305
Cdd:COG0110     9 ARIGDGVVIGPGVRIyGGNITIGDNVYIGPGVTIDdpGGITIgdnvligPGVTILTGNhpiddpatfplrtgpvTIGDDV 88

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2158414772 306 WV-SGSIIGRECHIGSWvrmenvCVLGDD-VVVKDevylneasvLPHKVIAVNVPSKDI 362
Cdd:COG0110    89 WIgAGATILPGVTIGDG------AVVGAGsVVTKD---------VPPYAIVAGNPARVI 132
Hexapep pfam00132
Bacterial transferase hexapeptide (six repeats);
252-280 6.64e-03

Bacterial transferase hexapeptide (six repeats);


Pssm-ID: 459684 [Multi-domain]  Cd Length: 30  Bit Score: 33.85  E-value: 6.64e-03
                          10        20
                  ....*....|....*....|....*....
gi 2158414772 252 ATIRGSVLVDPSATVGENCVIGPDVVIGP 280
Cdd:pfam00132   2 TVIGDNVLIGPNAVIGGGVIIGDNVIIGA 30
COG4801 COG4801
Predicted acyltransferase, contains DUF342 domain [General function prediction only];
275-344 7.63e-03

Predicted acyltransferase, contains DUF342 domain [General function prediction only];


Pssm-ID: 443829 [Multi-domain]  Cd Length: 283  Bit Score: 37.58  E-value: 7.63e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2158414772 275 DVVIGPRVQIEGGVRIQhstilsDSTVGNYSWVSGSIIG-RECHIGSWvrmenvCVLGDDVVVKDEVYLNE 344
Cdd:COG4801    29 DVIVGGQSTIEYGVRGR------NVIAGERVTFGGDIEAeGDCRLDMW------CEVGGNVLVGEDAYLGE 87
 
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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